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P01344 (IGF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 188. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Insulin-like growth factor II

Short name=IGF-II
Alternative name(s):
Somatomedin-A
Gene names
Name:IGF2
ORF Names:PP1446
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length180 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.28

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. Ref.28

Subcellular location

Secreted.

Post-translational modification

O-glycosylated with core 1 or possibly core 8 glycans. Thr-96 is a minor glycosylation site compared to Thr-99. Ref.27 Ref.31 Ref.32

Polymorphism

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.

Involvement in disease

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. Ref.29

Sequence similarities

Belongs to the insulin family.

Mass spectrometry

Molecular mass is 7469.4 Da from positions 25 - 91. Determined by MALDI. Ref.25 Ref.26

Molecular mass is 7398.3 Da from positions 26 - 91. Determined by MALDI. Ref.25 Ref.26

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Glucose metabolism
Osteogenesis
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDwarfism
   DomainSignal
   Molecular functionGrowth factor
Hormone
Mitogen
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

cellular response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

exocrine pancreas development

Inferred from electronic annotation. Source: Ensembl

female pregnancy

Inferred from electronic annotation. Source: Ensembl

glucose metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

insulin receptor signaling pathway

Traceable author statement PubMed 1845984. Source: ProtInc

insulin receptor signaling pathway via phosphatidylinositol 3-kinase

Inferred from sequence or structural similarity. Source: BHF-UCL

memory

Inferred from electronic annotation. Source: Ensembl

multicellular organismal development

Traceable author statement Ref.1. Source: ProtInc

organ morphogenesis

Inferred from electronic annotation. Source: Ensembl

osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

positive regulation of MAPK cascade

Inferred from direct assay PubMed 11500939. Source: BHF-UCL

positive regulation of activated T cell proliferation

Inferred from direct assay PubMed 15694994. Source: BHF-UCL

positive regulation of catalytic activity

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cell division

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of cell proliferation

Inferred by curator PubMed 11500939. Source: BHF-UCL

positive regulation of glycogen (starch) synthase activity

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of glycogen biosynthetic process

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of insulin receptor signaling pathway

Inferred from direct assay PubMed 11500939. Source: BHF-UCL

positive regulation of mitosis

Inferred from direct assay PubMed 11500939. Source: BHF-UCL

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of protein kinase B signaling

Inferred from direct assay PubMed 11500939. Source: BHF-UCL

positive regulation of protein phosphorylation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of steroid hormone biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

regulation of gene expression by genetic imprinting

Traceable author statement PubMed 8968759. Source: ProtInc

regulation of transcription, DNA-templated

Non-traceable author statement PubMed 12881524. Source: BHF-UCL

response to drug

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to nicotine

Inferred from electronic annotation. Source: Ensembl

response to nutrient levels

Inferred from electronic annotation. Source: Ensembl

response to radiation

Inferred from electronic annotation. Source: Ensembl

skeletal system development

Traceable author statement PubMed 8298652. Source: ProtInc

striated muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

platelet alpha granule lumen

Traceable author statement. Source: Reactome

   Molecular_functiongrowth factor activity

Inferred from direct assay PubMed 11500939. Source: BHF-UCL

insulin receptor binding

Inferred from physical interaction PubMed 12138094. Source: BHF-UCL

insulin-like growth factor receptor binding

Traceable author statement PubMed 1845984. Source: ProtInc

protein binding

Inferred from physical interaction PubMed 10611375. Source: UniProtKB

protein serine/threonine kinase activator activity

Inferred from sequence or structural similarity. Source: BHF-UCL

receptor activator activity

Inferred from sequence or structural similarity. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

IGF2RP1171717EBI-7178764,EBI-1048580

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P01344-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P01344-2)

The sequence of this isoform differs from the canonical sequence as follows:
     53-53: S → RLPG
Isoform 3 (identifier: P01344-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MVSPDPQIIVVAPETELASMQVQRTEDGVTIIQIFWVGRKGELLRRTPVSSAMQTPM
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.21 Ref.23
Chain25 – 9167Insulin-like growth factor II
PRO_0000015717
Chain26 – 9166Insulin-like growth factor II Ala-25 Del
PRO_0000015718
Propeptide92 – 18089E peptide
PRO_0000015719
Peptide93 – 12634Preptin
PRO_0000370376

Regions

Region25 – 5228B
Region53 – 6412C
Region65 – 8521A
Region86 – 916D

Amino acid modifications

Glycosylation961O-linked (GalNAc...) Ref.31 Ref.32
Glycosylation991O-linked (GalNAc...) Ref.27 Ref.31
Glycosylation1631O-linked (GalNAc...) Ref.30 Ref.31
Disulfide bond33 ↔ 71 Ref.22 Ref.35
Disulfide bond45 ↔ 84 Ref.22 Ref.35
Disulfide bond70 ↔ 75 Ref.22 Ref.35

Natural variations

Alternative sequence11M → MVSPDPQIIVVAPETELASM QVQRTEDGVTIIQIFWVGRK GELLRRTPVSSAMQTPM in isoform 3.
VSP_045624
Alternative sequence531S → RLPG in isoform 2.
VSP_002708
Natural variant1201K → N.
Corresponds to variant rs14367 [ dbSNP | Ensembl ].
VAR_011959
Natural variant1731P → Q.
Corresponds to variant rs1050342 [ dbSNP | Ensembl ].
VAR_011960
Natural variant1801K → N.
Corresponds to variant rs12993 [ dbSNP | Ensembl ].
VAR_011961

Experimental info

Sequence conflict31I → M in AAA52544. Ref.6
Sequence conflict107 – 1104RYPV → EIPL in CAA27249. Ref.1
Sequence conflict1471E → ELE in AAA60088. Ref.5

Secondary structure

.............. 180
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: C1B0EB1E016BA37A

FASTA18020,140
        10         20         30         40         50         60 
MGIPMGKSML VLLTFLAFAS CCIAAYRPSE TLCGGELVDT LQFVCGDRGF YFSRPASRVS 

        70         80         90        100        110        120 
RRSRGIVEEC CFRSCDLALL ETYCATPAKS ERDVSTPPTV LPDNFPRYPV GKFFQYDTWK 

       130        140        150        160        170        180 
QSTQRLRRGL PALLRARRGH VLAKELEAFR EAKRHRPLIA LPTQDPAHGG APPEMASNRK 

« Hide

Isoform 2 [UniParc].

Checksum: A54CD97B56C2B96F
Show »

FASTA18320,477
Isoform 3 [UniParc].

Checksum: CF1395E851055BF6
Show »

FASTA23626,331

References

« Hide 'large scale' references
[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]"Organization of the human genes for insulin-like growth factors I and II."
de Pagter-Holthuizen P., van Schaik F.M.A., Verduijn G.M., van Ommen G.J.B., Bouma B.N., Jansen M., Sussenbach J.S.
FEBS Lett. 195:179-184(1986) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[16]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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]"Structure and functional analysis of the IGF-II/IGF2R interaction."
Brown J., Delaine C., Zaccheo O.J., Siebold C., Gilbert R.J., van Boxel G., Denley A., Wallace J.C., Hassan A.B., Forbes B.E., Jones E.Y.
EMBO J. 27:265-276(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (4.1 ANGSTROMS) OF 25-91 IN COMPLEX WITH IGF2R, DISULFIDE BONDS.
+Additional computationally mapped references.

Web resources

Wikipedia

Insulin-like growth factor 2 entry

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS44517.1. [P01344-3]
CCDS7728.1. [P01344-1]
PIRIGHU2. B23614.
I67610.
S02423.
RefSeqNP_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.
NP_001278791.1. NM_001291862.1.
UniGeneHs.272259.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP01344.
SMRP01344. Positions 29-88.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109702. 14 interactions.
DIPDIP-29508N.
IntActP01344. 4 interactions.
MINTMINT-6380943.
STRING9606.ENSP00000338297.

PTM databases

PhosphoSiteP01344.

Polymorphism databases

DMDM124255.

Proteomic databases

MaxQBP01344.
PaxDbP01344.
PRIDEP01344.

Protocols and materials databases

DNASU3481.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000300632; 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]
GeneID3481.
KEGGhsa:3481.
UCSCuc001lvg.3. human. [P01344-1]

Organism-specific databases

CTD3481.
GeneCardsGC11M002113.
GeneReviewsIGF2.
H-InvDBHIX0128667.
HGNCHGNC:5466. IGF2.
HPACAB024999.
HPA007993.
MIM147470. gene+phenotype.
180860. phenotype.
neXtProtNX_P01344.
Orphanet231117. 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.
PharmGKBPA29699.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG44017.
HOVERGENHBG006137.
KOK13769.
OMARYRWQAE.
OrthoDBEOG7TF7CG.
PhylomeDBP01344.
TreeFamTF332820.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_17015. Metabolism of proteins.
REACT_604. Hemostasis.
SignaLinkP01344.

Gene expression databases

ArrayExpressP01344.
BgeeP01344.
CleanExHS_IGF2.
GenevestigatorP01344.

Family and domain databases

Gene3D1.10.100.10. 1 hit.
InterProIPR022334. IGF2.
IPR013576. IGF2_C.
IPR016179. Insulin-like.
IPR022350. Insulin-like_growth_factor.
IPR022353. Insulin_CS.
IPR022352. Insulin_family.
[Graphical view]
PfamPF08365. IGF2_C. 1 hit.
PF00049. Insulin. 2 hits.
[Graphical view]
PRINTSPR02002. INSLNLIKEGF.
PR02006. INSLNLIKEGF2.
PR00276. INSULINFAMLY.
ProDomPD005188. IGF2_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00078. IlGF. 1 hit.
[Graphical view]
SUPFAMSSF56994. SSF56994. 1 hit.
PROSITEPS00262. INSULIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIGF2. human.
EvolutionaryTraceP01344.
GeneWikiInsulin-like_growth_factor_2.
GenomeRNAi3481.
NextBio13686.
PMAP-CutDBP01344.
PROP01344.
SOURCESearch...

Entry information

Entry nameIGF2_HUMAN
AccessionPrimary (citable) accession number: P01344
Secondary accession number(s): B3KX48 expand/collapse secondary AC list , B7WP08, C9JAF2, E3UN45, P78449, Q14299, Q1WM26, Q9UC68, Q9UC69
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 188 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM