Guanylate-binding protein 1

<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%5Fsection">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

• GTP

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  + H₂O

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  • See the description of this molecule in ChEBI.

  = GDP

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  • See the description of this molecule in ChEBI.

  + H⁺

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  • See the description of this molecule in ChEBI.

  + phosphate

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  • See the description of this molecule in ChEBI.

  2 Publications

  Manual assertion based on experiment inⁱ

  • Ref.14

    "Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins."
    Prakash B., Praefcke G.J.K., Renault L., Wittinghofer A., Herrmann C.
    Nature 403:567-571(2000) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
  • Ref.16

    "How guanylate-binding proteins achieve assembly-stimulated processive cleavage of GTP to GMP."
    Ghosh A., Praefcke G.J., Renault L., Wittinghofer A., Herrmann C.
    Nature 440:101-104(2006) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS) OF 1-317, SUBUNIT.
  Source: Rhea

  • Search for this reaction in UniProtKB.
  • See the description of this reaction in Rhea.

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  GTP

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  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  

  +

  H₂O

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  

  =

  GDP

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  

  +

  H⁺

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  

  +

  phosphate

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  zoom

Regions

<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

• actin binding 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%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Guanylate binding protein 1-mediated interaction of T cell antigen receptor signaling with the cytoskeleton."
    Forster F., Paster W., Supper V., Schatzlmaier P., Sunzenauer S., Ostler N., Saliba A., Eckerstorfer P., Britzen-Laurent N., Schutz G., Schmid J.A., Zlabinger G.J., Naschberger E., Sturzl M., Stockinger H.
    J Immunol 192:771-781(2014) [PubMed] [Europe PMC] [Abstract]
• cytokine 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%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • "Guanylate binding protein 1-mediated interaction of T cell antigen receptor signaling with the cytoskeleton."
    Forster F., Paster W., Supper V., Schatzlmaier P., Sunzenauer S., Ostler N., Saliba A., Eckerstorfer P., Britzen-Laurent N., Schutz G., Schmid J.A., Zlabinger G.J., Naschberger E., Sturzl M., Stockinger H.
    J Immunol 192:771-781(2014) [PubMed] [Europe PMC] [Abstract]
• enzyme binding Source: UniProtKBInferred from physical interactionⁱ
  • "Guanylate binding protein 1-mediated interaction of T cell antigen receptor signaling with the cytoskeleton."
    Forster F., Paster W., Supper V., Schatzlmaier P., Sunzenauer S., Ostler N., Saliba A., Eckerstorfer P., Britzen-Laurent N., Schutz G., Schmid J.A., Zlabinger G.J., Naschberger E., Sturzl M., Stockinger H.
    J Immunol 192:771-781(2014) [PubMed] [Europe PMC] [Abstract]
• GDP binding Source: CAFAInferred from direct assayⁱ
  • Ref.14

    "Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins."
    Prakash B., Praefcke G.J.K., Renault L., Wittinghofer A., Herrmann C.
    Nature 403:567-571(2000) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
• GTPase activity Source: CAFAInferred from direct assayⁱ
  • Ref.14

    "Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins."
    Prakash B., Praefcke G.J.K., Renault L., Wittinghofer A., Herrmann C.
    Nature 403:567-571(2000) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
• GTP binding Source: CAFAInferred from direct assayⁱ
  • Ref.14

    "Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins."
    Prakash B., Praefcke G.J.K., Renault L., Wittinghofer A., Herrmann C.
    Nature 403:567-571(2000) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
• Hsp90 protein binding Source: UniProtKBInferred from physical interactionⁱ
  • "Guanylate binding protein 1-mediated interaction of T cell antigen receptor signaling with the cytoskeleton."
    Forster F., Paster W., Supper V., Schatzlmaier P., Sunzenauer S., Ostler N., Saliba A., Eckerstorfer P., Britzen-Laurent N., Schutz G., Schmid J.A., Zlabinger G.J., Naschberger E., Sturzl M., Stockinger H.
    J Immunol 192:771-781(2014) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: IntActInferred from physical interactionⁱ
  • Ref.16

    "How guanylate-binding proteins achieve assembly-stimulated processive cleavage of GTP to GMP."
    Ghosh A., Praefcke G.J., Renault L., Wittinghofer A., Herrmann C.
    Nature 440:101-104(2006) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS) OF 1-317, SUBUNIT.
  • "The guanine cap of human guanylate-binding protein 1 is responsible for dimerization and self-activation of GTP hydrolysis."
    Wehner M., Kunzelmann S., Herrmann C.
    FEBS J 279:203-210(2012) [PubMed] [Europe PMC] [Abstract]
  • "Tetramerization of human guanylate-binding protein 1 is mediated by coiled-coil formation of the C-terminal alpha-helices."
    Syguda A., Bauer M., Benscheid U., Ostler N., Naschberger E., Ince S., Sturzl M., Herrmann C.
    FEBS J 279:2544-2554(2012) [PubMed] [Europe PMC] [Abstract]
• protein homodimerization activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.12

    "Intracellular trafficking of guanylate-binding proteins is regulated by heterodimerization in a hierarchical manner."
    Britzen-Laurent N., Bauer M., Berton V., Fischer N., Syguda A., Reipschlager S., Naschberger E., Herrmann C., Sturzl M.
    PLoS ONE 5:E14246-E14246(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBCELLULAR LOCATION, DIMERIZATION, ISOPRENYLATION, MUTAGENESIS OF LYS-51; 227-ARG-LYS-228 AND 589-CYS--SER-592.
• spectrin binding Source: UniProtKBInferred from physical interactionⁱ
  • "Guanylate binding protein 1-mediated interaction of T cell antigen receptor signaling with the cytoskeleton."
    Forster F., Paster W., Supper V., Schatzlmaier P., Sunzenauer S., Ostler N., Saliba A., Eckerstorfer P., Britzen-Laurent N., Schutz G., Schmid J.A., Zlabinger G.J., Naschberger E., Sturzl M., Stockinger H.
    J Immunol 192:771-781(2014) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• cellular response to interferon-gamma Source: UniProtKBInferred from direct assayⁱ
  • Ref.10

    "Unique features of different members of the human guanylate-binding protein family."
    Tripal P., Bauer M., Naschberger E., Mortinger T., Hohenadl C., Cornali E., Thurau M., Sturzl M.
    J. Interferon Cytokine Res. 27:44-52(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBCELLULAR LOCATION, INDUCTION.
  • Ref.12

    "Intracellular trafficking of guanylate-binding proteins is regulated by heterodimerization in a hierarchical manner."
    Britzen-Laurent N., Bauer M., Berton V., Fischer N., Syguda A., Reipschlager S., Naschberger E., Herrmann C., Sturzl M.
    PLoS ONE 5:E14246-E14246(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBCELLULAR LOCATION, DIMERIZATION, ISOPRENYLATION, MUTAGENESIS OF LYS-51; 227-ARG-LYS-228 AND 589-CYS--SER-592.
• cellular response to interleukin-1 Source: UniProtKB <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ
  • Ref.10

    "Unique features of different members of the human guanylate-binding protein family."
    Tripal P., Bauer M., Naschberger E., Mortinger T., Hohenadl C., Cornali E., Thurau M., Sturzl M.
    J. Interferon Cytokine Res. 27:44-52(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBCELLULAR LOCATION, INDUCTION.
• cellular response to tumor necrosis factor Source: UniProtKBInferred from expression patternⁱ
  • Ref.10

    "Unique features of different members of the human guanylate-binding protein family."
    Tripal P., Bauer M., Naschberger E., Mortinger T., Hohenadl C., Cornali E., Thurau M., Sturzl M.
    J. Interferon Cytokine Res. 27:44-52(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBCELLULAR LOCATION, INDUCTION.
• defense response to virus Source: UniProtKB-KW
• interferon-gamma-mediated signaling pathway Source: Reactome
• negative regulation of ERK1 and ERK2 cascade 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
  • "Guanylate binding protein 1-mediated interaction of T cell antigen receptor signaling with the cytoskeleton."
    Forster F., Paster W., Supper V., Schatzlmaier P., Sunzenauer S., Ostler N., Saliba A., Eckerstorfer P., Britzen-Laurent N., Schutz G., Schmid J.A., Zlabinger G.J., Naschberger E., Sturzl M., Stockinger H.
    J Immunol 192:771-781(2014) [PubMed] [Europe PMC] [Abstract]
• negative regulation of interleukin-2 production Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Guanylate binding protein 1-mediated interaction of T cell antigen receptor signaling with the cytoskeleton."
    Forster F., Paster W., Supper V., Schatzlmaier P., Sunzenauer S., Ostler N., Saliba A., Eckerstorfer P., Britzen-Laurent N., Schutz G., Schmid J.A., Zlabinger G.J., Naschberger E., Sturzl M., Stockinger H.
    J Immunol 192:771-781(2014) [PubMed] [Europe PMC] [Abstract]
• negative regulation of protein localization to plasma membrane Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Guanylate binding protein 1-mediated interaction of T cell antigen receptor signaling with the cytoskeleton."
    Forster F., Paster W., Supper V., Schatzlmaier P., Sunzenauer S., Ostler N., Saliba A., Eckerstorfer P., Britzen-Laurent N., Schutz G., Schmid J.A., Zlabinger G.J., Naschberger E., Sturzl M., Stockinger H.
    J Immunol 192:771-781(2014) [PubMed] [Europe PMC] [Abstract]
• negative regulation of substrate adhesion-dependent cell spreading Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Guanylate binding protein 1-mediated interaction of T cell antigen receptor signaling with the cytoskeleton."
    Forster F., Paster W., Supper V., Schatzlmaier P., Sunzenauer S., Ostler N., Saliba A., Eckerstorfer P., Britzen-Laurent N., Schutz G., Schmid J.A., Zlabinger G.J., Naschberger E., Sturzl M., Stockinger H.
    J Immunol 192:771-781(2014) [PubMed] [Europe PMC] [Abstract]
• negative regulation of T cell receptor signaling pathway Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Guanylate binding protein 1-mediated interaction of T cell antigen receptor signaling with the cytoskeleton."
    Forster F., Paster W., Supper V., Schatzlmaier P., Sunzenauer S., Ostler N., Saliba A., Eckerstorfer P., Britzen-Laurent N., Schutz G., Schmid J.A., Zlabinger G.J., Naschberger E., Sturzl M., Stockinger H.
    J Immunol 192:771-781(2014) [PubMed] [Europe PMC] [Abstract]
• protein localization to vacuole Source: UniProtKBInferred from direct assayⁱ
  • Ref.12

    "Intracellular trafficking of guanylate-binding proteins is regulated by heterodimerization in a hierarchical manner."
    Britzen-Laurent N., Bauer M., Berton V., Fischer N., Syguda A., Reipschlager S., Naschberger E., Herrmann C., Sturzl M.
    PLoS ONE 5:E14246-E14246(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBCELLULAR LOCATION, DIMERIZATION, ISOPRENYLATION, MUTAGENESIS OF LYS-51; 227-ARG-LYS-228 AND 589-CYS--SER-592.
• regulation of calcium-mediated signaling Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Guanylate binding protein 1-mediated interaction of T cell antigen receptor signaling with the cytoskeleton."
    Forster F., Paster W., Supper V., Schatzlmaier P., Sunzenauer S., Ostler N., Saliba A., Eckerstorfer P., Britzen-Laurent N., Schutz G., Schmid J.A., Zlabinger G.J., Naschberger E., Sturzl M., Stockinger H.
    J Immunol 192:771-781(2014) [PubMed] [Europe PMC] [Abstract]
• regulation of protein localization to plasma membrane Source: UniProtKB <p>Inferred from Genetic Interaction</p> <p>Used to describe "traditional" genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#igi">GO evidence code guide</a></p> Inferred from genetic interactionⁱ
  • "Guanylate binding protein 1-mediated interaction of T cell antigen receptor signaling with the cytoskeleton."
    Forster F., Paster W., Supper V., Schatzlmaier P., Sunzenauer S., Ostler N., Saliba A., Eckerstorfer P., Britzen-Laurent N., Schutz G., Schmid J.A., Zlabinger G.J., Naschberger E., Sturzl M., Stockinger H.
    J Immunol 192:771-781(2014) [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

<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

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%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 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

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

• actin binding Source: UniProtKBInferred from direct assayⁱ
  • "Guanylate binding protein 1-mediated interaction of T cell antigen receptor signaling with the cytoskeleton."
    Forster F., Paster W., Supper V., Schatzlmaier P., Sunzenauer S., Ostler N., Saliba A., Eckerstorfer P., Britzen-Laurent N., Schutz G., Schmid J.A., Zlabinger G.J., Naschberger E., Sturzl M., Stockinger H.
    J Immunol 192:771-781(2014) [PubMed] [Europe PMC] [Abstract]
• cytokine binding Source: UniProtKBInferred from physical interactionⁱ
  • "Guanylate binding protein 1-mediated interaction of T cell antigen receptor signaling with the cytoskeleton."
    Forster F., Paster W., Supper V., Schatzlmaier P., Sunzenauer S., Ostler N., Saliba A., Eckerstorfer P., Britzen-Laurent N., Schutz G., Schmid J.A., Zlabinger G.J., Naschberger E., Sturzl M., Stockinger H.
    J Immunol 192:771-781(2014) [PubMed] [Europe PMC] [Abstract]
• enzyme binding Source: UniProtKBInferred from physical interactionⁱ
  • "Guanylate binding protein 1-mediated interaction of T cell antigen receptor signaling with the cytoskeleton."
    Forster F., Paster W., Supper V., Schatzlmaier P., Sunzenauer S., Ostler N., Saliba A., Eckerstorfer P., Britzen-Laurent N., Schutz G., Schmid J.A., Zlabinger G.J., Naschberger E., Sturzl M., Stockinger H.
    J Immunol 192:771-781(2014) [PubMed] [Europe PMC] [Abstract]
• Hsp90 protein binding Source: UniProtKBInferred from physical interactionⁱ
  • "Guanylate binding protein 1-mediated interaction of T cell antigen receptor signaling with the cytoskeleton."
    Forster F., Paster W., Supper V., Schatzlmaier P., Sunzenauer S., Ostler N., Saliba A., Eckerstorfer P., Britzen-Laurent N., Schutz G., Schmid J.A., Zlabinger G.J., Naschberger E., Sturzl M., Stockinger H.
    J Immunol 192:771-781(2014) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: IntActInferred from physical interactionⁱ
  • Ref.16

    "How guanylate-binding proteins achieve assembly-stimulated processive cleavage of GTP to GMP."
    Ghosh A., Praefcke G.J., Renault L., Wittinghofer A., Herrmann C.
    Nature 440:101-104(2006) [PubMed] [Europe PMC] [Abstract]

    Cited for: X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS) OF 1-317, SUBUNIT.
  • "The guanine cap of human guanylate-binding protein 1 is responsible for dimerization and self-activation of GTP hydrolysis."
    Wehner M., Kunzelmann S., Herrmann C.
    FEBS J 279:203-210(2012) [PubMed] [Europe PMC] [Abstract]
  • "Tetramerization of human guanylate-binding protein 1 is mediated by coiled-coil formation of the C-terminal alpha-helices."
    Syguda A., Bauer M., Benscheid U., Ostler N., Naschberger E., Ince S., Sturzl M., Herrmann C.
    FEBS J 279:2544-2554(2012) [PubMed] [Europe PMC] [Abstract]
• protein homodimerization activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.12

    "Intracellular trafficking of guanylate-binding proteins is regulated by heterodimerization in a hierarchical manner."
    Britzen-Laurent N., Bauer M., Berton V., Fischer N., Syguda A., Reipschlager S., Naschberger E., Herrmann C., Sturzl M.
    PLoS ONE 5:E14246-E14246(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBCELLULAR LOCATION, DIMERIZATION, ISOPRENYLATION, MUTAGENESIS OF LYS-51; 227-ARG-LYS-228 AND 589-CYS--SER-592.
• spectrin binding Source: UniProtKBInferred from physical interactionⁱ
  • "Guanylate binding protein 1-mediated interaction of T cell antigen receptor signaling with the cytoskeleton."
    Forster F., Paster W., Supper V., Schatzlmaier P., Sunzenauer S., Ostler N., Saliba A., Eckerstorfer P., Britzen-Laurent N., Schutz G., Schmid J.A., Zlabinger G.J., Naschberger E., Sturzl M., Stockinger H.
    J Immunol 192:771-781(2014) [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

Region

<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

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>Sequenceⁱ

<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.

        10         20         30         40         50
MASEIHMTGP MCLIENTNGR LMANPEALKI LSAITQPMVV VAIVGLYRTG 
        60         70         80         90        100
KSYLMNKLAG KKKGFSLGST VQSHTKGIWM WCVPHPKKPG HILVLLDTEG 
       110        120        130        140        150
LGDVEKGDNQ NDSWIFALAV LLSSTFVYNS IGTINQQAMD QLYYVTELTH 
       160        170        180        190        200
RIRSKSSPDE NENEVEDSAD FVSFFPDFVW TLRDFSLDLE ADGQPLTPDE 
       210        220        230        240        250
YLTYSLKLKK GTSQKDETFN LPRLCIRKFF PKKKCFVFDR PVHRRKLAQL 
       260        270        280        290        300
EKLQDEELDP EFVQQVADFC SYIFSNSKTK TLSGGIQVNG PRLESLVLTY 
       310        320        330        340        350
VNAISSGDLP CMENAVLALA QIENSAAVQK AIAHYEQQMG QKVQLPTETL 
       360        370        380        390        400
QELLDLHRDS EREAIEVFIR SSFKDVDHLF QKELAAQLEK KRDDFCKQNQ 
       410        420        430        440        450
EASSDRCSAL LQVIFSPLEE EVKAGIYSKP GGYRLFVQKL QDLKKKYYEE 
       460        470        480        490        500
PRKGIQAEEI LQTYLKSKES MTDAILQTDQ TLTEKEKEIE VERVKAESAQ 
       510        520        530        540        550
ASAKMLQEMQ RKNEQMMEQK ERSYQEHLKQ LTEKMENDRV QLLKEQERTL 
       560        570        580        590 
ALKLQEQEQL LKEGFQKESR IMKNEIQDLQ TKMRRRKACT IS         

Natural variant

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%5Freferences%5Fsection">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

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 polymorphisms and disease mutations
   Index of human polymorphisms and disease mutations
2. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
3. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
4. SIMILARITY comments
   Index of protein domains and families
5. Human chromosome 1
   Human chromosome 1: entries, gene names and cross-references to MIM
6. Human entries with polymorphisms or disease mutations
   List of human entries with polymorphisms or disease mutations