Junctional adhesion molecule A

<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

• cadherin binding Source: BHF-UCLInferred from high throughput direct assayⁱ
  • "E-cadherin interactome complexity and robustness resolved by quantitative proteomics."
    Guo Z., Neilson L.J., Zhong H., Murray P.S., Zanivan S., Zaidel-Bar R.
    Sci Signal 7:rs7-rs7(2014) [PubMed] [Europe PMC] [Abstract]
• integrin binding Source: ARUK-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%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • Ref.14

    "JAM-1 is a ligand of the beta(2) integrin LFA-1 involved in transendothelial migration of leukocytes."
    Ostermann G., Weber K.S., Zernecke A., Schroeder A., Weber C.
    Nat. Immunol. 3:151-158(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN.
  • "Signaling pathways of the F11 receptor (F11R; a.k.a. JAM-1, JAM-A) in human platelets: F11R dimerization, phosphorylation and complex formation with the integrin GPIIIa."
    Sobocka M.B., Sobocki T., Babinska A., Hartwig J.H., Li M., Ehrlich Y.H., Kornecki E.
    J Recept Signal Transduct Res 24:85-105(2004) [PubMed] [Europe PMC] [Abstract]
• PDZ domain binding Source: UniProtKBInferred from physical interactionⁱ
  • "JAM-A associates with ZO-2, afadin, and PDZ-GEF1 to activate Rap2c and regulate epithelial barrier function."
    Monteiro A.C., Sumagin R., Rankin C.R., Leoni G., Mina M.J., Reiter D.M., Stehle T., Dermody T.S., Schaefer S.A., Hall R.A., Nusrat A., Parkos C.A.
    Mol Biol Cell 24:2849-2860(2013) [PubMed] [Europe PMC] [Abstract]
• protein homodimerization activity Source: ARUK-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%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Involvement of the junctional adhesion molecule-1 (JAM1) homodimer interface in regulation of epithelial barrier function."
    Mandell K.J., McCall I.C., Parkos C.A.
    J Biol Chem 279:16254-16262(2004) [PubMed] [Europe PMC] [Abstract]
  • "Signaling pathways of the F11 receptor (F11R; a.k.a. JAM-1, JAM-A) in human platelets: F11R dimerization, phosphorylation and complex formation with the integrin GPIIIa."
    Sobocka M.B., Sobocki T., Babinska A., Hartwig J.H., Li M., Ehrlich Y.H., Kornecki E.
    J Recept Signal Transduct Res 24:85-105(2004) [PubMed] [Europe PMC] [Abstract]
• virus receptor activity Source: UniProtKB-KW

GO - Biological processⁱ

• actomyosin structure organization 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%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "JAM-A associates with ZO-2, afadin, and PDZ-GEF1 to activate Rap2c and regulate epithelial barrier function."
    Monteiro A.C., Sumagin R., Rankin C.R., Leoni G., Mina M.J., Reiter D.M., Stehle T., Dermody T.S., Schaefer S.A., Hall R.A., Nusrat A., Parkos C.A.
    Mol Biol Cell 24:2849-2860(2013) [PubMed] [Europe PMC] [Abstract]
• bicellular tight junction assembly Source: Reactome
• cell-cell adhesion Source: ARUK-UCLInferred from direct assayⁱ
  • "Involvement of the junctional adhesion molecule-1 (JAM1) homodimer interface in regulation of epithelial barrier function."
    Mandell K.J., McCall I.C., Parkos C.A.
    J Biol Chem 279:16254-16262(2004) [PubMed] [Europe PMC] [Abstract]
• cellular response to mechanical stimulus Source: ARUK-UCLInferred from direct assayⁱ
  • "Tension on JAM-A activates RhoA via GEF-H1 and p115 RhoGEF."
    Scott D.W., Tolbert C.E., Burridge K.
    Mol Biol Cell 27:1420-1430(2016) [PubMed] [Europe PMC] [Abstract]
• establishment of endothelial intestinal barrier Source: UniProtKBInferred from mutant phenotypeⁱ
  • "JAM-A associates with ZO-2, afadin, and PDZ-GEF1 to activate Rap2c and regulate epithelial barrier function."
    Monteiro A.C., Sumagin R., Rankin C.R., Leoni G., Mina M.J., Reiter D.M., Stehle T., Dermody T.S., Schaefer S.A., Hall R.A., Nusrat A., Parkos C.A.
    Mol Biol Cell 24:2849-2860(2013) [PubMed] [Europe PMC] [Abstract]
• extracellular matrix organization Source: Reactome
• inflammatory response Source: ProtInc <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%2Dgo%2Devidence%2Dcodes#tas">GO evidence code guide</a></p> Traceable author statementⁱ
  • Ref.1

    "Combined treatment of TNF-alpha and IFN-gamma causes redistribution of junctional adhesion molecule in human endothelial cells."
    Ozaki H., Ishii K., Horiuchi H., Arai H., Kawamoto T., Okawa K., Iwamatsu A., Kita T.
    J. Immunol. 163:553-557(1999) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
• intestinal absorption Source: UniProtKBInferred from mutant phenotypeⁱ
  • "JAM-A associates with ZO-2, afadin, and PDZ-GEF1 to activate Rap2c and regulate epithelial barrier function."
    Monteiro A.C., Sumagin R., Rankin C.R., Leoni G., Mina M.J., Reiter D.M., Stehle T., Dermody T.S., Schaefer S.A., Hall R.A., Nusrat A., Parkos C.A.
    Mol Biol Cell 24:2849-2860(2013) [PubMed] [Europe PMC] [Abstract]
• leukocyte cell-cell adhesion Source: ARUK-UCLInferred from mutant phenotypeⁱ
  • Ref.14

    "JAM-1 is a ligand of the beta(2) integrin LFA-1 involved in transendothelial migration of leukocytes."
    Ostermann G., Weber K.S., Zernecke A., Schroeder A., Weber C.
    Nat. Immunol. 3:151-158(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN.
• leukocyte migration Source: Reactome
• maintenance of blood-brain barrier Source: ARUK-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%2Dgo%2Devidence%2Dcodes#nas">GO evidence code guide</a></p> Non-traceable author statementⁱ
  • "Blood-Brain Barrier: From Physiology to Disease and Back."
    Sweeney M.D., Zhao Z., Montagne A., Nelson A.R., Zlokovic B.V.
    Physiol Rev 99:21-78(2019) [PubMed] [Europe PMC] [Abstract]
• memory T cell extravasation Source: ARUK-UCLInferred from direct assayⁱ
  • Ref.14

    "JAM-1 is a ligand of the beta(2) integrin LFA-1 involved in transendothelial migration of leukocytes."
    Ostermann G., Weber K.S., Zernecke A., Schroeder A., Weber C.
    Nat. Immunol. 3:151-158(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN.
• negative regulation of GTPase activity Source: UniProtKBInferred from mutant phenotypeⁱ
  • "JAM-A associates with ZO-2, afadin, and PDZ-GEF1 to activate Rap2c and regulate epithelial barrier function."
    Monteiro A.C., Sumagin R., Rankin C.R., Leoni G., Mina M.J., Reiter D.M., Stehle T., Dermody T.S., Schaefer S.A., Hall R.A., Nusrat A., Parkos C.A.
    Mol Biol Cell 24:2849-2860(2013) [PubMed] [Europe PMC] [Abstract]
• negative regulation of stress fiber assembly Source: ARUK-UCLInferred from mutant phenotypeⁱ
  • "ZO-1 controls endothelial adherens junctions, cell-cell tension, angiogenesis, and barrier formation."
    Tornavaca O., Chia M., Dufton N., Almagro L.O., Conway D.E., Randi A.M., Schwartz M.A., Matter K., Balda M.S.
    J Cell Biol 208:821-838(2015) [PubMed] [Europe PMC] [Abstract]
• positive regulation of blood pressure Source: Ensembl
• positive regulation of establishment of endothelial barrier Source: ARUK-UCLInferred from mutant phenotypeⁱ
  • "Tension on JAM-A activates RhoA via GEF-H1 and p115 RhoGEF."
    Scott D.W., Tolbert C.E., Burridge K.
    Mol Biol Cell 27:1420-1430(2016) [PubMed] [Europe PMC] [Abstract]
• positive regulation of GTPase activity Source: UniProtKBInferred from mutant phenotypeⁱ
  • "JAM-A associates with ZO-2, afadin, and PDZ-GEF1 to activate Rap2c and regulate epithelial barrier function."
    Monteiro A.C., Sumagin R., Rankin C.R., Leoni G., Mina M.J., Reiter D.M., Stehle T., Dermody T.S., Schaefer S.A., Hall R.A., Nusrat A., Parkos C.A.
    Mol Biol Cell 24:2849-2860(2013) [PubMed] [Europe PMC] [Abstract]
• positive regulation of platelet aggregation Source: ARUK-UCLInferred from direct assayⁱ
  • "Signaling pathways of the F11 receptor (F11R; a.k.a. JAM-1, JAM-A) in human platelets: F11R dimerization, phosphorylation and complex formation with the integrin GPIIIa."
    Sobocka M.B., Sobocki T., Babinska A., Hartwig J.H., Li M., Ehrlich Y.H., Kornecki E.
    J Recept Signal Transduct Res 24:85-105(2004) [PubMed] [Europe PMC] [Abstract]
• positive regulation of Rho protein signal transduction Source: ARUK-UCLInferred from direct assayⁱ
  • "Tension on JAM-A activates RhoA via GEF-H1 and p115 RhoGEF."
    Scott D.W., Tolbert C.E., Burridge K.
    Mol Biol Cell 27:1420-1430(2016) [PubMed] [Europe PMC] [Abstract]
• protein localization to bicellular tight junction Source: ARUK-UCLInferred from mutant phenotypeⁱ
  • "ZO-1 controls endothelial adherens junctions, cell-cell tension, angiogenesis, and barrier formation."
    Tornavaca O., Chia M., Dufton N., Almagro L.O., Conway D.E., Randi A.M., Schwartz M.A., Matter K., Balda M.S.
    J Cell Biol 208:821-838(2015) [PubMed] [Europe PMC] [Abstract]
• protein localization to plasma membrane Source: UniProtKBInferred from mutant phenotypeⁱ
  • "JAM-A associates with ZO-2, afadin, and PDZ-GEF1 to activate Rap2c and regulate epithelial barrier function."
    Monteiro A.C., Sumagin R., Rankin C.R., Leoni G., Mina M.J., Reiter D.M., Stehle T., Dermody T.S., Schaefer S.A., Hall R.A., Nusrat A., Parkos C.A.
    Mol Biol Cell 24:2849-2860(2013) [PubMed] [Europe PMC] [Abstract]
• regulation of actin cytoskeleton organization Source: ARUK-UCLInferred from direct assayⁱ
  • "Signaling pathways of the F11 receptor (F11R; a.k.a. JAM-1, JAM-A) in human platelets: F11R dimerization, phosphorylation and complex formation with the integrin GPIIIa."
    Sobocka M.B., Sobocki T., Babinska A., Hartwig J.H., Li M., Ehrlich Y.H., Kornecki E.
    J Recept Signal Transduct Res 24:85-105(2004) [PubMed] [Europe PMC] [Abstract]
• regulation of actin cytoskeleton reorganization Source: UniProtKBInferred from mutant phenotypeⁱ
  • "JAM-A associates with ZO-2, afadin, and PDZ-GEF1 to activate Rap2c and regulate epithelial barrier function."
    Monteiro A.C., Sumagin R., Rankin C.R., Leoni G., Mina M.J., Reiter D.M., Stehle T., Dermody T.S., Schaefer S.A., Hall R.A., Nusrat A., Parkos C.A.
    Mol Biol Cell 24:2849-2860(2013) [PubMed] [Europe PMC] [Abstract]
• regulation of bicellular tight junction assembly Source: ARUK-UCLInferred from mutant phenotypeⁱ
  • "ZO-1 controls endothelial adherens junctions, cell-cell tension, angiogenesis, and barrier formation."
    Tornavaca O., Chia M., Dufton N., Almagro L.O., Conway D.E., Randi A.M., Schwartz M.A., Matter K., Balda M.S.
    J Cell Biol 208:821-838(2015) [PubMed] [Europe PMC] [Abstract]
• regulation of cell shape Source: ARUK-UCLInferred from direct assayⁱ
  • "Signaling pathways of the F11 receptor (F11R; a.k.a. JAM-1, JAM-A) in human platelets: F11R dimerization, phosphorylation and complex formation with the integrin GPIIIa."
    Sobocka M.B., Sobocki T., Babinska A., Hartwig J.H., Li M., Ehrlich Y.H., Kornecki E.
    J Recept Signal Transduct Res 24:85-105(2004) [PubMed] [Europe PMC] [Abstract]
• regulation of cytokine production Source: Ensembl
• regulation of cytoskeleton organization Source: ARUK-UCLInferred from mutant phenotypeⁱ
  • "ZO-1 controls endothelial adherens junctions, cell-cell tension, angiogenesis, and barrier formation."
    Tornavaca O., Chia M., Dufton N., Almagro L.O., Conway D.E., Randi A.M., Schwartz M.A., Matter K., Balda M.S.
    J Cell Biol 208:821-838(2015) [PubMed] [Europe PMC] [Abstract]
• regulation of membrane permeability Source: UniProtKBInferred from mutant phenotypeⁱ
  • "JAM-A associates with ZO-2, afadin, and PDZ-GEF1 to activate Rap2c and regulate epithelial barrier function."
    Monteiro A.C., Sumagin R., Rankin C.R., Leoni G., Mina M.J., Reiter D.M., Stehle T., Dermody T.S., Schaefer S.A., Hall R.A., Nusrat A., Parkos C.A.
    Mol Biol Cell 24:2849-2860(2013) [PubMed] [Europe PMC] [Abstract]
• response to radiation Source: Ensembl
• transforming growth factor beta receptor signaling 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

• UniProt annotation
• GO - Cellular component

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

Organism-specific databases

Miscellaneous databases

Genetic variation 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%5Fprocessing%5Fsection">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%5Fsection">'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%5Fsection">'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%5Fsection">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

• cadherin binding Source: BHF-UCLInferred from high throughput direct assayⁱ
  • "E-cadherin interactome complexity and robustness resolved by quantitative proteomics."
    Guo Z., Neilson L.J., Zhong H., Murray P.S., Zanivan S., Zaidel-Bar R.
    Sci Signal 7:rs7-rs7(2014) [PubMed] [Europe PMC] [Abstract]
• integrin binding Source: ARUK-UCLInferred from physical interactionⁱ
  • Ref.14

    "JAM-1 is a ligand of the beta(2) integrin LFA-1 involved in transendothelial migration of leukocytes."
    Ostermann G., Weber K.S., Zernecke A., Schroeder A., Weber C.
    Nat. Immunol. 3:151-158(2002) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN.
  • "Signaling pathways of the F11 receptor (F11R; a.k.a. JAM-1, JAM-A) in human platelets: F11R dimerization, phosphorylation and complex formation with the integrin GPIIIa."
    Sobocka M.B., Sobocki T., Babinska A., Hartwig J.H., Li M., Ehrlich Y.H., Kornecki E.
    J Recept Signal Transduct Res 24:85-105(2004) [PubMed] [Europe PMC] [Abstract]
• PDZ domain binding Source: UniProtKBInferred from physical interactionⁱ
  • "JAM-A associates with ZO-2, afadin, and PDZ-GEF1 to activate Rap2c and regulate epithelial barrier function."
    Monteiro A.C., Sumagin R., Rankin C.R., Leoni G., Mina M.J., Reiter D.M., Stehle T., Dermody T.S., Schaefer S.A., Hall R.A., Nusrat A., Parkos C.A.
    Mol Biol Cell 24:2849-2860(2013) [PubMed] [Europe PMC] [Abstract]
• protein homodimerization activity Source: ARUK-UCLInferred from direct assayⁱ
  • "Involvement of the junctional adhesion molecule-1 (JAM1) homodimer interface in regulation of epithelial barrier function."
    Mandell K.J., McCall I.C., Parkos C.A.
    J Biol Chem 279:16254-16262(2004) [PubMed] [Europe PMC] [Abstract]
  • "Signaling pathways of the F11 receptor (F11R; a.k.a. JAM-1, JAM-A) in human platelets: F11R dimerization, phosphorylation and complex formation with the integrin GPIIIa."
    Sobocka M.B., Sobocki T., Babinska A., Hartwig J.H., Li M., Ehrlich Y.H., Kornecki E.
    J Recept Signal Transduct Res 24:85-105(2004) [PubMed] [Europe PMC] [Abstract]

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

<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

<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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingⁱ: The displayed sequence is further processed into a mature form.

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

        10         20         30         40         50
MGTKAQVERK LLCLFILAIL LCSLALGSVT VHSSEPEVRI PENNPVKLSC 
        60         70         80         90        100
AYSGFSSPRV EWKFDQGDTT RLVCYNNKIT ASYEDRVTFL PTGITFKSVT 
       110        120        130        140        150
REDTGTYTCM VSEEGGNSYG EVKVKLIVLV PPSKPTVNIP SSATIGNRAV 
       160        170        180        190        200
LTCSEQDGSP PSEYTWFKDG IVMPTNPKST RAFSNSSYVL NPTTGELVFD 
       210        220        230        240        250
PLSASDTGEY SCEARNGYGT PMTSNAVRME AVERNVGVIV AAVLVTLILL 
       260        270        280        290 
GILVFGIWFA YSRGHFDRTK KGTSSKKVIY SQPSARSEGE FKQTSSFLV  

        10         20         30         40         50
MGTKAQVERK LLCLFILAIL LCSLALGSVT VHSSEPEVRI PENNPVKLSC 
        60         70         80         90        100
AYSGFSSPRV EWKFDQGDTT RLVCYNNKIT VPPSKPTVNI PSSATIGNRA 
       110        120        130        140        150
VLTCSEQDGS PPSEYTWFKD GIVMPTNPKS TRAFSNSSYV LNPTTGELVF 
       160        170        180        190        200
DPLSASDTGE YSCEARNGYG TPMTSNAVRM EAVERNVGVI VAAVLVTLIL 
       210        220        230        240        250
LGILVFGIWF AYSRGHFDRT KKGTSSKKVI YSQPSARSEG EFKQTSSFLV 

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

PTM databases

Genetic variation 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 cell differentiation molecules
   CD nomenclature of surface proteins of human leucocytes and list of entries
2. Human chromosome 1
   Human chromosome 1: entries, gene names and cross-references to MIM
3. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
4. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
5. SIMILARITY comments
   Index of protein domains and families