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P05019

- IGF1_HUMAN

UniProt

P05019 - IGF1_HUMAN

Protein

Insulin-like growth factor I

Gene

IGF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 176 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      Previous versions | rss
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    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: BHF-UCL
    3. insulin receptor binding Source: BHF-UCL
    4. integrin binding Source: BHF-UCL
    5. protein binding Source: IntAct

    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. cellular component movement Source: ProtInc
    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. multicellular organism growth Source: Ensembl
    21. muscle hypertrophy Source: BHF-UCL
    22. muscle organ development Source: ProtInc
    23. myoblast differentiation Source: BHF-UCL
    24. myoblast proliferation Source: BHF-UCL
    25. myotube cell development Source: BHF-UCL
    26. negative regulation of androgen receptor signaling pathway Source: Ensembl
    27. negative regulation of cell proliferation Source: Ensembl
    28. negative regulation of ERK1 and ERK2 cascade Source: Ensembl
    29. negative regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL
    30. negative regulation of release of cytochrome c from mitochondria Source: UniProtKB
    31. negative regulation of smooth muscle cell apoptotic process Source: BHF-UCL
    32. phosphatidylinositol-mediated signaling Source: BHF-UCL
    33. platelet activation Source: Reactome
    34. platelet degranulation Source: Reactome
    35. positive regulation of activated T cell proliferation Source: BHF-UCL
    36. positive regulation of calcineurin-NFAT signaling cascade Source: UniProtKB
    37. positive regulation of cardiac muscle hypertrophy Source: UniProtKB
    38. positive regulation of cell proliferation Source: BHF-UCL
    39. positive regulation of cerebellar granule cell precursor proliferation Source: Ensembl
    40. positive regulation of DNA binding Source: UniProtKB
    41. positive regulation of DNA replication Source: BHF-UCL
    42. positive regulation of epithelial cell proliferation Source: BHF-UCL
    43. positive regulation of fibroblast proliferation Source: BHF-UCL
    44. positive regulation of glucose import Source: UniProtKB
    45. positive regulation of glycogen biosynthetic process Source: UniProtKB
    46. positive regulation of glycolytic process Source: BHF-UCL
    47. positive regulation of insulin-like growth factor receptor signaling pathway Source: BHF-UCL
    48. positive regulation of MAPK cascade Source: UniProtKB
    49. positive regulation of mitosis Source: UniProtKB
    50. positive regulation of myoblast proliferation Source: Ensembl
    51. positive regulation of osteoblast differentiation Source: BHF-UCL
    52. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
    53. positive regulation of phosphatidylinositol 3-kinase signaling Source: BHF-UCL
    54. positive regulation of protein import into nucleus, translocation Source: UniProtKB
    55. positive regulation of protein kinase B signaling Source: Ensembl
    56. positive regulation of Ras protein signal transduction Source: BHF-UCL
    57. positive regulation of smooth muscle cell migration Source: BHF-UCL
    58. positive regulation of smooth muscle cell proliferation Source: BHF-UCL
    59. positive regulation of transcription, DNA-templated Source: UniProtKB
    60. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    61. positive regulation of tyrosine phosphorylation of Stat5 protein Source: BHF-UCL
    62. prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis Source: Ensembl
    63. prostate gland growth Source: Ensembl
    64. prostate gland stromal morphogenesis Source: Ensembl
    65. proteoglycan biosynthetic process Source: BHF-UCL
    66. Ras protein signal transduction Source: ProtInc
    67. regulation of establishment or maintenance of cell polarity Source: Ensembl
    68. regulation of multicellular organism growth Source: BHF-UCL
    69. signal transduction Source: ProtInc
    70. skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration Source: BHF-UCL
    71. skeletal system development Source: ProtInc
    72. Type II pneumocyte differentiation Source: Ensembl
    73. Type I pneumocyte differentiation Source: Ensembl
    74. water homeostasis Source: Ensembl

    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.
    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: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:5464. IGF1.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Insulin-like growth factor I deficiency (IGF1 deficiency) [MIM:608747]: Autosomal recessive disorder characterized by growth retardation, sensorineural deafness and mental retardation.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Deafness

    Organism-specific databases

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

    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

    ArrayExpressiP05019.
    BgeeiP05019.
    CleanExiHS_IGF1.
    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 – 6615
    Helixi67 – 693
    Beta strandi71 – 733
    Beta strandi79 – 813
    Beta strandi82 – 854
    Helixi90 – 956
    Beta strandi96 – 983
    Helixi102 – 1087
    Beta strandi109 – 1113
    Beta strandi112 – 1165

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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. Align

    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

    MGKISSLPTQ LFKCCFCDFL KVKMHTMSSS HLFYLALCLL TFTSSATAGP    50
    ETLCGAELVD ALQFVCGDRG FYFNKPTGYG SSSRRAPQTG IVDECCFRSC 100
    DLRRLEMYCA PLKPAKSARS VRAQRHTDMP KTQKYQPPST NKNTKSQRRK 150
    GWPKTHPGGE QKEGTEASLQ IRGKKKEQRR EIGSRNAECR GKKGK 195
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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.
    UCSCiuc001tjn.2. human. [P05019-3]
    uc001tjp.4. human. [P05019-1]

    Polymorphism databases

    DMDMi124263.

    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:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS44960.1. [P05019-3 ]
    CCDS44961.1. [P05019-4 ]
    CCDS44962.1. [P05019-1 ]
    CCDS9091.1. [P05019-2 ]
    PIRi A01611. IGHU1B.
    A92581. IGHU1.
    RefSeqi NP_000609.1. NM_000618.3. [P05019-2 ]
    NP_001104754.1. NM_001111284.1. [P05019-3 ]
    NP_001104755.1. NM_001111285.1. [P05019-1 ]
    UniGenei Hs.160562.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 49-77 [» ]
    A/B 90-110 [» ]
    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 [» ]
    ProteinModelPortali P05019.
    SMRi P05019. Positions 50-111.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109700. 12 interactions.
    DIPi DIP-41933N.
    DIP-6021N.
    IntActi P05019. 2 interactions.
    MINTi MINT-204184.
    STRINGi 9606.ENSP00000302665.

    PTM databases

    PhosphoSitei P05019.

    Polymorphism databases

    DMDMi 124263.

    Proteomic databases

    PaxDbi P05019.
    PRIDEi P05019.

    Protocols and materials databases

    DNASUi 3479.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000307046 ; ENSP00000302665 ; ENSG00000017427 . [P05019-1 ]
    ENST00000337514 ; ENSP00000337612 ; ENSG00000017427 . [P05019-2 ]
    ENST00000392904 ; ENSP00000376637 ; ENSG00000017427 . [P05019-4 ]
    ENST00000424202 ; ENSP00000416811 ; ENSG00000017427 . [P05019-3 ]
    ENST00000456098 ; ENSP00000394999 ; ENSG00000017427 . [P05019-4 ]
    GeneIDi 3479.
    KEGGi hsa:3479.
    UCSCi uc001tjn.2. human. [P05019-3 ]
    uc001tjp.4. human. [P05019-1 ]

    Organism-specific databases

    CTDi 3479.
    GeneCardsi GC12M102748.
    HGNCi HGNC:5464. IGF1.
    HPAi HPA048946.
    MIMi 147440. gene.
    608747. phenotype.
    neXtProti NX_P05019.
    Orphaneti 73272. Growth delay due to insulin-like growth factor type 1 deficiency.
    PharmGKBi PA29697.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG39886.
    HOGENOMi HOG000233362.
    HOVERGENi HBG006137.
    InParanoidi P05019.
    KOi K05459.
    OMAi HTVSYIH.
    OrthoDBi EOG7TF7CG.
    PhylomeDBi P05019.
    TreeFami TF332820.

    Enzyme and pathway databases

    Reactomei REACT_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.
    SignaLinki P05019.

    Miscellaneous databases

    ChiTaRSi IGF1. human.
    EvolutionaryTracei P05019.
    GeneWikii Insulin-like_growth_factor_1.
    GenomeRNAii 3479.
    NextBioi 13678.
    PMAP-CutDB P01343.
    PROi P05019.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P05019.
    Bgeei P05019.
    CleanExi HS_IGF1.
    Genevestigatori P05019.

    Family and domain databases

    Gene3Di 1.10.100.10. 1 hit.
    InterProi IPR022341. IGF-I.
    IPR016179. Insulin-like.
    IPR022350. Insulin-like_growth_factor.
    IPR022353. Insulin_CS.
    IPR022352. Insulin_family.
    [Graphical view ]
    Pfami PF00049. Insulin. 1 hit.
    [Graphical view ]
    PRINTSi PR02002. INSLNLIKEGF.
    PR02005. INSLNLIKEGF1.
    PR00276. INSULINFAMLY.
    SMARTi SM00078. IlGF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56994. SSF56994. 1 hit.
    PROSITEi PS00262. INSULIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 176 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