IGFBP5

Protein-coding gene in the species Homo sapiens
IGFBP5
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1BOE, 1H59

Identifiers
AliasesIGFBP5, IBP5, insulin like growth factor binding protein 5
External IDsOMIM: 146734 MGI: 96440 HomoloGene: 56489 GeneCards: IGFBP5
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for IGFBP5
Genomic location for IGFBP5
Band2q35Start216,672,105 bp[1]
End216,695,549 bp[1]
Gene location (Mouse)
Chromosome 1 (mouse)
Chr.Chromosome 1 (mouse)[2]
Chromosome 1 (mouse)
Genomic location for IGFBP5
Genomic location for IGFBP5
Band1 C3|1 36.94 cMStart72,897,091 bp[2]
End72,914,043 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • renal medulla

  • urethra

  • saphenous vein

  • nipple

  • vena cava

  • cardia

  • pylorus

  • canal of the cervix

  • left uterine tube

  • synovial joint
Top expressed in
  • ciliary body

  • external carotid artery

  • molar

  • saccule

  • extraocular muscle

  • ankle

  • otic placode

  • internal carotid artery

  • pituitary gland

  • median eminence
More reference expression data
BioGPS




More reference expression data
Gene ontology
Molecular function
  • fibronectin binding
  • insulin-like growth factor binding
  • growth factor binding
  • insulin-like growth factor I binding
  • insulin-like growth factor II binding
  • protein binding
Cellular component
  • insulin-like growth factor ternary complex
  • extracellular region
  • insulin-like growth factor binding protein complex
  • endoplasmic reticulum lumen
  • extracellular space
Biological process
  • negative regulation of smooth muscle cell proliferation
  • negative regulation of translation
  • positive regulation of protein kinase B signaling
  • intracellular signal transduction
  • negative regulation of growth
  • glucose homeostasis
  • female pregnancy
  • cellular response to organic cyclic compound
  • negative regulation of smooth muscle cell migration
  • negative regulation of osteoblast differentiation
  • regulation of glucose metabolic process
  • negative regulation of cell migration
  • positive regulation of insulin-like growth factor receptor signaling pathway
  • regulation of cell growth
  • osteoblast differentiation
  • response to growth hormone
  • glucose metabolic process
  • negative regulation of insulin-like growth factor receptor signaling pathway
  • hair follicle morphogenesis
  • regulation of growth
  • negative regulation of muscle tissue development
  • striated muscle cell differentiation
  • lung alveolus development
  • negative regulation of skeletal muscle hypertrophy
  • type B pancreatic cell proliferation
  • cellular response to cAMP
  • signal transduction
  • mammary gland involution
  • human ageing
  • post-translational protein modification
  • positive regulation of vascular associated smooth muscle cell proliferation
  • positive regulation of vascular associated smooth muscle cell migration
  • regulation of insulin-like growth factor receptor signaling pathway
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

3488

16011

Ensembl

ENSG00000115461

ENSMUSG00000026185

UniProt

P24593

Q07079

RefSeq (mRNA)

NM_000599

NM_010518

RefSeq (protein)

NP_000590

NP_034648

Location (UCSC)Chr 2: 216.67 – 216.7 MbChr 1: 72.9 – 72.91 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Insulin-like growth factor-binding protein 5 (IBF-5) is a protein that in humans is encoded by the IGFBP5 gene.[5] An IGFBP5 gene was recently identified as being important for adaptation to varying water salinity in fish.[6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000115461 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026185 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Allander SV, Larsson C, Ehrenborg E, Suwanichkul A, Weber G, Morris SL, Bajalica S, Kiefer MC, Luthman H, Powell DR (May 1994). "Characterization of the chromosomal gene and promoter for human insulin-like growth factor binding protein-5". J Biol Chem. 269 (14): 10891–8. doi:10.1016/S0021-9258(17)34142-X. PMID 7511611.
  6. ^ Kusakabe M, Ishikawa A, Ravinet M, Yoshida K, Makino T, Toyoda A, Fujiyama A, Kitano J (2017). "Genetic basis for variation in salinity tolerance between stickleback ecotypes". Molecular Ecology. 26 (1): 304–319. Bibcode:2017MolEc..26..304K. doi:10.1111/mec.13875. PMID 27706866. S2CID 7821799.

Further reading

  • Mohan S, Farley JR, Baylink DJ (1996). "Age-related changes in IGFBP-4 and IGFBP-5 levels in human serum and bone: implications for bone loss with aging". Prog. Growth Factor Res. 6 (2–4): 465–73. doi:10.1016/0955-2235(95)00027-5. PMID 8817691.
  • Schneider MR, Wolf E, Hoeflich A, Lahm H (2002). "IGF-binding protein-5: flexible player in the IGF system and effector on its own". J. Endocrinol. 172 (3): 423–40. doi:10.1677/joe.0.1720423. PMID 11874691.
  • Firth SM, Baxter RC (2003). "Cellular actions of the insulin-like growth factor binding proteins". Endocr. Rev. 23 (6): 824–54. doi:10.1210/er.2001-0033. PMID 12466191.
  • Shimasaki S, Shimonaka M, Zhang HP, Ling N (1991). "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". J. Biol. Chem. 266 (16): 10646–53. doi:10.1016/S0021-9258(18)99272-0. PMID 1709938.
  • Ehrenborg E, Vilhelmsdotter S, Bajalica S, et al. (1991). "Structure and localization of the human insulin-like growth factor-binding protein 2 gene". Biochem. Biophys. Res. Commun. 176 (3): 1250–5. doi:10.1016/0006-291X(91)90420-C. PMID 1710112.
  • Andress DL, Birnbaum RS (1991). "A novel human insulin-like growth factor binding protein secreted by osteoblast-like cells". Biochem. Biophys. Res. Commun. 176 (1): 213–8. doi:10.1016/0006-291X(91)90911-P. PMID 1850257.
  • Kiefer MC, Ioh RS, Bauer DM, Zapf J (1991). "Molecular cloning of a new human insulin-like growth factor binding protein". Biochem. Biophys. Res. Commun. 176 (1): 219–25. doi:10.1016/0006-291X(91)90912-Q. PMID 1850258.
  • Ilvesmäki V, Blum WF, Voutilainen R (1994). "Insulin-like growth factor binding proteins in the human adrenal gland". Mol. Cell. Endocrinol. 97 (1–2): 71–9. doi:10.1016/0303-7207(93)90212-3. PMID 7511544. S2CID 22503525.
  • Kou K, James PL, Clemmons DR, et al. (1994). "Identification of two clusters of mouse insulin-like growth factor binding protein genes on chromosomes 1 and 11". Genomics. 21 (3): 653–5. doi:10.1006/geno.1994.1329. PMID 7525452.
  • Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
  • Yu W, Andersson B, Worley KC, et al. (1997). "Large-Scale Concatenation cDNA Sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
  • Nam TJ, Busby W, Clemmons DR (1997). "Insulin-like growth factor binding protein-5 binds to plasminogen activator inhibitor-I". Endocrinology. 138 (7): 2972–8. doi:10.1210/endo.138.7.5230. PMID 9202242.
  • Twigg SM, Baxter RC (1998). "Insulin-like growth factor (IGF)-binding protein 5 forms an alternative ternary complex with IGFs and the acid-labile subunit". J. Biol. Chem. 273 (11): 6074–9. doi:10.1074/jbc.273.11.6074. PMID 9497324.
  • Zheng B, Clarke JB, Busby WH, et al. (1998). "Insulin-like growth factor-binding protein-5 is cleaved by physiological concentrations of thrombin". Endocrinology. 139 (4): 1708–14. doi:10.1210/endo.139.4.5945. PMID 9528953.
  • Twigg SM, Kiefer MC, Zapf J, Baxter RC (1998). "Insulin-like growth factor-binding protein 5 complexes with the acid-labile subunit. Role of the carboxyl-terminal domain". J. Biol. Chem. 273 (44): 28791–8. doi:10.1074/jbc.273.44.28791. PMID 9786878.
  • Kalus W, Zweckstetter M, Renner C, et al. (1999). "Structure of the IGF-binding domain of the insulin-like growth factor-binding protein-5 (IGFBP-5): implications for IGF and IGF-I receptor interactions". EMBO J. 17 (22): 6558–72. doi:10.1093/emboj/17.22.6558. PMC 1171003. PMID 9822601.
  • Ständker L, Wobst P, Mark S, Forssmann WG (1999). "Isolation and characterization of circulating 13-kDa C-terminal fragments of human insulin-like growth factor binding protein-5". FEBS Lett. 441 (2): 281–6. doi:10.1016/S0014-5793(98)01497-5. PMID 9883900. S2CID 23392744.
  • Kecha O, Martens H, Franchimont N, et al. (1999). "Characterization of the insulin-like growth factor axis in the human thymus". J. Neuroendocrinol. 11 (6): 435–40. doi:10.1046/j.1365-2826.1999.00343.x. PMID 10336724. S2CID 36605514.
  • v
  • t
  • e
  • 1boe: STRUCTURE OF THE IGF BINDING DOMAIN OF THE INSULIN-LIKE GROWTH FACTOR-BINDING PROTEIN-5 (IGFBP-5): IMPLICATIONS FOR IGF AND IGF-I RECEPTOR INTERACTIONS
    1boe: STRUCTURE OF THE IGF BINDING DOMAIN OF THE INSULIN-LIKE GROWTH FACTOR-BINDING PROTEIN-5 (IGFBP-5): IMPLICATIONS FOR IGF AND IGF-I RECEPTOR INTERACTIONS
  • 1h59: COMPLEX OF IGFBP-5 WITH IGF-I
    1h59: COMPLEX OF IGFBP-5 WITH IGF-I
  • v
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Fatty acid
Hormone
Metal/element
Vitamin
Pigment
Other
  • v
  • t
  • e
Angiopoietin
  • Kinase inhibitors: Altiratinib
  • CE-245677
  • Rebastinib
CNTF
EGF (ErbB)
EGF
(ErbB1/HER1)
ErbB2/HER2
  • Agonists: Unknown/none
ErbB3/HER3
ErbB4/HER4
FGF
FGFR1
FGFR2
  • Antibodies: Aprutumab
  • Aprutumab ixadotin
FGFR3
FGFR4
Unsorted
HGF (c-Met)
IGF
IGF-1
  • Kinase inhibitors: BMS-754807
  • Linsitinib
  • NVP-ADW742
  • NVP-AEW541
  • OSl-906
IGF-2
  • Antibodies: Dusigitumab
  • Xentuzumab (against IGF-1 and IGF-2)
Others
  • Cleavage products/derivatives with unknown target: Glypromate (GPE, (1-3)IGF-1)
  • Trofinetide
LNGF (p75NTR)
  • Aptamers: Against NGF: RBM-004
  • Decoy receptors: LEVI-04 (p75NTR-Fc)
PDGF
RET (GFL)
GFRα1
GFRα2
GFRα3
GFRα4
Unsorted
  • Kinase inhibitors: Agerafenib
SCF (c-Kit)
TGFβ
  • See here instead.
Trk
TrkA
  • Negative allosteric modulators: VM-902A
  • Aptamers: Against NGF: RBM-004
  • Decoy receptors: ReN-1820 (TrkAd5)
TrkB
TrkC
VEGF
Others


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