P05019 (IGF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	195 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. Ref.17
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 component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Deafness
Domain	Signal
Molecular function	Growth factor
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA 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: Compara Type II pneumocyte differentiation Inferred from electronic annotation. Source: Compara blood vessel remodeling Inferred from electronic annotation. Source: Compara 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: Compara cellular component movement Traceable author statement PubMed 10766744. Source: ProtInc chondroitin sulfate proteoglycan biosynthetic process Inferred from electronic annotation. Source: Compara exocrine pancreas development Inferred from electronic annotation. Source: Compara glial cell differentiation Inferred from electronic annotation. Source: Compara glycolate metabolic process Traceable author statement PubMed 10448861. Source: ProtInc inner ear development Inferred from electronic annotation. Source: Compara insulin-like growth factor receptor signaling pathway Inferred from electronic annotation. Source: Compara lung alveolus development Inferred from electronic annotation. Source: Compara lung lobe morphogenesis Inferred from electronic annotation. Source: Compara lung vasculature development Inferred from electronic annotation. Source: Compara mammary gland development Inferred from electronic annotation. Source: Compara multicellular organism growth Inferred from electronic annotation. Source: Compara muscle hypertrophy Inferred from mutant phenotype PubMed 10191278. Source: BHF-UCL 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: Compara negative regulation of androgen receptor signaling pathway Inferred from electronic annotation. Source: Compara negative regulation of cell proliferation Inferred from electronic annotation. Source: Compara 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 cerebellar granule cell precursor proliferation Inferred from electronic annotation. Source: Compara 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: Compara positive regulation of osteoblast differentiation Inferred from direct assay PubMed 16433617. Source: BHF-UCL positive regulation of phosphatidylinositol 3-kinase cascade 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 cascade Inferred from electronic annotation. Source: Compara 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 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: Compara prostate gland growth Inferred from electronic annotation. Source: Compara prostate gland stromal morphogenesis Inferred from electronic annotation. Source: Compara 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: Compara 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 water homeostasis Inferred from electronic annotation. Source: Compara
Cellular_component	insulin-like growth factor binding protein complex Inferred by curator PubMed 10766744. Source: BHF-UCL platelet alpha granule lumen Traceable author statement. Source: Reactome
Molecular_function	hormone activity Inferred from direct assay PubMed 7188854. Source: BHF-UCL integrin binding Inferred from direct assay PubMed 19578119. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 3 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Potential

Propeptide

22 – 48

27

PRO_0000015663

Chain

49 – 118

70

Insulin-like growth factor I

PRO_0000015664

Propeptide

119 – 195

77

E peptide

PRO_0000015665

Regions

Region

49 – 77

29

B

Region

78 – 89

12

C

Region

90 – 110

21

A

Region

111 – 118

8

D

Amino acid modifications

Disulfide bond

54 ↔ 96

Ref.16

Disulfide bond

66 ↔ 109

Ref.16

Disulfide bond

95 ↔ 100

Ref.16

Natural variations

Alternative sequence

1 – 21

21

MGKIS…CDFLK → MITPT in isoform 3.

VSP_043317

Alternative sequence

135 – 195

61

YQPPS…GKKGK → EVHLKNASRGSAGNKNYRM in isoform 2 and isoform 3.

VSP_039637

Natural variant

115

1

A → T.
Corresponds to variant rs17884626 [ dbSNP | Ensembl ].

VAR_056113

Natural variant

187

1

A → D. Ref.22
Corresponds to variant rs6213 [ dbSNP | Ensembl ].

VAR_013945

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

195

Helix Strand Turn

Details...

Helix

52 – 66

15

Helix

67 – 69

3

Beta strand

71 – 73

3

Beta strand

79 – 81

3

Beta strand

82 – 85

4

Helix

87 – 95

9

Beta strand

96 – 98

3

Helix

102 – 108

7

Beta strand

109 – 111

3

Beta strand

112 – 116

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (IGF-IB) [UniParc]. Last modified August 13, 1987. Version 1. Checksum: E88A8CFBD1CD1873	FASTA	195	21,841
	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
	Isoform 2 (IGF-IA) [UniParc]. Checksum: C6ECD92DCA9B37BC	FASTA	153	17,026
	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 VRAQRHTDMP KTQKEVHLKN ASRGSAGNKN YRM
	Isoform 3 [UniParc]. Checksum: BFCC0D11E32AB75D	FASTA	137	15,177
	10 20 30 40 50 60 MITPTVKMHT MSSSHLFYLA LCLLTFTSSA TAGPETLCGA ELVDALQFVC GDRGFYFNKP 70 80 90 100 110 120 TGYGSSSRRA PQTGIVDECC FRSCDLRRLE MYCAPLKPAK SARSVRAQRH TDMPKTQKEV 130 HLKNASRGSA GNKNYRM

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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.
[19]	"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.
[20]	"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.
[21]	"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.
[22]	"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.
[23]	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 , M12659, M14153, M14154 Genomic DNA. Translation: AAA52537.1.
M14156 , 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.

IPI

IPI00001610.
IPI00433029.
IPI00793994.

PIR

IGHU1B. A01611.
IGHU1. A92581.

RefSeq

NP_000609.1. NM_000618.3.
NP_001104754.1. NM_001111284.1.
NP_001104755.1. NM_001111285.1.

UniGene

Hs.160562.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B9G	NMR	-	A	49-118	[»]
1BQT	NMR	-	A	49-118	[»]
1GF1	model	-	A	49-118	[»]
1GZR	X-ray	2.00	B	49-118	[»]
1GZY	X-ray	2.54	B	49-118	[»]
1GZZ	X-ray	2.30	B	49-118	[»]
1H02	X-ray	2.00	B	49-118	[»]
1H59	X-ray	2.10	A	49-118	[»]
1IMX	X-ray	1.82	A	49-118	[»]
1PMX	NMR	-	A	49-118	[»]
1TGR	X-ray	1.42	A/B	49-110	[»]
1WQJ	X-ray	1.60	I	49-118	[»]
2DSP	X-ray	2.50	I	49-118	[»]
2DSQ	X-ray	2.80	C/I	49-118	[»]
2DSR	X-ray	2.10	I	49-118	[»]
2GF1	NMR	-	A	49-118	[»]
3GF1	NMR	-	A	49-118	[»]
3LRI	NMR	-	A	49-118	[»]

ProteinModelPortal

P05019.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-41933N.
DIP-6021N.

MINT

MINT-204184.

STRING

9606.ENSP00000302665.

PTM databases

PhosphoSite

P05019.

Polymorphism databases

DMDM

124263.

Proteomic databases

PaxDb

P05019.

PRIDE

P05019.

Protocols and materials databases

DNASU

3479.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000307046; ENSP00000302665; ENSG00000017427.
ENST00000337514; ENSP00000337612; ENSG00000017427.
ENST00000424202; ENSP00000416811; ENSG00000017427.

GeneID

3479.

KEGG

hsa:3479.

UCSC

uc001tjp.4. human.

Organism-specific databases

CTD

3479.

GeneCards

GC12M102748.

HGNC

HGNC:5464. IGF1.

HPA

HPA048946.

MIM

147440. gene.
608747. phenotype.

neXtProt

NX_P05019.

Orphanet

73272. Growth delay due to insulin-like growth factor I deficiency.

PharmGKB

PA29697.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG39886.

HOGENOM

HOG000233362.

HOVERGEN

HBG006137.

InParanoid

P05019.

KO

K05459.

OMA

HTVSYIH.

PhylomeDB

P05019.

Enzyme and pathway databases

Pathway_Interaction_DB

ceramidepathway. Ceramide signaling pathway.
igf1_pathway. IGF1 pathway.
avb3_integrin_pathway. Integrins in angiogenesis.
er_nongenomic_pathway. Plasma membrane estrogen receptor signaling.

Reactome

REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P05019.

Bgee

P05019.

CleanEx

HS_IGF1.

Genevestigator

P05019.

GermOnline

ENSG00000017427. Homo sapiens.

Family and domain databases

Gene3D

1.10.100.10. 1 hit.

InterPro

IPR022341. IGF-I.
IPR016179. Insulin-like.
IPR022350. Insulin-like_growth_factor.
IPR022353. Insulin_CS.
IPR022352. Insulin_family.
[Graphical view]

Pfam

PF00049. Insulin. 1 hit.
[Graphical view]

PRINTS

PR02002. INSLNLIKEGF.
PR02005. INSLNLIKEGF1.
PR00276. INSULINFAMLY.

SMART

SM00078. IlGF. 1 hit.
[Graphical view]

SUPFAM

SSF56994. Insulin-like. 1 hit.

PROSITE

PS00262. INSULIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

IGF1. human.

EvolutionaryTrace

P05019.

GenomeRNAi

3479.

NextBio

13678.

PMAP-CutDB

P01343.

SOURCE

Search...

Entry information

Entry name

IGF1_HUMAN

Accession

Primary (citable) accession number: P05019
Secondary accession number(s): B2RWM7, P01343, Q14620

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	May 1, 2013
This is version 160 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.