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Protein

Insulin-like growth factor I

Gene

IGF1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  1. hormone activity Source: BHF-UCL
  2. insulin-like growth factor receptor binding Source: AgBase
  3. insulin receptor binding Source: BHF-UCL
  4. integrin binding Source: BHF-UCL

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. blood vessel remodeling Source: Ensembl
  3. bone mineralization involved in bone maturation Source: BHF-UCL
  4. branching morphogenesis of an epithelial tube Source: Ensembl
  5. cell activation Source: MGI
  6. cell proliferation Source: AgBase
  7. cellular protein metabolic process Source: Reactome
  8. chondroitin sulfate proteoglycan biosynthetic process Source: Ensembl
  9. DNA replication Source: ProtInc
  10. exocrine pancreas development Source: Ensembl
  11. extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
  12. glial cell differentiation Source: Ensembl
  13. glycolate metabolic process Source: ProtInc
  14. inner ear development Source: Ensembl
  15. insulin-like growth factor receptor signaling pathway Source: Ensembl
  16. lung alveolus development Source: Ensembl
  17. lung lobe morphogenesis Source: Ensembl
  18. lung vasculature development Source: Ensembl
  19. mammary gland development Source: Ensembl
  20. movement of cell or subcellular component Source: ProtInc
  21. multicellular organism growth Source: Ensembl
  22. muscle hypertrophy Source: BHF-UCL
  23. muscle organ development Source: ProtInc
  24. myoblast differentiation Source: BHF-UCL
  25. myoblast proliferation Source: BHF-UCL
  26. myotube cell development Source: BHF-UCL
  27. negative regulation of androgen receptor signaling pathway Source: Ensembl
  28. negative regulation of apoptotic process Source: AgBase
  29. negative regulation of cell proliferation Source: Ensembl
  30. negative regulation of ERK1 and ERK2 cascade Source: Ensembl
  31. negative regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL
  32. negative regulation of oocyte development Source: AgBase
  33. negative regulation of release of cytochrome c from mitochondria Source: UniProtKB
  34. negative regulation of smooth muscle cell apoptotic process Source: BHF-UCL
  35. phosphatidylinositol-mediated signaling Source: BHF-UCL
  36. platelet activation Source: Reactome
  37. platelet degranulation Source: Reactome
  38. positive regulation of activated T cell proliferation Source: BHF-UCL
  39. positive regulation of calcineurin-NFAT signaling cascade Source: UniProtKB
  40. positive regulation of cardiac muscle hypertrophy Source: UniProtKB
  41. positive regulation of cell proliferation Source: BHF-UCL
  42. positive regulation of cerebellar granule cell precursor proliferation Source: Ensembl
  43. positive regulation of DNA binding Source: UniProtKB
  44. positive regulation of DNA replication Source: BHF-UCL
  45. positive regulation of epithelial cell proliferation Source: BHF-UCL
  46. positive regulation of fibroblast proliferation Source: BHF-UCL
  47. positive regulation of glucose import Source: UniProtKB
  48. positive regulation of glycogen biosynthetic process Source: UniProtKB
  49. positive regulation of glycolytic process Source: BHF-UCL
  50. positive regulation of insulin-like growth factor receptor signaling pathway Source: BHF-UCL
  51. positive regulation of MAPK cascade Source: UniProtKB
  52. positive regulation of mitotic nuclear division Source: UniProtKB
  53. positive regulation of myoblast proliferation Source: Ensembl
  54. positive regulation of osteoblast differentiation Source: BHF-UCL
  55. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  56. positive regulation of phosphatidylinositol 3-kinase signaling Source: BHF-UCL
  57. positive regulation of protein import into nucleus, translocation Source: UniProtKB
  58. positive regulation of protein kinase B signaling Source: Ensembl
  59. positive regulation of Ras protein signal transduction Source: BHF-UCL
  60. positive regulation of smooth muscle cell migration Source: BHF-UCL
  61. positive regulation of smooth muscle cell proliferation Source: BHF-UCL
  62. positive regulation of transcription, DNA-templated Source: UniProtKB
  63. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  64. positive regulation of tyrosine phosphorylation of Stat5 protein Source: BHF-UCL
  65. prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis Source: Ensembl
  66. prostate gland growth Source: Ensembl
  67. prostate gland stromal morphogenesis Source: Ensembl
  68. proteoglycan biosynthetic process Source: BHF-UCL
  69. Ras protein signal transduction Source: ProtInc
  70. regulation of establishment or maintenance of cell polarity Source: Ensembl
  71. regulation of gene expression Source: AgBase
  72. regulation of multicellular organism growth Source: BHF-UCL
  73. response to heat Source: AgBase
  74. signal transduction Source: ProtInc
  75. skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration Source: BHF-UCL
  76. skeletal system development Source: ProtInc
  77. Type II pneumocyte differentiation Source: Ensembl
  78. Type I pneumocyte differentiation Source: Ensembl
  79. water homeostasis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Growth factor

Enzyme and pathway databases

ReactomeiREACT_150139. SHC-related events triggered by IGF1R.
REACT_150203. IRS-related events triggered by IGF1R.
REACT_150359. Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R).
REACT_15428. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
REACT_19189. Synthesis, secretion, and deacylation of Ghrelin.
REACT_318. Platelet degranulation.
SignaLinkiP05019.

Names & Taxonomyi

Protein namesi
Recommended name:
Insulin-like growth factor I
Short name:
IGF-I
Alternative name(s):
Mechano growth factor
Short name:
MGF
Somatomedin-C
Gene namesi
Name:IGF1
Synonyms:IBP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:5464. IGF1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
  2. extracellular space Source: AgBase
  3. insulin-like growth factor binding protein complex Source: BHF-UCL
  4. plasma membrane Source: Reactome
  5. platelet alpha granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Insulin-like growth factor I deficiency (IGF1 deficiency)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAutosomal recessive disorder characterized by growth retardation, sensorineural deafness and mental retardation.

See also OMIM:608747

Keywords - Diseasei

Deafness

Organism-specific databases

MIMi608747. phenotype.
Orphaneti73272. Growth delay due to insulin-like growth factor type 1 deficiency.
PharmGKBiPA29697.

Polymorphism and mutation databases

BioMutaiIGF1.
DMDMi124263.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Propeptidei22 – 4827PRO_0000015663Add
BLAST
Chaini49 – 11870Insulin-like growth factor IPRO_0000015664Add
BLAST
Propeptidei119 – 19577E peptidePRO_0000015665Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi54 ↔ 961 Publication
Disulfide bondi66 ↔ 1091 Publication
Disulfide bondi95 ↔ 1001 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP05019.
PRIDEiP05019.

PTM databases

PhosphoSiteiP05019.

Miscellaneous databases

PMAP-CutDBP01343.

Expressioni

Gene expression databases

BgeeiP05019.
CleanExiHS_IGF1.
ExpressionAtlasiP05019. baseline and differential.
GenevestigatoriP05019.

Organism-specific databases

HPAiHPA048946.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
IGF1RP080695EBI-7902275,EBI-475981
INSRP062134EBI-7902275,EBI-475899

Protein-protein interaction databases

BioGridi109700. 12 interactions.
DIPiDIP-41933N.
DIP-6021N.
IntActiP05019. 2 interactions.
MINTiMINT-204184.
STRINGi9606.ENSP00000302665.

Structurei

Secondary structure

1
195
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi52 – 6615Combined sources
Helixi67 – 693Combined sources
Beta strandi71 – 733Combined sources
Beta strandi79 – 813Combined sources
Beta strandi82 – 854Combined sources
Helixi90 – 956Combined sources
Beta strandi96 – 983Combined sources
Helixi102 – 1087Combined sources
Beta strandi109 – 1113Combined sources
Beta strandi112 – 1165Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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/B49-77[»]
A/B90-110[»]
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[»]
ProteinModelPortaliP05019.
SMRiP05019. Positions 50-111.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05019.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 7729BAdd
BLAST
Regioni78 – 8912CAdd
BLAST
Regioni90 – 11021AAdd
BLAST
Regioni111 – 1188D

Sequence similaritiesi

Belongs to the insulin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG39886.
GeneTreeiENSGT00530000063856.
HOGENOMiHOG000233362.
HOVERGENiHBG006137.
InParanoidiP05019.
KOiK05459.
OMAiHTVSYIH.
OrthoDBiEOG7TF7CG.
PhylomeDBiP05019.
TreeFamiTF332820.

Family and domain databases

Gene3Di1.10.100.10. 1 hit.
InterProiIPR022341. IGF-I.
IPR016179. Insulin-like.
IPR022350. Insulin-like_growth_factor.
IPR022353. Insulin_CS.
IPR022352. Insulin_family.
[Graphical view]
PfamiPF00049. Insulin. 1 hit.
[Graphical view]
PRINTSiPR02002. INSLNLIKEGF.
PR02005. INSLNLIKEGF1.
PR00276. INSULINFAMLY.
SMARTiSM00078. IlGF. 1 hit.
[Graphical view]
SUPFAMiSSF56994. SSF56994. 1 hit.
PROSITEiPS00262. INSULIN. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P05019-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MGKISSLPTQ LFKCCFCDFL KVKMHTMSSS HLFYLALCLL TFTSSATAGP
60 70 80 90 100
ETLCGAELVD ALQFVCGDRG FYFNKPTGYG SSSRRAPQTG IVDECCFRSC
110 120 130 140 150
DLRRLEMYCA PLKPAKSARS VRAQRHTDMP KTQKYQPPST NKNTKSQRRK
160 170 180 190
GWPKTHPGGE QKEGTEASLQ IRGKKKEQRR EIGSRNAECR GKKGK
Length:195
Mass (Da):21,841
Last modified:August 13, 1987 - v1
Checksum:iE88A8CFBD1CD1873
GO
Isoform 2 (identifier: P05019-2) [UniParc]FASTAAdd to basket

Also known as: IGF-IA

The sequence of this isoform differs from the canonical sequence as follows:
     135-195: YQPPSTNKNT...NAECRGKKGK → EVHLKNASRGSAGNKNYRM

Show »
Length:153
Mass (Da):17,026
Checksum:iC6ECD92DCA9B37BC
GO
Isoform 3 (identifier: P05019-3) [UniParc]FASTAAdd to basket

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.

Show »
Length:137
Mass (Da):15,177
Checksum:iBFCC0D11E32AB75D
GO
Isoform 4 (identifier: P05019-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     152-195: WPKTHPGGEQKEGTEASLQIRGKKKEQRREIGSRNAECRGKKGK → STFEERK

Note: Gene prediction based on EST data.

Show »
Length:158
Mass (Da):17,762
Checksum:i59DB4A0437679B6A
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti115 – 1151A → T.
Corresponds to variant rs17884626 [ dbSNP | Ensembl ].
VAR_056113
Natural varianti187 – 1871A → D.1 Publication
Corresponds to variant rs6213 [ dbSNP | Ensembl ].
VAR_013945

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2121MGKIS…CDFLK → MITPT in isoform 3. 1 PublicationVSP_043317Add
BLAST
Alternative sequencei135 – 19561YQPPS…GKKGK → EVHLKNASRGSAGNKNYRM in isoform 2 and isoform 3. 5 PublicationsVSP_039637Add
BLAST
Alternative sequencei152 – 19544WPKTH…GKKGK → STFEERK in isoform 4. CuratedVSP_047399Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS44960.1. [P05019-3]
CCDS44961.1. [P05019-4]
CCDS44962.1. [P05019-1]
CCDS9091.1. [P05019-2]
PIRiA01611. IGHU1B.
A92581. IGHU1.
RefSeqiNP_000609.1. NM_000618.3. [P05019-2]
NP_001104754.1. NM_001111284.1. [P05019-3]
NP_001104755.1. NM_001111285.1. [P05019-1]
UniGeneiHs.160562.

Genome annotation databases

EnsembliENST00000307046; ENSP00000302665; ENSG00000017427. [P05019-1]
ENST00000337514; ENSP00000337612; ENSG00000017427. [P05019-2]
ENST00000392904; ENSP00000376637; ENSG00000017427. [P05019-4]
ENST00000424202; ENSP00000416811; ENSG00000017427. [P05019-3]
ENST00000456098; ENSP00000394999; ENSG00000017427. [P05019-4]
GeneIDi3479.
KEGGihsa:3479.
UCSCiuc001tjm.2. human.
uc001tjn.2. human. [P05019-3]
uc001tjp.4. human. [P05019-1]

Polymorphism and mutation databases

BioMutaiIGF1.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SHMPD

The Singapore human mutation and polymorphism database

NIEHS-SNPs
Wikipedia

Insulin-like growth factor 1 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS44960.1. [P05019-3]
CCDS44961.1. [P05019-4]
CCDS44962.1. [P05019-1]
CCDS9091.1. [P05019-2]
PIRiA01611. IGHU1B.
A92581. IGHU1.
RefSeqiNP_000609.1. NM_000618.3. [P05019-2]
NP_001104754.1. NM_001111284.1. [P05019-3]
NP_001104755.1. NM_001111285.1. [P05019-1]
UniGeneiHs.160562.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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/B49-77[»]
A/B90-110[»]
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[»]
ProteinModelPortaliP05019.
SMRiP05019. Positions 50-111.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109700. 12 interactions.
DIPiDIP-41933N.
DIP-6021N.
IntActiP05019. 2 interactions.
MINTiMINT-204184.
STRINGi9606.ENSP00000302665.

Chemistry

ChEMBLiCHEMBL3217394.

PTM databases

PhosphoSiteiP05019.

Polymorphism and mutation databases

BioMutaiIGF1.
DMDMi124263.

Proteomic databases

PaxDbiP05019.
PRIDEiP05019.

Protocols and materials databases

DNASUi3479.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000307046; ENSP00000302665; ENSG00000017427. [P05019-1]
ENST00000337514; ENSP00000337612; ENSG00000017427. [P05019-2]
ENST00000392904; ENSP00000376637; ENSG00000017427. [P05019-4]
ENST00000424202; ENSP00000416811; ENSG00000017427. [P05019-3]
ENST00000456098; ENSP00000394999; ENSG00000017427. [P05019-4]
GeneIDi3479.
KEGGihsa:3479.
UCSCiuc001tjm.2. human.
uc001tjn.2. human. [P05019-3]
uc001tjp.4. human. [P05019-1]

Organism-specific databases

CTDi3479.
GeneCardsiGC12M102748.
HGNCiHGNC:5464. IGF1.
HPAiHPA048946.
MIMi147440. gene.
608747. phenotype.
neXtProtiNX_P05019.
Orphaneti73272. Growth delay due to insulin-like growth factor type 1 deficiency.
PharmGKBiPA29697.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG39886.
GeneTreeiENSGT00530000063856.
HOGENOMiHOG000233362.
HOVERGENiHBG006137.
InParanoidiP05019.
KOiK05459.
OMAiHTVSYIH.
OrthoDBiEOG7TF7CG.
PhylomeDBiP05019.
TreeFamiTF332820.

Enzyme and pathway databases

ReactomeiREACT_150139. SHC-related events triggered by IGF1R.
REACT_150203. IRS-related events triggered by IGF1R.
REACT_150359. Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R).
REACT_15428. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
REACT_19189. Synthesis, secretion, and deacylation of Ghrelin.
REACT_318. Platelet degranulation.
SignaLinkiP05019.

Miscellaneous databases

ChiTaRSiIGF1. human.
EvolutionaryTraceiP05019.
GeneWikiiInsulin-like_growth_factor_1.
GenomeRNAii3479.
NextBioi13678.
PMAP-CutDBP01343.
PROiP05019.
SOURCEiSearch...

Gene expression databases

BgeeiP05019.
CleanExiHS_IGF1.
ExpressionAtlasiP05019. baseline and differential.
GenevestigatoriP05019.

Family and domain databases

Gene3Di1.10.100.10. 1 hit.
InterProiIPR022341. IGF-I.
IPR016179. Insulin-like.
IPR022350. Insulin-like_growth_factor.
IPR022353. Insulin_CS.
IPR022352. Insulin_family.
[Graphical view]
PfamiPF00049. Insulin. 1 hit.
[Graphical view]
PRINTSiPR02002. INSLNLIKEGF.
PR02005. INSLNLIKEGF1.
PR00276. INSULINFAMLY.
SMARTiSM00078. IlGF. 1 hit.
[Graphical view]
SUPFAMiSSF56994. SSF56994. 1 hit.
PROSITEiPS00262. INSULIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. 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. 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. 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. 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. Cited for: VARIANT ASP-187.

Entry informationi

Entry nameiIGF1_HUMAN
AccessioniPrimary (citable) accession number: P05019
Secondary accession number(s): B2RWM7
, E9PD02, P01343, Q14620
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: April 29, 2015
This is version 183 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.