Protein motif that contains a 33-amino acid long sequence that often occurs in tandem arrays. This repeating sequence of 33-amino acids was discovered in ANKYRIN where it is involved in interaction with the anion exchanger (ANION EXCHANGE PROTEIN 1, ERYTHROCYTE). Ankyrin repeats cooperatively fold into domains that mediate molecular recognition via protein-protein interactions.
A family of membrane-associated proteins responsible for the attachment of the cytoskeleton. Erythrocyte-related isoforms of ankyrin attach the SPECTRIN cytoskeleton to a transmembrane protein (ANION EXCHANGE PROTEIN 1, ERYTHROCYTE) in the erythrocyte plasma membrane. Brain-related isoforms of ankyrin also exist.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Sequences of DNA or RNA that occur in multiple copies. There are several types: INTERSPERSED REPETITIVE SEQUENCES are copies of transposable elements (DNA TRANSPOSABLE ELEMENTS or RETROELEMENTS) dispersed throughout the genome. TERMINAL REPEAT SEQUENCES flank both ends of another sequence, for example, the long terminal repeats (LTRs) on RETROVIRUSES. Variations may be direct repeats, those occurring in the same direction, or inverted repeats, those opposite to each other in direction. TANDEM REPEAT SEQUENCES are copies which lie adjacent to each other, direct or inverted (INVERTED REPEAT SEQUENCES).
A group of telomere associated proteins that interact with TRF1 PROTEIN, contain ANKYRIN REPEATS and have poly(ADP-ribose) polymerase activity.
Microsatellite repeats consisting of three nucleotides dispersed in the euchromatic arms of chromosomes.
A sequential pattern of amino acids occurring more than once in the same protein sequence.
A high molecular weight (220-250 kDa) water-soluble protein which can be extracted from erythrocyte ghosts in low ionic strength buffers. The protein contains no lipids or carbohydrates, is the predominant species of peripheral erythrocyte membrane proteins, and exists as a fibrous coating on the inner, cytoplasmic surface of the membrane.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
A family of inhibitory proteins which bind to the REL PROTO-ONCOGENE PROTEINS and modulate their activity. In the CYTOPLASM, I-kappa B proteins bind to the transcription factor NF-KAPPA B. Cell stimulation causes its dissociation and translocation of active NF-kappa B to the nucleus.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Copies of DNA sequences which lie adjacent to each other in the same orientation (direct tandem repeats) or in the opposite direction to each other (INVERTED TANDEM REPEATS).
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
A poxvirus infection of poultry and other birds characterized by the formation of wart-like nodules on the skin and diphtheritic necrotic masses (cankers) in the upper digestive and respiratory tracts.
A family of conserved cell surface receptors that contain EPIDERMAL GROWTH FACTOR repeats in their extracellular domain and ANKYRIN repeats in their cytoplasmic domains. The cytoplasmic domain of notch receptors is released upon ligand binding and translocates to the CELL NUCLEUS where it acts as transcription factor.
A ubiquitously expressed sequence-specific transcriptional repressor that is normally the target of signaling by NOTCH PROTEINS.
A notch receptor that interacts with a variety of ligands and regulates SIGNAL TRANSDUCTION PATHWAYS for multiple cellular processes. It is widely expressed during EMBRYOGENESIS and is essential for EMBRYONIC DEVELOPMENT.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
Proteins which maintain the transcriptional quiescence of specific GENES or OPERONS. Classical repressor proteins are DNA-binding proteins that are normally bound to the OPERATOR REGION of an operon, or the ENHANCER SEQUENCES of a gene until a signal occurs that causes their release.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
A major integral transmembrane protein of the ERYTHROCYTE MEMBRANE. It is the anion exchanger responsible for electroneutral transporting in CHLORIDE IONS in exchange of BICARBONATE IONS allowing CO2 uptake and transport from tissues to lungs by the red blood cells. Genetic mutations that result in a loss of the protein function have been associated with type 4 HEREDITARY SPHEROCYTOSIS.
The protein constituents of muscle, the major ones being ACTINS and MYOSINS. More than a dozen accessory proteins exist including TROPONIN; TROPOMYOSIN; and DYSTROPHIN.
A component of NF-kappa B transcription factor. It is proteolytically processed from NF-kappa B p105 precursor protein and is capable of forming dimeric complexes with itself or with TRANSCRIPTION FACTOR RELA. It regulates expression of GENES involved in immune and inflammatory responses.
Tandem arrays of moderately repetitive, short (10-60 bases) DNA sequences which are found dispersed throughout the GENOME, at the ends of chromosomes (TELOMERES), and clustered near telomeres. Their degree of repetition is two to several hundred at each locus. Loci number in the thousands but each locus shows a distinctive repeat unit.
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
An increased number of contiguous trinucleotide repeats in the DNA sequence from one generation to the next. The presence of these regions is associated with diseases such as FRAGILE X SYNDROME and MYOTONIC DYSTROPHY. Some CHROMOSOME FRAGILE SITES are composed of sequences where trinucleotide repeat expansion occurs.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
A broad group of eukaryotic six-transmembrane cation channels that are classified by sequence homology because their functional involvement with SENSATION is varied. They have only weak voltage sensitivity and ion selectivity. They are named after a DROSOPHILA mutant that displayed transient receptor potentials in response to light. A 25-amino-acid motif containing a TRP box (EWKFAR) just C-terminal to S6 is found in TRPC, TRPV and TRPM subgroups. ANKYRIN repeats are found in TRPC, TRPV & TRPN subgroups. Some are functionally associated with TYROSINE KINASE or TYPE C PHOSPHOLIPASES.
Proteins found in the nucleus of a cell. Do not confuse with NUCLEOPROTEINS which are proteins conjugated with nucleic acids, that are not necessarily present in the nucleus.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
Established cell cultures that have the potential to propagate indefinitely.
Cellular DNA-binding proteins encoded by the rel gene (GENES, REL). They are expressed predominately in hematopoietic cells and may play a role in lymphocyte differentiation. Rel frequently combines with other related proteins (NF-KAPPA B, I-kappa B, relA) to form heterodimers that regulate transcription. Rearrangement or overexpression of c-rel can cause tumorigenesis.
A group of familial congenital hemolytic anemias characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. The erythrocytes have increased osmotic fragility and are abnormally permeable to sodium ions.
Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.
A plant genus of the family NYCTAGINACEAE. Members contain Mirabilis antiviral protein (a ribosome-inactivating protein).
Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.
Procedures by which protein structure and function are changed or created in vitro by altering existing or synthesizing new structural genes that direct the synthesis of proteins with sought-after properties. Such procedures may include the design of MOLECULAR MODELS of proteins using COMPUTER GRAPHICS or other molecular modeling techniques; site-specific mutagenesis (MUTAGENESIS, SITE-SPECIFIC) of existing genes; and DIRECTED MOLECULAR EVOLUTION techniques to create new genes.
Transport proteins that carry specific substances in the blood or across cell membranes.
A variety of simple repeat sequences that are distributed throughout the GENOME. They are characterized by a short repeat unit of 2-8 basepairs that is repeated up to 100 times. They are also known as short tandem repeats (STRs).
Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.
A subgroup of TRP cation channels named after vanilloid receptor. They are very sensitive to TEMPERATURE and hot spicy food and CAPSAICIN. They have the TRP domain and ANKYRIN repeats. Selectivity for CALCIUM over SODIUM ranges from 3 to 100 fold.
A family of structurally related proteins that are induced by CYTOKINES and negatively regulate cytokine-mediated SIGNAL TRANSDUCTION PATHWAYS. SOCS proteins contain a central SH2 DOMAIN and a C-terminal region of homology known as the SOCS box.
The semi-permeable outer structure of a red blood cell. It is known as a red cell 'ghost' after HEMOLYSIS.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The type species of LEPORIPOXVIRUS causing infectious myxomatosis, a severe generalized disease, in rabbits. Tumors are not always present.
The most common of the microsatellite tandem repeats (MICROSATELLITE REPEATS) dispersed in the euchromatic arms of chromosomes. They consist of two nucleotides repeated in tandem; guanine and thymine, (GT)n, is the most frequently seen.
The genetic complement of an organism, including all of its GENES, as represented in its DNA, or in some cases, its RNA.
The addition of descriptive information about the function or structure of a molecular sequence to its MOLECULAR SEQUENCE DATA record.
A multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.

The ankyrin repeat-containing adaptor protein Tvl-1 is a novel substrate and regulator of Raf-1. (1/285)

Tvl-1 is a 269-amino acid ankyrin repeat protein expressed primarily in thymus, lung, and testes that was identified by screening a murine T-cell two-hybrid cDNA library for proteins that associate with the serine-threonine kinase Raf-1. The interaction of Tvl-1 with Raf-1 was confirmed by co-immunoprecipitation of the two proteins from COS-1 cells transiently transfected with Tvl-1 and Raf-1 expression constructs as well as by co-immunoprecipitation of the endogenous proteins from CV-1 and NB2 cells. Tvl-1 interacts with Raf-1 via its carboxyl-terminal ankyrin repeat domain. The same domain also mediates Tvl-1 homodimerization. Tvl-1 was detected by immunofluorescence in both the cytoplasm and the nucleus suggesting that in addition to Raf-1 it may also interact with nuclear proteins. Activated Raf-1 phosphorylates Tvl-1 both in vitro and in vivo. In baculovirus-infected Sf9 insect cells, Tvl-1 potentiates the activation of Raf-1 by Src and Ras while in COS-1 cells it potentiates the activation of Raf-1 by EGF. These data suggest that Tvl-1 is both a target as well as a regulator of Raf-1. The human homologue of Tvl-1 maps to chromosome 19p12, upstream of MEF2B with the two genes in a head to head arrangement.  (+info)

Improved sensitivity of PCR for diagnosis of human granulocytic ehrlichiosis using epank1 genes of Ehrlichia phagocytophila-group ehrlichiae. (2/285)

The agent of human granulocytic ehrlichiosis (HGE), Ehrlichia phagocytophila, and Ehrlichia equi probably comprise variants of a single Ehrlichia species now called the Ehrlichia phagocytophila genogroup. These variants share a unique 153-kDa protein antigen with ankyrin repeat motifs encoded by the epank1 gene. The epank1 gene was investigated as an improved target for PCR diagnosis of HGE compared with the currently used 16S rRNA gene target. Primers for epank1 flanking a region that spans part of the 5' ankyrin repeat coding region and part of the unique 3' region were synthesized. Blood samples from 31 patients with suspected HGE who were previously tested by 16S rRNA gene (16S) PCR and indirect immunofluorescent antibody test (IFA) were retrospectively tested with the epank1 primers. Eleven patients were 16S PCR positive and had a seroconversion detected by IFA (group A), 10 patients were 16S PCR negative but had a seroconversion detected by IFA (group B), and 10 patients were 16S PCR negative and seronegative (group C). Ten of the 11 group A patients were epank1 PCR positive, all 10 of the group B patients were epank1 PCR positive, and all of the PCR-negative and seronegative patients (group C) were epank1 PCR negative. The epank1 primers are more sensitive than the previously used 16S rRNA gene primers and therefore may be more useful in diagnostic testing for HGE.  (+info)

Alastrim smallpox variola minor virus genome DNA sequences. (3/285)

Alastrim variola minor virus, which causes mild smallpox, was first recognized in Florida and South America in the late 19th century. Genome linear double-stranded DNA sequences (186,986 bp) of the alastrim virus Garcia-1966, a laboratory reference strain from an outbreak associated with 0.8% case fatalities in Brazil in 1966, were determined except for a 530-bp fragment of hairpin-loop sequences at each terminus. The DNA sequences (EMBL Accession No. Y16780) showed 206 potential open reading frames for proteins containing >/=60 amino acids. The amino acid sequences of the putative proteins were compared with those reported for vaccinia virus strain Copenhagen and the Asian variola major strains India-1967 and Bangladesh-1975. About one-third of the alastrim viral proteins were 100% identical to correlates in the variola major strains and the remainder were >/=95% identical. Compared with variola major virus DNA, alastrim virus DNA has additional segments of 898 and 627 bp, respectively, within the left and right terminal regions. The former segment aligns well with sequences in other orthopoxviruses, particularly cowpox and vaccinia viruses, and the latter is apparently alastrim-specific.  (+info)

SKIP, a CBF1-associated protein, interacts with the ankyrin repeat domain of NotchIC To facilitate NotchIC function. (4/285)

Notch proteins are transmembrane receptors that mediate intercell communication and direct individual cell fate decisions. The activated intracellular form of Notch, NotchIC, translocates to the nucleus, where it targets the DNA binding protein CBF1. CBF1 mediates transcriptional repression through the recruitment of an SMRT-histone deacetylase-containing corepressor complex. We have examined the mechanism whereby NotchIC overcomes CBF1-mediated transcriptional repression. We identified SKIP (Ski-interacting protein) as a CBF1 binding protein in a yeast two-hybrid screen. Both CBF1 and SKIP are highly conserved evolutionarily, and the SKIP-CBF1 interaction is also conserved in assays using the Caenorhabditis elegans and Drosophila melanogaster SKIP homologs. Protein-protein interaction assays demonstrated interaction between SKIP and the corepressor SMRT. More surprisingly, SKIP also interacted with NotchIC. The SMRT and NotchIC interactions were mutually exclusive. In competition binding experiments SMRT displaced NotchIC from CBF1 and from SKIP. Contact with SKIP is required for biological activity of NotchIC. A mutation in the fourth ankyrin repeat that abolished Notch signal transduction did not affect interaction with CBF1 but abolished interaction with SKIP. Further, NotchIC was unable to block muscle cell differentiation in myoblasts expressing antisense SKIP. The results suggest a model in which NotchIC activates responsive promoters by competing with the SMRT-corepressor complex for contacts on both CBF1 and SKIP.  (+info)

Analysis of notch lacking the carboxyl terminus identified in Drosophila embryos. (5/285)

The cell surface receptor Notch is required during development of Drosophila melanogaster for differentiation of numerous tissues. Notch is often required for specification of precursor cells by lateral inhibition and subsequently for differentiation of tissues from these precursor cells. We report here that certain embryonic cells and tissues that develop after lateral inhibition, like the connectives and commissures of the central nervous system, are enriched for a form of Notch not recognized by antibodies made against the intracellular region carboxy-terminal of the CDC10/Ankyrin repeats. Western blotting and immunoprecipitation analyses show that Notch molecules lacking this region are produced during embryogenesis and form protein complexes with the ligand Delta. Experiments with cultured cells indicate that Delta promotes accumulation of a Notch intracellular fragment lacking the carboxyl terminus. Furthermore, Notch lacking the carboxyl terminus functions as a receptor for Delta. These results suggest that Notch activities during development include generation and activity of a truncated receptor we designate NDeltaCterm.  (+info)

Molecular cloning and characterization of SRAM, a novel insect rel/ankyrin-family protein present in nuclei. (6/285)

Previously, we purified a 59-kDa protein that binds to the kappaB motif of the Sarcophaga lectin gene. Here we report its cDNA cloning and some of its characteristics as a novel member of the Rel/Ankyrin-family. This protein, named SRAM, contained a Rel homology domain, a nuclear localization signal and 4 ankyrin repeats, but lacked the Ser-rich domain and PEST sequence that Relish contained. We found that SRAM was localized in the nuclei of NIH-Sape-4 cells, which are an embryonic cell line of Sarcophaga. The Sarcophaga lectin gene promoter containing tandem repeats of the kappaB motifs was activated in NIH-Sape-4 cells. In Drosophila mbn-2 cells, Dif alone activated this reporter gene and a cooperative effect was detected when SRAM and Dif were co-transfected, although SRAM alone did not activate it. This is the first report of a Rel/Ankyrin molecule that exists in the nuclei.  (+info)

The L1-type cell adhesion molecule neuroglian influences the stability of neural ankyrin in the Drosophila embryo but not its axonal localization. (7/285)

Ankyrins are linker proteins, which connect various membrane proteins, including members of the L1 family of neural cell adhesion molecules, with the submembranous actin-spectrin skeleton. Here we report the cloning and characterization of a second, novel Drosophila ankyrin gene (Dank2) that appears to be the result of a gene duplication event during arthropod evolution. The Drosophila L1-type protein neuroglian interacts with products from both Drosophila ankyrin genes. Whereas the previously described ankyrin gene is ubiquitously expressed during embryogenesis, the expression of Dank2 is restricted to the nervous system in the Drosophila embryo. The absence of neuroglian protein in a neuroglian null mutant line causes decreased levels of Dank2 protein in most neuronal cells. This suggests that neuroglian is important for the stability of Dank2 protein. However, neuroglian is not required for Dank2 axonal localization. In temperature-sensitive neuroglian mutants in which neuroglian protein is mislocated at the restrictive temperature to an intracellular location in the neuronal soma, Dank2 protein can still be detected along embryonic nerve tracts.  (+info)

Cardiac ankyrin repeat protein is a novel marker of cardiac hypertrophy: role of M-CAT element within the promoter. (8/285)

CARP, a cardiac doxorubicin (adriamycin)-responsive protein, has been identified as a nuclear protein whose expression is downregulated in response to doxorubicin. In the present study, we tested the hypothesis that CARP serves as a reliable genetic marker of cardiac hypertrophy in vivo and in vitro. CARP expression was markedly increased in 3 distinct models of cardiac hypertrophy in rats: constriction of abdominal aorta, spontaneously hypertensive rats, and Dahl salt-sensitive rats. In addition, we found that CARP mRNA levels correlate very strongly with the brain natriuretic peptide mRNA levels in Dahl rats. Transient transfection assays into primary cultures of neonatal rat cardiac myocytes indicate that transcription from the CARP and brain natriuretic peptide promoters is stimulated by overexpression of p38 and Rac1, components of the stress-activated mitogen-activated protein kinase pathways. Mutation analysis and electrophoretic mobility shift assays indicated that the M-CAT element can serve as a binding site for nuclear factors, and this element is important for the induction of CARP promoter activity by p38 and Rac1. Thus, our data suggest that M-CAT element is responsible for the regulation of the CARP gene in response to the activation of stress-responsive mitogen-activated protein kinase pathways. Moreover, given that activation of these pathways is associated with cardiac hypertrophy, we propose that CARP represents a novel genetic marker of cardiac hypertrophy.  (+info)

Nanion offers analysis instruments for ion channel analysis, as patch clamp, impedance and bilayer recordings, used for drug development as cardiac safety and basic research.
TY - JOUR. T1 - Structure and stability of the ankyrin domain of the Drosophila Notch receptor. AU - Zweifel, Mark E.. AU - Leahy, Daniel J.. AU - Hughson, Frederick M.. AU - Barrick, Doug. PY - 2003/11. Y1 - 2003/11. N2 - The Notch receptor contains a conserved ankyrin repeat domain that is required for Notch-mediated signal transduction. The ankyrin domain of Drosophila Notch contains six ankyrin sequence repeats previously identified as closely matching the ankyrin repeat consensus sequence, and a putative seventh C-terminal sequence repeat that exhibits lower similarity to the consensus sequence. To better understand the role of the Notch ankyrin domain in Notch-mediated signaling and to examine how structure is distributed among the seven ankyrin sequence repeats, we have determined the crystal structure of this domain to 2.0 Å resolution. The seventh, C-terminal, ankyrin sequence repeat adopts a regular ankyrin fold, but the first, N-terminal ankyrin repeat, which contains a 15-residue ...
Scrub typhus is an understudied, potentially fatal infection that threatens one billion persons in the Asia-Pacific region. How the causative obligate intracellular bacterium, Orientia tsutsugamushi facilitates its intracellular survival and pathogenesis is poorly understood. Many intracellular bacterial pathogens utilize the Type 1 (T1SS) or Type 4 secretion system (T4SS) to translocate ankyrin repeat-containing proteins (Anks) that traffic to distinct subcellular locations and modulate host cell processes. The O. tsutsugamushi genome encodes one of the largest known bacterial Ank repertoires plus T1SS and T4SS components. Whether these potential virulence factors are expressed during infection, how the Anks are potentially secreted, and to where they localize in the host cell are not known. We determined that O. tsutsugamushi transcriptionally expresses 20 unique ank genes as well as genes for both T1SS and T4SS during infection of mammalian host cells. Examination of the Anks C-termini revealed that
The structural integrity of synaptic connections critically depends on the interaction between synaptic cell adhesion molecules (CAMs) and the underlying actin and microtubule cytoskeleton. This interaction is mediated by giant Ankyrins, that act as specialized adaptors to establish and maintain axonal and synaptic compartments. In Drosophila, two giant isoforms of Ankyrin2 (Ank2) control synapse stability and organization at the larval neuromuscular junction (NMJ). Both Ank2-L and Ank2-XL are highly abundant in motoneuron axons and within the presynaptic terminal, where they control synaptic CAMs distribution and organization of microtubules. Here, we address the role of the conserved N-terminal ankyrin repeat domain (ARD) for subcellular localization and function of these giant Ankyrins in vivo. We used a P[acman] based rescue approach to generate deletions of ARD subdomains, that contain putative binding sites of interacting transmembrane proteins. We show that specific subdomains control synaptic
Involved in the control of cytoskeleton formation by regulating actin polymerization. Inhibits actin fiber formation and cell migration. Inhibits RhoA activity; the function involves phosphorylation through PI3K/Akt signaling and may depend on the competetive interaction with 14-3-3 adapter proteins to sequester them from active complexes. Inhibits the formation of lamellipodia but not of filopodia; the function may depend on the competetive interaction with BAIAP2 to block its association with activated RAC1. Inhibits fibronectin-mediated cell spreading; the function is partially mediated by BAIAP2. Inhibits neurite outgrowth. Involved in the establishment and persistence of cell polarity during directed cell movement in wound healing. In the nucleus, is involved in beta-catenin-dependent activation of transcription. Potential tumor suppressor for renal cell carcinoma.
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class=publication>Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href=http://www.nrbook.com/b/bookcpdf.php>Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
Ubiquitin-binding protein that specifically recognizes and binds Lys-63-linked ubiquitin. Does not bind Lys-48-linked ubiquitin. Positively regulates the internalization of ligand-activated EGFR by binding to the Ub moiety of ubiquitinated EGFR at the cell membrane ...
MRKLFSFGRRLGQALLSSMDQEYAGPGYDIRDWELRKIHRAAIKGDAAEVERCLTRRFRDLDARDRKDRT 1 - 70 VLHLACAHGRVQVVTLLLHRRCQIDICDRLNRTPLMKAVHSQEEACAIVLLECGANPNIEDIYGNTALHY 71 - 140 AVYNKGTSLAERLLSHHANIEALNKEGNTPLLFAINSRRQHMVEFLLKNQANIHAVDNFKRTALILAVQH 141 - 210 NLSSIVTLLLQQNIRISSQDMFGQTAEDYALCSDLRSIRQQILEHKNKMLKNHLRNDNQETAAMKPANLK 211 - 280 KRKERAKAEHNLKVASEEKQERLQRSENKQPQDSQSYGKKKDAMYGNFMLKKDIAMLKEELYAIKNDSLR 281 - 350 KEKKYIQEIKSITEINANFEKSVRLNEKMITKTVARYSQQLNDLKAENARLNSELEKEKHNKERLEAEVE 351 - 420 SLHSSLATAINEYNEIVERKDLELVLWRADDVSRHEKMGSNISQLTDKNELLTEQVHKARVKFNTLKGKL 421 - 490 RETRDALREKTLALGSVQLDLRQAQHRIKEMKQMHPNGEAKESQSIGKQNSLEERIRQQELENLLLERQL 491 - 560 EDARKEGDNKEIVINIHRDCLENGKEDLLEERNKELMKEYNYLKEKLLQCEKEKAEREVIVREFQEELVD 561 - 630 HLKTFSISESPLEGTSHCHINLNETWTSKKKLFQVEIQPEEKHEEFRKLFELISLLNYTADQIRKKNREL 631 - 700 EEEATGYKKCLEMTINMLNAFANEDFSCHGDLNTDQLKMDILFKKLKQKFNDLVAEKEAVSSECVNLAKD 701 - 770 NEVLHQELLSMRNVQEKCEKLEKDKKMLEEEVLNLKTHMEKDMVELGKLQEYKSELDERAVQEIEKLEEI 771 - 840 ...
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Spinal muscular atrophies (SMA, also known as hereditary motor neuropathies) and hereditary motor and sensory neuropathies (HMSN) are clinically and genetically heterogeneous disorders of the peripheral nervous system. Here we report that mutations in the TRPV4 gene cause congenital distal SMA, scapuloperoneal SMA, HMSN 2C. We identified three missense substitutions (R269H, R315W and R316C) affecting the intracellular N-terminal ankyrin domain of the TRPV4 ion channel in five families. Expression of mutant TRPV4 constructs in cells from the HeLa line revealed diminished surface localization of mutant proteins. In addition, TRPV4-regulated Ca(2+) influx was substantially reduced even after stimulation with 4alphaPDD, a TRPV4 channel-specific agonist, and with hypo-osmotic solution. In summary, we describe a new hereditary channelopathy caused by mutations in TRPV4 and present evidence that the resulting substitutions in the N-terminal ankyrin domain affect channel maturation, leading to reduced ...
Dilated cardiomyopathy (DCM), a primary disorder of the cardiac muscle characterized by ventricular chamber dilation and diminished cardiac contractility (1), is the most common cause of chronic heart failure (CHF) in the young and the most common indication for cardiac transplantation (2). The underlying etiologies are varied and include genetic, viral (myocarditis), toxins like alcohol, mitochondrial, and metabolic disorders (3-6).. Familial inheritance is seen in ≈30% to 40% of DCM patients (5). Autosomal dominant mode of inheritance is the most common (≈90%), followed by X-linked (5% to 10%), autosomal recessive, and mitochondrial inheritance patterns (,5%) (7). To date, mutations in ≈20 genes have been discovered in patients with DCM (8). Of these genes, the genes encoding Z-band alternatively spliced PDZ-motif protein, titin, lamin A/C, and β-myosin heavy chain may each be responsible for 5% to 10% of familial DCM cases (9-12), with dystrophin thought to contribute in 10% to 15% of ...
Delivering genes selectively to the therapeutically relevant cell type is among the prime goals of vector development. Here, we present a high-throughput selection and screening process that identifies designed ankyrin repeat proteins (DARPins) optimally suited for receptor-targeted gene delivery using adeno-associated viral (AAV) and lentiviral (LV) vectors. In particular, the process includes expression, purification, and biotinylation of the extracellular domains of target receptors as Fc fusion proteins in mammalian cells and the selection of high-affinity binders by ribosome display from DARPin libraries each covering more than 10 variants. This way, DARPins specific for the glutamate receptor subunit GluA4, the endothelial surface marker CD105, and the natural killer cell marker NKp46 were generated. The identification of DARPins best suited for gene delivery was achieved by screening small-scale vector productions. Both LV and AAV particles displaying the selected DARPins transduced only ...
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
8.A.114. The Huntington-interacting protein 14 (HIP14) Family. The Huntington-interacting protein 14 (HIP14) is reported to be a palmitoyltransferase required for exocytosis and targeting of the palmitoylated cysteine string protein (CSP) and the SNAP25 protein which are mislocalized in a HIP14 mutant (Ohyama et al., 2007). HIP14 also palmitoylates CSP. HIP14 may be necessary for presynaptic function including neurotransmitter release by regulating the trafficking of CSP to synapses (Ducker et al., 2004; Ohyama et al., 2007; Stowers and Isacoff, 2007; Yanai et al., 2006).. HIP14 is reported to be a divalent cation transporter capable of transporting Mg2+ found only in eukaryotes (Quamme, 2009). It has up to eight N-terminal Ankyrin repeats (residues 25-270) followed by the transmembrane domain (residues 300-560; The zfDHHC domain superfamily).. The reaction proposed for HIP14 in the second paragraph (above) is:. M2+(in) ⇌ M2+(out) ...
Radiolabelled DARPin (HE)3-G3 is a versatile radioligand with potential to allow the acquisition of whole-body HER2 scans on the day of administration.
Kidney ankyrin repeat-containing proteins (KANK1/2/3/4) belong to a family of scaffold proteins, playing critical roles in cytoskeleton organization, cell polarity and migration. Mutations in KANK proteins are implicated in cancers and genetic diseases, such as nephrotic syndrome. KANK proteins can bind various target proteins through different protein regions, including a highly conserved ankyrin repeat domain (ANKRD). However, the molecular basis for target recognition by the ANKRD remains elusive. In this study, we solved a high-resolution crystal structure of the ANKRD of KANK1 in complex with a short sequence of the motor protein kinesin family member 21A (KIF21A), revealing that the highly specific target-binding mode of the ANKRD involves combinatorial use of two interfaces ...
Purpose: : Vascular endothelial growth factor (VEGF) is a key controller of pathological angiogenesis and leakage in various retinal diseases. Clinically, anti-VEGF agents have revolutionized treatment of exudative age related macular degeneration (AMD), diabetic retinopathy and retinal vein occlusion. However, one of the main limitations of current VEGF inhibitors remains the need for repeated intravitreal injections. Second-generation VEGF inhibitors should thus aim at providing more efficient VEGF-inhibition to reduce injection frequency. Methods: : In the current study, we use highly potent anti-VEGF DARPins (designed ankyrin repeat proteins) to inhibit VEGF receptor phosphorylation and endothelial cell sprouting in vitro, retinal vascular leakage in rabbits and choroidal angiogenesis in the Laser CNV model in rats. Results: : Our results demonstrate the successful isolation and purification of several DARPins with picomolar affinity to VEGF. In vitro, VEGF receptor phosphorylation was ...
All vertebrates have a left-right body axis with invariant asymmetries of the heart and the positions of the abdominal viscera. Major advances have recently been made in defining molecular components of the pathway specifying the vertebrate left-right axis, but our knowledge of the early determinants is extremely limited. In the inv mouse the left-right axis is consistently reversed, unlike other vertebrate mutants where randomisation of situs is apparent. The gene disrupted in this mouse encodes a 1062-amino-acid protein, inversin. We previously reported 16 tandem ankyrin repeats, spanning amino acids 13-557, and two putative nuclear localisation sequences, but otherwise the sequence offered few clues to the possible function. In order to identify regions likely to be functionally important, we have identified and characterised orthologous sequences in several species, including chick, Xenopus and zebrafish. Sequence comparisons show strong conservation of the ankyrin repeat region and also a lysine
Product Pig Ankyrin repeat and BTB/POZ domain containing protein BTBD11(BTBD11) ELISA kit From B-Gene - A competitive ELISA for quantitative measurement of Porcine Ankyrin repeat and BTB/POZ domain containing protein BTBD11(BTBD11) in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species. Kit contents: 1. MICROTITER PLATE * 1 2. ENZYME CONJUGATE*1 vial 3. STANDARD A*1 vial 4. STANDARD B*1 vial 5. STANDARD C*1 vial 6. STANDARD D*1 vial 7. STANDARD E*1 vial 8. STANDARD F*1 vial 9. SUBSTRATE A*1 vial 10. SUBSTRATE B*1 vial 11. STOP SOLUTION*1 vial 12. WASH SOLUTION (100 x)*1 vial 13. BALANCE SOLUTION*1 vial 14. INSTRUCTION*1
Affinity agents coupled to a functional moiety play an ever-increasing role in modern medicine, ranging from radiolabeled selective binders in diagnosis to antibody-drug conjugates in targeted therapies. In biomedical research, protein coupling to fluorophores, surfaces and nanoparticles has become an integral part of many procedures. In addition to antibodies, small scaffold proteins with similar target binding properties are being widely explored as alternative targeting moieties. To label these binders of interest with different functional moieties, conventional chemical coupling methods can be employed, but often result in heterogeneously modified protein products. In contrast, enzymatic labeling methods are highly site-specific and efficient. Protein farnesyltransferase (PFTase) catalyzes the transfer of an isoprenoid moiety from farnesyl diphosphate (FPP) to a cysteine residue in a C-terminal CaaX motif at the C-terminus of a protein substrate. The addition of only four amino acid residues ...
Molecular Biology International is a peer-reviewed, Open Access journal that publishes original research articles as well as review articles in all areas of molecular biology.
Inhibiting the RAS oncogenic protein has largely been through targeting the switch regions that interact with signalling effector proteins. Here, we report designed ankyrin repeat proteins (DARPins) macromolecules that specifically inhibit the KRAS isoform by binding to an allosteric site encompassing the region around KRAS-specific residue histidine 95 at the helix α3/loop 7/helix α4 interface. We show that these DARPins specifically inhibit KRAS/effector interactions and the dependent downstream signalling pathways in cancer cells. Binding by the DARPins at that region influences KRAS/effector interactions in different ways, including KRAS nucleotide exchange and inhibiting KRAS dimerization at the plasma membrane. These results highlight the importance of targeting the α3/loop 7/α4 interface, a previously untargeted site in RAS, for specifically inhibiting KRAS function ...
Multi-subunit Cullin-RING E3 ligases often use repeat domain proteins as substrate-specific adaptors. Structures of these macromolecular assemblies are determined for the F-box-containing leucine-rich repeat and WD40 repeat families, but not for the suppressor of cytokine signaling (SOCS)-box-containing ankyrin repeat proteins (ASB1-18), which assemble with Elongins B and C and Cul5. We determined the crystal structures of the ternary complex of ASB9-Elongin B/C as well as the interacting N-terminal domain of Cul5 and used structural comparisons to establish a model for the complete Cul5-based E3 ligase. The structures reveal a distinct architecture of the ASB9 complex that positions the ankyrin domain coaxial to the SOCS box-Elongin B/C complex and perpendicular to other repeat protein complexes. This alternative architecture appears favorable to present the ankyrin domain substrate-binding site to the E2-ubiquitin, while also providing spacing suitable for bulky ASB9 substrates, such as the creatine
The asparaginyl hydroxylase FIH [factor inhibiting HIF (hypoxia-inducible factor)] was first identified as a protein that inhibits transcriptional activation by HIF, through hydroxylation of an asparagine residue in the CAD (C-terminal activation domain). More recently, several ARD [AR (ankyrin repeat) domain]-containing proteins were identified as FIH substrates using FIH interaction assays. Although the function(s) of these ARD hydroxylations is unclear, expression of the ARD protein Notch1 was shown to compete efficiently with HIF CAD for asparagine hydroxylation and thus to enhance HIF activity. The ARD is a common protein domain with over 300 examples in the human proteome. However, the extent of hydroxylation among ARD proteins, and the ability of other members to compete with HIF-CAD for FIH, is not known. In the present study we assay for asparagine hydroxylation in a bioinformatically predicted FIH substrate, the targeting subunit of myosin phosphatase, MYPT1. Our results confirm hydroxylation
Recently, missense mutations in titin-associated proteins have been linked to the pathogenesis of dilated cardiomyopathy (DCM). The objective of this study was to search for novel disease-associated mutations in the two human titin-binding proteins myopalladin and its amino-terminal-interacting partner cardiac ankyrin-repeat protein (CARP). In a cohort of 255 cases with familial and sporadic DCM, we analyzed the coding regions and all corresponding intron flanks located in the MYPN and CARP-encoding ANKRD1 gene. Two heterozygous missense mutations were detected in the MYPN gene (p.R955W and p.P961L), but neither of these mutations was found in 300 healthy controls. Both mutations were located in the alpha-actinin-binding region of myopalladin. Endomyocardial biopsies from the p.R955W carrier showed normal subcellular localization of myopalladin and alpha-actinin in cardiac myocytes, while their regular sarcomeric staining pattern was significantly disrupted in the p.P961L carrier, indicating ...
Ankyrin Repeat (ANK Repeat) is a protein interaction motif that contains a 33-amino acid long sequence that often occurs in tandem arrays (as amino acid repetitive sequences)
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These reference sequences exist independently of genome builds. Explain. These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above. ...
These reference sequences exist independently of genome builds. Explain. These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above. ...
View mouse Shank2 Chr7:144001928-144424494 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
ID: http://www.ncbi.nlm.nih.gov/gene/22941 Type: http://bio2vec.net/ontology/gene Label: SHANK2 Synonyms: SHANK2, AUTS17, CORTBP1, CTTNBP1, ProSAP1, SHANK, SPANK-3, SH3 and multiple ankyrin repeat domains 2, SH3 and multiple ankyrin repeat domains protein 2, GKAP/SAPAP interacting protein, cortactin SH3 domain-binding protein, cortactin-binding protein 1, proline-rich synapse associated protein 1 Alternative IDs: als API: GO SPARQL: GO ...
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ANKS3 (ankyrin repeat and sterile alpha motif domain containing 3), Authors: Dessen P. Published in: Atlas Genet Cytogenet Oncol Haematol.
Ankyrin Repeat and SOCS Box Containing 8 Recombinant Protein. The ASB8 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
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Monolayer cultures of immortalised cell lines are a popular screening tool for novel anti-cancer therapeutics, but these methods can be a poor surrogate for disease states, and there is a need for drug screening platforms which are more predictive of clinical outcome. In this study, we describe a phenotypic antibody screen using three-dimensional cultures of primary cells, and image-based multi-parametric profiling in PC-3 cells, to identify anti-cancer biologics against new therapeutic targets. ScFv Antibodies and designed ankyrin repeat proteins (DARPins) were isolated using phage display selections against primary non-small cell lung carcinoma cells. The selected molecules were screened for anti-proliferative and pro-apoptotic activity against primary cells grown in three-dimensional culture, and in an ultra-high content screen on a 3-D cultured cell line using multi-parametric profiling to detect treatment-induced phenotypic changes. The targets of molecules of interest were identified using a cell
PIKE-A (PIKE-activating gene differs from PIKE-S with the addition of a 40-kDa C-terminal extension containing Arf-GAP and two ankyrin-repeat domains. and peripheral bloodstream leukocytes (4-6). Weve proven that PIKE-A is certainly coamplified with CDK4 on chromosome 12 in a number of human malignancies including sarcoma RG7112 neuroblastoma and glioblastoma (32). PIKE-A is certainly readily discovered in 12q-amplified cell lines including RMS13 rhabdomyosarcoma and OSA osteosarcoma however not in regular muscles (6). PIKE-A provides the GTPase PH ArfGAP and two Ankyrin repeats domains within PIKE-L but does not have the N-terminal proline-rich area which binds proteins 4.1N PLC-γ1 and PI3-kinase. PIKE-A particularly binds to energetic Akt and up-regulates its activity within a GTP-dependent way mediating human cancers cell invasion (32). Akt/PKB is an essential regulator of divergent cellular procedures including apoptosis proliferation fat burning capacity and differentiation. Constitutive ...
FUNCTION: [Summary is not available for the mouse gene. This summary is for the human ortholog.] This gene is a member of the ankyrin-repeat family and is induced by lipopolysaccharide (LPS). The C-terminal portion of the encoded product which contains the ankyrin repeats, shares high sequence similarity with the I kappa B family of proteins. The latter are known to play a role in inflammatory responses to LPS by their interaction with NF-B proteins through ankyrin-repeat domains. Studies in mouse indicate that this gene product is one of the nuclear I kappa B proteins and an activator of IL-6 production. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008 ...
Based on the observation that even in the presence of an oxygen supply, tumor cells preferentially use glycolysis over mitochondrial oxidative phosphorylation (OXPHOS) for glucose-dependent ATP production to fuel mitochondrial respiration, Otto Warburg put forward the notion of the Warburg effect in the 1920s (29). Advances in the understanding of the biology of tumor progression and metastasis have clearly highlighted the importance of aberrant tumor metabolism. The manifestation of the Warburg effect in todays clinical setting is the use of 18F-FDG to detect tumors with an increased glucose uptake. The elevated uptake visualized by 18F-FDG PET/CT correlates with a poor prognosis and a higher metabolic burden in many types of tumors (23, 30).. Mounting evidence indicates that the reprogramming of tumor metabolism is controlled by various oncogenic signals (31, 32). In pancreatic cancer, the Ras oncoprotein has been shown to promote metabolic transformation (33-35). Although KRAS mutations ...
J:44447 Baumeister A, Arber S, Caroni P, Accumulation of muscle ankyrin repeat protein transcript reveals local activation of primary myotube endcompartments during muscle morphogenesis. J Cell Biol. 1997 Dec 1;139(5):1231-42 ...
Complete information for ANKRD20A15P gene (Pseudogene), Ankyrin Repeat Domain 20 Family Member A15, Pseudogene, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Complete information for ANKRD53 gene (Protein Coding), Ankyrin Repeat Domain 53, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Looking for online definition of ankyrin repeat domain 3 in the Medical Dictionary? ankyrin repeat domain 3 explanation free. What is ankyrin repeat domain 3? Meaning of ankyrin repeat domain 3 medical term. What does ankyrin repeat domain 3 mean?
Gtf2ird1 (untagged) - Mouse general transcription factor II I repeat domain-containing 1 (Gtf2ird1), transcript variant 9, (10ug), 10 µg.
Protein Motif that contains a 33-amino acid long sequence that often occurs in tandem arrays. This repeating sequence of 33-Amino Acids was discovered in Ankyrin where it is involved in interaction with the anion exchanger (Anion Exchange Protein 1, Erythrocyte). Ankyrin repeats cooperatively fold into domains that mediate molecular recognition via protein-protein interactions ...
Microbial pathogens employ sophisticated virulence strategies to cause infections in humans. The intracellular pathogen Legionella pneumophila encodes RidL to hijack the host scaffold protein VPS29, a component of retromer and retriever complexes critical for endosomal cargo recycling. Here, we determined the crystal structure of L. pneumophila RidL in complex with the human VPS29-VPS35 retromer subcomplex. A hairpin loop protruding from RidL inserts into a conserved pocket on VPS29 that is also used by cellular ligands, such as Tre-2/Bub2/Cdc16 domain family member 5 (TBC1D5) and VPS9-ankyrin repeat protein for VPS29 binding. Consistent with the idea of molecular mimicry in protein interactions, RidL outcompeted TBC1D5 for binding to VPS29. Furthermore, the interaction of RidL with retromer did not interfere with retromer dimerization but was essential for association of RidL with retromer-coated vacuolar and tubular endosomes. Our work thus provides structural and mechanistic evidence into how ...
Nephrotic syndrome (NS) results from disruption of the kidney filtration barrier and is associated with proteinuria, hypoalbuminemia, and edema. Many children with NS respond to steroid therapy; however, steroid-resistant NS (SRNS) progresses to end-stage disease that requires renal replacement therapy. In many cases, the underlying cause of SNRS is unknown; however, recent studies have identified monogenic mutations that underlie disease. Several proteins encoded by NS-associated genes localize to podocytes, which are essential for maintenance of the glomerular filtration barrier. Heon Yung Gee, Fujian Zhang, and colleagues at Harvard Medical School and Childrens National Medical Center evaluated families with NS and identified recessive mutations in the kidney ankyrin repeat-containing protein-encoding genes KANK1, KANK2, and KANK4. Additionally, an independent screen in a Drosophila model determined that the Drosophila KANK homologue (dKank) is required for nephrite function. KANK1, KANK2, ...
The protein encoded by this gene belongs to the Kank family of proteins, which contain multiple ankyrin repeat domains. This family member functions in cytoskeleton formation by regulating actin polymerization. This gene is a candidate tumor suppressor for renal cell carcinoma. Mutations in this gene cause cerebral palsy spastic quadriplegic type 2, a central nervous system development disorder. A t(5;9) translocation results in fusion of the platelet-derived growth factor receptor beta gene (PDGFRB) on chromosome 5 with this gene in a myeloproliferative neoplasm featuring severe thrombocythemia. Alternative splicing of this gene results in multiple transcript variants. A related pseuodgene has been identified on chromosome 20 ...
The Elongin BC complex interacts with the conserved SOCS-box motif present in members of the SOCS, ras, WD-40 repeat, and ankyrin repeat families
FUNCTION: [Summary is not available for the mouse gene. This summary is for the human ortholog.] This gene encodes a protein that is a member of the Shank family of synaptic proteins that may function as molecular scaffolds in the postsynaptic density of excitatory synapses. Shank proteins contain multiple domains for protein-protein interaction, including ankyrin repeats, and an SH3 domain. This particular family member contains a PDZ domain, a consensus sequence for cortactin SH3 domain-binding peptides and a sterile alpha motif. The alternative splicing demonstrated in Shank genes has been suggested as a mechanism for regulating the molecular structure of Shank and the spectrum of Shank-interacting proteins in the postsynaptic densities of the adult and developing brain. Alterations in the encoded protein may be associated with susceptibility to autism spectrum disorder. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Feb 2014 ...
https://doi.org/10.18632/oncotarget.24351 Luigia Rao, Kim De Veirman, Donato Giannico, Ilaria Saltarella, Vanessa Desantis, Maria Antonia Frassanito, Antonio Giovanni Solimando, Domenico Ribatti,...
ANKRA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 336 amino acids and having a molecular mass of 36.7kDa.
Summary of RFXANK (ANKRA1, BLS, F14150_1, MGC138628, RFX-B) expression in human tissue. Mainly nuclear expression in all tissues.
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(ID:15338) The modular architecture of repeat proteins determines the molecular folding mechanism of this class of proteins. Anykr
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They contain multiple ankyrin repeats. The INK4a/ARF/INK4b locus encodes three genes (p15INK4b, ARF, and p16INK4a) in a 35- ... P15 is also formed from four ankyrin repeat (AR) motifs. Expression of P15INK4b is induced by TGF-b indicating its role as a ... P16 is formed from four ankyrin repeat (AR) motifs that exhibit a helix-turn-helix conformation except that the first helix in ...
"Altered expression of cardiac ankyrin repeat protein and its homologue, ankyrin repeat protein with PEST and proline-rich ... "Altered expression of cardiac ankyrin repeat protein and its homologue, ankyrin repeat protein with PEST and proline-rich ... Shen L, Chen C, Wei X, Li X, Luo G, Zhang J, Bin J, Huang X, Cao S, Li G, Liao Y (May 2015). "Overexpression of ankyrin repeat ... Song Y, Xu J, Li Y, Jia C, Ma X, Zhang L, Xie X, Zhang Y, Gao X, Zhang Y, Zhu D (2012). "Cardiac ankyrin repeat protein ...
Ankyrin repeat domain 31 is a protein that in humans is encoded by the ANKRD31 gene. GRCh38: Ensembl release 89: ... "Entrez Gene: Ankyrin repeat domain 31". Retrieved 2016-05-13. CS1 maint: discouraged parameter (link) v t e. ...
NUC-2 contains several ankyrin repeats. Several members of this family are annotated as XPR1 proteins: the xenotropic and ...
Ankyrin repeat domain-containing protein 17 is a protein that in humans is encoded by the ANKRD17 gene. This gene encodes a ... "Entrez Gene: ANKRD17 ankyrin repeat domain 17". Human ANKRD17 genome location and ANKRD17 gene details page in the UCSC Genome ... protein with ankyrin repeats, which are associated with protein-protein interactions. Studies in mice suggest that this protein ...
KN motif and ankyrin repeat domain-containing protein 2 is a protein that in humans is encoded by the KANK2 gene. GRCh38: ... "Entrez Gene: ANKRD25 ankyrin repeat domain 25". Human KANK2 genome location and KANK2 gene details page in the UCSC Genome ... Zhu Y, Kakinuma N, Wang Y, Kiyama R (Jan 2008). "Kank proteins: a new family of ankyrin-repeat domain-containing proteins". ... 2007). "SIP, a novel ankyrin repeat containing protein, sequesters steroid receptor coactivators in the cytoplasm". EMBO J. 26 ...
Ankyrin repeat domain-containing protein 13C is a protein that in humans is encoded by the ANKRD13C gene. ANKRD13C is predicted ... "Entrez Gene: ANKRD13C ankyrin repeat domain 13C". Chatr-Aryamontri A, Oughtred R, Boucher L, Rust J, Chang C, Kolas NK, ...
KN motif and ankyrin repeat domain-containing protein 1 is a protein that in humans is encoded by the KANK1 gene. This gene ... "Entrez Gene: ANKRD15 ankyrin repeat domain 15". Human KANK1 genome location and KANK1 gene details page in the UCSC Genome ... Sarkar S, Roy BC, Hatano N, Aoyagi T, Gohji K, Kiyama R (Sep 2002). "A novel ankyrin repeat-containing gene (Kank) located at ... Zhu Y, Kakinuma N, Wang Y, Kiyama R (Jan 2008). "Kank proteins: a new family of ankyrin-repeat domain-containing proteins". ...
"Entrez Gene: KRIT1 KRIT1, ankyrin repeat containing". Pagenstecher A, Stahl S, Sure U, Felbor U (Mar 2009). "A two-hit ... a novel ankyrin repeat-containing protein encoded by a gene mapping to 7q21-22". Oncogene. 15 (9): 1043-9. doi:10.1038/sj.onc. ...
NOTCH regulated ankyrin repeat protein is a protein that in humans is encoded by the NRARP gene. GRCh38: Ensembl release 89: ... Chu BF, Qin YY, Zhang SL, Quan ZW, Zhang MD, Bi JW (July 2016). "Downregulation of Notch-regulated Ankyrin Repeat Protein ... Imaoka T, Okutani T, Daino K, Iizuka D, Nishimura M, Shimada Y (May 2014). "Overexpression of NOTCH-regulated ankyrin repeat ... "Entrez Gene: NOTCH regulated ankyrin repeat protein". Retrieved 2018-04-27. ...
This gene is a member of the muscle ankyrin repeat protein (MARP) family and encodes a protein with four tandem ankyrin-like ... 2003), "The muscle ankyrin repeat proteins: CARP, ankrd2/Arpp and DARP as a family of titin filament-based stress response ... Ankyrin repeat domain-containing protein 23 is a protein that in humans is encoded by the ANKRD23 gene. ... "Entrez Gene: ANKRD23 ankyrin repeat domain 23". Miller, Melanie K; Bang Marie-Louise; Witt Christian C; Labeit Dietmar; ...
They are derived from natural ankyrin repeat proteins. Repeat proteins are among the most common classes of binding proteins in ... "Designing repeat proteins: well-expressed, soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat ... Plückthun, A (2015). "Designed ankyrin repeat proteins (DARPins): binding proteins for research, diagnostics, and therapy". ... "High-affinity binders selected from designed ankyrin repeat protein libraries". Nature Biotechnology. 22 (5): 575-582. doi: ...
Tetratricopeptide repeat and ankyrin repeat containing 1 is a protein that in humans is encoded by the TRANK1 gene. Through a ... "Entrez Gene: Tetratricopeptide repeat and ankyrin repeat containing 1". Mühleisen TW, Leber M, Schulze TG, Strohmaier J, ...
Ankyrin repeat domain-1 was overexpressed in both groups. Underexpressed genes in both groups included myosin light chain ... This action was repeated a few more times and it seems that the PRR32 gene is only relevant in mammals. The google spreadsheet ... leucine-rich repeat kinase-2, follistatin, collagen type XIX alpha-1, ceramide kinase-like, sestrin-3 and CXorf64. No genes ... Validation analysis using RT-PCR confirmed the data for leucine-rich repeat kinase-2, follistatin, collagen type XIX alpha-1, ...
These orthologs share a similarity with POTEB largely due to the presence of ankyrin repeats, suggesting that ankyrin domain- ... Its secondary structure is mainly five helical ankyrin repeat domains, which contain the TALHL motif. There is also one ... Mosavi LK, Cammett TJ, Desrosiers DC, Peng ZY (June 2004). "The ankyrin repeat as molecular architecture for protein ... "Duplication and extensive remodeling shaped POTE family genes encoding proteins containing ankyrin repeat and coiled coil ...
In addition, ankyrin repeats are known to mediate protein-protein interactions. Furthermore, CLIP1, a paralog of CLIP4 in ... In terms of conserved domains, the CLIP4 gene contains primarily ankyrin repeats and the eponymous CAP-Gly domains. The ... Li J, Mahajan A, Tsai MD (December 2006). "Ankyrin repeat: a unique motif mediating protein-protein interactions". Biochemistry ... Two CAP-Gly domains and numerous ankyrin repeats. The secondary structure of CLIP4 consists largely of random coil, with alpha ...
Ankyrin repeats were believe to assist in the protein-protein interactions. The ankyrin repeat proteins could interact directly ... Li J, Mahajan A, Tsai MD (December 2006). "Ankyrin repeat: a unique motif mediating protein-protein interactions". Biochemistry ...
Ankyrin repeat and SOCS box protein 1 is a protein that is in humans, encoded by the ASB1 gene. The protein encoded by this ... gene is a member of the ankyrin repeat and SOCS box-containing (ASB) family of proteins. They contain ankyrin repeat sequence ... "Entrez Gene: ASB1 ankyrin repeat and SOCS box-containing 1". CS1 maint: discouraged parameter (link) Human ASB1 genome location ... 2001). "Cloning and characterization of the genes encoding the ankyrin repeat and SOCS box-containing proteins Asb-1, Asb-2, ...
Ankyrin repeat and SOCS box protein 3 is a protein that in humans is encoded by the ASB3 gene. The protein encoded by this gene ... is a member of the ankyrin repeat and SOCS box-containing (ASB) family of proteins. They contain ankyrin repeat sequence and ... "Entrez Gene: ASB3 ankyrin repeat and SOCS box-containing 3". CS1 maint: discouraged parameter (link) Human ASB3 genome location ... Chung AS, Guan YJ, Yuan ZL, Albina JE, Chin YE (May 2005). "Ankyrin repeat and SOCS box 3 (ASB3) mediates ubiquitination and ...
... is in the protein family that contains ankyrin-repeat domains. Ankyrin repeats are known for mediating protein-protein ... Ankyrin repeat domain-containing protein 24 is a protein in humans that is coded for by the ANKRD24 gene. The gene is also ... "ANKRD24 ankyrin repeat domain 24 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2016-05-09. "Gene Card ... "ANKRD24 ankyrin repeat domain 24 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2016-04-27. "EST ...
Ankyrin repeat domain-containing protein 27 is a protein that in humans is encoded by the ANKRD27 gene. GRCh38: Ensembl release ... "Entrez Gene: ANKRD27 ankyrin repeat domain 27 (VPS9 domain)". Human ANKRD27 genome location and ANKRD27 gene details page in ...
... s correspond to the average size of natural ankyrin repeat protein domains. Proteins with fewer than three repeats (i.e ... Typically, DARPins comprise four or five repeats, of which the first (N-capping repeat) and last (C-capping repeat) serve to ... They are derived from natural ankyrin repeat proteins, one of the most common classes of binding proteins in nature, which are ... Mosavi, L. K.; Minor, D. L.; Peng, Z. -Y. (2002). "Consensus-derived structural determinants of the ankyrin repeat motif". ...
Either the ankyrin repeats alone or the AAA+ domain were found to be insufficient to support disaggregation activity. With only ... Notably, the presence of ankyrin repeats replaced the first of two ATPase domains found in bacteria and fungi. Skd3 belongs to ... In humans, the presence of ankyrin repeats replaced the first of two ATPase domains found in bacteria and fungi, which might ... Mosavi LK, Cammett TJ, Desrosiers DC, Peng ZY (June 2004). "The ankyrin repeat as molecular architecture for protein ...
Ankyrin Repeat, PEST sequence and Proline-rich region (ARPP), also known as Ankyrin repeat domain-containing protein 2 is a ... "Altered expression of cardiac ankyrin repeat protein and its homologue, ankyrin repeat protein with PEST and proline-rich ... "Altered expression of cardiac ankyrin repeat protein and its homologue, ankyrin repeat protein with PEST and proline-rich ... ANKRD2 has nine exons, four of which encode ankyrin repeats in the middle region of the protein, a PEST-like and Lysine-rich ...
The gene is also known as HARP (Harmonin-interacting, ankyrin repeat-containing protein). Ankyrin repeats mediate protein- ... Ankyrin repeat and sterile alpha motif domain containing 4B is a protein that in humans is encoded by the ANKS4B gene. ... "Ankyrin repeat and sterile alpha motif domain containing 4B". Retrieved 2011-12-06. "Dysmorphology data for Anks4b". Wellcome ... ankyrin repeat-containing protein), a novel protein that interacts with harmonin in epithelial tissues". Genes to Cells. 9 (10 ...
The human BARD1 protein is 777 amino acids long and contains a RING finger domain (residues 46-90), four ankyrin repeats ( ... The BARD1 protein also contains three tandem ankyrin repeats. The BARD1/BRCA1 interaction is disrupted by tumorigenic amino ... "Crystal structure of the BARD1 ankyrin repeat domain and its functional consequences". The Journal of Biological Chemistry. 283 ...
Ankyrin repeat and KH domain-containing protein 1 is a protein that in humans is encoded by the ANKHD1 gene. This gene encodes ... "Entrez Gene: ANKHD1 ankyrin repeat and KH domain containing 1". Human ANKHD1 genome location and ANKHD1 gene details page in ... Traina F, Favaro PM, Medina Sde S, Duarte Ada S, Winnischofer SM, Costa FF, Saad ST (Sep 2006). "ANKHD1, ankyrin repeat and KH ... a protein with multiple ankyrin repeat domains and a single KH domain. Co-transcription of this gene and the neighboring ...
... subunits contain three to five N-terminal ankyrin repeats. TRPV proteins respond to the taste of garlic (allicin). TRPV1 ...
SH3 and multiple ankyrin repeat domains 3 (Shank3), also known as proline-rich synapse-associated protein 2 (ProSAP2), is a ... A rat model of SHANK3 was developed using zinc finger nucleases targeting exon 6 of the ankyrin (ANK) repeat domain. The ... The gene encodes a protein that contains 5 interaction domains or motifs including the ankyrin repeats domain (ANK), a src 3 ... "Entrez Gene: SHANK3 SH3 and multiple ankyrin repeat domains 3". Sheng M, Kim E (June 2000). "The Shank family of scaffold ...
SH3 and multiple ankyrin repeat domains protein 1 is a protein that in humans is encoded by the SHANK1 gene. SHANK1 has been ... "Entrez Gene: SHANK1 SH3 and multiple ankyrin repeat domains 1". Park E, Na M, Choi J, Kim S, Lee JR, Yoon J, Park D, Sheng M, ... Ankyrin repeats of the multidomain Shank protein family interact with the cytoskeletal protein alpha-fodrin". J. Biol. Chem. ... Ankyrin repeats of the multidomain Shank protein family interact with the cytoskeletal protein alpha-fodrin". J. Biol. Chem. ...
ankyrin repeat binding. • zinc ion binding. • dioxygenase activity. • зв'язування з іоном металу. • NF-kappaB binding. • Notch ...
Ankyrin-based macromolecular complex - proteins linking the bilayer to the membrane skeleton through the interaction of their ... In the absence of nuclear elimination, the accumulation of repeat sequences is constrained by the volume occupied by the ... cytoplasmic domains with Ankyrin. *Band 3 - also assembles various glycolytic enzymes, the presumptive CO2 transporter, and ...
... which stands for ankyrin repeat domain-containing protein A. Additionally, T4SS coupling proteins are VirD4, which bind to ...
The filaments are organized into repeated subunits along the length of the myofibril. These subunits are called sarcomeres. ...
... is a protein that in humans is encoded by the ANKRD11 gene.[5] ... ANKRD11, ANCO-1, ANCO1, LZ16, T13, ankyrin repeat domain 11. External IDs. OMIM: 611192 MGI: 1924337 HomoloGene: 69134 ... This locus encodes an ankyrin repeat domain-containing protein. The encoded protein inhibits ligand-dependent activation of ... "Characterization of transcriptional regulatory domains of ankyrin repeat cofactor-1". Biochem. Biophys. Res. Commun. 358 (4): ...
"Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: A role in cytoskeletal remodeling" ...
ankyrin binding. • gamma-catenin binding. • beta-catenin binding. • GTPase activating protein binding. • metal ion binding. • ... Yoon YM, Baek KH, Jeong SJ, Shin HJ, Ha GH, Jeon AH, Hwang SG, Chun JS, Lee CW (September 2004). "WD repeat-containing mitotic ... The encoded protein is a calcium-dependent cell-cell adhesion glycoprotein composed of five extracellular cadherin repeats, a ... It consists of 5 cadherin repeats (EC1 ~ EC5) in the extracellular domain, one transmembrane domain, and an intracellular ...
TRANK1: encoding protein Tetratricopeptide repeat and ankyrin repeat containing 1. *TUSC2: tumor suppressor candidate 2 ...
... subunits contain three to five N-terminal ankyrin repeats.[9] ...
... heavy chains dimerize through the tail domain forming a long alpha-helical coiled-coil rod composed of typical heptad repeats. ...
Sun N, Critchley DR, Paulin D, Li Z, Robson RM (May 2008). "Identification of a repeated domain within mammalian alpha-synemin ...
Low copy repeats. *Christina's World. References[edit]. *^ a b c Krajewski, K. M. (2000). "Neurological dysfunction and axonal ... Ankyrin: Long QT syndrome 4 *Hereditary spherocytosis 1. Catenin. *APC *Gardner's syndrome ...
"Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: A role in cytoskeletal remodeling" ...
Beatus P, Lundkvist J, Oberg C, Pedersen K, Lendahl U (Jun 2001). "The origin of the ankyrin repeat region in Notch ... Beatus P, Lundkvist J, Oberg C, Pedersen K, Lendahl U (Jun 2001). "The origin of the ankyrin repeat region in Notch ... interacts with the ankyrin repeat domain of NotchIC To facilitate NotchIC function". Molecular and Cellular Biology. 20 (7): ... interacts with the ankyrin repeat domain of NotchIC To facilitate NotchIC function". Molecular and Cellular Biology. 20 (7): ...
One projection, the coiled-coil stalk, binds to and "walks" along the surface of the microtubule via a repeated cycle of ...
"Crystal structure of the CDK4/6 inhibitory protein p18INK4c provides insights into ankyrin-like repeat structure/function and ...
HACE1: HECT domain and Ankyrin repeat containing, E3 ubiquitin protein ligase 1 (6q21) ...
Further studies have shown that the beta-hairpin loops within the ankyrin repeat domain of ankyrin-B are required for the ... Ankyrin-B, also known as Ankyrin-2, is a protein which in humans is encoded by the ANK2 gene.[1][2] Ankyrin-B is ubiquitously ... Ankyrin-B is a member of the ankyrin family of proteins. ankyrin-1 has shown to be essential in normal function of erythrocytes ... and determines ankyrin-B activity.[1][7][8] The membrane-binding region of ankyrin-B is composed of 24 consecutive ankyrin ...
... repeat region in which there is a simple relationship between the identity of two critical residues in sequential repeats and ... 4.1.1 Family: Rel/ankyrin; NF-kappaB. *4.1.2 Family: ankyrin only ...
ATP hydrolysis within the myosin will cause it to bind to actin again to repeat the cycle. The combined effect of the myriad ...
Wang AH, Grégoire S, Zika E, Xiao L, Li CS, Li H, Wright KL, Ting JP, Yang XJ (Aug 2005). "Identification of the ankyrin repeat ... This protein contains ankyrin repeats involved in protein-protein interactions. Mutations in this gene have been linked to bare ... Lin JH, Makris A, McMahon C, Bear SE, Patriotis C, Prasad VR, Brent R, Golemis EA, Tsichlis PN (May 1999). "The ankyrin repeat- ... "Analysis of ankyrin repeats reveals how a single point mutation in RFXANK results in bare lymphocyte syndrome". Molecular and ...
Into this repeated pattern, the first and fourth residues are hydrophobic and the charged residues show alternate positive and ... have been probed to associate also with the ankyrin and spectrin complex protein network that underlies the cell membrane.[ ... The α-helical domain has 310-150 amino acids and comprises four segments in which a seven-residue pattern repeats. ...
... and this mechanoenzymatic cycle is then repeated, starting this time on the other sub-filament growth site. ...
Ankyrin. *Ankyrin-G binding motif of KCNQ2-3. *Anosmin-1. *Anthrax toxin ... Calponin family repeat. *Calsequestrin. *Calsyntenin. *Cannabinoid receptor. *Carbamoyl phosphate synthase II. *Carbamoyl ...
AAH repeats that possess high affinity binding to transition metal ions Cu(II), Ni(II), Zn(II) and Co(II).[27] The Tx segment ...
Ankyrin repeats of the multidomain Shank protein family interact with the cytoskeletal protein alpha-fodrin". J. Biol. Chem. ... First, a cardiac-specific, 21 amino acid sequence insert in the 21st spectrin repeat, termed alpha II-cardi+, was identified as ... Thirdly, an insert of five amino acids in the fifteenth spectrin motif bears a highly antigenic epitope resembling an ankyrin- ... Secondly, another insert of 20 amino acids in the 10th spectrin repeat, termed SH3i+, contains protein kinase A and protein ...
Ankyrin repeat and BTB/POZ domain-containing protein 1 is a protein that in humans is encoded by the ABTB1 gene. This gene ... "Entrez Gene: ABTB1 ankyrin repeat and BTB (POZ) domain containing 1". Human ABTB1 genome location and ABTB1 gene details page ... Dai KS, Wei W, Liew CC (Sep 2000). "Molecular cloning and characterization of a novel human gene containing ankyrin repeat and ... encodes a protein with an ankyrin repeat region and two BTB/POZ domains, which are thought to be involved in protein-protein ...
... tandem repeat sequence - taste bud - TATA box - tax gene product - taxonomy - telophase - Tertiary structure - tetrodotoxin - ... ankyrin - annexin II - antibiotic - antibody - apoenzyme - apolipoprotein - apoptosis - aquaporin - archaea - arginine - ... trinucleotide repeat - Triose - tropomyosin - troponin - Tryptophan - tubulin - tumor necrosis factors - tumor necrosis factor ... dinucleotide repeat - Diploid - Disaccharide - Dissociation constant - Disulfide bond - Disulfide bridge - DNA - DNA ...
Ankyrin repeat domain 11 is a protein that in humans is encoded by the ANKRD11 gene.[5] ... ANKRD11, ANCO-1, ANCO1, LZ16, T13, ankyrin repeat domain 11. External IDs. OMIM: 611192 MGI: 1924337 HomoloGene: 69134 ... This locus encodes an ankyrin repeat domain-containing protein. The encoded protein inhibits ligand-dependent activation of ... "Characterization of transcriptional regulatory domains of ankyrin repeat cofactor-1". Biochem. Biophys. Res. Commun. 358 (4): ...
Ankyrin repeat (IPR002110). Short name: Ankyrin_rpt Description. The ankyrin repeat is one of the most common protein-protein ... Ankyrin repeats are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse ... Hundreds of ankyrin-like repeats in functionally diverse proteins: mobile modules that cross phyla horizontally?. Proteins 17 ... Consensus-derived structural determinants of the ankyrin repeat motif.. Proc. Natl. Acad. Sci. U.S.A. 99 16029-34 2002 ...
Ankyrin repeat and death domain-containing protein 1A/1B (IPR039194). *Ankyrin repeat domain-containing protein 60 (IPR039323) ... The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats are tandemly ... Ankyrin repeat-containing domain superfamily (IPR036770). Short name: Ankyrin_rpt-contain_sf ... This entry represents the ankyrin repeat-containing domain. These domains contain multiple repeats of a beta(2)-alpha(2) motif ...
Ankyrin repeats typically fold together to form a single, linear solenoid structure called ankyrin repeat domains. These ... designed ankyrin repeat protein), an engineered antibody mimetic based on the structure of ankyrin repeats PDB: 1N11​; Michaely ... A specialized family of ankyrin proteins known as muscle ankyrin repeat proteins (MARPs) are involved with the repair and ... Ankyrin repeats, by contrast, contain very few such contacts (that is, they have a low contact order). Most studies have found ...
Ank_2; Ankyrin repeats (3 copies). pfam13637. Location:75 → 128. Ank_4; Ankyrin repeats (many copies). ... Ank_2; Ankyrin repeats (3 copies). pfam13637. Location:75 → 128. Ank_4; Ankyrin repeats (many copies). ... ANKRD49 ankyrin repeat domain 49 [Homo sapiens] ANKRD49 ankyrin repeat domain 49 [Homo sapiens]. Gene ID:54851 ... ankyrin repeat domain 49provided by HGNC. Primary source. HGNC:HGNC:25970 See related. Ensembl:ENSG00000168876 Gene type. ...
"Entrez Gene: Ankyrin repeat domain 22". Retrieved 2018-07-11. Grupe A, Li Y, Rowland C, Nowotny P, Hinrichs AL, Smemo S, Kauwe ... Ankyrin repeat domain 22 is a protein that in humans is encoded by the ANKRD22 gene. GRCh38: Ensembl release 89: ...
Ank_2; Ankyrin repeats (3 copies). pfam13637. Location:42 → 93. Ank_4; Ankyrin repeats (many copies). sd00045. Location:74 → ... Ank_4; Ankyrin repeats (many copies). pfam12796. Location:77 → 167. Ank_2; Ankyrin repeats (3 copies). pfam14915. Location:1104 ... Ank_2; Ankyrin repeats (3 copies). pfam13637. Location:42 → 93. Ank_4; Ankyrin repeats (many copies). pfam14915. Location:1251 ... ANK; ankyrin repeats; ankyrin repeats mediate protein-protein interactions in very diverse families of proteins. The number of ...
... Niaz Mahmood1 and Nahid Tamanna2 ... Ankyrin (ANK) repeat containing proteins are evolutionary conserved and have functions in crucial cellular processes like cell ...
Tam H.K., Malviya V.N., Pos K.M. (2018) High-Resolution Crystallographic Analysis of AcrB Using Designed Ankyrin Repeat ... High-Resolution Crystallographic Analysis of AcrB Using Designed Ankyrin Repeat Proteins (DARPins). ... High-affinity binders selected from designed ankyrin repeat protein libraries. Nat Biotechnol 22:575-582CrossRefPubMedGoogle ... soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins. J Mol Biol 332:489-503CrossRef ...
Compare Ankyrin repeat domain 12 ELISA Kits from leading suppliers on Biocompare. View specifications, prices, citations, ... Ankyrin repeat domain 12 ELISA Kits. The ELISA (enzyme-linked immunosorbent assay) is a widely used application for detecting ... Your search returned 20 Ankyrin repeat domain 12 ELISA ELISA Kit across 6 suppliers. ... Easy to use, small volume, room temperature, enough reagents to use the repeating pipette. read more ...
... uses its ankyrin repeat clusters (ARCs) to bind a wide range of proteins and thereby controls diverse cellular functions. A ... Tankyrase-1 Ankyrin Repeats Form an Adaptable Binding Platform for Targets of ADP-Ribose Modification. Structure 24, 1679-1692 ... The PARP enzyme and scaffolding protein tankyrase (TNKS, TNKS2) uses its ankyrin repeat clusters (ARCs) to bind a wide range of ... Tankyrase contains five N-terminal ankyrin repeat clusters (ARCs), four of which, namely ARCs 1, 2, 4 and 5, can recruit ...
Ankyrin Repeat. Protein Motif that contains a 33-amino acid long sequence that often occurs in tandem arrays. This repeating ... Ankyrin repeats cooperatively fold into domains that mediate molecular recognition via protein-protein interactions. ... sequence of 33-Amino Acids was discovered in Ankyrin where it is involved in interaction with the anion exchanger (Anion ...
Compare Ankyrin repeat domain 29 ELISA Kits from leading suppliers on Biocompare. View specifications, prices, citations, ... Ankyrin repeat domain 29 ELISA Kits. The ELISA (enzyme-linked immunosorbent assay) is a well-established antibody-based tool ... Your search returned 13 Ankyrin repeat domain 29 ELISA ELISA Kit across 1 supplier. ...
X-ray structural analysis of the yeast cell cycle regulator Swi6 reveals variations of the ankyrin fold and has implications ...
IPR002110, Ankyrin_rpt. IPR020683, Ankyrin_rpt-contain_dom. IPR036770, Ankyrin_rpt-contain_sf. ... IPR002110, Ankyrin_rpt. IPR020683, Ankyrin_rpt-contain_dom. IPR036770, Ankyrin_rpt-contain_sf. ... Ankyrin repeat domain 46aImported. ,p>Information which has been imported from another database using automatic procedures.,/p ... tr,E7F3W1,E7F3W1_DANRE Ankyrin repeat domain 46a OS=Danio rerio OX=7955 GN=ankrd46a PE=1 SV=1 ...
... ankyrin repeat explanation free. What is ankyrin repeat? Meaning of ankyrin repeat medical term. What does ankyrin repeat mean? ... Looking for online definition of ankyrin repeat in the Medical Dictionary? ... ankyrin repeat. Also found in: Wikipedia. ankyrin repeat. A short repetitive sequence of amino acids consisting of a beta ... The beta strands on adjacent ankyrin repeats combine to form a short antiparallel beta sheet. Ankyrin repeats were first ...
... there is an ankyrin repeat domain (ARD) in their intracellular N-termini. Ankyrin (ANK) repeat, a common motif with typically ... there is an ankyrin repeat domain (ARD) in their intracellular N-termini. Ankyrin (ANK) repeat, a common motif with typically ... Here, we report the crystal structure of TRPV3-ARD solved at 1.95 Å resolution, which reveals six-ankyrin repeats. While ... Crystal structure of the N-terminal ankyrin repeat domain of TRPV3 reveals unique conformation of finger 3 loop critical for ...
IPR002110. Ankyrin_rpt. IPR020683. Ankyrin_rpt-contain_dom. IPR036770. Ankyrin_rpt-contain_sf. ... IPR002110. Ankyrin_rpt. IPR020683. Ankyrin_rpt-contain_dom. IPR036770. Ankyrin_rpt-contain_sf. ... Ankyrin repeat protein, putativeImported. ,p>Information which has been imported from another database using automatic ... tr,A2DW52,A2DW52_TRIVA Ankyrin repeat protein, putative OS=Trichomonas vaginalis GN=TVAG_224290 PE=4 SV=1 ...
Browse our Ankyrin Repeat Domain 33B product catalog backed by our Guarantee+. ... Ankyrin Repeat Domain 33B products available through Novus Biologicals. ... Bioinformatics Tool for Ankyrin Repeat Domain 33B. Discover related pathways, diseases and genes to Ankyrin Repeat Domain 33B. ... Ankyrin Repeat Domain 33B Antibodies (2). Ankyrin Repeat Domain 33B Protein (1) ...
Sus scrofa (pig) : ANKRD13C (ankyrin repeat domain 13C) Chlorocebus sabaeus (green monkey) : ANKRD13C (ankyrin repeat domain ... ankyrin repeat domain 13C) HGNC Alliance Rattus norvegicus (Norway rat) : Ankrd13c (ankyrin repeat domain 13C) Alliance ... ankyrin repeat domain 13C) Pan paniscus (bonobo/pygmy chimpanzee) : ANKRD13C (ankyrin repeat domain 13C) Canis lupus familiaris ... ankyrin repeat domain 13C) Ictidomys tridecemlineatus (thirteen-lined ground squirrel) : Ankrd13c (ankyrin repeat domain 13C) ...
... Eur J Nucl Med Mol Imaging. 2015 Feb; ... The designed ankyrin repeat protein (DARPin) G3 binds HER2 with high affinity at an epitope that does not overlap with ...
SHANK2, SH3 and multiple ankyrin repeat domains 2. Orthology source: HomoloGene, HGNC ...
2). The two DARPins E40 and pE59 in the complex have the expected ankyrin repeat domain fold (Fig. 2 and Fig. 3A). The ... 2003) Designed to be stable: Crystal structure of a consensus ankyrin repeat protein. Proc Natl Acad Sci USA 100:1700-1705. ... 2010) Designed ankyrin repeat proteins: A novel tool for testing epidermal growth factor receptor 2 expression in breast cancer ... 2012) Designed Ankyrin Repeat Proteins (DARPins) as novel isoform-specific intracellular inhibitors of c-Jun N-terminal kinases ...
Homo sapiens (human) : ANKRD2 (ankyrin repeat domain 2) HGNC Alliance Rattus norvegicus (Norway rat) : Ankrd2 (ankyrin repeat ... Pan paniscus (bonobo/pygmy chimpanzee) : ANKRD2 (ankyrin repeat domain 2) Canis lupus familiaris (dog) : ANKRD2 (ankyrin repeat ... ankyrin repeat domain-containing protein 2; Arpp; mArpp; skeletal muscle ankyrin repeat protein. ... ANKRD2 (ankyrin repeat domain 2). Transitive Ortholog Pipeline. Transitive Ortholog Pipeline. Canis lupus familiaris (dog):. ...
We report that the ankyrin repeat domains of ANKRA2 and its close paralog regulatory factor X-associated ankyrin-containing ... the ankyrin repeat domain of ANKRA2 in complex with its binding peptides revealed that each of the middle three ankyrin repeats ... Ankyrin repeat family A protein 2 (ANKRA2) interacts with the plasma membrane receptor megalin and the class IIa histone ... Phosphorylation of a motif that binds to ankyrin repeat domains switches its binding preference to 14-3-3 proteins. ...
Tumor Targeting with Designed Ankyrin Repeat Proteins GRS-054/04 CHF 241000 Michael Stumpp 07.2005 - 07.2008 ... Tumor Targeting with Designed Ankyrin Repeat Proteins. Rédaction. Für den Inhalt der Angaben zeichnet die Projektleitung ... In den letzten fünf Jahren wurden von uns "Designed Ankyrin Repeat Proteins" (DARPins) entwickelt, die eine neue Klasse von ... High-affinity binders selected from designed ankyrin repeat protein libraries. Nature Biotechnol. 22, 575-582. Zahnd C., ...
Compare and order KRIT1, Ankyrin Repeat Containing ELISA Kits. View citations, images, detection ranges, sensitivity, prices ... More product categories related to KRIT1, Ankyrin Repeat Containing ELISA Kit * 49 anti-KRIT1, Ankyrin Repeat Containing ... KRIT1, Ankyrin Repeat Containing ELISA Kit. 4 products by 2 suppliers: Wuhan Fine biotech , Cloud-Clone ... This gene encodes a protein containing four ankyrin repeats, a band 4.1/ezrin/radixin/moesin (FERM) domain, and multiple NPXY ...
... : Biological Overview , References Gene name - Ankyrin- ... Classification - Ankyrin-repeat, SH3-domain, and Proline-rich-region Cellular location - cytoplasmic ... dASPP is the homolog of mammalian ASPP1 and -2 (Ankyrin-repeat, SH3-domain and Proline-rich-region containing Protein). ASPP1 ... Drosophila Ankyrin-repeat, SH3-domain, and Proline-rich-region containing Protein (dASPP) has been identified as a regulator of ...
... ankyrin repeat and sterile alpha motif domain containing 3), Authors: Dessen P. Published in: Atlas Genet Cytogenet Oncol ...
A microbial protein containing ankyrin repeats is injected into host cells through a specialized secretion system where it ... A microbial protein containing ankyrin repeats is injected into host cells through a specialized secretion system where it ... Ankyrin Repeat Proteins Comprise a Diverse Family of Bacterial Type IV Effectors ... Ankyrin Repeat Proteins Comprise a Diverse Family of Bacterial Type IV Effectors ...
  • The repeat has been found in proteins of diverse function such as transcriptional initiators, cell-cycle regulators, cytoskeletal, ion transporters and signal transducers. (ebi.ac.uk)
  • Hundreds of ankyrin-like repeats in functionally diverse proteins: mobile modules that cross phyla horizontally? (ebi.ac.uk)
  • The ankyrin repeat is a 33-residue motif in proteins consisting of two alpha helices separated by loops, first discovered in signaling proteins in yeast Cdc10 and Drosophila Notch. (wikipedia.org)
  • Domains consisting of ankyrin tandem repeats mediate protein-protein interactions and are among the most common structural motifs in known proteins. (wikipedia.org)
  • Ankyrin repeat proteins, though absent in most viruses, are common among poxviruses. (wikipedia.org)
  • Most proteins that contain the motif have four to six repeats, although its namesake ankyrin contains 24, and the largest known number of repeats is 34, predicted in a protein expressed by Giardia lamblia. (wikipedia.org)
  • A structure-based study involving a range of ankyrin proteins of known structures, shows that consensus-based ankyrin proteins are very stable since they maximize the energetic gap between the folding and unfolding structures, encoding a densely connected network of favourable interactions among conserved sequence motifs, like the TPLX motif. (wikipedia.org)
  • Ankyrin-repeat proteins present an unusual problem in the study of protein folding, which has largely focused on globular proteins that form well-defined tertiary structure stabilized by long-range, nonlocal residue-residue contacts. (wikipedia.org)
  • Some evidence, based on synthesis of truncated versions of natural repeat proteins, and on the examination of phi values, suggests that the C-terminus forms the folding nucleation site. (wikipedia.org)
  • Ankyrin-repeat proteins have been associated with a number of human diseases. (wikipedia.org)
  • These proteins include the cell cycle inhibitor p16, which is associated with cancer, and the Notch protein (a key component of cell signalling pathways) which can cause the neurological disorder CADASIL when the repeat domain is disrupted by mutations. (wikipedia.org)
  • A specialized family of ankyrin proteins known as muscle ankyrin repeat proteins (MARPs) are involved with the repair and regeneration of muscle tissue following damage due to injury and stress. (wikipedia.org)
  • Ankyrin (ANK) repeat containing proteins are evolutionary conserved and have functions in crucial cellular processes like cell cycle regulation and signal transduction. (hindawi.com)
  • The PARP enzyme and scaffolding protein tankyrase (TNKS, TNKS2) uses its ankyrin repeat clusters (ARCs) to bind a wide range of proteins and thereby controls diverse cellular functions. (nature.com)
  • Ankyrin repeats were first identified in ankyrin, which tethers different proteins (e.g., nuclear and cytoplasmic proteins), helping regulate gene expression and embryonic development. (thefreedictionary.com)
  • The active ingredient, which comprises several DARPins (designed ankyrin repeat proteins), is also easy to produce. (thefreedictionary.com)
  • The Z-disk proteins include [alpha]-actinin 2, cardiac ankyrin repeat protein, muscle LIM protein, LIM binding domain 3, myozenin 2, telethonin, and vinculin/metavinculin. (thefreedictionary.com)
  • Conformation-dependent recognition of HIV gp120 by designed ankyrin repeat proteins provides access to novel HIV entry inhibitors," Journal of Virology 87(10): 5868-5881. (thefreedictionary.com)
  • We have selected designed ankyrin repeat proteins (DARPins) from a synthetic library by using ribosome display that selectively bind to the mitogen-activated protein kinase ERK2 (extracellular signal-regulated kinase 2) in either its nonphosphorylated (inactive) or doubly phosphorylated (active) form. (pnas.org)
  • In den letzten fünf Jahren wurden von uns "Designed Ankyrin Repeat Proteins" (DARPins) entwickelt, die eine neue Klasse von vielversprechenden Proteintherapeutika darstellen. (grstiftung.ch)
  • Selection and Characterization of Her2 Binding-designed Ankyrin Repeat Proteins. (grstiftung.ch)
  • We found that the intracellular pathogens Legionella pneumophila and Coxiella burnetii use a type IV secretion system to deliver into eukaryotic cells a large number of different bacterial proteins containing ankyrin repeat homology domains called Anks. (sciencemag.org)
  • Many bacterial pathogens and endosymbionts use TFSSs to regulate host processes important for survival and replication ( 2 ), and several of these organisms have a large number of genes encoding proteins with multiple ankyrin repeat homology domains (ARHDs) ( 3 - 7 ). (sciencemag.org)
  • Many intracellular bacterial pathogens utilize the Type 1 (T1SS) or Type 4 secretion system (T4SS) to translocate ankyrin repeat-containing proteins (Anks) that traffic to distinct subcellular locations and modulate host cell processes. (frontiersin.org)
  • We show here that with very small high-affinity proteins such as designed ankyrin repeat proteins (DARPins), these limits can be overcome. (aacrjournals.org)
  • We show here that with very small high-affinity proteins such as designed ankyrin repeat proteins (DARPins), these limits can be overcome, and we present a systematic approach that establishes the observed tumor accumulation and targeting contrast as a function of affinity, targeting molecule size, and pharmacokinetics. (aacrjournals.org)
  • Recently, we have developed combinatorial libraries of a new class of small proteins, termed "designed ankyrin repeat proteins" ( 19 , 20 ) that can act as an alternative to antibodies, as they are particularly robust to engineering. (aacrjournals.org)
  • The protein encoded by this gene is a member of the ankyrin repeat and SOCS box-containing (ASB) family of proteins. (creative-biogene.com)
  • Site-Selective Enzymatic Labeling of Designed Ankyrin Repeat Proteins Using Protein Farnesyltransferase. (uzh.ch)
  • In this protocol, we present a detailed procedure for labeling Designed Ankyrin Repeat Proteins (DARPins) engineered with a C-terminal CVIA sequence using an azide-containing FPP analog by yeast PFTase (yPFTase). (uzh.ch)
  • Designed ankyrin repeat proteins (DARPins) are engineered scaffold proteins with high potential as probes for radionuclide molecular imaging. (diva-portal.org)
  • Recently, major species-specific antibody epitopes in three immunoreactive tandem repeat proteins (TRPs) of Ehrlichia chaffeensis , TRP32, TRP47, and TRP120, have been identified and molecularly characterized within tandem repeat (TR) regions. (asm.org)
  • Nuclear import may be a conserved property of ankyrin repeat domains (ARDs), as the ARDs from two other ARD-containing proteins, 53BP2 and GABPbeta , are also able to function as nuclear import sequences. (caltech.edu)
  • Single-channel electrophysiological recordings of heterologously expressed and purified Anopheles gambiae TRPA1 (AgTRPA1), with and without the N-terminal ankyrin repeat domain, demonstrate that both proteins are functional because they responded to the electrophilic compounds allyl isothiocyanate and cinnamaldehyde as well as heat. (lu.se)
  • We have identified two Nicotiana plumbaginifolia ankyrin-repeat proteins, designated $$\underline{G}$$ lucanohydrolase $$\underline{B}$$ inding $$\underline{P}$$ roteins (GBP) 1 and 2, that bind GLU I and CHN I both in vitro and when expressed in yeast cells. (deepdyve.com)
  • GBP1/2 are members of a conserved $$\underline{P}$$ lant-specific $$\underline{Ank}$$ yrin- repeat (PANK) family that includes proteins implicated in carbohydrate allocation, reactive oxygen metabolism, hypersensitive cell death, rapid elicitor responses, virus pathogenesis, and auxin signaling. (deepdyve.com)
  • Ankyrin repeats (ARs) are one of the most common structural motifs among eukaryotic proteins. (ox.ac.uk)
  • The ankyrin (ANK) repeat was named after the cytoskeletal protein ankyrin and is found in a wide range of eukaryotic and bacterial proteins where it mediates protein-protein interactions. (otago.ac.nz)
  • Viruses, especially the Poxviridae and Polydnaviridae families, also encode ANK repeat containing proteins. (otago.ac.nz)
  • ANK repeat proteins form the largest family of Chordopoxvirus proteins but knowledge of their functions remains limited. (otago.ac.nz)
  • Consistent with this, some mammalian ANK repeat containing proteins have been shown to interact with FIH-1 and undergo asparaginyl hydroxylation. (otago.ac.nz)
  • The role of asparaginyl hydroxylation of cellular ANK repeat proteins remains elusive but these observations raised the possibility that viral ANK repeat proteins might interact with FIH-1 in infected cells. (otago.ac.nz)
  • Here it is demonstrated that the five orf virus (ORFV) ANK repeat proteins ov008, ov123, ov126, ov128, and ov129 interact with endogenous FIH-1. (otago.ac.nz)
  • The results reveal a possible link between poxviral ANK repeat proteins and the HIF pathway. (otago.ac.nz)
  • FIH-dependent asparaginyl hydroxylation of ankyrin repeat domain-containing proteins. (ox.ac.uk)
  • Proteins containing a common interaction motif known as the ankyrin repeat domain (ARD) have been shown to be efficiently hydroxylated by FIH. (ox.ac.uk)
  • Shank1-3 proteins (also called ProSAP, SSTRIP, cortBP, Synamon, and Spank) contain ankyrin repeats, an Src homology 3 (SH3) domain, a PSD-95-Discs Large-zona occludens-1 (PDZ) domain, a proline-rich domain, and a sterile alpha motif (SAM) domain. (jneurosci.org)
  • The ankyrin (ANK) repeat genes encode for proteins characterized by the repetitive motifs in its amino acid sequence. (wmich.edu)
  • Bacterial endosymbiont genes were identified in this dataset, some of which have a copy number consistent with being lateral gene transfers between endosymbiont genomes and Hemiptera, including ankyrin-repeat related proteins, lysozyme, and mannanase. (biomedcentral.com)
  • In both proteins, the second ankyrin (ANK) repeat region and the β-hairpin loops connecting this repeat with the rest of the protein are significantly unfolded. (uconn.edu)
  • Thus, p16C is the smallest ANK repeat module that can fold independently and the two ANK repeat fold may represent the minimum structural unit for all ANK repeat proteins. (uconn.edu)
  • Other discoveries include the apparent inability of w Mel to synthesize lipopolysaccharide and the presence of the most genes encoding proteins with ankyrin repeat domains of any prokaryotic genome yet sequenced. (plos.org)
  • Proteomics-based identification of novel factor inhibiting hypoxia-inducible factor (FIH) substrates indicates widespread asparaginyl hydroxylation of ankyrin repeat domain-containing proteins. (ox.ac.uk)
  • In support of this certain ankyrin repeat domain (ARD)-containing proteins, including members of the IkappaB and Notch families, have been identified as alternative substrates of the HIF asparaginyl hydroxylase factor inhibiting HIF (FIH). (ox.ac.uk)
  • Overall the work has defined 13 new FIH-dependent hydroxylation sites with a degenerate consensus corresponding to that of the ankyrin repeat and a range of ARD-containing proteins as actual and potential substrates for FIH. (ox.ac.uk)
  • 2009). AA: A truncated two-alpha-helix F-box present in poxvirus ankyrin-repeat proteins is sufficient for binding the SCF1 ubiquitin ligase complex. (core.ac.uk)
  • 2008). AA: Poxvirus ankyrin repeat proteins are a unique class of F-box proteins that associate with cellular SCF1 ubiquitin ligase complexes. (core.ac.uk)
  • 2005). F-box-like domains are present in most poxvirus ankyrin repeat proteins. (core.ac.uk)
  • Nonantibody scaffolds such as designed ankyrin repeat proteins (DARPins) can be rapidly engineered to detect diverse target proteins with high specificity and offer an attractive alternative to antibodies. (elsevier.com)
  • In addition to the hypoxia-inducible factor C-terminal transcriptional activation domain (HIF-CAD), FIH also catalyses asparaginyl hydroxylation of many ankyrin repeat domain-containing proteins, revealing a broad sequence selectivity. (ox.ac.uk)
  • Ankyrin repeat domain 11 is a protein that in humans is encoded by the ANKRD11 gene . (wikipedia.org)
  • ANKRD1, the gene encoding cardiac ankyrin repeat protein, is a novel dilated cardiomyopathy gene. (thefreedictionary.com)
  • This gene encodes a protein with multiple ankyrin repeat domains and a single KH-domain. (mybiosource.com)
  • Objectives We evaluated ankyrin repeat domain 1 ( ANKRD1) , the gene encoding cardiac ankyrin repeat protein (CARP), as a novel candidate gene for dilated cardiomyopathy (DCM) through mutation analysis of a cohort of familial or idiopathic DCM patients, based on the hypothesis that inherited dysfunction of mechanical stretch-based signaling is present in a subset of DCM patients. (onlinejacc.org)
  • ANKRD34A (Ankyrin Repeat Domain 34A) is a Protein Coding gene. (genecards.org)
  • The ANKRD11 gene provides instructions for making a protein called ankyrin repeat domain 11 (ANKRD11). (nih.gov)
  • Suryawanshi, Yogesh, "Generation of Tanapoxvirus Ankyrin Repeat Gene Deletion Mutant for Evaluating its Role in Cell Tropism" (2012). (wmich.edu)
  • This gene encodes a cytoplasmic protein that contains a coiled-coil structure and a BTB/POZ domain at its N-terminus, ankyrin repeats in the middle portion, and a FYVE-finger motif at its C-terminus. (gen-script.com)
  • Here, we focus on MNF gene, which has been shown to express a nuclear protein presenting nine ANK repeats, one of which has been identified as a nuclear localization signal. (core.ac.uk)
  • 2009). The orthopoxvirus 68-kilodalton ankyrin-like protein is essential for DNA replication and complete gene expression of modified vaccinia virus Ankara in nonpermissive human and murine cells. (core.ac.uk)
  • Consensus-derived structural determinants of the ankyrin repeat motif. (ebi.ac.uk)
  • The ankyrin-repeat sequence motif has been studied using multiple sequence alignment to determine conserved amino acid residues critical for folding and stability. (wikipedia.org)
  • These domains contain multiple repeats of a beta(2)-alpha(2) motif. (ebi.ac.uk)
  • Source:RefSeq mRNA;Acc :NM_001109946] ENSSSCG00000005 607 RALGPS 1 Ral GEF with PH domain and SH3 binding motif 1 [Source:HGNC Symbol;Acc:16851] ENSSSCG00000005 679 ASB6 Sus scrofa ankyrin repeat and SOCS box containing 6 (ASB6), mRNA. (thefreedictionary.com)
  • Ankyrin (ANK) repeat, a common motif with typically 33 residues in each repeat, is primarily involved in protein-protein interactions. (rcsb.org)
  • Two GABPα/β heterodimers associate via the COOH-terminal residues of GABPβ, resulting in a heterotetramer that binds to DNA sequences containing two tandem repeats of the GGA motif ( 19 ). (sciencemag.org)
  • p16 contains four ANK repeats, a 33-residue sequence motif that mediates protein-protein interactions. (uconn.edu)
  • Because it contains several domains for protein-protein interactions, including ankyrin repeats, tetratricopeptide repeats (TPRs), a coiled-coil domain, and a C-terminal PDZ (PSD-95/Dlg/ZO-1) domain-binding motif, TANC1 is thought to function as a scaffold/adaptor protein. (jneurosci.org)
  • C terminal to the RAM domain lie six interated ankyrin repeats (ANK) (amino acids 1860 to 2155), a highly conserved domain necessary for all known Notch functions ( 1 ). (asm.org)
  • Recent analyses have shown that factor inhibiting hypoxia-inducible factor (FIH) catalyses the hydroxylation of highly conserved Asn-residues within ankyrin repeat domains (ARDs). (ox.ac.uk)
  • 2008). The highly conserved orthopoxvirus 68k ankyrin-like protein is part of a cellular SCF ubiquitin ligase complex. (core.ac.uk)
  • The N-terminal cytoplasmic domain of TRPC, TRPV, and ANKTM (TRPA) channels contain ankyrin repeats, whereas the TRPC and TRPM contain proline-rich regions in the region just C-terminal to the predicted 6TM segment ( Fig. 2 ). (aspetjournals.org)
  • High-affinity binders selected from designed ankyrin repeat protein libraries. (grstiftung.ch)
  • We now report that nuclear localization of Ikappa Balpha is mediated by a novel nuclear import sequence within the second ankyrin repeat. (caltech.edu)
  • Furthermore, a region encompassing the second ankyrin repeat of Ikappa Balpha is able to function as a discrete nuclear import sequence. (caltech.edu)
  • Interacts (via the second ankyrin repeat cluster) with DDX58 . (sdsc.edu)
  • Ankyrin repeats are tandemly repeated modules of about 33 amino acids. (ebi.ac.uk)
  • This repeating sequence of 33- Amino Acids was discovered in Ankyrin where it is involved in interaction with the anion exchanger ( Anion Exchange Protein 1, Erythrocyte ). (online-medical-dictionary.org)
  • They are based on a very different structure (Supplementary Fig. S1) and are built from consecutive 33-amino acid repeats, each forming a β-turn followed by two antiparallel α-helices. (aacrjournals.org)
  • Canonical-type transient receptor potential 3 (TRPC3) contains an ankyrin repeat (AR) region at the N-terminus (38-188 amino acids) and forms extracellular Ca2 +- entry channels by homo or heteromerization with other TRP subtypes in various cells including skeletal myotubes. (bentham.co.uk)
  • Biochemical studies and deletion mutation analyses indicate that the 11-amino acid sequence between amino acids 717 and 727 of Tiam1 ( 717 GEGTDAVKRS 727 L) is the ankyrin-binding domain. (rupress.org)
  • Using an Escherichia coli -derived calmodulin-binding peptide (CBP)-tagged recombinant Tiam1 (amino acids 393-728) fragment that contains the ankyrin-binding domain, we have detected a specific binding interaction between the Tiam1 (amino acids 393-738) fragment and ankyrin in vitro. (rupress.org)
  • Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2. (ebi.ac.uk)
  • Ankyrin repeats typically fold together to form a single, linear solenoid structure called ankyrin repeat domains. (wikipedia.org)
  • Ankyrin repeats cooperatively fold into domains that mediate molecular recognition via protein-protein interactions. (online-medical-dictionary.org)
  • Both the ankyrin repeat and C-terminal transactivation domains were required for T-cell leukemogenesis, whereas the N-terminal RAM domain and a C-terminal domain that includes a PEST sequence were nonessential. (asm.org)
  • Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domains. (ox.ac.uk)
  • In a one-year re-integration phase I will perform follow-up mechanistic structural studies in the Olga Mayans lab (University of Liverpool) to determine the structural basis how the CARP (cardiac ankyrin repeat protein)-titin signaling axis mediates cardiomyocyte protection, and in the Labeit lab (University of Heidelberg, Medical Faculty Mannheim) how to perturb activity of this complex by small molecules. (thefreedictionary.com)
  • A multiprotein complex encompassing a transcription regulator, cardiac ankyrin repeat protein (CARP), and the calpain 3 protease was identified in the N2A elastic region of the giant sarcomeric protein titin. (elsevier.com)
  • This locus encodes an ankyrin repeat domain-containing protein. (wikipedia.org)
  • Lr14a encodes a membrane-localized protein containing twelve ankyrin (ANK) repeats and structural similarities to Ca$^{2+}$-permeable non-selective cation channels. (edu.sa)
  • Biopharmaceutical company Cubist Pharmaceuticals Inc (NASDAQ:CBST) and Hydra Biosciences Inc announced on Tuesday the joint proposal to commence a Phase 1 clinical study for a small molecule antagonist of the human Transient Receptor Potential Ankyrin repeat 1 (TRPA1) ion channel. (thefreedictionary.com)
  • today announced plans to begin a Phase 1 clinical trial for a small molecule antagonist of the human Transient Receptor Potential Ankyrin repeat 1 (TRPA1) ion channel discovered in a collaboration between Cubist and Hydra. (thefreedictionary.com)
  • o-Chlorobenzylidene malononitrile (CS) is a selective and potent agonist of the transient receptor potential ankyrin repeat 1 (TRPA1), which is a transducer molecule in nociceptors sensing reactive chemical species. (ovid.com)
  • Here, we demonstrate based on Förster resonance energy transfer (FRET) and bilayer patch-clamp studies, a direct calmodulin-independent action of calcium on the purified human TRPA1 (hTRPA1), causing structural changes and activation without immediate subsequent desensitization of hTRPA1 with and without its N-terminal ankyrin repeat domain (N-ARD). (nanion.de)
  • Transient receptor potential ankyrin 1 (TRPA1) is an ion channel known to mediate nociception and neurogenic inflammation, and to be activated by reactive oxygen and nitrogen species (ROS and RNS) produced at the sites of inflammation. (bioportfolio.com)
  • Transient Receptor Potential Ankyrin-1 (TRPA1) Channel Contributes to Myocardial Ischemia-Reperfusion Injury. (bioportfolio.com)
  • Ionic channels such as the transient receptor potential ankyrin 1 (TRPA1) are essential for the detection and transmission of painful stimuli. (bioportfolio.com)
  • The residues on the wide lateral surface of ankyrin repeat structures are variable, often hydrophobic, and involved mainly in mediating protein-protein interactions. (wikipedia.org)
  • Asparagine beta-hydroxylation stabilizes the ankyrin repeat domain fold. (ox.ac.uk)
  • Immunoprecipitation and immunoblot analyses indicate that Tiam1 and the cytoskeletal protein, ankyrin, are physically associated as a complex in vivo. (rupress.org)
  • GABPβ contains four-and-a-half ankyrin repeats at its NH 2 -terminus that mediate heterodimerization with GABPα ( 17 ). (sciencemag.org)
  • The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. (ebi.ac.uk)
  • This interaction is mediated by giant Ankyrins, that act as specialized adaptors to establish and maintain axonal and synaptic compartments. (uni-kl.de)
  • Analysis of truncated forms of ov008 revealed that the ANK repeat domain is the site of interaction between ov008 and FIH-1. (otago.ac.nz)
  • Together the results suggest the 1st ANK repeat of ov008 determines the interaction of ov008 with FIH-1 while the 4th repeat may have a role in maintain the overall structure of the ov008 ANK repeat domain. (otago.ac.nz)
  • Shank1 when it is not associated to GKAP, which binds to the Shank PSD-95-Discs Large-zona occludens-1 domain, forms filamentous and fusiform structures in which the Src homology 3 domain specifically interacts with the ankyrin repeat domain, thus allowing its multimerization via a novel form of intermolecular interaction. (jneurosci.org)
  • These findings suggest that ankyrin-Tiam1 interaction plays a pivotal role in regulating Rac1 signaling and cytoskeleton function required for oncogenic signaling and metastatic breast tumor cell progression. (rupress.org)
  • The ankyrin fold appears to be defined by its structure rather than its function since there is no specific sequence or structure which is universally recognised by it. (ebi.ac.uk)
  • The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures [ PMID: 8875926 , PMID: 9353127 , PMID: 9461436 , PMID: 9865693 ]. (ebi.ac.uk)
  • An artificial protein design based on a consensus sequence derived from sequence alignment has been synthesized and found to fold stably, representing the first designed protein with multiple repeats. (wikipedia.org)
  • Most studies have found that ankyrin repeats fold in a two-state folding mechanism, suggesting a high degree of folding cooperativity despite the local inter-residue contacts and the evident need for successful folding with varying numbers of repeats. (wikipedia.org)
  • p16C has moderately stable secondary and tertiary structure, with the ANK repeats adopting a similar topological fold as in the full-length protein. (uconn.edu)
  • Heteromeric TRPC3 with TRPC1 formed via its ankyrin repeats regulates the resting cytosolic Ca 2+ levels in skeletal muscle. (bentham.co.uk)
  • In all six members of TRPV channel subfamily, there is an ankyrin repeat domain (ARD) in their intracellular N-termini. (rcsb.org)
  • We identified three missense substitutions (R269H, R315W and R316C) affecting the intracellular N-terminal ankyrin domain of the TRPV4 ion channel in five families. (nih.gov)
  • Your search returned 20 Ankyrin repeat domain 12 ELISA ELISA Kit across 6 suppliers. (biocompare.com)
  • Your search returned 13 Ankyrin repeat domain 29 ELISA ELISA Kit across 1 supplier. (biocompare.com)
  • failed verification] The variation may affect the specificity of protein interactions made by the ANKK1 protein kinase through this repeat[citation needed]. (wikipedia.org)
  • Receptor interacting protein kinase (RIPK) family: ankyrin repeat and kinase domain containing 1. (guidetopharmacology.org)
  • The Ankyrin-Repeat Rich Membrane Spanning (ARMS)/kinase D-interacting substrate-220 kDa (Kidins220) serves as a unique downstream adaptor protein of Trk receptor tyrosine kinases. (snu.ac.kr)
  • Cotransfection of SP1 cells with green fluorescent protein (GFP)-tagged Tiam1 fragment cDNA and Tiam1 cDNA effectively blocks Tiam1-ankyrin colocalization in the cell membrane, and inhibits GDP/GTP exchange on Rac1 by ankyrin-associated Tiam1 and tumor-specific phenotypes. (rupress.org)
  • Here, we report that histidinyl residues within the ankyrin repeat domain of tankyrase-2 can be hydroxylated by FIH. (ox.ac.uk)
  • We describe the structure of the cytosolic ankyrin repeat domain (ARD) of TRPV1 and identify a multiligand-binding site important in regulating channel sensitivity within the TRPV1-ARD. (semanticscholar.org)
  • The designed ankyrin repeat protein (DARPin) G3 binds HER2 with high affinity at an epitope that does not overlap with trastuzumab and is biologically inert. (nih.gov)
  • Transient Receptor Potential Ankyrin 1 Enhances Ovalbumin-Induced Acute Allergic Inflammation in Murine Models. (bioportfolio.com)
  • The beta strands on adjacent ankyrin repeats combine to form a short antiparallel beta sheet. (thefreedictionary.com)