E3 ubiquitin-protein ligase CHIP

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityⁱ

• S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.2 Publications

  Manual assertion based on experiment inⁱ

  • Ref.4

    "U box proteins as a new family of ubiquitin-protein ligases."
    Hatakeyama S., Yada M., Matsumoto M., Ishida N., Nakayama K.I.
    J. Biol. Chem. 276:33111-33120(2001) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF HIS-261 AND PRO-270.
  • Ref.9

    "Ube2w and ataxin-3 coordinately regulate the ubiquitin ligase CHIP."
    Scaglione K.M., Zavodszky E., Todi S.V., Patury S., Xu P., Rodriguez-Lebron E., Fischer S., Konen J., Djarmati A., Peng J., Gestwicki J.E., Paulson H.L.
    Mol. Cell 43:599-612(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INTERACTION WITH UBE2W AND ATXN3, UBIQUITINATION AT LYS-2, MUTAGENESIS OF LYS-2; LYS-4 AND LYS-7.

  EC:2.3.2.27

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• chaperone binding Source: MGI
• enzyme binding Source: MGI
• G protein-coupled receptor binding Source: MGI
• heat shock protein binding Source: MGI
• Hsp70 protein binding Source: HGNC-UCL <p>Inferred from Sequence or Structural Similarity<br />Used for any analysis based on sequence alignment, structure comparison, or evaluation of sequence features such as composition.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iss">GO evidence code guide</a></p> Inferred from sequence or structural similarityⁱ
  • Ref.1

    "Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions."
    Ballinger C.A., Connell P., Wu Y., Hu Z., Thompson L.J., Yin L.-Y., Patterson C.
    Mol. Cell. Biol. 19:4535-4545(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
• Hsp90 protein binding Source: BHF-UCL
• kinase binding Source: MGI
• misfolded protein binding Source: MGI
• protein homodimerization activity Source: HGNC-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.11

    "Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex."
    Zhang M., Windheim M., Roe S.M., Peggie M., Cohen P., Prodromou C., Pearl L.H.
    Mol. Cell 20:525-538(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 24-304 IN COMPLEX WITH UBE2N AND UBE2V1, X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 227-304 IN COMPLEX WITH HSP90AA1, HOMODIMERIZATION.
• protein-macromolecule adaptor activity Source: HGNC-UCL <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementⁱ
  • Ref.11

    "Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex."
    Zhang M., Windheim M., Roe S.M., Peggie M., Cohen P., Prodromou C., Pearl L.H.
    Mol. Cell 20:525-538(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 24-304 IN COMPLEX WITH UBE2N AND UBE2V1, X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 227-304 IN COMPLEX WITH HSP90AA1, HOMODIMERIZATION.
• SMAD binding Source: HGNC-UCL
• TPR domain binding Source: HGNC-UCLInferred from sequence or structural similarityⁱ
  • Ref.1

    "Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions."
    Ballinger C.A., Connell P., Wu Y., Hu Z., Thompson L.J., Yin L.-Y., Patterson C.
    Mol. Cell. Biol. 19:4535-4545(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
• ubiquitin protein ligase activity Source: MGIInferred from direct assayⁱ
  • Ref.9

    "Ube2w and ataxin-3 coordinately regulate the ubiquitin ligase CHIP."
    Scaglione K.M., Zavodszky E., Todi S.V., Patury S., Xu P., Rodriguez-Lebron E., Fischer S., Konen J., Djarmati A., Peng J., Gestwicki J.E., Paulson H.L.
    Mol. Cell 43:599-612(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INTERACTION WITH UBE2W AND ATXN3, UBIQUITINATION AT LYS-2, MUTAGENESIS OF LYS-2; LYS-4 AND LYS-7.
• ubiquitin protein ligase binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • Ref.9

    "Ube2w and ataxin-3 coordinately regulate the ubiquitin ligase CHIP."
    Scaglione K.M., Zavodszky E., Todi S.V., Patury S., Xu P., Rodriguez-Lebron E., Fischer S., Konen J., Djarmati A., Peng J., Gestwicki J.E., Paulson H.L.
    Mol. Cell 43:599-612(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INTERACTION WITH UBE2W AND ATXN3, UBIQUITINATION AT LYS-2, MUTAGENESIS OF LYS-2; LYS-4 AND LYS-7.
• ubiquitin-protein transferase activity Source: UniProtKB
• ubiquitin-ubiquitin ligase activity Source: MGIInferred from direct assayⁱ
  • Ref.4

    "U box proteins as a new family of ubiquitin-protein ligases."
    Hatakeyama S., Yada M., Matsumoto M., Ishida N., Nakayama K.I.
    J. Biol. Chem. 276:33111-33120(2001) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF HIS-261 AND PRO-270.

GO - Biological processⁱ

• cellular response to heat Source: MGI
• cellular response to hypoxia Source: MGI
• cellular response to misfolded protein Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • Ref.9

    "Ube2w and ataxin-3 coordinately regulate the ubiquitin ligase CHIP."
    Scaglione K.M., Zavodszky E., Todi S.V., Patury S., Xu P., Rodriguez-Lebron E., Fischer S., Konen J., Djarmati A., Peng J., Gestwicki J.E., Paulson H.L.
    Mol. Cell 43:599-612(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INTERACTION WITH UBE2W AND ATXN3, UBIQUITINATION AT LYS-2, MUTAGENESIS OF LYS-2; LYS-4 AND LYS-7.
• chaperone-mediated autophagy Source: MGI
• DNA repair Source: UniProtKB-KW
• endoplasmic reticulum unfolded protein response Source: ParkinsonsUK-UCLInferred from direct assayⁱ
  • "CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity."
    Imai Y., Soda M., Hatakeyama S., Akagi T., Hashikawa T., Nakayama K., Takahashi R.
    Mol. Cell 10:55-67(2002) [PubMed] [Europe PMC] [Abstract]
• negative regulation of protein binding Source: ParkinsonsUK-UCLInferred from direct assayⁱ
  • "CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity."
    Imai Y., Soda M., Hatakeyama S., Akagi T., Hashikawa T., Nakayama K., Takahashi R.
    Mol. Cell 10:55-67(2002) [PubMed] [Europe PMC] [Abstract]
• negative regulation of transforming growth factor beta receptor signaling pathway Source: MGI
• positive regulation of chaperone-mediated protein complex assembly Source: MGI
• positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: HGNC-UCLInferred from sequence or structural similarityⁱ
  • Ref.1

    "Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions."
    Ballinger C.A., Connell P., Wu Y., Hu Z., Thompson L.J., Yin L.-Y., Patterson C.
    Mol. Cell. Biol. 19:4535-4545(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
• positive regulation of protein ubiquitination Source: ParkinsonsUK-UCLInferred from direct assayⁱ
  • "CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity."
    Imai Y., Soda M., Hatakeyama S., Akagi T., Hashikawa T., Nakayama K., Takahashi R.
    Mol. Cell 10:55-67(2002) [PubMed] [Europe PMC] [Abstract]
• positive regulation of proteolysis Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• positive regulation of ubiquitin-protein transferase activity Source: ParkinsonsUK-UCLInferred from direct assayⁱ
  • "CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity."
    Imai Y., Soda M., Hatakeyama S., Akagi T., Hashikawa T., Nakayama K., Takahashi R.
    Mol. Cell 10:55-67(2002) [PubMed] [Europe PMC] [Abstract]
• proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.9

    "Ube2w and ataxin-3 coordinately regulate the ubiquitin ligase CHIP."
    Scaglione K.M., Zavodszky E., Todi S.V., Patury S., Xu P., Rodriguez-Lebron E., Fischer S., Konen J., Djarmati A., Peng J., Gestwicki J.E., Paulson H.L.
    Mol. Cell 43:599-612(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INTERACTION WITH UBE2W AND ATXN3, UBIQUITINATION AT LYS-2, MUTAGENESIS OF LYS-2; LYS-4 AND LYS-7.
• protein autoubiquitination Source: UniProtKB
• protein folding Source: HGNC-UCLTraceable author statementⁱ
  • Ref.11

    "Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex."
    Zhang M., Windheim M., Roe S.M., Peggie M., Cohen P., Prodromou C., Pearl L.H.
    Mol. Cell 20:525-538(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 24-304 IN COMPLEX WITH UBE2N AND UBE2V1, X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 227-304 IN COMPLEX WITH HSP90AA1, HOMODIMERIZATION.
• protein K63-linked ubiquitination Source: UniProtKB
• protein maturation Source: HGNC-UCLTraceable author statementⁱ
  • Ref.11

    "Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex."
    Zhang M., Windheim M., Roe S.M., Peggie M., Cohen P., Prodromou C., Pearl L.H.
    Mol. Cell 20:525-538(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 24-304 IN COMPLEX WITH UBE2N AND UBE2V1, X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 227-304 IN COMPLEX WITH HSP90AA1, HOMODIMERIZATION.
• protein polyubiquitination Source: MGIInferred from direct assayⁱ
  • Ref.4

    "U box proteins as a new family of ubiquitin-protein ligases."
    Hatakeyama S., Yada M., Matsumoto M., Ishida N., Nakayama K.I.
    J. Biol. Chem. 276:33111-33120(2001) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF HIS-261 AND PRO-270.
• protein quality control for misfolded or incompletely synthesized proteins Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.9

    "Ube2w and ataxin-3 coordinately regulate the ubiquitin ligase CHIP."
    Scaglione K.M., Zavodszky E., Todi S.V., Patury S., Xu P., Rodriguez-Lebron E., Fischer S., Konen J., Djarmati A., Peng J., Gestwicki J.E., Paulson H.L.
    Mol. Cell 43:599-612(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INTERACTION WITH UBE2W AND ATXN3, UBIQUITINATION AT LYS-2, MUTAGENESIS OF LYS-2; LYS-4 AND LYS-7.
• protein ubiquitination Source: MGI
• regulation of glucocorticoid metabolic process Source: HGNC-UCLInferred from sequence or structural similarityⁱ
  • Ref.1

    "Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions."
    Ballinger C.A., Connell P., Wu Y., Hu Z., Thompson L.J., Yin L.-Y., Patterson C.
    Mol. Cell. Biol. 19:4535-4545(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
• regulation of protein stability Source: MGI
• response to ischemia Source: MGI
• ubiquitin-dependent ERAD pathway Source: MGI
• ubiquitin-dependent protein catabolic process Source: ARUK-UCLInferred from mutant phenotypeⁱ
  • "Akt and CHIP coregulate tau degradation through coordinated interactions."
    Dickey C.A., Koren J., Zhang Y.J., Xu Y.F., Jinwal U.K., Birnbaum M.J., Monks B., Sun M., Cheng J.Q., Patterson C., Bailey R.M., Dunmore J., Soresh S., Leon C., Morgan D., Petrucelli L.
    Proc Natl Acad Sci U S A 105:3622-3627(2008) [PubMed] [Europe PMC] [Abstract]
• ubiquitin-dependent SMAD protein catabolic process Source: HGNC-UCL

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

• UniProt annotation
• GO - Cellular component

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductionⁱ

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• chaperone binding Source: MGI
• enzyme binding Source: MGI
• G protein-coupled receptor binding Source: MGI
• heat shock protein binding Source: MGI
• Hsp70 protein binding Source: HGNC-UCLInferred from sequence or structural similarityⁱ
  • Ref.1

    "Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions."
    Ballinger C.A., Connell P., Wu Y., Hu Z., Thompson L.J., Yin L.-Y., Patterson C.
    Mol. Cell. Biol. 19:4535-4545(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
• Hsp90 protein binding Source: BHF-UCL
• kinase binding Source: MGI
• misfolded protein binding Source: MGI
• protein homodimerization activity Source: HGNC-UCLInferred from direct assayⁱ
  • Ref.11

    "Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex."
    Zhang M., Windheim M., Roe S.M., Peggie M., Cohen P., Prodromou C., Pearl L.H.
    Mol. Cell 20:525-538(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 24-304 IN COMPLEX WITH UBE2N AND UBE2V1, X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 227-304 IN COMPLEX WITH HSP90AA1, HOMODIMERIZATION.
• SMAD binding Source: HGNC-UCL
• TPR domain binding Source: HGNC-UCLInferred from sequence or structural similarityⁱ
  • Ref.1

    "Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions."
    Ballinger C.A., Connell P., Wu Y., Hu Z., Thompson L.J., Yin L.-Y., Patterson C.
    Mol. Cell. Biol. 19:4535-4545(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
• ubiquitin protein ligase binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.9

    "Ube2w and ataxin-3 coordinately regulate the ubiquitin ligase CHIP."
    Scaglione K.M., Zavodszky E., Todi S.V., Patury S., Xu P., Rodriguez-Lebron E., Fischer S., Konen J., Djarmati A., Peng J., Gestwicki J.E., Paulson H.L.
    Mol. Cell 43:599-612(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INTERACTION WITH UBE2W AND ATXN3, UBIQUITINATION AT LYS-2, MUTAGENESIS OF LYS-2; LYS-4 AND LYS-7.

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

Region

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domainⁱ

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MKGKEEKEGG ARLGTGGGGS PDKSPSAQEL KEQGNRLFVG RKYPEAAACY 
        60         70         80         90        100
GRAITRNPLV AVYYTNRALC YLKMQQPEQA LADCRRALEL DGQSVKAHFF 
       110        120        130        140        150
LGQCQLEMES YDEAIANLQR AYSLAKEQRL NFGDDIPSAL RIAKKKRWNS 
       160        170        180        190        200
IEERRIHQES ELHSYLTRLI AAERERELEE CQRNHEGHED DGHIRAQQAC 
       210        220        230        240        250
IEAKHDKYMA DMDELFSQVD EKRKKRDIPD YLCGKISFEL MREPCITPSG 
       260        270        280        290        300
ITYDRKDIEE HLQRVGHFDP VTRSPLTQEQ LIPNLAMKEV IDAFISENGW 

VEDY                                                   

Experimental Info

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. MGD cross-references
   Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
2. PATHWAY comments
   Index of metabolic and biosynthesis pathways
3. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references