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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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.16
Subcellular location	Secreted.
Involvement in disease	Defects in IGF1 are the cause of insulin-like growth factor I deficiency (IGF1 deficiency) [MIM:608747]. IGF1 deficiency is an autosomal recessive disorder characterized by growth retardation, sensorineural deafness and mental retardation.
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. Source: ProtInc Ras protein signal transduction Traceable author statement. Source: ProtInc anti-apoptosis Inferred from direct assay. Source: BHF-UCL bone mineralization involved in bone maturation Inferred from direct assay. Source: BHF-UCL cellular component movement Traceable author statement. Source: ProtInc glycolate metabolic process Traceable author statement. Source: ProtInc muscle hypertrophy Inferred from mutant phenotype. Source: BHF-UCL myoblast differentiation Inferred from direct assay. Source: BHF-UCL myoblast proliferation Inferred from direct assay. Source: BHF-UCL myotube cell development Inferred from direct assay. 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 apoptosis Inferred from direct assay. Source: BHF-UCL phosphatidylinositol-mediated signaling Inferred from direct assay. 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. Source: UniProtKB positive regulation of DNA replication Inferred from direct assay. Source: BHF-UCL positive regulation of MAPKKK cascade Inferred from direct assay. Source: UniProtKB positive regulation of Ras protein signal transduction Inferred from direct assay. Source: BHF-UCL positive regulation of activated T cell proliferation Inferred from direct assay. Source: BHF-UCL positive regulation of calcineurin-NFAT signaling pathway Inferred from direct assay. Source: UniProtKB positive regulation of cardiac muscle hypertrophy Inferred from direct assay. Source: UniProtKB positive regulation of epithelial cell proliferation Inferred from direct assay. Source: BHF-UCL positive regulation of fibroblast proliferation Inferred from direct assay. Source: BHF-UCL positive regulation of glucose import Inferred from direct assay Ref.16. Source: UniProtKB positive regulation of glycogen biosynthetic process Inferred from direct assay Ref.16. Source: UniProtKB positive regulation of glycolysis Inferred from direct assay. Source: BHF-UCL positive regulation of insulin-like growth factor receptor signaling pathway Inferred from direct assay. Source: BHF-UCL positive regulation of mitosis Inferred from direct assay. Source: UniProtKB positive regulation of osteoblast differentiation Inferred from direct assay. Source: BHF-UCL positive regulation of phosphatidylinositol 3-kinase cascade Inferred from direct assay. Source: BHF-UCL positive regulation of protein import into nucleus, translocation Inferred from direct assay. Source: UniProtKB positive regulation of smooth muscle cell migration Inferred from direct assay. Source: BHF-UCL positive regulation of smooth muscle cell proliferation Inferred from direct assay. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay. Source: BHF-UCL positive regulation of tyrosine phosphorylation of Stat5 protein Inferred from direct assay. Source: BHF-UCL regulation of multicellular organism growth Inferred from expression pattern. Source: BHF-UCL satellite cell maintenance involved in skeletal muscle regeneration Inferred from direct assay. Source: BHF-UCL
Cellular component	insulin-like growth factor binding protein complex Inferred by curator. Source: BHF-UCL platelet alpha granule lumen Traceable author statement. Source: Reactome
Molecular function	growth factor activity Inferred from electronic annotation. Source: UniProtKB-KW hormone activity Inferred from direct assay. Source: BHF-UCL insulin receptor binding Inferred from physical interaction. Source: BHF-UCL insulin-like growth factor receptor binding Inferred from physical interaction. Source: BHF-UCL integrin binding Inferred from direct assay. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 2 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

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.15

Disulfide bond

66 ↔ 109

Ref.15

Disulfide bond

95 ↔ 100

Ref.15

Natural variations

Alternative sequence

135 – 195

61

YQPPS…GKKGK → EVHLKNASRGSAGNKNYRM in isoform 2.

VSP_039637

Natural variant

115

1

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

VAR_056113

Natural variant

187

1

A → D. Ref.21
Corresponds to variant rs6213 [ dbSNP | Ensembl ].

VAR_013945

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

195

Helix Strand Turn

Details...

Helix

55 – 66

12

Helix

67 – 69

3

Beta strand

73 – 76

4

Beta strand

87 – 90

4

Helix

91 – 95

5

Turn

96 – 98

3

Helix

102 – 106

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

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: 6358902] [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: 3002851] [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: 2935423] [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: 2937782] [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: 3455760] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[6]	"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: 2018498] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Liver.
[7]	"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: 1372070] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Brain.
[8]	"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: 8495408] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[9]	NIEHS SNPs program Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[10]	"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: 16541075] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]	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].
[12]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[13]	"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: 6382022] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-73.
[14]	"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: 632300] [Abstract] Cited for: PROTEIN SEQUENCE OF 49-118 (ISOFORMS 1 AND 2).
[15]	"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: 3242681] [Abstract] Cited for: DISULFIDE BONDS.
[16]	"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: 21076856] [Abstract] Cited for: FUNCTION.
[17]	"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: 6189745] [Abstract] Cited for: 3D-STRUCTURE MODELING.
[18]	"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: 2036417] [Abstract] Cited for: STRUCTURE BY NMR.
[19]	"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: 1319992] [Abstract] Cited for: STRUCTURE BY NMR.
[20]	"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: 8857020] [Abstract] Cited for: INVOLVEMENT IN IGF1 DEFICIENCY.
[21]	"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: 10391209] [Abstract] Cited for: VARIANT ASP-187.
[22]	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.
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.
BC148266 mRNA. Translation: AAI48267.1.
X03563 Genomic DNA. Translation: CAA27250.1. Sequence problems.

IPI

IPI00001610.
IPI00433029.

PIR

IGHU1B. A01611.
IGHU1. A92581.

RefSeq

NP_000609.1. NM_000618.3.
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.

SMR

P05019. Positions 49-118.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-41933N.

MINT

MINT-204184.

STRING

P05019.

Polymorphism databases

DMDM

124263.

Proteomic databases

PRIDE

P05019.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000307046; ENSP00000302665; ENSG00000017427.

GeneID

3479.

KEGG

hsa:3479.

UCSC

uc001tjp.2. human.

Organism-specific databases

CTD

3479.

GeneCards

GC12M102748.

HGNC

HGNC:5464. IGF1.

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

HOGENOM

HBG714444.

HOVERGEN

HBG006137.

InParanoid

P05019.

OMA

LLYLALC.

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_15380. Diabetes pathways.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P05019.

Bgee

P05019.

CleanEx

HS_IGF1.

Genevestigator

P05019.

GermOnline

ENSG00000017427. Homo sapiens.

Family and domain databases

InterPro

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

Gene3D

G3DSA:1.10.100.10. Ins/IGF/relaxin. 1 hit.

KO

K05459.

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

NextBio

13678.

SOURCE

Search...

Entry information

Entry name

IGF1_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	August 13, 1987
Last modified:	January 25, 2012
This is version 146 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.