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P05019 (IGF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 171. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Insulin-like growth factor I

Short name=IGF-I
Alternative name(s):
Mechano growth factor
Short name=MGF
Somatomedin-C
Gene names
Name:IGF1
Synonyms:IBP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length195 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. May be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. Stimulates glucose transport in rat bone-derived osteoblastic (PyMS) cells and is effective at much lower concentrations than insulin, not only regarding glycogen and DNA synthesis but also with regard to enhancing glucose uptake. May play a role in synapse maturation. Ref.17 Ref.18

Subcellular location

Secreted.

Involvement in disease

Insulin-like growth factor I deficiency (IGF1 deficiency) [MIM:608747]: Autosomal recessive disorder characterized by growth retardation, sensorineural deafness and mental retardation.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Sequence similarities

Belongs to the insulin family.

Sequence caution

The sequence CAA27250.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDeafness
   DomainSignal
   Molecular functionGrowth factor
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Traceable author statement PubMed 10766744. Source: ProtInc

Ras protein signal transduction

Traceable author statement PubMed 10848592. Source: ProtInc

Type I pneumocyte differentiation

Inferred from electronic annotation. Source: Ensembl

Type II pneumocyte differentiation

Inferred from electronic annotation. Source: Ensembl

blood coagulation

Traceable author statement. Source: Reactome

blood vessel remodeling

Inferred from electronic annotation. Source: Ensembl

bone mineralization involved in bone maturation

Inferred from direct assay PubMed 16433617. Source: BHF-UCL

branching morphogenesis of an epithelial tube

Inferred from electronic annotation. Source: Ensembl

cellular component movement

Traceable author statement PubMed 10766744. Source: ProtInc

cellular protein metabolic process

Traceable author statement. Source: Reactome

chondroitin sulfate proteoglycan biosynthetic process

Inferred from electronic annotation. Source: Ensembl

exocrine pancreas development

Inferred from electronic annotation. Source: Ensembl

extrinsic apoptotic signaling pathway in absence of ligand

Inferred from electronic annotation. Source: Ensembl

glial cell differentiation

Inferred from electronic annotation. Source: Ensembl

glycolate metabolic process

Traceable author statement PubMed 10448861. Source: ProtInc

inner ear development

Inferred from electronic annotation. Source: Ensembl

insulin-like growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

lung alveolus development

Inferred from electronic annotation. Source: Ensembl

lung lobe morphogenesis

Inferred from electronic annotation. Source: Ensembl

lung vasculature development

Inferred from electronic annotation. Source: Ensembl

mammary gland development

Inferred from electronic annotation. Source: Ensembl

multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

muscle hypertrophy

Inferred from mutant phenotype PubMed 10191278. Source: BHF-UCL

muscle organ development

Traceable author statement PubMed 10448861. Source: ProtInc

myoblast differentiation

Inferred from direct assay PubMed 17531227. Source: BHF-UCL

myoblast proliferation

Inferred from direct assay PubMed 17531227. Source: BHF-UCL

myotube cell development

Inferred from direct assay PubMed 17531227. Source: BHF-UCL

negative regulation of ERK1 and ERK2 cascade

Inferred from electronic annotation. Source: Ensembl

negative regulation of androgen receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of extrinsic apoptotic signaling pathway

Inferred from direct assay PubMed 16942485. Source: BHF-UCL

negative regulation of release of cytochrome c from mitochondria

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of smooth muscle cell apoptotic process

Inferred from direct assay PubMed 16942485. Source: BHF-UCL

phosphatidylinositol-mediated signaling

Inferred from direct assay PubMed 7692086. Source: BHF-UCL

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

positive regulation of DNA binding

Inferred from direct assay PubMed 19654000. Source: UniProtKB

positive regulation of DNA replication

Inferred from direct assay PubMed 7688386PubMed 9722506. Source: BHF-UCL

positive regulation of MAPK cascade

Inferred from direct assay PubMed 19654000. Source: UniProtKB

positive regulation of Ras protein signal transduction

Inferred from direct assay PubMed 9722506. Source: BHF-UCL

positive regulation of activated T cell proliferation

Inferred from direct assay PubMed 15694994. Source: BHF-UCL

positive regulation of calcineurin-NFAT signaling cascade

Inferred from direct assay PubMed 19654000. Source: UniProtKB

positive regulation of cardiac muscle hypertrophy

Inferred from direct assay PubMed 19654000. Source: UniProtKB

positive regulation of cell proliferation

Inferred from direct assay PubMed 12746903PubMed 9722506. Source: BHF-UCL

positive regulation of cerebellar granule cell precursor proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of epithelial cell proliferation

Inferred from direct assay PubMed 7188854. Source: BHF-UCL

positive regulation of fibroblast proliferation

Inferred from direct assay PubMed 7188854. Source: BHF-UCL

positive regulation of glucose import

Inferred from direct assay Ref.17. Source: UniProtKB

positive regulation of glycogen biosynthetic process

Inferred from direct assay Ref.17. Source: UniProtKB

positive regulation of glycolysis

Inferred from direct assay PubMed 7688386. Source: BHF-UCL

positive regulation of insulin-like growth factor receptor signaling pathway

Inferred from direct assay PubMed 10766744PubMed 7688386. Source: BHF-UCL

positive regulation of mitosis

Inferred from direct assay PubMed 10644978. Source: UniProtKB

positive regulation of myoblast proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of osteoblast differentiation

Inferred from direct assay PubMed 16433617. Source: BHF-UCL

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 7782332. Source: BHF-UCL

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from direct assay PubMed 7688386. Source: BHF-UCL

positive regulation of protein import into nucleus, translocation

Inferred from direct assay PubMed 19654000. Source: UniProtKB

positive regulation of protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

positive regulation of smooth muscle cell migration

Inferred from direct assay PubMed 10766744. Source: BHF-UCL

positive regulation of smooth muscle cell proliferation

Inferred from direct assay PubMed 10766744PubMed 16942485. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 16433617. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 19654000. Source: UniProtKB

positive regulation of tyrosine phosphorylation of Stat5 protein

Inferred from direct assay PubMed 9722506. Source: BHF-UCL

prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis

Inferred from electronic annotation. Source: Ensembl

prostate gland growth

Inferred from electronic annotation. Source: Ensembl

prostate gland stromal morphogenesis

Inferred from electronic annotation. Source: Ensembl

proteoglycan biosynthetic process

Inferred from direct assay PubMed 12746903. Source: BHF-UCL

regulation of establishment or maintenance of cell polarity

Inferred from electronic annotation. Source: Ensembl

regulation of multicellular organism growth

Inferred from expression pattern PubMed 8421089. Source: BHF-UCL

satellite cell maintenance involved in skeletal muscle regeneration

Inferred from direct assay PubMed 17531227. Source: BHF-UCL

signal transduction

Traceable author statement PubMed 10448861. Source: ProtInc

skeletal system development

Traceable author statement PubMed 10448861. Source: ProtInc

water homeostasis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular region

Non-traceable author statement PubMed 14718574. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 17119061PubMed 7188854. Source: BHF-UCL

insulin-like growth factor binding protein complex

Inferred by curator PubMed 10766744. Source: BHF-UCL

plasma membrane

Traceable author statement. Source: Reactome

platelet alpha granule lumen

Traceable author statement. Source: Reactome

   Molecular_functionhormone activity

Inferred from direct assay PubMed 7188854. Source: BHF-UCL

insulin receptor binding

Inferred from physical interaction PubMed 8452530. Source: BHF-UCL

insulin-like growth factor receptor binding

Inferred from physical interaction PubMed 8452530. Source: BHF-UCL

integrin binding

Inferred from direct assay PubMed 19578119. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P05019-1)

Also known as: IGF-IB;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P05019-2)

Also known as: IGF-IA;

The sequence of this isoform differs from the canonical sequence as follows:
     135-195: YQPPSTNKNT...NAECRGKKGK → EVHLKNASRGSAGNKNYRM
Isoform 3 (identifier: P05019-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: MGKISSLPTQLFKCCFCDFLK → MITPT
     135-195: YQPPSTNKNT...NAECRGKKGK → EVHLKNASRGSAGNKNYRM
Note: Expressed in liver.
Isoform 4 (identifier: P05019-4)

The sequence of this isoform differs from the canonical sequence as follows:
     152-195: WPKTHPGGEQKEGTEASLQIRGKKKEQRREIGSRNAECRGKKGK → STFEERK
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Propeptide22 – 4827
PRO_0000015663
Chain49 – 11870Insulin-like growth factor I
PRO_0000015664
Propeptide119 – 19577E peptide
PRO_0000015665

Regions

Region49 – 7729B
Region78 – 8912C
Region90 – 11021A
Region111 – 1188D

Amino acid modifications

Disulfide bond54 ↔ 96 Ref.16
Disulfide bond66 ↔ 109 Ref.16
Disulfide bond95 ↔ 100 Ref.16

Natural variations

Alternative sequence1 – 2121MGKIS…CDFLK → MITPT in isoform 3.
VSP_043317
Alternative sequence135 – 19561YQPPS…GKKGK → EVHLKNASRGSAGNKNYRM in isoform 2 and isoform 3.
VSP_039637
Alternative sequence152 – 19544WPKTH…GKKGK → STFEERK in isoform 4.
VSP_047399
Natural variant1151A → T.
Corresponds to variant rs17884626 [ dbSNP | Ensembl ].
VAR_056113
Natural variant1871A → D. Ref.23
Corresponds to variant rs6213 [ dbSNP | Ensembl ].
VAR_013945

Secondary structure

................ 195
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (IGF-IB) [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: E88A8CFBD1CD1873

FASTA19521,841
        10         20         30         40         50         60 
MGKISSLPTQ LFKCCFCDFL KVKMHTMSSS HLFYLALCLL TFTSSATAGP ETLCGAELVD 

        70         80         90        100        110        120 
ALQFVCGDRG FYFNKPTGYG SSSRRAPQTG IVDECCFRSC DLRRLEMYCA PLKPAKSARS 

       130        140        150        160        170        180 
VRAQRHTDMP KTQKYQPPST NKNTKSQRRK GWPKTHPGGE QKEGTEASLQ IRGKKKEQRR 

       190 
EIGSRNAECR GKKGK 

« Hide

Isoform 2 (IGF-IA) [UniParc].

Checksum: C6ECD92DCA9B37BC
Show »

FASTA15317,026
Isoform 3 [UniParc].

Checksum: BFCC0D11E32AB75D
Show »

FASTA13715,177
Isoform 4 [UniParc].

Checksum: 59DB4A0437679B6A
Show »

FASTA15817,762

References

« Hide 'large scale' references
[1]"Sequence of cDNA encoding human insulin-like growth factor I precursor."
Jansen M., van Schaik F.M.A., Ricker A.T., Bullock B., Woods D.E., Gabbay K.H., Nussbaum A.L., Sussenbach J.S., van den Brande J.L.
Nature 306:609-611(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"Organization of the human genes for insulin-like growth factors I and II."
de Pagter-Holthuizen P., van Schaik F.M.A., Verduijn G.M., van Ommen G.J.B., Bouma B.N., Jansen M., Sussenbach J.S.
FEBS Lett. 195:179-184(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Complete characterization of the human IGF-I nucleotide sequence isolated from a newly constructed adult liver cDNA library."
le Bouc Y., Dreyer D., Jaeger F., Binoux M., Sondermeyer P.
FEBS Lett. 196:108-112(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[4]"Organization and sequence of the human insulin-like growth factor I gene. Alternative RNA processing produces two insulin-like growth factor I precursor peptides."
Rotwein P., Pollock K.M., Didier D.K., Krivi G.G.
J. Biol. Chem. 261:4828-4832(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Two insulin-like growth factor I messenger RNAs are expressed in human liver."
Rotwein P.
Proc. Natl. Acad. Sci. U.S.A. 83:77-81(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[6]"A novel human insulin-like growth factor I messenger RNA is expressed in normal and tumor cells."
Tobin G., Yee D., Brunner N., Rotwein P.
Mol. Endocrinol. 4:1914-1920(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[7]"Complete nucleotide sequence of the high molecular weight human IGF-I mRNA."
Steenbergh P.H., Koonen-Reemst A.M.C.B., Cleutjens C.B.J.M., Sussenbach J.S.
Biochem. Biophys. Res. Commun. 175:507-514(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Liver.
[8]"Characterization of two cDNAs encoding insulin-like growth factor 1 (IGF-1) in the human fetal brain."
Sandberg-Nordqvist A.-C., Staehlbom P.-A., Lake M., Sara V.R.
Brain Res. Mol. Brain Res. 12:275-277(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Brain.
[9]"Characterization of insulin-like growth factor 1 in human primary brain tumors."
Sandberg-Nordqvist A.-C., Staehlbom P.-A., Reinecke M., Collins V.P., von Holst H., Sara V.
Cancer Res. 53:2475-2478(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[10]NIEHS SNPs program
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[11]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[14]"Insulin-like growth factor II precursor gene organization in relation to insulin gene family."
Dull T.J., Gray A., Hayflick J.S., Ullrich A.
Nature 310:777-781(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-73.
[15]"The amino acid sequence of human insulin-like growth factor I and its structural homology with proinsulin."
Rinderknecht E., Humbel R.E.
J. Biol. Chem. 253:2769-2776(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 49-118 (ISOFORMS 1 AND 2).
[16]"Location of disulphide bonds in human insulin-like growth factors (IGFs) synthesized by recombinant DNA technology."
Raschdorf F., Dahinden R., Maerki W., Richter W.J., Merryweather J.P.
Biomed. Environ. Mass Spectrom. 16:3-8(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.
[17]"Stimulation of glucose transport in osteoblastic cells by parathyroid hormone and insulin-like growth factor I."
Zoidis E., Ghirlanda-Keller C., Schmid C.
Mol. Cell. Biochem. 348:33-42(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[18]"SHANK3 and IGF1 restore synaptic deficits in neurons from 22q13 deletion syndrome patients."
Shcheglovitov A., Shcheglovitova O., Yazawa M., Portmann T., Shu R., Sebastiano V., Krawisz A., Froehlich W., Bernstein J.A., Hallmayer J.F., Dolmetsch R.E.
Nature 503:267-271(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN SYNAPSE FORMATION.
[19]"Tertiary structures, receptor binding, and antigenicity of insulinlike growth factors."
Blundell T.L., Bedarkar S., Humbel R.E.
Fed. Proc. 42:2592-2597(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[20]"Solution structure of human insulin-like growth factor 1: a nuclear magnetic resonance and restrained molecular dynamics study."
Cooke R.M., Harvey T.S., Campbell I.D.
Biochemistry 30:5484-5491(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[21]"1H-NMR assignment and secondary structure of human insulin-like growth factor-I (IGF-I) in solution."
Sato A., Nishimura S., Ohkubo T., Kyogoku Y., Koyama S., Kobayashi M., Yasuda T., Kobayashi Y.
J. Biochem. 111:529-536(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[22]"Intrauterine growth retardation and postnatal growth failure associated with deletion of the insulin-like growth factor I gene."
Woods K.A., Camacho-Hubner C., Savage M.O., Clark A.J.
N. Engl. J. Med. 335:1363-1367(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN IGF1 DEFICIENCY.
[23]"Characterization of single-nucleotide polymorphisms in coding regions of human genes."
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ASP-187.
[24]Erratum
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 23:373-373(1999)
+Additional computationally mapped references.

Web resources

SHMPD

The Singapore human mutation and polymorphism database

NIEHS-SNPs
Wikipedia

Insulin-like growth factor 1 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X00173 mRNA. Translation: CAA24998.1.
X03420 Genomic DNA. Translation: CAA27152.1.
X03421 Genomic DNA. Translation: CAA27153.1.
X03422 Genomic DNA. Translation: CAA27154.1.
M27544 mRNA. Translation: AAA52787.1.
M14155 expand/collapse EMBL AC list , M12659, M14153, M14154 Genomic DNA. Translation: AAA52537.1.
M14156 expand/collapse EMBL AC list , M12659, M14153, M14154 Genomic DNA. Translation: AAA52538.1.
M11568 mRNA. Translation: AAA52539.1.
M37484 mRNA. Translation: AAA52789.1.
X57025 mRNA. Translation: CAA40342.1.
X56773 mRNA. Translation: CAA40092.1.
X56774 mRNA. Translation: CAA40093.1.
AY260957 Genomic DNA. Translation: AAO74829.1.
AC010202 Genomic DNA. No translation available.
AC068648 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97696.1.
CH471054 Genomic DNA. Translation: EAW97697.1.
BC148266 mRNA. Translation: AAI48267.1.
X03563 Genomic DNA. Translation: CAA27250.1. Sequence problems.
PIRIGHU1B. A01611.
IGHU1. A92581.
RefSeqNP_000609.1. NM_000618.3.
NP_001104754.1. NM_001111284.1.
NP_001104755.1. NM_001111285.1.
UniGeneHs.160562.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B9GNMR-A49-118[»]
1BQTNMR-A49-118[»]
1GF1model-A49-118[»]
1GZRX-ray2.00B49-118[»]
1GZYX-ray2.54B49-118[»]
1GZZX-ray2.30B49-118[»]
1H02X-ray2.00B49-118[»]
1H59X-ray2.10A49-118[»]
1IMXX-ray1.82A49-118[»]
1PMXNMR-A49-118[»]
1TGRX-ray1.42A/B49-110[»]
1WQJX-ray1.60I49-118[»]
2DSPX-ray2.50I49-118[»]
2DSQX-ray2.80C/I49-118[»]
2DSRX-ray2.10I49-118[»]
2GF1NMR-A49-118[»]
3GF1NMR-A49-118[»]
3LRINMR-A49-118[»]
ProteinModelPortalP05019.
SMRP05019. Positions 50-111.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109700. 12 interactions.
DIPDIP-41933N.
DIP-6021N.
IntActP05019. 2 interactions.
MINTMINT-204184.
STRING9606.ENSP00000302665.

PTM databases

PhosphoSiteP05019.

Polymorphism databases

DMDM124263.

Proteomic databases

PaxDbP05019.
PRIDEP05019.

Protocols and materials databases

DNASU3479.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000307046; ENSP00000302665; ENSG00000017427. [P05019-1]
ENST00000337514; ENSP00000337612; ENSG00000017427. [P05019-2]
ENST00000392904; ENSP00000376637; ENSG00000017427. [P05019-4]
ENST00000424202; ENSP00000416811; ENSG00000017427. [P05019-3]
ENST00000456098; ENSP00000394999; ENSG00000017427. [P05019-4]
GeneID3479.
KEGGhsa:3479.
UCSCuc001tjn.2. human. [P05019-3]
uc001tjp.4. human. [P05019-1]

Organism-specific databases

CTD3479.
GeneCardsGC12M102748.
HGNCHGNC:5464. IGF1.
HPAHPA048946.
MIM147440. gene.
608747. phenotype.
neXtProtNX_P05019.
Orphanet73272. Growth delay due to insulin-like growth factor type 1 deficiency.
PharmGKBPA29697.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG39886.
HOGENOMHOG000233362.
HOVERGENHBG006137.
InParanoidP05019.
KOK05459.
OMAHTVSYIH.
OrthoDBEOG7TF7CG.
PhylomeDBP05019.
TreeFamTF332820.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_17015. Metabolism of proteins.
REACT_604. Hemostasis.
SignaLinkP05019.

Gene expression databases

ArrayExpressP05019.
BgeeP05019.
CleanExHS_IGF1.
GenevestigatorP05019.

Family and domain databases

Gene3D1.10.100.10. 1 hit.
InterProIPR022341. IGF-I.
IPR016179. Insulin-like.
IPR022350. Insulin-like_growth_factor.
IPR022353. Insulin_CS.
IPR022352. Insulin_family.
[Graphical view]
PfamPF00049. Insulin. 1 hit.
[Graphical view]
PRINTSPR02002. INSLNLIKEGF.
PR02005. INSLNLIKEGF1.
PR00276. INSULINFAMLY.
SMARTSM00078. IlGF. 1 hit.
[Graphical view]
SUPFAMSSF56994. SSF56994. 1 hit.
PROSITEPS00262. INSULIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIGF1. human.
EvolutionaryTraceP05019.
GeneWikiInsulin-like_growth_factor_1.
GenomeRNAi3479.
NextBio13678.
PMAP-CutDBP01343.
PROP05019.
SOURCESearch...

Entry information

Entry nameIGF1_HUMAN
AccessionPrimary (citable) accession number: P05019
Secondary accession number(s): B2RWM7 expand/collapse secondary AC list , E9PD02, P01343, Q14620
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: April 16, 2014
This is version 171 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM