P2X purinoceptor 4

<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>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

• ATP binding Source: BHF-UCL <p>Inferred by Curator</p> <p>Used for cases where an annotation is not supported by any evidence but can be reasonably inferred by a curator from other GO annotations for which evidence <br />is available.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ic">GO evidence code guide</a></p> Inferred by curatorⁱ
  • "A novel contractile phenotype with cardiac transgenic expression of the human P2X4 receptor."
    Hu B., Mei Q.B., Yao X.J., Smith E., Barry W.H., Liang B.T.
    FASEB J. 15:2739-2741(2001) [PubMed] [Europe PMC] [Abstract]
• cadherin 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
  • "P2X4 and P2X6 receptors associate with VE-cadherin in human endothelial cells."
    Glass R., Loesch A., Bodin P., Burnstock G.
    Cell. Mol. Life Sci. 59:870-881(2002) [PubMed] [Europe PMC] [Abstract]
• copper ion binding Source: BHF-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
  • "Histidine 140 plays a key role in the inhibitory modulation of the P2X4 nucleotide receptor by copper but not zinc."
    Coddou C., Morales B., Gonzalez J., Grauso M., Gordillo F., Bull P., Rassendren F., Huidobro-Toro J.P.
    J. Biol. Chem. 278:36777-36785(2003) [PubMed] [Europe PMC] [Abstract]
• extracellularly ATP-gated cation channel activity Source: UniProtKB <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.9

    "Site-specific splice variation of the human P2X4 receptor."
    Carpenter D., Meadows H.J., Brough S., Chapman G., Clarke C., Coldwell M., Davis R., Harrison D., Meakin J., McHale M., Rice S.Q., Tomlinson W.J., Wood M., Sanger G.J.
    Neurosci. Lett. 273:183-186(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION.
• ligand-gated calcium channel activity Source: BHF-UCLInferred from direct assayⁱ
  • Ref.1

    "Characterization of recombinant human P2X4 receptor reveals pharmacological differences to the rat homologue."
    Garcia-Guzman M., Soto F., Gomez-Hernandez J.M., Lund P.E., Stuhmer W.
    Mol. Pharmacol. 51:109-118(1997) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-6.
• protein homodimerization activity 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
  • "Go it alone no more--P2X7 joins the society of heteromeric ATP-gated receptor channels."
    Dubyak G.R.
    Mol. Pharmacol. 72:1402-1405(2007) [PubMed] [Europe PMC] [Abstract]
• purinergic nucleotide receptor activity Source: BHF-UCLInferred from direct assayⁱ
  • Ref.1

    "Characterization of recombinant human P2X4 receptor reveals pharmacological differences to the rat homologue."
    Garcia-Guzman M., Soto F., Gomez-Hernandez J.M., Lund P.E., Stuhmer W.
    Mol. Pharmacol. 51:109-118(1997) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-6.
• signaling receptor binding Source: BHF-UCLInferred from sequence or structural similarityⁱ
  • "Evidence for functional P2X4/P2X7 heteromeric receptors."
    Guo C., Masin M., Qureshi O.S., Murrell-Lagnado R.D.
    Mol. Pharmacol. 72:1447-1456(2007) [PubMed] [Europe PMC] [Abstract]
• zinc ion binding Source: BHF-UCLInferred from sequence or structural similarityⁱ
  • "Histidine 140 plays a key role in the inhibitory modulation of the P2X4 nucleotide receptor by copper but not zinc."
    Coddou C., Morales B., Gonzalez J., Grauso M., Gordillo F., Bull P., Rassendren F., Huidobro-Toro J.P.
    J. Biol. Chem. 278:36777-36785(2003) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• apoptotic signaling pathway Source: BHF-UCLInferred from direct assayⁱ
  • "Multiple P2X receptors are involved in the modulation of apoptosis in human mesangial cells: evidence for a role of P2X4."
    Solini A., Santini E., Chimenti D., Chiozzi P., Pratesi F., Cuccato S., Falzoni S., Lupi R., Ferrannini E., Pugliese G., Di Virgilio F.
    Am. J. Physiol. Renal Physiol. 292:F1537-47(2007) [PubMed] [Europe PMC] [Abstract]
• behavioral response to pain Source: ARUK-UCL
• blood coagulation Source: Reactome
• calcium ion transmembrane transport Source: BHF-UCLInferred from direct assayⁱ
  • Ref.1

    "Characterization of recombinant human P2X4 receptor reveals pharmacological differences to the rat homologue."
    Garcia-Guzman M., Soto F., Gomez-Hernandez J.M., Lund P.E., Stuhmer W.
    Mol. Pharmacol. 51:109-118(1997) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-6.
• calcium-mediated signaling Source: ARUK-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
  • "Involvement of P2X4 and P2Y12 receptors in ATP-induced microglial chemotaxis."
    Ohsawa K., Irino Y., Nakamura Y., Akazawa C., Inoue K., Kohsaka S.
    Glia 55:604-616(2007) [PubMed] [Europe PMC] [Abstract]
• cellular response to ATP Source: UniProtKBInferred from direct assayⁱ
  • Ref.9

    "Site-specific splice variation of the human P2X4 receptor."
    Carpenter D., Meadows H.J., Brough S., Chapman G., Clarke C., Coldwell M., Davis R., Harrison D., Meakin J., McHale M., Rice S.Q., Tomlinson W.J., Wood M., Sanger G.J.
    Neurosci. Lett. 273:183-186(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION.
• cellular response to zinc ion Source: UniProtKB
• endothelial cell activation Source: BHF-UCLTraceable author statementⁱ
  • "P2X4 and P2X6 receptors associate with VE-cadherin in human endothelial cells."
    Glass R., Loesch A., Bodin P., Burnstock G.
    Cell. Mol. Life Sci. 59:870-881(2002) [PubMed] [Europe PMC] [Abstract]
• ion transmembrane transport Source: UniProtKBInferred from direct assayⁱ
  • Ref.9

    "Site-specific splice variation of the human P2X4 receptor."
    Carpenter D., Meadows H.J., Brough S., Chapman G., Clarke C., Coldwell M., Davis R., Harrison D., Meakin J., McHale M., Rice S.Q., Tomlinson W.J., Wood M., Sanger G.J.
    Neurosci. Lett. 273:183-186(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION.
• membrane depolarization Source: BHF-UCLInferred from direct assayⁱ
  • Ref.1

    "Characterization of recombinant human P2X4 receptor reveals pharmacological differences to the rat homologue."
    Garcia-Guzman M., Soto F., Gomez-Hernandez J.M., Lund P.E., Stuhmer W.
    Mol. Pharmacol. 51:109-118(1997) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-6.
• microglial cell migration Source: ARUK-UCLTraceable author statementⁱ
  • "Key Aging-Associated Alterations in Primary Microglia Response to Beta-Amyloid Stimulation."
    Caldeira C., Cunha C., Vaz A.R., Falcao A.S., Barateiro A., Seixas E., Fernandes A., Brites D.
    Front Aging Neurosci 9:277-277(2017) [PubMed] [Europe PMC] [Abstract]
• negative regulation of cardiac muscle hypertrophy Source: BHF-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
  • "A beneficial role of cardiac P2X4 receptors in heart failure: rescue of the calsequestrin overexpression model of cardiomyopathy."
    Yang A., Sonin D., Jones L., Barry W.H., Liang B.T.
    Am. J. Physiol. Heart Circ. Physiol. 287:H1096-103(2004) [PubMed] [Europe PMC] [Abstract]
• neuronal action potential Source: Ensembl
• positive regulation of blood vessel endothelial cell migration Source: CAFAInferred from mutant phenotypeⁱ
  • "Regenerative protein thymosin beta-4 is a novel regulator of purinergic signaling."
    Freeman K.W., Bowman B.R., Zetter B.R.
    FASEB J. 25:907-915(2011) [PubMed] [Europe PMC] [Abstract]
• positive regulation of calcium ion transport Source: BHF-UCLNon-traceable author statementⁱ
  • "A beneficial role of cardiac P2X4 receptors in heart failure: rescue of the calsequestrin overexpression model of cardiomyopathy."
    Yang A., Sonin D., Jones L., Barry W.H., Liang B.T.
    Am. J. Physiol. Heart Circ. Physiol. 287:H1096-103(2004) [PubMed] [Europe PMC] [Abstract]
• positive regulation of calcium ion transport into cytosol Source: BHF-UCLInferred from direct assayⁱ
  • "Fluid shear stress activates Ca(2+) influx into human endothelial cells via P2X4 purinoceptors."
    Yamamoto K., Korenaga R., Kamiya A., Ando J.
    Circ. Res. 87:385-391(2000) [PubMed] [Europe PMC] [Abstract]
• positive regulation of calcium-mediated signaling Source: BHF-UCLInferred from direct assayⁱ
  • "Fluid shear stress activates Ca(2+) influx into human endothelial cells via P2X4 purinoceptors."
    Yamamoto K., Korenaga R., Kamiya A., Ando J.
    Circ. Res. 87:385-391(2000) [PubMed] [Europe PMC] [Abstract]
• positive regulation of endothelial cell chemotaxis Source: CAFAInferred from mutant phenotypeⁱ
  • "Regenerative protein thymosin beta-4 is a novel regulator of purinergic signaling."
    Freeman K.W., Bowman B.R., Zetter B.R.
    FASEB J. 25:907-915(2011) [PubMed] [Europe PMC] [Abstract]
• positive regulation of microglial cell migration Source: ARUK-UCL
• positive regulation of nitric oxide biosynthetic process Source: BHF-UCLNon-traceable author statementⁱ
  • "P2X(4) receptors mediate ATP-induced calcium influx in human vascular endothelial cells."
    Yamamoto K., Korenaga R., Kamiya A., Qi Z., Sokabe M., Ando J.
    Am. J. Physiol. Heart Circ. Physiol. 279:H285-92(2000) [PubMed] [Europe PMC] [Abstract]
• positive regulation of prostaglandin secretion Source: BHF-UCLNon-traceable author statementⁱ
  • "P2X(4) receptors mediate ATP-induced calcium influx in human vascular endothelial cells."
    Yamamoto K., Korenaga R., Kamiya A., Qi Z., Sokabe M., Ando J.
    Am. J. Physiol. Heart Circ. Physiol. 279:H285-92(2000) [PubMed] [Europe PMC] [Abstract]
• positive regulation of protein kinase B signaling Source: ARUK-UCL
• protein homooligomerization Source: Ensembl
• purinergic nucleotide receptor signaling pathway Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "A novel contractile phenotype with cardiac transgenic expression of the human P2X4 receptor."
    Hu B., Mei Q.B., Yao X.J., Smith E., Barry W.H., Liang B.T.
    FASEB J. 15:2739-2741(2001) [PubMed] [Europe PMC] [Abstract]
• regulation of blood pressure Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "A novel contractile phenotype with cardiac transgenic expression of the human P2X4 receptor."
    Hu B., Mei Q.B., Yao X.J., Smith E., Barry W.H., Liang B.T.
    FASEB J. 15:2739-2741(2001) [PubMed] [Europe PMC] [Abstract]
  • "A beneficial role of cardiac P2X4 receptors in heart failure: rescue of the calsequestrin overexpression model of cardiomyopathy."
    Yang A., Sonin D., Jones L., Barry W.H., Liang B.T.
    Am. J. Physiol. Heart Circ. Physiol. 287:H1096-103(2004) [PubMed] [Europe PMC] [Abstract]
• regulation of cardiac muscle contraction Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "A novel contractile phenotype with cardiac transgenic expression of the human P2X4 receptor."
    Hu B., Mei Q.B., Yao X.J., Smith E., Barry W.H., Liang B.T.
    FASEB J. 15:2739-2741(2001) [PubMed] [Europe PMC] [Abstract]
  • "A beneficial role of cardiac P2X4 receptors in heart failure: rescue of the calsequestrin overexpression model of cardiomyopathy."
    Yang A., Sonin D., Jones L., Barry W.H., Liang B.T.
    Am. J. Physiol. Heart Circ. Physiol. 287:H1096-103(2004) [PubMed] [Europe PMC] [Abstract]
• regulation of chemotaxis Source: ARUK-UCL
• regulation of sodium ion transport Source: BHF-UCLInferred from sequence or structural similarityⁱ
  • "Evidence for functional P2X4/P2X7 heteromeric receptors."
    Guo C., Masin M., Qureshi O.S., Murrell-Lagnado R.D.
    Mol. Pharmacol. 72:1447-1456(2007) [PubMed] [Europe PMC] [Abstract]
• relaxation of cardiac muscle Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "A novel contractile phenotype with cardiac transgenic expression of the human P2X4 receptor."
    Hu B., Mei Q.B., Yao X.J., Smith E., Barry W.H., Liang B.T.
    FASEB J. 15:2739-2741(2001) [PubMed] [Europe PMC] [Abstract]
  • "A beneficial role of cardiac P2X4 receptors in heart failure: rescue of the calsequestrin overexpression model of cardiomyopathy."
    Yang A., Sonin D., Jones L., Barry W.H., Liang B.T.
    Am. J. Physiol. Heart Circ. Physiol. 287:H1096-103(2004) [PubMed] [Europe PMC] [Abstract]
• response to ATP Source: BHF-UCLInferred from direct assayⁱ
  • Ref.1

    "Characterization of recombinant human P2X4 receptor reveals pharmacological differences to the rat homologue."
    Garcia-Guzman M., Soto F., Gomez-Hernandez J.M., Lund P.E., Stuhmer W.
    Mol. Pharmacol. 51:109-118(1997) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-6.
• response to axon injury Source: ARUK-UCL
• response to fluid shear stress Source: BHF-UCLInferred from direct assayⁱ
  • "Fluid shear stress activates Ca(2+) influx into human endothelial cells via P2X4 purinoceptors."
    Yamamoto K., Korenaga R., Kamiya A., Ando J.
    Circ. Res. 87:385-391(2000) [PubMed] [Europe PMC] [Abstract]
• response to ischemia Source: ARUK-UCL
• sensory perception of pain Source: ARUK-UCL
• sensory perception of touch Source: ARUK-UCL
• signal transduction Source: BHF-UCLInferred from direct assayⁱ
  • Ref.1

    "Characterization of recombinant human P2X4 receptor reveals pharmacological differences to the rat homologue."
    Garcia-Guzman M., Soto F., Gomez-Hernandez J.M., Lund P.E., Stuhmer W.
    Mol. Pharmacol. 51:109-118(1997) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-6.
• tissue homeostasis Source: BHF-UCLNon-traceable author statementⁱ
  • "Multiple P2X receptors are involved in the modulation of apoptosis in human mesangial cells: evidence for a role of P2X4."
    Solini A., Santini E., Chimenti D., Chiozzi P., Pratesi F., Cuccato S., Falzoni S., Lupi R., Ferrannini E., Pugliese G., Di Virgilio F.
    Am. J. Physiol. Renal Physiol. 292:F1537-47(2007) [PubMed] [Europe PMC] [Abstract]

<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

Protein family/group 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

Topology

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

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

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

• cadherin binding Source: BHF-UCLInferred from physical interactionⁱ
  • "P2X4 and P2X6 receptors associate with VE-cadherin in human endothelial cells."
    Glass R., Loesch A., Bodin P., Burnstock G.
    Cell. Mol. Life Sci. 59:870-881(2002) [PubMed] [Europe PMC] [Abstract]
• protein homodimerization activity Source: BHF-UCLNon-traceable author statementⁱ
  • "Go it alone no more--P2X7 joins the society of heteromeric ATP-gated receptor channels."
    Dubyak G.R.
    Mol. Pharmacol. 72:1402-1405(2007) [PubMed] [Europe PMC] [Abstract]
• signaling receptor binding Source: BHF-UCLInferred from sequence or structural similarityⁱ
  • "Evidence for functional P2X4/P2X7 heteromeric receptors."
    Guo C., Masin M., Qureshi O.S., Murrell-Lagnado R.D.
    Mol. Pharmacol. 72:1447-1456(2007) [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

3D structure 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

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

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 (3+)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 3 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MAGCCAALAA FLFEYDTPRI VLIRSRKVGL MNRAVQLLIL AYVIGWVFVW 
        60         70         80         90        100
EKGYQETDSV VSSVTTKVKG VAVTNTSKLG FRIWDVADYV IPAQEENSLF 
       110        120        130        140        150
VMTNVILTMN QTQGLCPEIP DATTVCKSDA SCTAGSAGTH SNGVSTGRCV 
       160        170        180        190        200
AFNGSVKTCE VAAWCPVEDD THVPQPAFLK AAENFTLLVK NNIWYPKFNF 
       210        220        230        240        250
SKRNILPNIT TTYLKSCIYD AKTDPFCPIF RLGKIVENAG HSFQDMAVEG 
       260        270        280        290        300
GIMGIQVNWD CNLDRAASLC LPRYSFRRLD TRDVEHNVSP GYNFRFAKYY 
       310        320        330        340        350
RDLAGNEQRT LIKAYGIRFD IIVFGKAGKF DIIPTMINIG SGLALLGMAT 
       360        370        380 
VLCDIIVLYC MKKRLYYREK KYKYVEDYEQ GLASELDQ              

        10         20         30         40         50
MAGCCAALAA FLFEYDTPRI VLIRSRKVGL MNRAVQLLIL AYVIGCYHPH 
        60         70         80         90        100
LAEVEMESPR RWVFVWEKGY QETDSVVSSV TTKVKGVAVT NTSKLGFRIW 
       110        120        130        140        150
DVADYVIPAQ EENSLFVMTN VILTMNQTQG LCPEIPDATT VCKSDASCTA 
       160        170        180        190        200
GSAGTHSNGV STGRCVAFNG SVKTCEVAAW CPVEDDTHVP QPAFLKAAEN 
       210        220        230        240        250
FTLLVKNNIW YPKFNFSKRN ILPNITTTYL KSCIYDAKTD PFCPIFRLGK 
       260        270        280        290        300
IVENAGHSFQ DMAVEGGIMG IQVNWDCNLD RAASLCLPRY SFRRLDTRDV 
       310        320        330        340        350
EHNVSPGYNF RFAKYYRDLA GNEQRTLIKA YGIRFDIIVF GKAGKFDIIP 
       360        370        380        390        400
TMINIGSGLA LLGMATVLCD IIVLYCMKKR LYYREKKYKY VEDYEQGLAS 

ELDQ                                                   

        10         20         30         40         50
MAGCCAALAA FLFEYDTPRI VLIRSRKVGL MNRAVQLLIL AYVIGWVFVW 
        60         70         80         90        100
EKGYQETDSV VSSVTTKVKG VAVTNTSKLG FRIWDVADYV IPAQEENSLF 
       110        120        130        140        150
VMTNVILTMN QTQGLCPEIP DATTVCKSDA SCTAGSAGTH SNGVSTGRPA 
       160        170        180        190        200
FLKAAENFTL LVKNNIWYPK FNFSKRNILP NITTTYLKSC IYDAKTDPFC 
       210        220        230        240        250
PIFRLGKIVE NAGHSFQDMA VEGGIMGIQV NWDCNLDRAA SLCLPRYSFR 
       260        270        280        290        300
RLDTRDVEHN VSPGYNFRFA KYYRDLAGNE QRTLIKAYGI RFDIIVFGKA 
       310        320        330        340        350
GKFDIIPTMI NIGSGLALLG MATVLCDIIV LYCMKKRLYY REKKYKYVED 
       360 
YEQGLASELD Q                                           

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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group 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 12
   Human chromosome 12: 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. SIMILARITY comments
   Index of protein domains and families
4. Human polymorphisms and disease mutations
   Index of human polymorphisms and disease mutations
5. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot