Girdin

<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

• 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
  • Ref.1

    "Akt/PKB regulates actin organization and cell motility via Girdin/APE."
    Enomoto A., Murakami H., Asai N., Morone N., Watanabe T., Kawai K., Murakumo Y., Usukura J., Kaibuchi K., Takahashi M.
    Dev. Cell 9:389-402(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH AKT1, INTERACTION WITH PHOSPHOINOSITIDES, HOMOOLIGOMERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-1417 BY AKT1, MUTAGENESIS OF SER-1417.
• dynein light intermediate chain binding 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%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• epidermal growth factor receptor 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
  • Ref.12

    "A G{alpha}i-GIV molecular complex binds epidermal growth factor receptor and determines whether cells migrate or proliferate."
    Ghosh P., Beas A.O., Bornheimer S.J., Garcia-Marcos M., Forry E.P., Johannson C., Ear J., Jung B.H., Cabrera B., Carethers J.M., Farquhar M.G.
    Mol. Biol. Cell 21:2338-2354(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, IDENTIFICATION IN COMPLEX WITH EGFR AND GNAI3, MUTAGENESIS OF PHE-1686.
  • Ref.20

    "Structural basis for activation of trimeric Gi proteins by multiple growth factor receptors via GIV/Girdin."
    Lin C., Ear J., Midde K., Lopez-Sanchez I., Aznar N., Garcia-Marcos M., Kufareva I., Abagyan R., Ghosh P.
    Mol. Biol. Cell 25:3654-3671(2014) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH EGFR; GNAI3; INSR AND KDR, SH2-LIKE REGION, MUTAGENESIS OF LYS-1723; LYS-1725; ARG-1746; LYS-1750; PHE-1766 AND GLN-1778.
• GDP-dissociation inhibitor activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.22

    "GIV/Girdin activates Galphai and inhibits Galphas via the same motif."
    Gupta V., Bhandari D., Leyme A., Aznar N., Midde K.K., Lo I.C., Ear J., Niesman I., Lopez-Sanchez I., Blanco-Canosa J.B., von Zastrow M., Garcia-Marcos M., Farquhar M.G., Ghosh P.
    Proc. Natl. Acad. Sci. U.S.A. 113:E5721-E5730(2016) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH GNAI3 AND GNAS, PHOSPHORYLATION AT SER-1675 AND SER-1690, MUTAGENESIS OF SER-1675; PHE-1686 AND SER-1690.
• G-protein alpha-subunit binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.10

    "GIV is a nonreceptor GEF for G alpha i with a unique motif that regulates Akt signaling."
    Garcia-Marcos M., Ghosh P., Farquhar M.G.
    Proc. Natl. Acad. Sci. U.S.A. 106:3178-3183(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH GNAI1; GNAI2 AND GNAI3, GBA MOTIF, MUTAGENESIS OF PHE-1686 AND GLU-1689.
  • Ref.18

    "Protein kinase C-theta (PKCtheta) phosphorylates and inhibits the guanine exchange factor, GIV/Girdin."
    Lopez-Sanchez I., Garcia-Marcos M., Mittal Y., Aznar N., Farquhar M.G., Ghosh P.
    Proc. Natl. Acad. Sci. U.S.A. 110:5510-5515(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH GNAI3 AND PRKCQ, PHOSPHORYLATION AT SER-1690, MUTAGENESIS OF PHE-1686 AND SER-1690.
  • Ref.22

    "GIV/Girdin activates Galphai and inhibits Galphas via the same motif."
    Gupta V., Bhandari D., Leyme A., Aznar N., Midde K.K., Lo I.C., Ear J., Niesman I., Lopez-Sanchez I., Blanco-Canosa J.B., von Zastrow M., Garcia-Marcos M., Farquhar M.G., Ghosh P.
    Proc. Natl. Acad. Sci. U.S.A. 113:E5721-E5730(2016) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH GNAI3 AND GNAS, PHOSPHORYLATION AT SER-1675 AND SER-1690, MUTAGENESIS OF SER-1675; PHE-1686 AND SER-1690.
• G-protein gamma-subunit binding Source: Ensembl
• guanyl-nucleotide exchange factor activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.10

    "GIV is a nonreceptor GEF for G alpha i with a unique motif that regulates Akt signaling."
    Garcia-Marcos M., Ghosh P., Farquhar M.G.
    Proc. Natl. Acad. Sci. U.S.A. 106:3178-3183(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH GNAI1; GNAI2 AND GNAI3, GBA MOTIF, MUTAGENESIS OF PHE-1686 AND GLU-1689.
  • Ref.18

    "Protein kinase C-theta (PKCtheta) phosphorylates and inhibits the guanine exchange factor, GIV/Girdin."
    Lopez-Sanchez I., Garcia-Marcos M., Mittal Y., Aznar N., Farquhar M.G., Ghosh P.
    Proc. Natl. Acad. Sci. U.S.A. 110:5510-5515(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH GNAI3 AND PRKCQ, PHOSPHORYLATION AT SER-1690, MUTAGENESIS OF PHE-1686 AND SER-1690.
  • Ref.21

    "Membrane recruitment of the non-receptor protein GIV/Girdin (Galpha-interacting, Vesicle-associated Protein/Girdin) is sufficient for activating heterotrimeric G protein signaling."
    Parag-Sharma K., Leyme A., DiGiacomo V., Marivin A., Broselid S., Garcia-Marcos M.
    J. Biol. Chem. 291:27098-27111(2016) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBCELLULAR LOCATION.
• insulin receptor binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.20

    "Structural basis for activation of trimeric Gi proteins by multiple growth factor receptors via GIV/Girdin."
    Lin C., Ear J., Midde K., Lopez-Sanchez I., Aznar N., Garcia-Marcos M., Kufareva I., Abagyan R., Ghosh P.
    Mol. Biol. Cell 25:3654-3671(2014) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH EGFR; GNAI3; INSR AND KDR, SH2-LIKE REGION, MUTAGENESIS OF LYS-1723; LYS-1725; ARG-1746; LYS-1750; PHE-1766 AND GLN-1778.
• microtubule binding Source: UniProtKB
• phosphatidylinositol binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.1

    "Akt/PKB regulates actin organization and cell motility via Girdin/APE."
    Enomoto A., Murakami H., Asai N., Morone N., Watanabe T., Kawai K., Murakumo Y., Usukura J., Kaibuchi K., Takahashi M.
    Dev. Cell 9:389-402(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH AKT1, INTERACTION WITH PHOSPHOINOSITIDES, HOMOOLIGOMERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-1417 BY AKT1, MUTAGENESIS OF SER-1417.
• protein homodimerization activity Source: UniProtKBInferred from physical interactionⁱ
  • Ref.1

    "Akt/PKB regulates actin organization and cell motility via Girdin/APE."
    Enomoto A., Murakami H., Asai N., Morone N., Watanabe T., Kawai K., Murakumo Y., Usukura J., Kaibuchi K., Takahashi M.
    Dev. Cell 9:389-402(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH AKT1, INTERACTION WITH PHOSPHOINOSITIDES, HOMOOLIGOMERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-1417 BY AKT1, MUTAGENESIS OF SER-1417.
• protein kinase B binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.1

    "Akt/PKB regulates actin organization and cell motility via Girdin/APE."
    Enomoto A., Murakami H., Asai N., Morone N., Watanabe T., Kawai K., Murakumo Y., Usukura J., Kaibuchi K., Takahashi M.
    Dev. Cell 9:389-402(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH AKT1, INTERACTION WITH PHOSPHOINOSITIDES, HOMOOLIGOMERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-1417 BY AKT1, MUTAGENESIS OF SER-1417.
• protein kinase C binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.18

    "Protein kinase C-theta (PKCtheta) phosphorylates and inhibits the guanine exchange factor, GIV/Girdin."
    Lopez-Sanchez I., Garcia-Marcos M., Mittal Y., Aznar N., Farquhar M.G., Ghosh P.
    Proc. Natl. Acad. Sci. U.S.A. 110:5510-5515(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH GNAI3 AND PRKCQ, PHOSPHORYLATION AT SER-1690, MUTAGENESIS OF PHE-1686 AND SER-1690.
• SH2 domain binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.15

    "Tyrosine phosphorylation of the Galpha-interacting protein GIV promotes activation of phosphoinositide 3-kinase during cell migration."
    Lin C., Ear J., Pavlova Y., Mittal Y., Kufareva I., Ghassemian M., Abagyan R., Garcia-Marcos M., Ghosh P.
    Sci. Signal. 4:RA64-RA64(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH GNAI3 AND PIK3R1, PHOSPHORYLATION AT TYR-1765 AND TYR-1799, MUTAGENESIS OF SER-1417; TYR-1765 AND TYR-1799.
• vascular endothelial growth factor receptor 2 binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.20

    "Structural basis for activation of trimeric Gi proteins by multiple growth factor receptors via GIV/Girdin."
    Lin C., Ear J., Midde K., Lopez-Sanchez I., Aznar N., Garcia-Marcos M., Kufareva I., Abagyan R., Ghosh P.
    Mol. Biol. Cell 25:3654-3671(2014) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH EGFR; GNAI3; INSR AND KDR, SH2-LIKE REGION, MUTAGENESIS OF LYS-1723; LYS-1725; ARG-1746; LYS-1750; PHE-1766 AND GLN-1778.

GO - Biological processⁱ

• activation of protein kinase activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.15

    "Tyrosine phosphorylation of the Galpha-interacting protein GIV promotes activation of phosphoinositide 3-kinase during cell migration."
    Lin C., Ear J., Pavlova Y., Mittal Y., Kufareva I., Ghassemian M., Abagyan R., Garcia-Marcos M., Ghosh P.
    Sci. Signal. 4:RA64-RA64(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH GNAI3 AND PIK3R1, PHOSPHORYLATION AT TYR-1765 AND TYR-1799, MUTAGENESIS OF SER-1417; TYR-1765 AND TYR-1799.
• activation of protein kinase B activity Source: UniProtKB
• cell migration 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
  • Ref.1

    "Akt/PKB regulates actin organization and cell motility via Girdin/APE."
    Enomoto A., Murakami H., Asai N., Morone N., Watanabe T., Kawai K., Murakumo Y., Usukura J., Kaibuchi K., Takahashi M.
    Dev. Cell 9:389-402(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH AKT1, INTERACTION WITH PHOSPHOINOSITIDES, HOMOOLIGOMERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-1417 BY AKT1, MUTAGENESIS OF SER-1417.
• cytoplasmic microtubule organization Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• cytoskeleton-dependent intracellular transport Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• DNA replication Source: UniProtKB-KW
• lamellipodium assembly Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.1

    "Akt/PKB regulates actin organization and cell motility via Girdin/APE."
    Enomoto A., Murakami H., Asai N., Morone N., Watanabe T., Kawai K., Murakumo Y., Usukura J., Kaibuchi K., Takahashi M.
    Dev. Cell 9:389-402(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH AKT1, INTERACTION WITH PHOSPHOINOSITIDES, HOMOOLIGOMERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-1417 BY AKT1, MUTAGENESIS OF SER-1417.
• maintenance of protein location in plasma membrane Source: UniProtKBInferred from direct assayⁱ
  • Ref.12

    "A G{alpha}i-GIV molecular complex binds epidermal growth factor receptor and determines whether cells migrate or proliferate."
    Ghosh P., Beas A.O., Bornheimer S.J., Garcia-Marcos M., Forry E.P., Johannson C., Ear J., Jung B.H., Cabrera B., Carethers J.M., Farquhar M.G.
    Mol. Biol. Cell 21:2338-2354(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, IDENTIFICATION IN COMPLEX WITH EGFR AND GNAI3, MUTAGENESIS OF PHE-1686.
• membrane organization Source: UniProtKBInferred from direct assayⁱ
  • Ref.2

    "A novel hook-related protein family and the characterization of hook-related protein 1."
    Simpson F., Martin S., Evans T.M., Kerr M., James D.E., Parton R.G., Teasdale R.D., Wicking C.
    Traffic 6:442-458(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING.
• nervous system development Source: UniProtKB-KW
• positive regulation of cilium assembly Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.24

    "A Conserved role for girdin in basal body positioning and ciliogenesis."
    Nechipurenko I.V., Olivier-Mason A., Kazatskaya A., Kennedy J., McLachlan I.G., Heiman M.G., Blacque O.E., Sengupta P.
    Dev. Cell 38:493-506(2016) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION.
• positive regulation of epidermal growth factor receptor signaling pathway Source: UniProtKBInferred from direct assayⁱ
  • Ref.12

    "A G{alpha}i-GIV molecular complex binds epidermal growth factor receptor and determines whether cells migrate or proliferate."
    Ghosh P., Beas A.O., Bornheimer S.J., Garcia-Marcos M., Forry E.P., Johannson C., Ear J., Jung B.H., Cabrera B., Carethers J.M., Farquhar M.G.
    Mol. Biol. Cell 21:2338-2354(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, IDENTIFICATION IN COMPLEX WITH EGFR AND GNAI3, MUTAGENESIS OF PHE-1686.
• positive regulation of protein localization to cilium Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.24

    "A Conserved role for girdin in basal body positioning and ciliogenesis."
    Nechipurenko I.V., Olivier-Mason A., Kazatskaya A., Kennedy J., McLachlan I.G., Heiman M.G., Blacque O.E., Sengupta P.
    Dev. Cell 38:493-506(2016) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION.
• positive regulation of stress fiber assembly Source: CACAOInferred from mutant phenotypeⁱ
  • Ref.1

    "Akt/PKB regulates actin organization and cell motility via Girdin/APE."
    Enomoto A., Murakami H., Asai N., Morone N., Watanabe T., Kawai K., Murakumo Y., Usukura J., Kaibuchi K., Takahashi M.
    Dev. Cell 9:389-402(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH AKT1, INTERACTION WITH PHOSPHOINOSITIDES, HOMOOLIGOMERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-1417 BY AKT1, MUTAGENESIS OF SER-1417.
• regulation of actin cytoskeleton organization Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.1

    "Akt/PKB regulates actin organization and cell motility via Girdin/APE."
    Enomoto A., Murakami H., Asai N., Morone N., Watanabe T., Kawai K., Murakumo Y., Usukura J., Kaibuchi K., Takahashi M.
    Dev. Cell 9:389-402(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH AKT1, INTERACTION WITH PHOSPHOINOSITIDES, HOMOOLIGOMERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-1417 BY AKT1, MUTAGENESIS OF SER-1417.
• regulation of cell population proliferation Source: UniProtKB
• regulation of DNA replication Source: UniProtKB
• regulation of neuron projection development Source: UniProtKB
• regulation of protein phosphorylation Source: UniProtKB
• small GTPase mediated signal transduction Source: UniProtKBInferred from direct assayⁱ
  • Ref.10

    "GIV is a nonreceptor GEF for G alpha i with a unique motif that regulates Akt signaling."
    Garcia-Marcos M., Ghosh P., Farquhar M.G.
    Proc. Natl. Acad. Sci. U.S.A. 106:3178-3183(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH GNAI1; GNAI2 AND GNAI3, GBA MOTIF, MUTAGENESIS OF PHE-1686 AND GLU-1689.
  • Ref.18

    "Protein kinase C-theta (PKCtheta) phosphorylates and inhibits the guanine exchange factor, GIV/Girdin."
    Lopez-Sanchez I., Garcia-Marcos M., Mittal Y., Aznar N., Farquhar M.G., Ghosh P.
    Proc. Natl. Acad. Sci. U.S.A. 110:5510-5515(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH GNAI3 AND PRKCQ, PHOSPHORYLATION AT SER-1690, MUTAGENESIS OF PHE-1686 AND SER-1690.
  • Ref.22

    "GIV/Girdin activates Galphai and inhibits Galphas via the same motif."
    Gupta V., Bhandari D., Leyme A., Aznar N., Midde K.K., Lo I.C., Ear J., Niesman I., Lopez-Sanchez I., Blanco-Canosa J.B., von Zastrow M., Garcia-Marcos M., Farquhar M.G., Ghosh P.
    Proc. Natl. Acad. Sci. U.S.A. 113:E5721-E5730(2016) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH GNAI3 AND GNAS, PHOSPHORYLATION AT SER-1675 AND SER-1690, MUTAGENESIS OF SER-1675; PHE-1686 AND SER-1690.
  • Ref.21

    "Membrane recruitment of the non-receptor protein GIV/Girdin (Galpha-interacting, Vesicle-associated Protein/Girdin) is sufficient for activating heterotrimeric G protein signaling."
    Parag-Sharma K., Leyme A., DiGiacomo V., Marivin A., Broselid S., Garcia-Marcos M.
    J. Biol. Chem. 291:27098-27111(2016) [PubMed] [Europe PMC] [Abstract]

    Cited for: SUBCELLULAR LOCATION.
• TOR signaling Source: UniProtKB

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

Enzyme and pathway databases

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

Organism-specific databases

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

• UniProt annotation
• GO - Cellular component

Keywords - Cellular componentⁱ

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

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseaseⁱ

Mutagenesis

Keywords - Diseaseⁱ

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

• actin binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.1

    "Akt/PKB regulates actin organization and cell motility via Girdin/APE."
    Enomoto A., Murakami H., Asai N., Morone N., Watanabe T., Kawai K., Murakumo Y., Usukura J., Kaibuchi K., Takahashi M.
    Dev. Cell 9:389-402(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH AKT1, INTERACTION WITH PHOSPHOINOSITIDES, HOMOOLIGOMERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-1417 BY AKT1, MUTAGENESIS OF SER-1417.
• dynein light intermediate chain binding Source: GO_CentralInferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• epidermal growth factor receptor binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.12

    "A G{alpha}i-GIV molecular complex binds epidermal growth factor receptor and determines whether cells migrate or proliferate."
    Ghosh P., Beas A.O., Bornheimer S.J., Garcia-Marcos M., Forry E.P., Johannson C., Ear J., Jung B.H., Cabrera B., Carethers J.M., Farquhar M.G.
    Mol. Biol. Cell 21:2338-2354(2010) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, IDENTIFICATION IN COMPLEX WITH EGFR AND GNAI3, MUTAGENESIS OF PHE-1686.
  • Ref.20

    "Structural basis for activation of trimeric Gi proteins by multiple growth factor receptors via GIV/Girdin."
    Lin C., Ear J., Midde K., Lopez-Sanchez I., Aznar N., Garcia-Marcos M., Kufareva I., Abagyan R., Ghosh P.
    Mol. Biol. Cell 25:3654-3671(2014) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH EGFR; GNAI3; INSR AND KDR, SH2-LIKE REGION, MUTAGENESIS OF LYS-1723; LYS-1725; ARG-1746; LYS-1750; PHE-1766 AND GLN-1778.
• G-protein alpha-subunit binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.10

    "GIV is a nonreceptor GEF for G alpha i with a unique motif that regulates Akt signaling."
    Garcia-Marcos M., Ghosh P., Farquhar M.G.
    Proc. Natl. Acad. Sci. U.S.A. 106:3178-3183(2009) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH GNAI1; GNAI2 AND GNAI3, GBA MOTIF, MUTAGENESIS OF PHE-1686 AND GLU-1689.
  • Ref.18

    "Protein kinase C-theta (PKCtheta) phosphorylates and inhibits the guanine exchange factor, GIV/Girdin."
    Lopez-Sanchez I., Garcia-Marcos M., Mittal Y., Aznar N., Farquhar M.G., Ghosh P.
    Proc. Natl. Acad. Sci. U.S.A. 110:5510-5515(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH GNAI3 AND PRKCQ, PHOSPHORYLATION AT SER-1690, MUTAGENESIS OF PHE-1686 AND SER-1690.
  • Ref.22

    "GIV/Girdin activates Galphai and inhibits Galphas via the same motif."
    Gupta V., Bhandari D., Leyme A., Aznar N., Midde K.K., Lo I.C., Ear J., Niesman I., Lopez-Sanchez I., Blanco-Canosa J.B., von Zastrow M., Garcia-Marcos M., Farquhar M.G., Ghosh P.
    Proc. Natl. Acad. Sci. U.S.A. 113:E5721-E5730(2016) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH GNAI3 AND GNAS, PHOSPHORYLATION AT SER-1675 AND SER-1690, MUTAGENESIS OF SER-1675; PHE-1686 AND SER-1690.
• G-protein gamma-subunit binding Source: Ensembl
• insulin receptor binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.20

    "Structural basis for activation of trimeric Gi proteins by multiple growth factor receptors via GIV/Girdin."
    Lin C., Ear J., Midde K., Lopez-Sanchez I., Aznar N., Garcia-Marcos M., Kufareva I., Abagyan R., Ghosh P.
    Mol. Biol. Cell 25:3654-3671(2014) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH EGFR; GNAI3; INSR AND KDR, SH2-LIKE REGION, MUTAGENESIS OF LYS-1723; LYS-1725; ARG-1746; LYS-1750; PHE-1766 AND GLN-1778.
• microtubule binding Source: UniProtKB
• protein homodimerization activity Source: UniProtKBInferred from physical interactionⁱ
  • Ref.1

    "Akt/PKB regulates actin organization and cell motility via Girdin/APE."
    Enomoto A., Murakami H., Asai N., Morone N., Watanabe T., Kawai K., Murakumo Y., Usukura J., Kaibuchi K., Takahashi M.
    Dev. Cell 9:389-402(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH AKT1, INTERACTION WITH PHOSPHOINOSITIDES, HOMOOLIGOMERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-1417 BY AKT1, MUTAGENESIS OF SER-1417.
• protein kinase B binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.1

    "Akt/PKB regulates actin organization and cell motility via Girdin/APE."
    Enomoto A., Murakami H., Asai N., Morone N., Watanabe T., Kawai K., Murakumo Y., Usukura J., Kaibuchi K., Takahashi M.
    Dev. Cell 9:389-402(2005) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH AKT1, INTERACTION WITH PHOSPHOINOSITIDES, HOMOOLIGOMERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-1417 BY AKT1, MUTAGENESIS OF SER-1417.
• protein kinase C binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.18

    "Protein kinase C-theta (PKCtheta) phosphorylates and inhibits the guanine exchange factor, GIV/Girdin."
    Lopez-Sanchez I., Garcia-Marcos M., Mittal Y., Aznar N., Farquhar M.G., Ghosh P.
    Proc. Natl. Acad. Sci. U.S.A. 110:5510-5515(2013) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH GNAI3 AND PRKCQ, PHOSPHORYLATION AT SER-1690, MUTAGENESIS OF PHE-1686 AND SER-1690.
• SH2 domain binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.15

    "Tyrosine phosphorylation of the Galpha-interacting protein GIV promotes activation of phosphoinositide 3-kinase during cell migration."
    Lin C., Ear J., Pavlova Y., Mittal Y., Kufareva I., Ghassemian M., Abagyan R., Garcia-Marcos M., Ghosh P.
    Sci. Signal. 4:RA64-RA64(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH GNAI3 AND PIK3R1, PHOSPHORYLATION AT TYR-1765 AND TYR-1799, MUTAGENESIS OF SER-1417; TYR-1765 AND TYR-1799.
• vascular endothelial growth factor receptor 2 binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.20

    "Structural basis for activation of trimeric Gi proteins by multiple growth factor receptors via GIV/Girdin."
    Lin C., Ear J., Midde K., Lopez-Sanchez I., Aznar N., Garcia-Marcos M., Kufareva I., Abagyan R., Ghosh P.
    Mol. Biol. Cell 25:3654-3671(2014) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH EGFR; GNAI3; INSR AND KDR, SH2-LIKE REGION, MUTAGENESIS OF LYS-1723; LYS-1725; ARG-1746; LYS-1750; PHE-1766 AND GLN-1778.

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

<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

Coiled coil

Motif

<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 (5+)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.

This entry has 5 described isoforms and 33 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MENEIFTPLL EQFMTSPLVT WVKTFGPLAA GNGTNLDEYV ALVDGVFLNQ 
        60         70         80         90        100
VMLQINPKLE SQRVNKKVNN DASLRMHNLS ILVRQIKFYY QETLQQLIMM 
       110        120        130        140        150
SLPNVLIIGK NPFSEQGTEE VKKLLLLLLG CAVQCQKKEE FIERIQGLDF 
       160        170        180        190        200
DTKAAVAAHI QEVTHNQENV FDLQWMEVTD MSQEDIEPLL KNMALHLKRL 
       210        220        230        240        250
IDERDEHSET IIELSEERDG LHFLPHASSS AQSPCGSPGM KRTESRQHLS 
       260        270        280        290        300
VELADAKAKI RRLRQELEEK TEQLLDCKQE LEQMEIELKR LQQENMNLLS 
       310        320        330        340        350
DARSARMYRD ELDALREKAV RVDKLESEVS RYKERLHDIE FYKARVEELK 
       360        370        380        390        400
EDNQVLLETK TMLEDQLEGT RARSDKLHEL EKENLQLKAK LHDMEMERDM 
       410        420        430        440        450
DRKKIEELME ENMTLEMAQK QSMDESLHLG WELEQISRTS ELSEAPQKSL 
       460        470        480        490        500
GHEVNELTSS RLLKLEMENQ SLTKTVEELR TTVDSVEGNA SKILKMEKEN 
       510        520        530        540        550
QRLSKKVEIL ENEIVQEKQS LQNCQNLSKD LMKEKAQLEK TIETLRENSE 
       560        570        580        590        600
RQIKILEQEN EHLNQTVSSL RQRSQISAEA RVKDIEKENK ILHESIKETS 
       610        620        630        640        650
SKLSKIEFEK RQIKKELEHY KEKGERAEEL ENELHHLEKE NELLQKKITN 
       660        670        680        690        700
LKITCEKIEA LEQENSELER ENRKLKKTLD SFKNLTFQLE SLEKENSQLD 
       710        720        730        740        750
EENLELRRNV ESLKCASMKM AQLQLENKEL ESEKEQLKKG LELLKASFKK 
       760        770        780        790        800
TERLEVSYQG LDIENQRLQK TLENSNKKIQ QLESELQDLE MENQTLQKNL 
       810        820        830        840        850
EELKISSKRL EQLEKENKSL EQETSQLEKD KKQLEKENKR LRQQAEIKDT 
       860        870        880        890        900
TLEENNVKIG NLEKENKTLS KEIGIYKESC VRLKELEKEN KELVKRATID 
       910        920        930        940        950
IKTLVTLRED LVSEKLKTQQ MNNDLEKLTH ELEKIGLNKE RLLHDEQSTD 
       960        970        980        990       1000
DSRYKLLESK LESTLKKSLE IKEEKIAALE ARLEESTNYN QQLRQELKTV 
      1010       1020       1030       1040       1050
KKNYEALKQR QDEERMVQSS PPISGEDNKW ERESQETTRE LLKVKDRLIE 
      1060       1070       1080       1090       1100
VERNNATLQA EKQALKTQLK QLETQNNNLQ AQILALQRQT VSLQEQNTTL 
      1110       1120       1130       1140       1150
QTQNAKLQVE NSTLNSQSTS LMNQNAQLLI QQSSLENENE SVIKEREDLK 
      1160       1170       1180       1190       1200
SLYDSLIKDH EKLELLHERQ ASEYESLISK HGTLKSAHKN LEVEHRDLED 
      1210       1220       1230       1240       1250
RYNQLLKQKG QLEDLEKMLK VEQEKMLLEN KNHETVAAEY KKLCGENDRL 
      1260       1270       1280       1290       1300
NHTYSQLLKE TEVLQTDHKN LKSLLNNSKL EQTRLEAEFS KLKEQYQQLD 
      1310       1320       1330       1340       1350
ITSTKLNNQC ELLSQLKGNL EEENRHLLDQ IQTLMLQNRT LLEQNMESKD 
      1360       1370       1380       1390       1400
LFHVEQRQYI DKLNELRRQK EKLEEKIMDQ YKFYDPSPPR RRGNWITLKM 
      1410       1420       1430       1440       1450
RKLIKSKKDI NRERQKSLTL TPTRSDSSEG FLQLPHQDSQ DSSSVGSNSL 
      1460       1470       1480       1490       1500
EDGQTLGTKK SSMVALKRLP FLRNRPKDKD KMKACYRRSM SMNDLVQSMV 
      1510       1520       1530       1540       1550
LAGQWTGSTE NLEVPDDIST GKRRKELGAM AFSTTAINFS TVNSSAGFRS 
      1560       1570       1580       1590       1600
KQLVNNKDTT SFEDISPQGV SDDSSTGSRV HASRPASLDS GRTSTSNSNN 
      1610       1620       1630       1640       1650
NASLHEVKAG AVNNQSRPQS HSSGEFSLLH DHEAWSSSGS SPIQYLKRQT 
      1660       1670       1680       1690       1700
RSSPVLQHKI SETLESRHHK IKTGSPGSEV VTLQQFLEES NKLTSVQIKS 
      1710       1720       1730       1740       1750
SSQENLLDEV MKSLSVSSDF LGKDKPVSCG LARSVSGKTP GDFYDRRTTK 
      1760       1770       1780       1790       1800
PEFLRPGPRK TEDTYFISSA GKPTPGTQGK IKLVKESSLS RQSKDSNPYA 
      1810       1820       1830       1840       1850
TLPRASSVIS TAEGTTRRTS IHDFLTKDSR LPISVDSPPA AADSNTTAAS 
      1860       1870 
NVDKVQESRN SKSRSREQQS S                                

        10         20         30         40         50
MENEIFTPLL EQFMTSPLVT WVKTFGPLAA GNGTNLDEYV ALVDGVFLNQ 
        60         70         80         90        100
VMLQINPKLE SQRVNKKVNN DASLRMHNLS ILVRQIKFYY QETLQQLIMM 
       110        120        130        140        150
SLPNVLIIGK NPFSEQGTEE VKKLLLLLLG CAVQCQKKEE FIERIQGLDF 
       160        170        180        190        200
DTKAAVAAHI QEVTHNQENV FDLQWMEVTD MSQEDIEPLL KNMALHLKRL 
       210        220        230        240        250
IDERDEHSET IIELSEERDG LHFLPHASSS AQSPCGSPGM KRTESRQHLS 
       260        270        280        290        300
VELADAKAKI RRLRQELEEK TEQLLDCKQE LEQMEIELKR LQQENMNLLS 
       310        320        330        340        350
DARSARMYRD ELDALREKAV RVDKLESEVS RYKERLHDIE FYKARVEELK 
       360        370        380        390        400
EDNQVLLETK TMLEDQLEGT RARSDKLHEL EKENLQLKAK LHDMEMERDM 
       410        420        430        440        450
DRKKIEELME ENMTLEMAQK QSMDESLHLG WELEQISRTS ELSEAPQKSL 
       460        470        480        490        500
GHEVNELTSS RLLKLEMENQ SLTKTVEELR TTVDSVEGNA SKILKMEKEN 
       510        520        530        540        550
QRLSKKVEIL ENEIVQEKQS LQNCQNLSKD LMKEKAQLEK TIETLRENSE 
       560        570        580        590        600
RQIKILEQEN EHLNQTVSSL RQRSQISAEA RVKDIEKENK ILHESIKETS 
       610        620        630        640        650
SKLSKIEFEK RQIKKELEHY KEKGERAEEL ENELHHLEKE NELLQKKITN 
       660        670        680        690        700
LKITCEKIEA LEQENSELER ENRKLKKTLD SFKNLTFQLE SLEKENSQLD 
       710        720        730        740        750
EENLELRRNV ESLKCASMKM AQLQLENKEL ESEKEQLKKG LELLKASFKK 
       760        770        780        790        800
TERLEVSYQG LDIENQRLQK TLENSNKKIQ QLESELQDLE MENQTLQKNL 
       810        820        830        840        850
EELKISSKRL EQLEKENKSL EQETSQLEKD KKQLEKENKR LRQQAEIKDT 
       860        870        880        890        900
TLEENNVKIG NLEKENKTLS KEIGIYKESC VRLKELEKEN KELVKRATID 
       910        920        930        940        950
IKTLVTLRED LVSEKLKTQQ MNNDLEKLTH ELEKIGLNKE RLLHDEQSTD 
       960        970        980        990       1000
DSRYKLLESK LESTLKKSLE IKEEKIAALE ARLEESTNYN QQLRQELKTV 
      1010       1020       1030       1040       1050
KKNYEALKQR QDEERMVQSS PPISGEDNKW ERESQETTRE LLKVKDRLIE 
      1060       1070       1080       1090       1100
VERNNATLQA EKQALKTQLK QLETQNNNLQ AQILALQRQT VSLQEQNTTL 
      1110       1120       1130       1140       1150
QTQNAKLQVE NSTLNSQSTS LMNQNAQLLI QQSSLENENE SVIKEREDLK 
      1160       1170       1180       1190       1200
SLYDSLIKDH EKLELLHERQ ASEYESLISK HGTLKSAHKN LEVEHRDLED 
      1210       1220       1230       1240       1250
RYNQLLKQKG QLEDLEKMLK VEQEKMLLEN KNHETVAAEY KKLCGENDRL 
      1260       1270       1280       1290       1300
NHTYSQLLKE TEVLQTDHKN LKSLLNNSKL EQTRLEAEFS KLKEQYQQLD 
      1310       1320       1330       1340       1350
ITSTKLNNQC ELLSQLKGNL EEENRHLLDQ IQTLMLQNRT LLEQNMESKD 
      1360       1370       1380       1390       1400
LFHVEQRQYI DKLNELRRQK EKLEEKIMDQ YKFYDPSPPR RRGNWITLKM 
      1410       1420       1430       1440       1450
RKLIKSKKDI NRERQKSLTL TPTRSDSSEG FLQLPHQDSQ DSSSVGSNSL 
      1460       1470       1480       1490       1500
EDGQTLGTKK SSTMNDLVQS MVLAGQWTGS TENLEVPDDI STGKRRKELG 
      1510       1520       1530       1540       1550
AMAFSTTAIN FSTVNSSAGF RSKQLVNNKD TTSFEDISPQ GVSDDSSTGS 
      1560       1570       1580       1590       1600
RVHASRPASL DSGRTSTSNS NNNASLHEVK AGAVNNQSRP QSHSSGEFSL 
      1610       1620       1630       1640       1650
LHDHEAWSSS GSSPIQYLKR QTRSSPVLQH KISETLESRH HKIKTGSPGS 
      1660       1670       1680       1690       1700
EVVTLQQFLE ESNKLTSVQI KSSSQENLLD EVMKSLSVSS DFLGKDKPVS 
      1710       1720       1730       1740       1750
CGLARSVSGK TPGDFYDRRT TKPEFLRPGP RKTEDTYFIS SAGKPTPGTQ 
      1760       1770       1780       1790       1800
GKIKLVKESS LSRQSKDSNP YATLPRASSV ISTAEGTTRR TSIHDFLTKD 
      1810       1820       1830       1840 
SRLPISVDSP PAAADSNTTA ASNVDKVQES RNSKSRSREQ QSS        

        10         20         30         40         50
MENEIFTPLL EQFMTSPLVT WVKTFGPLAA GNGTNLDEYV ALVDGVFLNQ 
        60         70         80         90        100
VMLQINPKLE SQRVNKKVNN DASLRMHNLS ILVRQIKFYY QETLQQLIMM 
       110        120        130        140        150
SLPNVLIIGK NPFSEQGTEE VKKLLLLLLG CAVQCQKKEE FIERIQGLDF 
       160        170        180        190        200
DTKAAVAAHI QEVTHNQENV FDLQWMEVTD MSQEDIEPLL KNMALHLKRL 
       210        220        230        240        250
IDERDEHSET IIELSEERDG LHFLPHASSS AQSPCGSPGM KRTESRQHLS 
       260        270        280        290        300
VELADAKAKI RRLRQELEEK TEQLLDCKQE LEQMEIELKR LQQENMNLLS 
       310        320        330        340        350
DARSARMYRD ELDALREKAV RVDKLESEVS RYKERLHDIE FYKARVEELK 
       360        370        380        390        400
EDNQVLLETK TMLEDQLEGT RARSDKLHEL EKENLQLKAK LHDMEMERDM 
       410        420        430        440        450
DRKKIEELME ENMTLEMAQK QSMDESLHLG WELEQISRTS ELSEAPQKSL 
       460        470        480        490        500
GHEVNELTSS RLLKLEMENQ SLTKTVEELR TTVDSVEGNA SKILKMEKEN 
       510        520        530        540        550
QRLSKKVEIL ENEIVQEKQS LQNCQNLSKD LMKEKAQLEK TIETLRENSE 
       560        570        580        590        600
RQIKILEQEN EHLNQTVSSL RQRSQISAEA RVKDIEKENK ILHESIKETS 
       610        620        630        640        650
SKLSKIEFEK RQIKKELEHY KEKGERAEEL ENELHHLEKE NELLQKKITN 
       660        670        680        690        700
LKITCEKIEA LEQENSELER ENRKLKKTLD SFKNLTFQLE SLEKENSQLD 
       710        720        730        740        750
EENLELRRNV ESLKCASMKM AQLQLENKEL ESEKEQLKKG LELLKASFKK 
       760        770        780        790        800
TERLEVSYQG LDIENQRLQK TLENSNKKIQ QLESELQDLE MENQTLQKNL 
       810        820        830        840        850
EELKISSKRL EQLEKENKSL EQETSQLEKD KKQLEKENKR LRQQAEIKDT 
       860        870        880        890        900
TLEENNVKIG NLEKENKTLS KEIGIYKESC VRLKELEKEN KELVKRATID 
       910        920        930        940        950
IKTLVTLRED LVSEKLKTQQ MNNDLEKLTH ELEKIGLNKE RLLHDEQSTD 
       960        970        980        990       1000
DRYKLLESKL ESTLKKSLEI KEEKIAALEA RLEESTNYNQ QLRQELKTVK 
      1010       1020       1030       1040       1050
KNYEALKQRQ DEERMVQSSP PISGEDNKWE RESQETTREL LKVKDRLIEV 
      1060       1070       1080       1090       1100
ERNNATLQAE KQALKTQLKQ LETQNNNLQA QILALQRQTV SLQEQNTTLQ 
      1110       1120       1130       1140       1150
TQNAKLQVEN STLNSQSTSL MNQNAQLLIQ QSSLENENES VIKEREDLKS 
      1160       1170       1180       1190       1200
LYDSLIKDHE KLELLHERQA SEYESLISKH GTLKSAHKNL EVEHRDLEDR 
      1210       1220       1230       1240       1250
YNQLLKQKGQ LEDLEKMLKV EQEKMLLENK NHETVAAEYK KLCGENDRLN 
      1260       1270       1280       1290       1300
HTYSQLLKET EVLQTDHKNL KSLLNNSKLE QTRLEAEFSK LKEQYQQLDI 
      1310       1320       1330       1340       1350
TSTKLNNQCE LLSQLKGNLE EENRHLLDQI QTLMLQNRTL LEQNMESKDL 
      1360       1370       1380       1390       1400
FHVEQRQYID KLNELRRQKE KLEEKIMDQY KFYDPSPPRR RGNWITLKMR 
      1410       1420       1430       1440       1450
KLIKSKKDIN RERQKSLTLT PTRSDSSEGF LQLPHQDSQD SSSVGSNSLE 
      1460       1470       1480       1490       1500
DGQTLGTKKS SMVALKRLPF LRNRPKDKDK MKACYRRSMS MNDLVQSMVL 
      1510       1520       1530       1540       1550
AGQWTGSTEN LEVPDDISTG KRRKELGAMA FSTTAINFST VNSSAGFRSK 
      1560       1570       1580       1590       1600
QLVNNKDTTS FEDISPQGVS DDSSTGSRVH ASRPASLDSG RTSTSNSNNN 
      1610       1620       1630       1640       1650
ASLHEVKAGA VNNQSRPQSH SSGEFSLLHD HEAWSSSGSS PIQYLKRQTR 
      1660       1670       1680       1690       1700
SSPVLQHKIS ETLESRHHKI KTGSPGSEVV TLQQFLEESN KLTSVQIKSS 
      1710       1720       1730       1740       1750
SQENLLDEVM KSLSVSSDFL GKDKPVSCGL ARSVSGKTPG DFYDRRTTKP 
      1760       1770       1780       1790       1800
EFLRPGPRKT EDTYFISSAG KPTPGTQGKI KLVKESSLSR QSKDSNPYAT 
      1810       1820       1830       1840       1850
LPRASSVIST AEGTTRRTSI HDFLTKDSRL PISVDSPPAA ADSNTTAASN 
      1860       1870
VDKVQESRNS KSRSREQQSS                                  

        10         20         30         40         50
MENEIFTPLL EQFMTSPLVT WVKTFGPLAA GNGTNLDEYV ALVDGVFLNQ 
        60         70         80         90        100
VMLQINPKLE SQRVNKKVNN DASLRMHNLS ILVRQIKFYY QETLQQLIMM 
       110        120        130        140        150
SLPNVLIIGK NPFSEQGTEE VKKLLLLLLG CAVQCQKKEE FIERIQGLDF 
       160        170        180        190        200
DTKAAVAAHI QEVTHNQENV FDLQWMEVTD MSQEDIEPLL KNMALHLKRL 
       210        220        230        240        250
IDERDEHSET IIELSEERDG LHFLPHASSS AQSPCGSPGM KRTESRQHLS 
       260        270        280        290        300
VELADAKAKI RRLRQELEEK TEQLLDCKQE LEQMEIELKR LQQENMNLLS 
       310        320        330        340        350
DARSARMYRD ELDALREKAV RVDKLESEVS RYKERLHDIE FYKARVEELK 
       360        370        380        390        400
EDNQVLLETK TMLEDQLEGT RARSDKLHEL EKENLQLKAK LHDMEMERDM 
       410        420        430        440        450
DRKKIEELME ENMTLEMAQK QSMDESLHLG WELEQISRTS ELSEAPQKSL 
       460        470        480        490        500
GHEVNELTSS RLLKLEMENQ SLTKTVEELR TTVDSVEGNA SKILKMEKEN 
       510        520        530        540        550
QRLSKKVEIL ENEIVQEKQS LQNCQNLSKD LMKEKAQLEK TIETLRENSE 
       560        570        580        590        600
RQIKILEQEN EHLNQTVSSL RQRSQISAEA RVKDIEKENK ILHESIKETS 
       610        620        630        640        650
SKLSKIEFEK RQIKKELEHY KEKGERAEEL ENELHHLEKE NELLQKKITN 
       660        670        680        690        700
LKITCEKIEA LEQENSELER ENRKLKKTLD SFKNLTFQLE SLEKENSQLD 
       710        720        730        740        750
EENLELRRNV ESLKCASMKM AQLQLENKEL ESEKEQLKKG LELLKASFKK 
       760        770        780        790        800
TERLEVSYQG LDIENQRLQK TLENSNKKIQ QLESELQDLE MENQTLQKNL 
       810        820        830        840        850
EELKISSKRL EQLEKENKSL EQETSQLEKD KKQLEKENKR LRQQAEIKDT 
       860        870        880        890        900
TLEENNVKIG NLEKENKTLS KEIGIYKESC VRLKELEKEN KELVKRATID 
       910        920        930        940        950
IKTLVTLRED LVSEKLKTQQ MNNDLEKLTH ELEKIGLNKE RLLHDEQSTD 
       960        970        980        990       1000
DRYKLLESKL ESTLKKSLEI KEEKIAALEA RLEESTNYNQ QLRQELKTVK 
      1010       1020       1030       1040       1050
KNYEALKQRQ DEERMVQSSP PISGEDNKWE RESQETTREL LKVKDRLIEV 
      1060       1070       1080       1090       1100
ERNNATLQAE KQALKTQLKQ LETQNNNLQA QILALQRQTV SLQEQNTTLQ 
      1110       1120       1130       1140       1150
TQNAKLQVEN STLNSQSTSL MNQNAQLLIQ QSSLENENES VIKEREDLKS 
      1160       1170       1180       1190       1200
LYDSLIKDHE KLELLHERQA SEYESLISKH GTLKSAHKNL EVEHRDLEDR 
      1210       1220       1230       1240       1250
YNQLLKQKGQ LEDLEKMLKV EQEKMLLENK NHETVAAEYK KLCGENDRLN 
      1260       1270       1280       1290       1300
HTYSQLLKET EVLQTDHKNL KSLLNNSKLE QTRLEAEFSK LKEQYQQLDI 
      1310       1320       1330       1340       1350
TSTKLNNQCE LLSQLKGNLE EENRHLLDQI QTLMLQNRTL LEQNMESKDL 
      1360       1370       1380       1390       1400
FHVEQRQYID KLNELRRQKE KLEEKIMDQY KFYDPSPPRR RGNWITLKMR 
      1410       1420       1430       1440       1450
KLIKSKKDIN RERQKSLTLT PTRSDSSEGF LQLPHQDSQD SSSVGSNSLE 
      1460       1470       1480       1490       1500
DGQTLGTKKS STMNDLVQSM VLAGQWTGST ENLEVPDDIS TGKRRKELGA 
      1510       1520       1530       1540       1550
MAFSTTAINF STVNSSAGFR SKQLVNNKDT TSFEDISPQG VSDDSSTGSR 
      1560       1570       1580       1590       1600
VHASRPASLD SGRTSTSNSN NNASLHEVKA GAVNNQSRPQ SHSSGEFSLL 
      1610       1620       1630       1640       1650
HDHEAWSSSG SSPIQYLKRQ TRSSPVLQHK ISETLESRHH KIKTGSPGSE 
      1660       1670       1680       1690       1700
VVTLQQFLEE SNKLTSVQIK SSSQENLLDE VMKSLSVSSD FLGKDKPVSC 
      1710       1720       1730       1740       1750
GLARSVSGKT PGDFYDRRTT KPEFLRPGPR KTEDTYFISS AGKPTPGTQG 
      1760       1770       1780       1790       1800
KIKLVKESSL SRQSKDSNPY ATLPRASSVI STAEGTTRRT SIHDFLTKDS 
      1810       1820       1830       1840 
RLPISVDSPP AAADSNTTAA SNVDKVQESR NSKSRSREQQ SS         

        10         20         30         40         50
MENEIFTPLL EQFMTSPLVT WVKTFGPLAA GNGTNLDEYV ALVDGVFLNQ 
        60         70         80         90        100
VMLQINPKLE SQRVNKKVNN DASLRMHNLS ILVRQIKFYY QETLQQLIMM 
       110        120        130        140        150
SLPNVLIIGK NPFSEQGTEE VKKLLLLLLG CAVQCQKKEE FIERIQGLDF 
       160        170        180        190        200
DTKAAVAAHI QEVTHNQENV FDLQWMEVTD MSQEDIEPLL KNMALHLKRL 
       210        220        230        240        250
IDERDEHSET IIELSEERDG LHFLPHASSS AQSPCGSPGM KRTESRQHLS 
       260        270        280        290        300
VELADAKAKI RRLRQELEEK TEQLLDCKQE LEQMEIELKR LQQENMNLLS 
       310        320        330        340        350
DARSARMYRD ELDALREKAV RVDKLESEVS RYKERLHDIE FYKARVEELK 
       360        370        380        390        400
EDNQVLLETK TMLEDQLEGT RARSDKLHEL EKENLQLKAK LHDMEMERDM 
       410        420        430        440        450
DRKKIEELME ENMTLEMAQK QSMDESLHLG WELEQISRTS ELSEAPQKSL 
       460        470        480        490        500
GHEVNELTSS RLLKLEMENQ SLTKTVEELR TTVDSVEGNA SKILKMEKEN 
       510        520        530        540        550
QRLSKKVEIL ENEIVQEKQS LQNCQNLSKD LMKEKAQLEK TIETLRENSE 
       560        570        580        590        600
RQIKILEQEN EHLNQTVSSL RQRSQISAEA RVKDIEKENK ILHESIKETS 
       610        620        630        640        650
SKLSKIEFEK RQIKKELEHY KEKGERAEEL ENELHHLEKE NELLQKKITN 
       660        670        680        690        700
LKITCEKIEA LEQENSELER ENRKLKKTLD SFKNLTFQLE SLEKENSQLD 
       710        720        730        740        750
EENLELRRNV ESLKCASMKM AQLQLENKEL ESEKEQLKKG LELLKASFKK 
       760        770        780        790        800
TERLEVSYQG LDIENQRLQK TLENSNKKIQ QLESELQDLE MENQTLQKNL 
       810        820        830        840        850
EELKISSKRL EQLEKENKSL EQETSQLEKD KKQLEKENKR LRQQAEIKDT 
       860        870        880        890        900
TLEENNVKIG NLEKENKTLS KEIGIYKESC VRLKELEKEN KELVKRATID 
       910        920        930        940        950
IKTLVTLRED LVSEKLKTQQ MNNDLEKLTH ELEKIGLNKE RLLHDEQSTD 
       960        970        980        990       1000
DRYKLLESKL ESTLKKSLEI KEEKIAALEA RLEESTNYNQ QLRQELKTVK 
      1010       1020       1030       1040       1050
KNYEALKQRQ DEERMVQSSP PISGEDNKWE RESQETTREL LKVKDRLIEV 
      1060       1070       1080       1090       1100
ERNNATLQAE KQALKTQLKQ LETQNNNLQA QILALQRQTV SLQEQNTTLQ 
      1110       1120       1130       1140       1150
TQNAKLQVEN STLNSQSTSL MNQNAQLLIQ QSSLENENES VIKEREDLKS 
      1160       1170       1180       1190       1200
LYDSLIKDHE KLELLHERQA SEYESLISKH GTLKSAHKNL EVEHRDLEDR 
      1210       1220       1230       1240       1250
YNQLLKQKGQ LEDLEKMLKV EQEKMLLENK NHETVAAEYK KLCGENDRLN 
      1260       1270       1280       1290       1300
HTYSQLLKET EVLQTDHKNL KSLLNNSKLE QTRLEAEFSK LKEQYQQLDI 
      1310       1320       1330       1340       1350
TSTKLNNQCE LLSQLKGNLE EENRHLLDQI QTLMLQNRTL LEQNMESKDL 
      1360       1370       1380       1390       1400
FHVEQRQYID KLNELRRQKE KLEEKIMDQY KFYDPSPPRR RGNWITLKMR 
      1410       1420       1430       1440       1450
KLIKSKKDIN RERQKSLTLT PTRSDSSEGF LQLPHQDSQD SSSVGSNSLE 
      1460       1470       1480       1490       1500
DGQTLGTKKS SMVALKRLPF LRNRPKDKDK MKACYRRSMS MNDLVQSMVL 
      1510       1520       1530       1540       1550
AGQWTGSTEN LEVPDDISTG KRRKELGAMA FSTTAINFST VNSSAGFRSK 
      1560       1570       1580       1590       1600
QLVNNKDTTS FEDISPQGVS DDSSTGSRVH ASRPASLDSG RTSTSNSNNN 
      1610       1620       1630       1640       1650
ASLHEVKAGA VNNQSRPQSH SSGEFSLLHD HEAWSSSGSS PIQYLKRQTR 
      1660       1670       1680       1690       1700
SSPVLQHKIS ETLESRHHKI KTGSPGSEVV TLQQFLEESN KLTSVQIKSS 
      1710       1720       1730       1740       1750
SQENLLDEVM KSLSVSSDFL GKDKPVSCGL ASVISTAEGT TRRTSIHDFL 
      1760       1770       1780       1790 
TKDSRLPISV DSPPAAADSN TTAASNVDKV QESRNSKSRS REQQSS     

<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

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