E3 ubiquitin-protein ligase SMURF1

<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.1 Publication

  Manual assertion based on experiment inⁱ

  • Ref.9

    "Ubiquitin ligase Smurf1 targets TRAF family proteins for ubiquitination and degradation."
    Li S., Lu K., Wang J., An L., Yang G., Chen H., Cui Y., Yin X., Xie P., Xing G., He F., Zhang L.
    Mol. Cell. Biochem. 338:11-17(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-725, INTERACTION WITH TRAF4.

  EC:2.3.2.26

Sites

<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

• activin binding Source: BHF-UCL <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementⁱ
  • "FKBP12 functions as an adaptor of the Smad7-Smurf1 complex on activin type I receptor."
    Yamaguchi T., Kurisaki A., Yamakawa N., Minakuchi K., Sugino H.
    J. Mol. Endocrinol. 36:569-579(2006) [PubMed] [Europe PMC] [Abstract]
• I-SMAD binding Source: BHF-UCL <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
  • "Smurf1 interacts with transforming growth factor-beta type I receptor through Smad7 and induces receptor degradation."
    Ebisawa T., Fukuchi M., Murakami G., Chiba T., Tanaka K., Imamura T., Miyazono K.
    J. Biol. Chem. 276:12477-12480(2001) [PubMed] [Europe PMC] [Abstract]
  • "Smurf1 regulates the inhibitory activity of Smad7 by targeting Smad7 to the plasma membrane."
    Suzuki C., Murakami G., Fukuchi M., Shimanuki T., Shikauchi Y., Imamura T., Miyazono K.
    J. Biol. Chem. 277:39919-39925(2002) [PubMed] [Europe PMC] [Abstract]
• phospholipid binding Source: ParkinsonsUK-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
  • "Image-based genome-wide siRNA screen identifies selective autophagy factors."
    Orvedahl A., Sumpter R. Jr., Xiao G., Ng A., Zou Z., Tang Y., Narimatsu M., Gilpin C., Sun Q., Roth M., Forst C.V., Wrana J.L., Zhang Y.E., Luby-Phelps K., Xavier R.J., Xie Y., Levine B.
    Nature 480:113-117(2011) [PubMed] [Europe PMC] [Abstract]
• R-SMAD binding Source: BHF-UCLInferred from physical interactionⁱ
  • "Smurf1 interacts with transforming growth factor-beta type I receptor through Smad7 and induces receptor degradation."
    Ebisawa T., Fukuchi M., Murakami G., Chiba T., Tanaka K., Imamura T., Miyazono K.
    J. Biol. Chem. 276:12477-12480(2001) [PubMed] [Europe PMC] [Abstract]
• ubiquitin protein ligase activity Source: BHF-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
  • "Smurf1 interacts with transforming growth factor-beta type I receptor through Smad7 and induces receptor degradation."
    Ebisawa T., Fukuchi M., Murakami G., Chiba T., Tanaka K., Imamura T., Miyazono K.
    J. Biol. Chem. 276:12477-12480(2001) [PubMed] [Europe PMC] [Abstract]
  • "Smurf1 regulates the inhibitory activity of Smad7 by targeting Smad7 to the plasma membrane."
    Suzuki C., Murakami G., Fukuchi M., Shimanuki T., Shikauchi Y., Imamura T., Miyazono K.
    J. Biol. Chem. 277:39919-39925(2002) [PubMed] [Europe PMC] [Abstract]
• ubiquitin-protein transferase activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.7

    "A SMAD ubiquitin ligase targets the BMP pathway and affects embryonic pattern formation."
    Zhu H., Kavsak P., Abdollah S., Wrana J.L., Thomsen G.H.
    Nature 400:687-693(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-731 (ISOFORM SHORT), FUNCTION.
  • Ref.9

    "Ubiquitin ligase Smurf1 targets TRAF family proteins for ubiquitination and degradation."
    Li S., Lu K., Wang J., An L., Yang G., Chen H., Cui Y., Yin X., Xie P., Xing G., He F., Zhang L.
    Mol. Cell. Biochem. 338:11-17(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-725, INTERACTION WITH TRAF4.

GO - Biological processⁱ

• BMP signaling pathway Source: UniProtKBInferred from direct assayⁱ
  • Ref.10

    "SCF(FBXL15) regulates BMP signalling by directing the degradation of HECT-type ubiquitin ligase Smurf1."
    Cui Y., He S., Xing C., Lu K., Wang J., Xing G., Meng A., Jia S., He F., Zhang L.
    EMBO J. 30:2675-2689(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-381 AND LYS-383, INTERACTION WITH FBXL15, MUTAGENESIS OF LYS-350; LYS-381; LYS-383 AND CYS-725.
• cell differentiation Source: UniProtKBInferred from direct assayⁱ
  • Ref.7

    "A SMAD ubiquitin ligase targets the BMP pathway and affects embryonic pattern formation."
    Zhu H., Kavsak P., Abdollah S., Wrana J.L., Thomsen G.H.
    Nature 400:687-693(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-731 (ISOFORM SHORT), FUNCTION.
• ectoderm development Source: UniProtKBTraceable author statementⁱ
  • Ref.7

    "A SMAD ubiquitin ligase targets the BMP pathway and affects embryonic pattern formation."
    Zhu H., Kavsak P., Abdollah S., Wrana J.L., Thomsen G.H.
    Nature 400:687-693(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-731 (ISOFORM SHORT), FUNCTION.
• engulfment of target by autophagosome Source: ParkinsonsUK-UCL <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
  • "Image-based genome-wide siRNA screen identifies selective autophagy factors."
    Orvedahl A., Sumpter R. Jr., Xiao G., Ng A., Zou Z., Tang Y., Narimatsu M., Gilpin C., Sun Q., Roth M., Forst C.V., Wrana J.L., Zhang Y.E., Luby-Phelps K., Xavier R.J., Xie Y., Levine B.
    Nature 480:113-117(2011) [PubMed] [Europe PMC] [Abstract]
• negative regulation of BMP signaling pathway Source: BHF-UCLInferred from direct assayⁱ
  • "MicroRNA-140-5p and SMURF1 regulate pulmonary arterial hypertension."
    Rothman A.M., Arnold N.D., Pickworth J.A., Iremonger J., Ciuclan L., Allen R.M., Guth-Gundel S., Southwood M., Morrell N.W., Thomas M., Francis S.E., Rowlands D.J., Lawrie A.
    J. Clin. Invest. 126:2495-2508(2016) [PubMed] [Europe PMC] [Abstract]
• negative regulation of ossification Source: Ensembl
• negative regulation of transforming growth factor beta receptor signaling pathway Source: BHF-UCLInferred from direct assayⁱ
  • "Smurf1 interacts with transforming growth factor-beta type I receptor through Smad7 and induces receptor degradation."
    Ebisawa T., Fukuchi M., Murakami G., Chiba T., Tanaka K., Imamura T., Miyazono K.
    J. Biol. Chem. 276:12477-12480(2001) [PubMed] [Europe PMC] [Abstract]
  • "Smurf1 regulates the inhibitory activity of Smad7 by targeting Smad7 to the plasma membrane."
    Suzuki C., Murakami G., Fukuchi M., Shimanuki T., Shikauchi Y., Imamura T., Miyazono K.
    J. Biol. Chem. 277:39919-39925(2002) [PubMed] [Europe PMC] [Abstract]
• parkin-mediated stimulation of mitophagy in response to mitochondrial depolarization Source: Ensembl
• positive regulation of dendrite extension Source: UniProtKBInferred from direct assayⁱ
  • Ref.12

    "SYT14L, especially its C2 domain, is involved in regulating melanocyte differentiation."
    Yoo J.C., Lim T.Y., Park J.S., Hah Y.S., Park N., Hong S.G., Park J.Y., Yoon T.J.
    J. Dermatol. Sci. 72:246-251(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, TISSUE SPECIFICITY.
• positive regulation of protein catabolic process 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. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• positive regulation of ubiquitin-dependent protein catabolic process Source: CACAOInferred from mutant phenotypeⁱ
  • "The E3 ligase Smurf1 regulates Wolfram syndrome protein stability at the endoplasmic reticulum."
    Guo X., Shen S., Song S., He S., Cui Y., Xing G., Wang J., Yin Y., Fan L., He F., Zhang L.
    J. Biol. Chem. 286:18037-18047(2011) [PubMed] [Europe PMC] [Abstract]
• proteasome-mediated ubiquitin-dependent protein catabolic process Source: BHF-UCLInferred from direct assayⁱ
  • "Smurf1 interacts with transforming growth factor-beta type I receptor through Smad7 and induces receptor degradation."
    Ebisawa T., Fukuchi M., Murakami G., Chiba T., Tanaka K., Imamura T., Miyazono K.
    J. Biol. Chem. 276:12477-12480(2001) [PubMed] [Europe PMC] [Abstract]
• protein export from nucleus Source: BHF-UCLInferred from direct assayⁱ
  • "Smurf1 interacts with transforming growth factor-beta type I receptor through Smad7 and induces receptor degradation."
    Ebisawa T., Fukuchi M., Murakami G., Chiba T., Tanaka K., Imamura T., Miyazono K.
    J. Biol. Chem. 276:12477-12480(2001) [PubMed] [Europe PMC] [Abstract]
• protein localization to cell surface Source: BHF-UCLInferred from direct assayⁱ
  • "Smurf1 regulates the inhibitory activity of Smad7 by targeting Smad7 to the plasma membrane."
    Suzuki C., Murakami G., Fukuchi M., Shimanuki T., Shikauchi Y., Imamura T., Miyazono K.
    J. Biol. Chem. 277:39919-39925(2002) [PubMed] [Europe PMC] [Abstract]
• protein localization to plasma membrane Source: ParkinsonsUK-UCLTraceable author statementⁱ
  • "Image-based genome-wide siRNA screen identifies selective autophagy factors."
    Orvedahl A., Sumpter R. Jr., Xiao G., Ng A., Zou Z., Tang Y., Narimatsu M., Gilpin C., Sun Q., Roth M., Forst C.V., Wrana J.L., Zhang Y.E., Luby-Phelps K., Xavier R.J., Xie Y., Levine B.
    Nature 480:113-117(2011) [PubMed] [Europe PMC] [Abstract]
• protein polyubiquitination Source: UniProtKBInferred from direct assayⁱ
  • Ref.9

    "Ubiquitin ligase Smurf1 targets TRAF family proteins for ubiquitination and degradation."
    Li S., Lu K., Wang J., An L., Yang G., Chen H., Cui Y., Yin X., Xie P., Xing G., He F., Zhang L.
    Mol. Cell. Biochem. 338:11-17(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-725, INTERACTION WITH TRAF4.
• protein targeting to vacuole involved in autophagy Source: ParkinsonsUK-UCLInferred from mutant phenotypeⁱ
  • "Image-based genome-wide siRNA screen identifies selective autophagy factors."
    Orvedahl A., Sumpter R. Jr., Xiao G., Ng A., Zou Z., Tang Y., Narimatsu M., Gilpin C., Sun Q., Roth M., Forst C.V., Wrana J.L., Zhang Y.E., Luby-Phelps K., Xavier R.J., Xie Y., Levine B.
    Nature 480:113-117(2011) [PubMed] [Europe PMC] [Abstract]
• protein ubiquitination Source: BHF-UCLInferred from direct assayⁱ
  • "Smurf1 interacts with transforming growth factor-beta type I receptor through Smad7 and induces receptor degradation."
    Ebisawa T., Fukuchi M., Murakami G., Chiba T., Tanaka K., Imamura T., Miyazono K.
    J. Biol. Chem. 276:12477-12480(2001) [PubMed] [Europe PMC] [Abstract]
• receptor catabolic process Source: BHF-UCLInferred from direct assayⁱ
  • "Smurf1 regulates the inhibitory activity of Smad7 by targeting Smad7 to the plasma membrane."
    Suzuki C., Murakami G., Fukuchi M., Shimanuki T., Shikauchi Y., Imamura T., Miyazono K.
    J. Biol. Chem. 277:39919-39925(2002) [PubMed] [Europe PMC] [Abstract]
• substrate localization to autophagosome Source: ParkinsonsUK-UCLInferred from mutant phenotypeⁱ
  • "Image-based genome-wide siRNA screen identifies selective autophagy factors."
    Orvedahl A., Sumpter R. Jr., Xiao G., Ng A., Zou Z., Tang Y., Narimatsu M., Gilpin C., Sun Q., Roth M., Forst C.V., Wrana J.L., Zhang Y.E., Luby-Phelps K., Xavier R.J., Xie Y., Levine B.
    Nature 480:113-117(2011) [PubMed] [Europe PMC] [Abstract]
• transforming growth factor beta receptor signaling pathway Source: Reactome
• ubiquitin-dependent protein catabolic process Source: UniProtKBInferred from direct assayⁱ
  • Ref.7

    "A SMAD ubiquitin ligase targets the BMP pathway and affects embryonic pattern formation."
    Zhu H., Kavsak P., Abdollah S., Wrana J.L., Thomsen G.H.
    Nature 400:687-693(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-731 (ISOFORM SHORT), FUNCTION.
  • Ref.9

    "Ubiquitin ligase Smurf1 targets TRAF family proteins for ubiquitination and degradation."
    Li S., Lu K., Wang J., An L., Yang G., Chen H., Cui Y., Yin X., Xie P., Xing G., He F., Zhang L.
    Mol. Cell. Biochem. 338:11-17(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-725, INTERACTION WITH TRAF4.
• ubiquitin-dependent SMAD protein catabolic process Source: BHF-UCLInferred from direct assayⁱ
  • "Smurf1 interacts with transforming growth factor-beta type I receptor through Smad7 and induces receptor degradation."
    Ebisawa T., Fukuchi M., Murakami G., Chiba T., Tanaka K., Imamura T., Miyazono K.
    J. Biol. Chem. 276:12477-12480(2001) [PubMed] [Europe PMC] [Abstract]
  • "Smurf1 regulates the inhibitory activity of Smad7 by targeting Smad7 to the plasma membrane."
    Suzuki C., Murakami G., Fukuchi M., Shimanuki T., Shikauchi Y., Imamura T., Miyazono K.
    J. Biol. Chem. 277:39919-39925(2002) [PubMed] [Europe PMC] [Abstract]
• Wnt signaling pathway, planar cell polarity pathway Source: Reactome

<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

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

Organism-specific databases

Miscellaneous databases

Chemistry databases

Polymorphism and mutation databases

<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 provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

Gene expression databases

Organism-specific 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%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• I-SMAD binding Source: BHF-UCLInferred from physical interactionⁱ
  • "Smurf1 interacts with transforming growth factor-beta type I receptor through Smad7 and induces receptor degradation."
    Ebisawa T., Fukuchi M., Murakami G., Chiba T., Tanaka K., Imamura T., Miyazono K.
    J. Biol. Chem. 276:12477-12480(2001) [PubMed] [Europe PMC] [Abstract]
  • "Smurf1 regulates the inhibitory activity of Smad7 by targeting Smad7 to the plasma membrane."
    Suzuki C., Murakami G., Fukuchi M., Shimanuki T., Shikauchi Y., Imamura T., Miyazono K.
    J. Biol. Chem. 277:39919-39925(2002) [PubMed] [Europe PMC] [Abstract]
• R-SMAD binding Source: BHF-UCLInferred from physical interactionⁱ
  • "Smurf1 interacts with transforming growth factor-beta type I receptor through Smad7 and induces receptor degradation."
    Ebisawa T., Fukuchi M., Murakami G., Chiba T., Tanaka K., Imamura T., Miyazono K.
    J. Biol. Chem. 276:12477-12480(2001) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

Chemistry 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

<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>Sequences (2)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.

        10         20         30         40         50
MSNPGTRRNG SSIKIRLTVL CAKNLAKKDF FRLPDPFAKI VVDGSGQCHS 
        60         70         80         90        100
TDTVKNTLDP KWNQHYDLYV GKTDSITISV WNHKKIHKKQ GAGFLGCVRL 
       110        120        130        140        150
LSNAISRLKD TGYQRLDLCK LNPSDTDAVR GQIVVSLQTR DRIGTGGSVV 
       160        170        180        190        200
DCRGLLENEG TVYEDSGPGR PLSCFMEEPA PYTDSTGAAA GGGNCRFVES 
       210        220        230        240        250
PSQDQRLQAQ RLRNPDVRGS LQTPQNRPHG HQSPELPEGY EQRTTVQGQV 
       260        270        280        290        300
YFLHTQTGVS TWHDPRIPSP SGTIPGGDAA FLYEFLLQGH TSEPRDLNSV 
       310        320        330        340        350
NCDELGPLPP GWEVRSTVSG RIYFVDHNNR TTQFTDPRLH HIMNHQCQLK 
       360        370        380        390        400
EPSQPLPLPS EGSLEDEELP AQRYERDLVQ KLKVLRHELS LQQPQAGHCR 
       410        420        430        440        450
IEVSREEIFE ESYRQIMKMR PKDLKKRLMV KFRGEEGLDY GGVAREWLYL 
       460        470        480        490        500
LCHEMLNPYY GLFQYSTDNI YMLQINPDSS INPDHLSYFH FVGRIMGLAV 
       510        520        530        540        550
FHGHYINGGF TVPFYKQLLG KPIQLSDLES VDPELHKSLV WILENDITPV 
       560        570        580        590        600
LDHTFCVEHN AFGRILQHEL KPNGRNVPVT EENKKEYVRL YVNWRFMRGI 
       610        620        630        640        650
EAQFLALQKG FNELIPQHLL KPFDQKELEL IIGGLDKIDL NDWKSNTRLK 
       660        670        680        690        700
HCVADSNIVR WFWQAVETFD EERRARLLQF VTGSTRVPLQ GFKALQGSTG 
       710        720        730        740        750
AAGPRLFTIH LIDANTDNLP KAHTCFNRID IPPYESYEKL YEKLLTAVEE 

TCGFAVE                                                

        10         20         30         40         50
MSNPGTRRNG SSIKIRLTVL CAKNLAKKDF FRLPDPFAKI VVDGSGQCHS 
        60         70         80         90        100
TDTVKNTLDP KWNQHYDLYV GKTDSITISV WNHKKIHKKQ GAGFLGCVRL 
       110        120        130        140        150
LSNAISRLKD TGYQRLDLCK LNPSDTDAVR GQIVVSLQTR DRIGTGGSVV 
       160        170        180        190        200
DCRGLLENEG TVYEDSGPGR PLSCFMEEPA PYTDSTGAAA GGGNCRFVES 
       210        220        230        240        250
PSQDQRLQAQ RLRNPDVRGS LQTPQNRPHG HQSPELPEGY EQRTTVQGQV 
       260        270        280        290        300
YFLHTQTGVS TWHDPRIPRD LNSVNCDELG PLPPGWEVRS TVSGRIYFVD 
       310        320        330        340        350
HNNRTTQFTD PRLHHIMNHQ CQLKEPSQPL PLPSEGSLED EELPAQRYER 
       360        370        380        390        400
DLVQKLKVLR HELSLQQPQA GHCRIEVSRE EIFEESYRQI MKMRPKDLKK 
       410        420        430        440        450
RLMVKFRGEE GLDYGGVARE WLYLLCHEML NPYYGLFQYS TDNIYMLQIN 
       460        470        480        490        500
PDSSINPDHL SYFHFVGRIM GLAVFHGHYI NGGFTVPFYK QLLGKPIQLS 
       510        520        530        540        550
DLESVDPELH KSLVWILEND ITPVLDHTFC VEHNAFGRIL QHELKPNGRN 
       560        570        580        590        600
VPVTEENKKE YVRLYVNWRF MRGIEAQFLA LQKGFNELIP QHLLKPFDQK 
       610        620        630        640        650
ELELIIGGLD KIDLNDWKSN TRLKHCVADS NIVRWFWQAV ETFDEERRAR 
       660        670        680        690        700
LLQFVTGSTR VPLQGFKALQ GSTGAAGPRL FTIHLIDANT DNLPKAHTCF 
       710        720        730 
NRIDIPPYES YEKLYEKLLT AVEETCGFAV E                     

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautionⁱ

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityⁱ

<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

Chemistry databases

PTM databases

Polymorphism and mutation 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. Human chromosome 7
   Human chromosome 7: entries, gene names and cross-references to MIM
2. Human entries with polymorphisms or disease mutations
   List of human entries with polymorphisms or disease mutations
3. Human polymorphisms and disease mutations
   Index of human polymorphisms and disease mutations
4. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
5. PATHWAY comments
   Index of metabolic and biosynthesis pathways
6. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references