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P01344

- IGF2_HUMAN

UniProt

P01344 - IGF2_HUMAN

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Protein

Insulin-like growth factor II

Gene
IGF2, PP1446
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.1 Publication
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 MAPK3.1 Publication

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
Complete GO annotation...

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
Complete GO annotation...

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.
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.1 Publication

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 ↔ 712 Publications
Disulfide bondi45 ↔ 842 Publications
Disulfide bondi70 ↔ 752 Publications
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-99.3 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. 4 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.

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.

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

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. VSP_045624
Alternative sequencei53 – 531S → RLPG in isoform 2. VSP_002708

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31I → M in AAA52544. 1 Publication
Sequence conflicti107 – 1104RYPV → EIPL in CAA27249. 1 Publication
Sequence conflicti147 – 1471E → ELE in AAA60088. 1 Publication

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. 4 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 189 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

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