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P01344

- IGF2_HUMAN

UniProt

P01344 - IGF2_HUMAN

Protein

Insulin-like growth factor II

Gene

IGF2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 190 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    The insulin-like growth factors possess growth-promoting activity. In vitro, they are potent mitogens for cultured cells. IGF-II is influenced by placental lactogen and may play a role in fetal development.
    Preptin undergoes glucose-mediated co-secretion with insulin, and acts as physiological amplifier of glucose-mediated insulin secretion. Exhibits osteogenic properties by increasing osteoblast mitogenic activity through phosphoactivation of MAPK1 and MAPK3.

    GO - Molecular functioni

    1. growth factor activity Source: BHF-UCL
    2. insulin-like growth factor receptor binding Source: ProtInc
    3. insulin receptor binding Source: BHF-UCL
    4. protein binding Source: UniProtKB
    5. protein serine/threonine kinase activator activity Source: BHF-UCL
    6. receptor activator activity Source: BHF-UCL

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. cellular protein metabolic process Source: Reactome
    3. cellular response to mechanical stimulus Source: Ensembl
    4. exocrine pancreas development Source: Ensembl
    5. female pregnancy Source: Ensembl
    6. glucose metabolic process Source: UniProtKB-KW
    7. insulin receptor signaling pathway Source: ProtInc
    8. insulin receptor signaling pathway via phosphatidylinositol 3-kinase Source: BHF-UCL
    9. memory Source: Ensembl
    10. multicellular organismal development Source: ProtInc
    11. organ morphogenesis Source: Ensembl
    12. osteoblast differentiation Source: Ensembl
    13. platelet activation Source: Reactome
    14. platelet degranulation Source: Reactome
    15. positive regulation of activated T cell proliferation Source: BHF-UCL
    16. positive regulation of catalytic activity Source: BHF-UCL
    17. positive regulation of cell division Source: UniProtKB-KW
    18. positive regulation of cell proliferation Source: BHF-UCL
    19. positive regulation of glycogen (starch) synthase activity Source: BHF-UCL
    20. positive regulation of glycogen biosynthetic process Source: BHF-UCL
    21. positive regulation of insulin receptor signaling pathway Source: BHF-UCL
    22. positive regulation of MAPK cascade Source: BHF-UCL
    23. positive regulation of mitosis Source: BHF-UCL
    24. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
    25. positive regulation of protein kinase B signaling Source: BHF-UCL
    26. positive regulation of protein phosphorylation Source: BHF-UCL
    27. positive regulation of steroid hormone biosynthetic process Source: Ensembl
    28. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    29. regulation of gene expression by genetic imprinting Source: ProtInc
    30. regulation of transcription, DNA-templated Source: BHF-UCL
    31. response to drug Source: Ensembl
    32. response to estradiol Source: Ensembl
    33. response to ethanol Source: Ensembl
    34. response to nicotine Source: Ensembl
    35. response to nutrient levels Source: Ensembl
    36. response to radiation Source: Ensembl
    37. skeletal system development Source: ProtInc
    38. striated muscle cell differentiation Source: Ensembl

    Keywords - Molecular functioni

    Growth factor, Hormone, Mitogen

    Keywords - Biological processi

    Carbohydrate metabolism, Glucose metabolism, Osteogenesis

    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).
    SignaLinkiP01344.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Insulin-like growth factor II
    Short name:
    IGF-II
    Alternative name(s):
    Somatomedin-A
    Cleaved into the following 3 chains:
    Gene namesi
    Name:IGF2
    ORF Names:PP1446
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:5466. IGF2.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular space Source: Ensembl
    3. extracellular vesicular exosome Source: UniProt
    4. plasma membrane Source: Reactome
    5. platelet alpha granule lumen Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Silver-Russell syndrome (SRS) [MIM:180860]: A clinically heterogeneous condition characterized by severe intrauterine growth retardation, poor postnatal growth, craniofacial features such as a triangular shaped face and a broad forehead, body asymmetry, and a variety of minor malformations. The phenotypic expression changes during childhood and adolescence, with the facial features and asymmetry usually becoming more subtle with age.1 Publication
    Note: The gene represented in this entry is involved in disease pathogenesis. Most of the cases of Silver-Russell syndrome are caused by the epigenetic changes of DNA hypomethylation at the telomeric imprinting control region (ICR1) on chromosome 11p15, involving the H19 and IGF2 genes.

    Keywords - Diseasei

    Dwarfism

    Organism-specific databases

    MIMi147470. gene+phenotype.
    180860. phenotype.
    Orphaneti231117. Beckwith-Wiedemann syndrome due to imprinting defect of 11p15.
    2128. Hemihypertrophy.
    231144. Silver-Russell syndrome due to 11p15 microduplication.
    231140. Silver-Russell syndrome due to imprinting defect of 11p15.
    PharmGKBiPA29699.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 24242 PublicationsAdd
    BLAST
    Chaini25 – 9167Insulin-like growth factor IIPRO_0000015717Add
    BLAST
    Chaini26 – 9166Insulin-like growth factor II Ala-25 DelPRO_0000015718Add
    BLAST
    Propeptidei92 – 18089E peptidePRO_0000015719Add
    BLAST
    Peptidei93 – 12634PreptinPRO_0000370376Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi33 ↔ 711 Publication
    Disulfide bondi45 ↔ 841 Publication
    Disulfide bondi70 ↔ 751 Publication
    Glycosylationi96 – 961O-linked (GalNAc...)2 Publications
    Glycosylationi99 – 991O-linked (GalNAc...)2 Publications
    Glycosylationi163 – 1631O-linked (GalNAc...)2 Publications

    Post-translational modificationi

    O-glycosylated with core 1 or possibly core 8 glycans. Thr-96 is a minor glycosylation site compared to Thr-99.4 Publications

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP01344.
    PaxDbiP01344.
    PRIDEiP01344.

    PTM databases

    PhosphoSiteiP01344.

    Miscellaneous databases

    PMAP-CutDBP01344.

    Expressioni

    Gene expression databases

    ArrayExpressiP01344.
    BgeeiP01344.
    CleanExiHS_IGF2.
    GenevestigatoriP01344.

    Organism-specific databases

    HPAiCAB024999.
    HPA007993.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IGF2RP1171717EBI-7178764,EBI-1048580

    Protein-protein interaction databases

    BioGridi109702. 14 interactions.
    DIPiDIP-29508N.
    IntActiP01344. 5 interactions.
    MINTiMINT-6380943.
    STRINGi9606.ENSP00000338297.

    Structurei

    Secondary structure

    1
    180
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi34 – 4411
    Turni45 – 484
    Beta strandi50 – 523
    Helixi55 – 584
    Helixi61 – 7212
    Helixi77 – 826
    Beta strandi86 – 883

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GF2model-A25-91[»]
    1IGLNMR-A25-91[»]
    2L29NMR-B25-91[»]
    2V5PX-ray4.10C/D25-91[»]
    3E4ZX-ray2.28C/D25-91[»]
    3KR3X-ray2.20D25-91[»]
    ProteinModelPortaliP01344.
    SMRiP01344. Positions 29-88.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP01344.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni25 – 5228BAdd
    BLAST
    Regioni53 – 6412CAdd
    BLAST
    Regioni65 – 8521AAdd
    BLAST
    Regioni86 – 916D

    Sequence similaritiesi

    Belongs to the insulin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG44017.
    HOVERGENiHBG006137.
    KOiK13769.
    OMAiRYRWQAE.
    OrthoDBiEOG7TF7CG.
    PhylomeDBiP01344.
    TreeFamiTF332820.

    Family and domain databases

    Gene3Di1.10.100.10. 1 hit.
    InterProiIPR022334. IGF2.
    IPR013576. IGF2_C.
    IPR016179. Insulin-like.
    IPR022350. Insulin-like_growth_factor.
    IPR022353. Insulin_CS.
    IPR022352. Insulin_family.
    [Graphical view]
    PfamiPF08365. IGF2_C. 1 hit.
    PF00049. Insulin. 2 hits.
    [Graphical view]
    PRINTSiPR02002. INSLNLIKEGF.
    PR02006. INSLNLIKEGF2.
    PR00276. INSULINFAMLY.
    ProDomiPD005188. IGF2_C. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00078. IlGF. 1 hit.
    [Graphical view]
    SUPFAMiSSF56994. SSF56994. 1 hit.
    PROSITEiPS00262. INSULIN. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P01344-1) [UniParc]FASTAAdd to Basket

    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

    MGIPMGKSML VLLTFLAFAS CCIAAYRPSE TLCGGELVDT LQFVCGDRGF    50
    YFSRPASRVS RRSRGIVEEC CFRSCDLALL ETYCATPAKS ERDVSTPPTV 100
    LPDNFPRYPV GKFFQYDTWK QSTQRLRRGL PALLRARRGH VLAKELEAFR 150
    EAKRHRPLIA LPTQDPAHGG APPEMASNRK 180
    Length:180
    Mass (Da):20,140
    Last modified:July 21, 1986 - v1
    Checksum:iC1B0EB1E016BA37A
    GO
    Isoform 2 (identifier: P01344-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         53-53: S → RLPG

    Show »
    Length:183
    Mass (Da):20,477
    Checksum:iA54CD97B56C2B96F
    GO
    Isoform 3 (identifier: P01344-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MVSPDPQIIVVAPETELASMQVQRTEDGVTIIQIFWVGRKGELLRRTPVSSAMQTPM

    Note: Gene prediction based on EST data.

    Show »
    Length:236
    Mass (Da):26,331
    Checksum:iCF1395E851055BF6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31I → M in AAA52544. (PubMed:3683205)Curated
    Sequence conflicti107 – 1104RYPV → EIPL in CAA27249. (PubMed:6382022)Curated
    Sequence conflicti147 – 1471E → ELE in AAA60088. (PubMed:3476948)Curated

    Mass spectrometryi

    Molecular mass is 7469.4 Da from positions 25 - 91. Determined by MALDI. 2 Publications
    Molecular mass is 7398.3 Da from positions 26 - 91. Determined by MALDI. 2 Publications

    Polymorphismi

    Genetic variations in IGF2 are associated with body mass index (BMI). The BMI is a statistical measurement which compares a person's weight and height.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti120 – 1201K → N.
    Corresponds to variant rs14367 [ dbSNP | Ensembl ].
    VAR_011959
    Natural varianti173 – 1731P → Q.
    Corresponds to variant rs1050342 [ dbSNP | Ensembl ].
    VAR_011960
    Natural varianti180 – 1801K → N.
    Corresponds to variant rs12993 [ dbSNP | Ensembl ].
    VAR_011961

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MVSPDPQIIVVAPETELASM QVQRTEDGVTIIQIFWVGRK GELLRRTPVSSAMQTPM in isoform 3. 1 PublicationVSP_045624
    Alternative sequencei53 – 531S → RLPG in isoform 2. 2 PublicationsVSP_002708

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03562 Genomic DNA. Translation: CAA27249.1.
    X00910 mRNA. Translation: CAA25426.1.
    J03242 mRNA. Translation: AAA52545.1.
    X03425 Genomic DNA. Translation: CAA27155.1.
    X03426 Genomic DNA. Translation: CAA27156.1.
    X03427 Genomic DNA. Translation: CAA27157.1.
    M17426 mRNA. Translation: AAA60088.1.
    M29645 mRNA. Translation: AAA52544.1.
    M17863 mRNA. Translation: AAA52443.1. Sequence problems.
    S77035 mRNA. Translation: AAB34155.1.
    DQ104203 mRNA. Translation: ABD93451.1.
    HM481219 mRNA. Translation: ADO21454.1.
    AF217977 mRNA. Translation: AAG17220.1.
    BT007013 mRNA. Translation: AAP35659.1.
    AF517226 Genomic DNA. Translation: AAM51825.1.
    AC132217 Genomic DNA. No translation available.
    AK126688 mRNA. Translation: BAG54360.1.
    CH471158 Genomic DNA. Translation: EAX02485.1.
    BC000531 mRNA. Translation: AAH00531.1.
    X07868 Genomic DNA. Translation: CAA30717.1.
    X06159 mRNA. Translation: CAA29516.1.
    X06160 Transcribed RNA. Translation: CAA29517.1.
    X06161 mRNA. Translation: CAA29518.1.
    M22373 Genomic DNA. Translation: AAA52536.1.
    CCDSiCCDS44517.1. [P01344-3]
    CCDS7728.1. [P01344-1]
    PIRiB23614. IGHU2.
    I67610.
    S02423.
    RefSeqiNP_000603.1. NM_000612.4. [P01344-1]
    NP_001007140.2. NM_001007139.4. [P01344-1]
    NP_001121070.1. NM_001127598.1. [P01344-3]
    NP_001278790.1. NM_001291861.1. [P01344-1]
    NP_001278791.1. NM_001291862.1. [P01344-1]
    UniGeneiHs.272259.

    Genome annotation databases

    EnsembliENST00000300632; ENSP00000300632; ENSG00000167244. [P01344-1]
    ENST00000381389; ENSP00000370796; ENSG00000167244. [P01344-1]
    ENST00000381392; ENSP00000370799; ENSG00000167244. [P01344-2]
    ENST00000381395; ENSP00000370802; ENSG00000167244. [P01344-1]
    ENST00000381406; ENSP00000370813; ENSG00000167244. [P01344-2]
    ENST00000416167; ENSP00000414497; ENSG00000167244. [P01344-1]
    ENST00000418738; ENSP00000402047; ENSG00000167244. [P01344-1]
    ENST00000434045; ENSP00000391826; ENSG00000167244. [P01344-3]
    GeneIDi3481.
    KEGGihsa:3481.
    UCSCiuc001lvg.3. human. [P01344-1]

    Polymorphism databases

    DMDMi124255.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Insulin-like growth factor 2 entry

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03562 Genomic DNA. Translation: CAA27249.1 .
    X00910 mRNA. Translation: CAA25426.1 .
    J03242 mRNA. Translation: AAA52545.1 .
    X03425 Genomic DNA. Translation: CAA27155.1 .
    X03426 Genomic DNA. Translation: CAA27156.1 .
    X03427 Genomic DNA. Translation: CAA27157.1 .
    M17426 mRNA. Translation: AAA60088.1 .
    M29645 mRNA. Translation: AAA52544.1 .
    M17863 mRNA. Translation: AAA52443.1 . Sequence problems.
    S77035 mRNA. Translation: AAB34155.1 .
    DQ104203 mRNA. Translation: ABD93451.1 .
    HM481219 mRNA. Translation: ADO21454.1 .
    AF217977 mRNA. Translation: AAG17220.1 .
    BT007013 mRNA. Translation: AAP35659.1 .
    AF517226 Genomic DNA. Translation: AAM51825.1 .
    AC132217 Genomic DNA. No translation available.
    AK126688 mRNA. Translation: BAG54360.1 .
    CH471158 Genomic DNA. Translation: EAX02485.1 .
    BC000531 mRNA. Translation: AAH00531.1 .
    X07868 Genomic DNA. Translation: CAA30717.1 .
    X06159 mRNA. Translation: CAA29516.1 .
    X06160 Transcribed RNA. Translation: CAA29517.1 .
    X06161 mRNA. Translation: CAA29518.1 .
    M22373 Genomic DNA. Translation: AAA52536.1 .
    CCDSi CCDS44517.1. [P01344-3 ]
    CCDS7728.1. [P01344-1 ]
    PIRi B23614. IGHU2.
    I67610.
    S02423.
    RefSeqi NP_000603.1. NM_000612.4. [P01344-1 ]
    NP_001007140.2. NM_001007139.4. [P01344-1 ]
    NP_001121070.1. NM_001127598.1. [P01344-3 ]
    NP_001278790.1. NM_001291861.1. [P01344-1 ]
    NP_001278791.1. NM_001291862.1. [P01344-1 ]
    UniGenei Hs.272259.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GF2 model - A 25-91 [» ]
    1IGL NMR - A 25-91 [» ]
    2L29 NMR - B 25-91 [» ]
    2V5P X-ray 4.10 C/D 25-91 [» ]
    3E4Z X-ray 2.28 C/D 25-91 [» ]
    3KR3 X-ray 2.20 D 25-91 [» ]
    ProteinModelPortali P01344.
    SMRi P01344. Positions 29-88.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109702. 14 interactions.
    DIPi DIP-29508N.
    IntActi P01344. 5 interactions.
    MINTi MINT-6380943.
    STRINGi 9606.ENSP00000338297.

    PTM databases

    PhosphoSitei P01344.

    Polymorphism databases

    DMDMi 124255.

    Proteomic databases

    MaxQBi P01344.
    PaxDbi P01344.
    PRIDEi P01344.

    Protocols and materials databases

    DNASUi 3481.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000300632 ; ENSP00000300632 ; ENSG00000167244 . [P01344-1 ]
    ENST00000381389 ; ENSP00000370796 ; ENSG00000167244 . [P01344-1 ]
    ENST00000381392 ; ENSP00000370799 ; ENSG00000167244 . [P01344-2 ]
    ENST00000381395 ; ENSP00000370802 ; ENSG00000167244 . [P01344-1 ]
    ENST00000381406 ; ENSP00000370813 ; ENSG00000167244 . [P01344-2 ]
    ENST00000416167 ; ENSP00000414497 ; ENSG00000167244 . [P01344-1 ]
    ENST00000418738 ; ENSP00000402047 ; ENSG00000167244 . [P01344-1 ]
    ENST00000434045 ; ENSP00000391826 ; ENSG00000167244 . [P01344-3 ]
    GeneIDi 3481.
    KEGGi hsa:3481.
    UCSCi uc001lvg.3. human. [P01344-1 ]

    Organism-specific databases

    CTDi 3481.
    GeneCardsi GC11M002113.
    GeneReviewsi IGF2.
    H-InvDB HIX0128667.
    HGNCi HGNC:5466. IGF2.
    HPAi CAB024999.
    HPA007993.
    MIMi 147470. gene+phenotype.
    180860. phenotype.
    neXtProti NX_P01344.
    Orphaneti 231117. Beckwith-Wiedemann syndrome due to imprinting defect of 11p15.
    2128. Hemihypertrophy.
    231144. Silver-Russell syndrome due to 11p15 microduplication.
    231140. Silver-Russell syndrome due to imprinting defect of 11p15.
    PharmGKBi PA29699.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG44017.
    HOVERGENi HBG006137.
    KOi K13769.
    OMAi RYRWQAE.
    OrthoDBi EOG7TF7CG.
    PhylomeDBi P01344.
    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).
    SignaLinki P01344.

    Miscellaneous databases

    ChiTaRSi IGF2. human.
    EvolutionaryTracei P01344.
    GeneWikii Insulin-like_growth_factor_2.
    GenomeRNAii 3481.
    NextBioi 13686.
    PMAP-CutDB P01344.
    PROi P01344.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P01344.
    Bgeei P01344.
    CleanExi HS_IGF2.
    Genevestigatori P01344.

    Family and domain databases

    Gene3Di 1.10.100.10. 1 hit.
    InterProi IPR022334. IGF2.
    IPR013576. IGF2_C.
    IPR016179. Insulin-like.
    IPR022350. Insulin-like_growth_factor.
    IPR022353. Insulin_CS.
    IPR022352. Insulin_family.
    [Graphical view ]
    Pfami PF08365. IGF2_C. 1 hit.
    PF00049. Insulin. 2 hits.
    [Graphical view ]
    PRINTSi PR02002. INSLNLIKEGF.
    PR02006. INSLNLIKEGF2.
    PR00276. INSULINFAMLY.
    ProDomi PD005188. IGF2_C. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00078. IlGF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56994. SSF56994. 1 hit.
    PROSITEi PS00262. INSULIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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] (ISOFORM 1).
    2. "Sequence of a cDNA clone encoding human preproinsulin-like growth factor II."
      Bell G.I., Merryweather J.P., Sanchez-Pescador R., Stempien M.M., Priestley L., Scott J., Rall L.B.
      Nature 310:775-777(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Isolation of an insulin-like growth factor II cDNA with a unique 5' untranslated region from human placenta."
      Shen S.-J., Daimon M., Wang C.-Y., Jansen M., Ilan J.
      Proc. Natl. Acad. Sci. U.S.A. 85:1947-1951(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    5. "Tissue-specific expression of insulin-like growth factor II mRNAs with distinct 5' untranslated regions."
      Irminger J.C., Rosen K.M., Humbel R.E., Villa-Komaroff L.
      Proc. Natl. Acad. Sci. U.S.A. 84:6330-6334(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    6. "Human insulin-like growth factor I and II messenger RNA: isolation of complementary DNA and analysis of expression."
      Rall L.B., Scott J., Bell G.I.
      Methods Enzymol. 146:239-248(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    7. "Nucleotide sequences of cDNAs encoding precursors of human insulin-like growth factor II (IGF-II) and an IGF-II variant."
      Jansen M., van Schaik F.M.A., van Tol H., van den Brande J.L., Sussenbach J.S.
      FEBS Lett. 179:243-246(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    8. "Isolation of a cDNA for a growth factor of vascular endothelial cells from human lung cancer cells: its identity with insulin-like growth factor II."
      Hagiwara K., Kobayashi T., Tobita M., Kikyo N., Yazaki Y., Okabe T.
      Jpn. J. Cancer Res. 86:202-207(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    9. "Imprinting of IGF2 P0 transcript and novel alternatively spliced INS-IGF2 isoforms show differences between mouse and human."
      Monk D., Sanches R., Arnaud P., Apostolidou S., Hills F.A., Abu-Amero S., Murrell A., Friess H., Reik W., Stanier P., Constancia M., Moore G.E.
      Hum. Mol. Genet. 15:1259-1269(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    10. "Down-regulation of achaete-scute complex homolog 1 (ASCL1) in neuroblastoma cells induces up-regulation of insulin-like growth factor 2 (IGF2)."
      Li J., Neumann I., Volkmer I., Staege M.S.
      Mol. Biol. Rep. 38:1515-1521(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-165 (ISOFORM 3), ALTERNATIVE SPLICING.
    11. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
      Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
      , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
      Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    12. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    13. SeattleSNPs variation discovery resource
      Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    14. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Cerebellum.
    15. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    16. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    17. "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).
      Tissue: Muscle.
    18. "Differential expression of the human insulin-like growth factor II gene. Characterization of the IGF-II mRNAs and an mRNA encoding a putative IGF-II-associated protein."
      de Pagter-Holthuizen P., van der Kammen R.A., Jansen M., van Schaik F.M.A., Sussenbach J.S.
      Biochim. Biophys. Acta 950:282-295(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 103-180.
    19. "A new 5'-non-coding region for human placental insulin-like growth factor II mRNA expression."
      le Bouc Y., Noguiez P., Sondermeijer P., Dreyer D., Girard F., Binoux M.
      FEBS Lett. 222:181-185(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-161 (ISOFORM 2).
    20. "Tissue-specific and developmentally regulated transcription of the insulin-like growth factor 2 gene."
      Gray A., Tam A.W., Dull T.J., Hayflick J.S., Pintar J., Cavenee W.K., Koufos A., Ullrich A.
      DNA 6:283-295(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52.
      Tissue: Liver.
    21. "Primary structure of human insulin-like growth factor II."
      Rinderknecht E., Humbel R.E.
      FEBS Lett. 89:283-286(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-91.
    22. "Structure and activity dependence of recombinant human insulin-like growth factor II on disulfide bond pairing."
      Smith M.C., Cook J.A., Furman T.C., Occolowitz J.L.
      J. Biol. Chem. 264:9314-9321(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, DISULFIDE BONDS.
    23. "Purification and characterization of insulin-like growth factor II (IGF II) and an IGF II variant from human placenta."
      De Ceuninck F., Willeput J., Corvol M.
      J. Chromatogr. B 666:203-214(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 25-68.
    24. "Positive associations between single nucleotide polymorphisms in the IGF2 gene region and body mass index in adult males."
      Gaunt T.R., Cooper J.A., Miller G.J., Day I.N.M., O'Dell S.D.
      Hum. Mol. Genet. 10:1491-1501(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: POLYMORPHISM, ASSOCIATION WITH WITH BODY MASS INDEX.
    25. "Detection of bound and free IGF-1 and IGF-2 in human plasma via biomolecular interaction analysis mass spectrometry."
      Nedelkov D., Nelson R.W., Kiernan U.A., Niederkofler E.E., Tubbs K.A.
      FEBS Lett. 536:130-134(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: MASS SPECTROMETRY, PROTEOLYTIC PROCESSING.
    26. "Quantitative mass spectrometric immunoassay of insulin like growth factor 1."
      Nelson R.W., Nedelkov D., Tubbs K.A., Kiernan U.A.
      J. Proteome Res. 3:851-855(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: MASS SPECTROMETRY, PROTEOLYTIC PROCESSING.
    27. "The identification of O-glycosylated precursors of insulin-like growth factor II."
      Hudgins W.R., Hampton B., Burgess W.H., Perdue J.F.
      J. Biol. Chem. 267:8153-8160(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT THR-99.
    28. "Preptin, another peptide product of the pancreatic beta-cell, is osteogenic in vitro and in vivo."
      Cornish J., Callon K.E., Bava U., Watson M., Xu X., Lin J.M., Chan V.A., Grey A.B., Naot D., Buchanan C.M., Cooper G.J., Reid I.R.
      Am. J. Physiol. 292:E117-E122(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: OSTEOGENIC FUNCTION OF PREPTIN.
    29. "Epigenetic mutations of the imprinted IGF2-H19 domain in Silver-Russell syndrome (SRS): results from a large cohort of patients with SRS and SRS-like phenotypes."
      Bartholdi D., Krajewska-Walasek M., Ounap K., Gaspar H., Chrzanowska K.H., Ilyana H., Kayserili H., Lurie I.W., Schinzel A., Baumer A.
      J. Med. Genet. 46:192-197(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN SRS.
    30. "Enrichment of glycopeptides for glycan structure and attachment site identification."
      Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
      Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-163, STRUCTURE OF CARBOHYDRATES.
      Tissue: Cerebrospinal fluid.
    31. "Human urinary glycoproteomics; attachment site specific analysis of N-and O-linked glycosylations by CID and ECD."
      Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.
      Mol. Cell. Proteomics 0:0-0(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT THR-96; THR-99 AND THR-163, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
    32. "LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins."
      Halim A., Ruetschi U., Larson G., Nilsson J.
      J. Proteome Res. 12:573-584(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT THR-96, IDENTIFICATION BY MASS SPECTROMETRY.
    33. "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.
    34. "Solution structure of human insulin-like growth factor II; recognition sites for receptors and binding proteins."
      Terasawa H., Kohda D., Hatanaka H., Nagata K., Higashihashi N., Fujiwara H., Sakano K., Inagaki F.
      EMBO J. 13:5590-5597(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    35. Cited for: X-RAY CRYSTALLOGRAPHY (4.1 ANGSTROMS) OF 25-91 IN COMPLEX WITH IGF2R, DISULFIDE BONDS.

    Entry informationi

    Entry nameiIGF2_HUMAN
    AccessioniPrimary (citable) accession number: P01344
    Secondary accession number(s): B3KX48
    , B7WP08, C9JAF2, E3UN45, P78449, Q14299, Q1WM26, Q9UC68, Q9UC69
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 190 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 11
      Human chromosome 11: 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