Insulin-like growth factor-binding protein 5

<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

• fibronectin binding Source: RGDInferred from sequence orthologyⁱ
  • "IGFBP-3 and IGFBP-5 associate with the cell binding domain (CBD) of fibronectin."
    Beattie J., Kreiner M., Allan G.J., Flint D.J., Domingues D., van der Walle C.F.
    Biochem. Biophys. Res. Commun. 381:572-576(2009) [PubMed] [Europe PMC] [Abstract]
• insulin-like growth factor binding Source: RGD <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

    "Identification of five different insulin-like growth factor binding proteins (IGFBPs) from adult rat serum and molecular cloning of a novel IGFBP-5 in rat and human."
    Shimasaki S., Shimonaka M., Zhang H.-P., Ling N.
    J. Biol. Chem. 266:10646-10653(1991) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-53.
• insulin-like growth factor I binding Source: RGDInferred from sequence orthologyⁱ
  • "Substitutions for hydrophobic amino acids in the N-terminal domains of IGFBP-3 and -5 markedly reduce IGF-I binding and alter their biologic actions."
    Imai Y., Moralez A., Andag U., Clarke J.B., Busby W.H. Jr., Clemmons D.R.
    J. Biol. Chem. 275:18188-18194(2000) [PubMed] [Europe PMC] [Abstract]
• insulin-like growth factor II 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. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• aging Source: RGD <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
  • "Skeletal muscle IGF-binding protein-3 and -5 expressions are age, muscle, and load dependent."
    Spangenburg E.E., Abraha T., Childs T.E., Pattison J.S., Booth F.W.
    Am. J. Physiol. Endocrinol. Metab. 284:E340-50(2003) [PubMed] [Europe PMC] [Abstract]
• cellular response to cAMP Source: RGDInferred from sequence orthologyⁱ
  • "Transcription factor AP-2 regulates human insulin-like growth factor binding protein-5 gene expression."
    Duan C., Clemmons D.R.
    J. Biol. Chem. 270:24844-24851(1995) [PubMed] [Europe PMC] [Abstract]
• cellular response to organic cyclic compound Source: RGDInferred from sequence orthologyⁱ
  • "Transcription factor AP-2 regulates human insulin-like growth factor binding protein-5 gene expression."
    Duan C., Clemmons D.R.
    J. Biol. Chem. 270:24844-24851(1995) [PubMed] [Europe PMC] [Abstract]
• female pregnancy Source: RGDInferred from sequence orthologyⁱ
  • "Insulin-like growth factor-binding protein 5 (Igfbp5) compromises survival, growth, muscle development, and fertility in mice."
    Salih D.A., Tripathi G., Holding C., Szestak T.A., Gonzalez M.I., Carter E.J., Cobb L.J., Eisemann J.E., Pell J.M.
    Proc. Natl. Acad. Sci. U.S.A. 101:4314-4319(2004) [PubMed] [Europe PMC] [Abstract]
• glucose homeostasis Source: RGDInferred from sequence orthologyⁱ
  • "Diminished growth and enhanced glucose metabolism in triple knockout mice containing mutations of insulin-like growth factor binding protein-3, -4, and -5."
    Ning Y., Schuller A.G., Bradshaw S., Rotwein P., Ludwig T., Frystyk J., Pintar J.E.
    Mol. Endocrinol. 20:2173-2186(2006) [PubMed] [Europe PMC] [Abstract]
  • "Role of insulin-like growth factor-binding protein 5 (IGFBP5) in organismal and pancreatic beta-cell growth."
    Gleason C.E., Ning Y., Cominski T.P., Gupta R., Kaestner K.H., Pintar J.E., Birnbaum M.J.
    Mol. Endocrinol. 24:178-192(2010) [PubMed] [Europe PMC] [Abstract]
• hair follicle morphogenesis Source: RGDInferred from sequence orthologyⁱ
  • "Segmental Igfbp5 expression is specifically associated with the bent structure of zigzag hairs."
    Schlake T.
    Mech. Dev. 122:988-997(2005) [PubMed] [Europe PMC] [Abstract]
• intracellular signal transduction Source: RGDInferred from expression patternⁱ
  • "Regulation of granulosa cell-derived insulin-like growth factor binding proteins (IGFBPs): role for protein kinase-C in the pre- and posttranslational modulation of IGFBP-4 and IGFBP-5."
    Chamoun D., Choi D., Tavares A.B., Udoff L.C., Levitas E., Resnick C.E., Rosenfeld R.G., Adashi E.Y.
    Biol. Reprod. 67:1003-1012(2002) [PubMed] [Europe PMC] [Abstract]
• lung alveolus development Source: RGDInferred from sequence orthologyⁱ
  • "Insulin-like growth factor-binding protein 5 (Igfbp5) compromises survival, growth, muscle development, and fertility in mice."
    Salih D.A., Tripathi G., Holding C., Szestak T.A., Gonzalez M.I., Carter E.J., Cobb L.J., Eisemann J.E., Pell J.M.
    Proc. Natl. Acad. Sci. U.S.A. 101:4314-4319(2004) [PubMed] [Europe PMC] [Abstract]
• mammary gland involution Source: RGDInferred from sequence orthologyⁱ
  • "Delayed mammary gland involution in mice with mutation of the insulin-like growth factor binding protein 5 gene."
    Ning Y., Hoang B., Schuller A.G., Cominski T.P., Hsu M.S., Wood T.L., Pintar J.E.
    Endocrinology 148:2138-2147(2007) [PubMed] [Europe PMC] [Abstract]
• negative regulation of cell migration Source: RGDInferred from sequence orthologyⁱ
  • "Insulin-like growth factor binding protein-5 (IGFBP-5) interacts with thrombospondin-1 to induce negative regulatory effects on IGF-I actions."
    Moralez A.M., Maile L.A., Clarke J., Busby W.H. Jr., Clemmons D.R.
    J. Cell. Physiol. 203:328-334(2005) [PubMed] [Europe PMC] [Abstract]
• negative regulation of growth Source: RGDInferred from sequence orthologyⁱ
  • "Insulin-like growth factor-binding protein 5 (Igfbp5) compromises survival, growth, muscle development, and fertility in mice."
    Salih D.A., Tripathi G., Holding C., Szestak T.A., Gonzalez M.I., Carter E.J., Cobb L.J., Eisemann J.E., Pell J.M.
    Proc. Natl. Acad. Sci. U.S.A. 101:4314-4319(2004) [PubMed] [Europe PMC] [Abstract]
• negative regulation of insulin-like growth factor receptor signaling pathway Source: RGDInferred from sequence orthologyⁱ
  • "Substitutions for hydrophobic amino acids in the N-terminal domains of IGFBP-3 and -5 markedly reduce IGF-I binding and alter their biologic actions."
    Imai Y., Moralez A., Andag U., Clarke J.B., Busby W.H. Jr., Clemmons D.R.
    J. Biol. Chem. 275:18188-18194(2000) [PubMed] [Europe PMC] [Abstract]
  • "Segmental Igfbp5 expression is specifically associated with the bent structure of zigzag hairs."
    Schlake T.
    Mech. Dev. 122:988-997(2005) [PubMed] [Europe PMC] [Abstract]
• negative regulation of muscle tissue development Source: RGDInferred from sequence orthologyⁱ
  • "Insulin-like growth factor-binding protein 5 (Igfbp5) compromises survival, growth, muscle development, and fertility in mice."
    Salih D.A., Tripathi G., Holding C., Szestak T.A., Gonzalez M.I., Carter E.J., Cobb L.J., Eisemann J.E., Pell J.M.
    Proc. Natl. Acad. Sci. U.S.A. 101:4314-4319(2004) [PubMed] [Europe PMC] [Abstract]
• negative regulation of osteoblast differentiation Source: RGDInferred from sequence orthologyⁱ
  • "Akt promotes BMP2-mediated osteoblast differentiation and bone development."
    Mukherjee A., Rotwein P.
    J. Cell. Sci. 122:716-726(2009) [PubMed] [Europe PMC] [Abstract]
• negative regulation of skeletal muscle hypertrophy Source: RGDInferred from sequence orthologyⁱ
  • "Insulin-like growth factor-binding protein 5 (Igfbp5) compromises survival, growth, muscle development, and fertility in mice."
    Salih D.A., Tripathi G., Holding C., Szestak T.A., Gonzalez M.I., Carter E.J., Cobb L.J., Eisemann J.E., Pell J.M.
    Proc. Natl. Acad. Sci. U.S.A. 101:4314-4319(2004) [PubMed] [Europe PMC] [Abstract]
• negative regulation of smooth muscle cell migration Source: RGDInferred from sequence orthologyⁱ
  • "Substitutions for hydrophobic amino acids in the N-terminal domains of IGFBP-3 and -5 markedly reduce IGF-I binding and alter their biologic actions."
    Imai Y., Moralez A., Andag U., Clarke J.B., Busby W.H. Jr., Clemmons D.R.
    J. Biol. Chem. 275:18188-18194(2000) [PubMed] [Europe PMC] [Abstract]
• negative regulation of smooth muscle cell proliferation Source: RGDInferred from sequence orthologyⁱ
  • "Substitutions for hydrophobic amino acids in the N-terminal domains of IGFBP-3 and -5 markedly reduce IGF-I binding and alter their biologic actions."
    Imai Y., Moralez A., Andag U., Clarke J.B., Busby W.H. Jr., Clemmons D.R.
    J. Biol. Chem. 275:18188-18194(2000) [PubMed] [Europe PMC] [Abstract]
• negative regulation of translation Source: RGDInferred from sequence orthologyⁱ
  • "Insulin-like growth factor binding protein-5 (IGFBP-5) interacts with thrombospondin-1 to induce negative regulatory effects on IGF-I actions."
    Moralez A.M., Maile L.A., Clarke J., Busby W.H. Jr., Clemmons D.R.
    J. Cell. Physiol. 203:328-334(2005) [PubMed] [Europe PMC] [Abstract]
• osteoblast differentiation Source: RGDInferred from sequence orthologyⁱ
  • "Regulation of insulin-like growth factor binding protein-5, four and a half lim-2, and a disintegrin and metalloprotease-9 expression in osteoblasts."
    Govoni K.E., Amaar Y.G., Kramer A., Winter E., Baylink D.J., Mohan S.
    Growth Horm. IGF Res. 16:49-56(2006) [PubMed] [Europe PMC] [Abstract]
• positive regulation of insulin-like growth factor receptor signaling pathway Source: RGDInferred from sequence orthologyⁱ
  • "Diminished growth and enhanced glucose metabolism in triple knockout mice containing mutations of insulin-like growth factor binding protein-3, -4, and -5."
    Ning Y., Schuller A.G., Bradshaw S., Rotwein P., Ludwig T., Frystyk J., Pintar J.E.
    Mol. Endocrinol. 20:2173-2186(2006) [PubMed] [Europe PMC] [Abstract]
• positive regulation of protein kinase B signaling Source: RGDInferred from sequence orthologyⁱ
  • "IGFBP-5 regulates muscle cell differentiation by binding to IGF-II and switching on the IGF-II auto-regulation loop."
    Ren H., Yin P., Duan C.
    J. Cell Biol. 182:979-991(2008) [PubMed] [Europe PMC] [Abstract]
• positive regulation of vascular associated smooth muscle cell migration Source: RGDInferred from sequence orthologyⁱ
  • "MiR-137 inhibited cell proliferation and migration of vascular smooth muscle cells via targeting IGFBP-5 and modulating the mTOR/STAT3 signaling."
    Pan J., Li K., Huang W., Zhang X.
    PLoS ONE 12:e0186245-e0186245(2017) [PubMed] [Europe PMC] [Abstract]
• positive regulation of vascular associated smooth muscle cell proliferation Source: RGDInferred from sequence orthologyⁱ
  • "MiR-137 inhibited cell proliferation and migration of vascular smooth muscle cells via targeting IGFBP-5 and modulating the mTOR/STAT3 signaling."
    Pan J., Li K., Huang W., Zhang X.
    PLoS ONE 12:e0186245-e0186245(2017) [PubMed] [Europe PMC] [Abstract]
• regulation of cell growth Source: RGDInferred from sequence orthologyⁱ
  • "Diminished growth and enhanced glucose metabolism in triple knockout mice containing mutations of insulin-like growth factor binding protein-3, -4, and -5."
    Ning Y., Schuller A.G., Bradshaw S., Rotwein P., Ludwig T., Frystyk J., Pintar J.E.
    Mol. Endocrinol. 20:2173-2186(2006) [PubMed] [Europe PMC] [Abstract]
• regulation of growth Source: RGDInferred from sequence orthologyⁱ
  • "Diminished growth and enhanced glucose metabolism in triple knockout mice containing mutations of insulin-like growth factor binding protein-3, -4, and -5."
    Ning Y., Schuller A.G., Bradshaw S., Rotwein P., Ludwig T., Frystyk J., Pintar J.E.
    Mol. Endocrinol. 20:2173-2186(2006) [PubMed] [Europe PMC] [Abstract]
• regulation of insulin-like growth factor receptor signaling pathway 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. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• response to growth hormone Source: AgBase
• striated muscle cell differentiation Source: RGDInferred from sequence orthologyⁱ
  • "IGFBP-5 regulates muscle cell differentiation by binding to IGF-II and switching on the IGF-II auto-regulation loop."
    Ren H., Yin P., Duan C.
    J. Cell Biol. 182:979-991(2008) [PubMed] [Europe PMC] [Abstract]
• type B pancreatic cell proliferation Source: RGDInferred from sequence orthologyⁱ
  • "Diminished growth and enhanced glucose metabolism in triple knockout mice containing mutations of insulin-like growth factor binding protein-3, -4, and -5."
    Ning Y., Schuller A.G., Bradshaw S., Rotwein P., Ludwig T., Frystyk J., Pintar J.E.
    Mol. Endocrinol. 20:2173-2186(2006) [PubMed] [Europe PMC] [Abstract]

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

Enzyme and pathway databases

Protein family/group databases

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

Organism-specific databases

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

Keywords - Cellular componentⁱ

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<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

<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

GO - Molecular functionⁱ

• fibronectin binding Source: RGDInferred from sequence orthologyⁱ
  • "IGFBP-3 and IGFBP-5 associate with the cell binding domain (CBD) of fibronectin."
    Beattie J., Kreiner M., Allan G.J., Flint D.J., Domingues D., van der Walle C.F.
    Biochem. Biophys. Res. Commun. 381:572-576(2009) [PubMed] [Europe PMC] [Abstract]
• insulin-like growth factor binding Source: RGDInferred from direct assayⁱ
  • Ref.1

    "Identification of five different insulin-like growth factor binding proteins (IGFBPs) from adult rat serum and molecular cloning of a novel IGFBP-5 in rat and human."
    Shimasaki S., Shimonaka M., Zhang H.-P., Ling N.
    J. Biol. Chem. 266:10646-10653(1991) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-53.
• insulin-like growth factor I binding Source: RGDInferred from sequence orthologyⁱ
  • "Substitutions for hydrophobic amino acids in the N-terminal domains of IGFBP-3 and -5 markedly reduce IGF-I binding and alter their biologic actions."
    Imai Y., Moralez A., Andag U., Clarke J.B., Busby W.H. Jr., Clemmons D.R.
    J. Biol. Chem. 275:18188-18194(2000) [PubMed] [Europe PMC] [Abstract]
• insulin-like growth factor II 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. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

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>Sequence (1+)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 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

        10         20         30         40         50
MVISVVLLLL AACAVPAQGL GSFVHCEPCD EKALSMCPPS PLGCELVKEP 
        60         70         80         90        100
GCGCCMTCAL AEGQSCGVYT ERCAQGLRCL PRQDEEKPLH ALLHGRGVCL 
       110        120        130        140        150
NEKSYGEQTK IERDSREHEE PTTSEMAEET YSPKVFRPKH TRISELKAEA 
       160        170        180        190        200
VKKDRRKKLT QSKFVGGAEN TAHPRVIPAP EMRQESDQGP CRRHMEASLQ 
       210        220        230        240        250
EFKASPRMVP RAVYLPNCDR KGFYKRKQCK PSRGRKRGIC WCVDKYGMKL 
       260        270 
PGMEYVDGDF QCHAFDSSNV E                                

Sequence databases

Genome annotation databases

<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

• 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

Protein family/group databases

PTM databases

Proteomic 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