P01344 (IGF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Insulin-like growth factor II
Short name=IGF-II

Alternative name(s):
Somatomedin-A

Cleaved into the following 3 chains:

1. Insulin-like growth factor II
2. Insulin-like growth factor II Ala-25 Del
3. Preptin

Gene names

Name:	IGF2
ORF Names:	PP1446

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	180 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Carbohydrate metabolism Glucose metabolism Osteogenesis
Cellular component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Dwarfism
Domain	Signal
Molecular function	Growth factor Hormone Mitogen
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW insulin receptor signaling pathway via phosphatidylinositol 3-kinase cascade Inferred from sequence or structural similarity. Source: BHF-UCL ossification Inferred from electronic annotation. Source: UniProtKB-KW 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 cell division Inferred from electronic annotation. Source: UniProtKB-KW 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 cascade Inferred from direct assay PubMed 11500939. Source: BHF-UCL regulation of gene expression by genetic imprinting Traceable author statement PubMed 8968759. Source: ProtInc regulation of transcription, DNA-dependent Non-traceable author statement PubMed 12881524. Source: BHF-UCL skeletal system development Traceable author statement PubMed 8298652. Source: ProtInc
Cellular_component	extracellular region Traceable author statement. Source: Reactome extracellular space Inferred from electronic annotation. Source: InterPro
Molecular_function	growth factor activity Inferred from direct assay PubMed 11500939. Source: BHF-UCL insulin-like growth factor receptor binding Traceable author statement PubMed 1845984. Source: ProtInc 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...

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
     110-180: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

24

Ref.21 Ref.23

Chain

25 – 91

67

Insulin-like growth factor II

PRO_0000015717

Chain

26 – 91

66

Insulin-like growth factor II Ala-25 Del

PRO_0000015718

Propeptide

92 – 180

89

E peptide

PRO_0000015719

Peptide

93 – 126

34

Preptin

PRO_0000370376

Regions

Region

25 – 52

28

B

Region

53 – 64

12

C

Region

65 – 85

21

A

Region

86 – 91

6

D

Amino acid modifications

Glycosylation

96

1

O-linked (GalNAc...) Ref.31 Ref.32

Glycosylation

99

1

O-linked (GalNAc...) Ref.27 Ref.31

Glycosylation

163

1

O-linked (GalNAc...) Ref.30 Ref.31

Disulfide bond

33 ↔ 71

Ref.22 Ref.35

Disulfide bond

45 ↔ 84

Ref.22 Ref.35

Disulfide bond

70 ↔ 75

Ref.22 Ref.35

Natural variations

Alternative sequence

1

1

M → MVSPDPQIIVVAPETELASM QVQRTEDGVTIIQIFWVGRK GELLRRTPVSSAMQTPM in isoform 3.

VSP_045624

Alternative sequence

53

1

S → RLPG in isoform 2.

VSP_002708

Alternative sequence

110 – 180

71

Missing in isoform 3.

VSP_045625

Natural variant

120

1

K → N.
Corresponds to variant rs14367 [ dbSNP | Ensembl ].

VAR_011959

Natural variant

173

1

P → Q.
Corresponds to variant rs1050342 [ dbSNP | Ensembl ].

VAR_011960

Natural variant

180

1

K → N.
Corresponds to variant rs12993 [ dbSNP | Ensembl ].

VAR_011961

Experimental info

Sequence conflict

3

1

I → M in AAA52544. Ref.6

Sequence conflict

107 – 110

4

RYPV → EIPL in CAA27249. Ref.1

Sequence conflict

147

1

E → ELE in AAA60088. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

180

Helix Strand Turn

Details...

Helix

34 – 44

11

Turn

45 – 48

4

Beta strand

50 – 52

3

Helix

55 – 58

4

Helix

61 – 72

12

Helix

77 – 82

6

Beta strand

86 – 88

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: C1B0EB1E016BA37A	FASTA	180	20,140
	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
	Isoform 2 [UniParc]. Checksum: A54CD97B56C2B96F	FASTA	183	20,477
	10 20 30 40 50 60 MGIPMGKSML VLLTFLAFAS CCIAAYRPSE TLCGGELVDT LQFVCGDRGF YFRLPGRPAS 70 80 90 100 110 120 RVSRRSRGIV EECCFRSCDL ALLETYCATP AKSERDVSTP PTVLPDNFPR YPVGKFFQYD 130 140 150 160 170 180 TWKQSTQRLR RGLPALLRAR RGHVLAKELE AFREAKRHRP LIALPTQDPA HGGAPPEMAS NRK
	Isoform 3 [UniParc]. Checksum: 26BAC778FCEB9ECC	FASTA	165	18,219
	10 20 30 40 50 60 MVSPDPQIIV VAPETELASM QVQRTEDGVT IIQIFWVGRK GELLRRTPVS SAMQTPMGIP 70 80 90 100 110 120 MGKSMLVLLT FLAFASCCIA AYRPSETLCG GELVDTLQFV CGDRGFYFSR PASRVSRRSR 130 140 150 160 GIVEECCFRS CDLALLETYC ATPAKSERDV STPPTVLPDN FPRYP

References

	« Hide 'large scale' referencesShow '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] (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]	"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. , 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. , 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, MASS SPECTROMETRY. 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, 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, 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

GeneReviews

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.

IPI

IPI00001611.
IPI00215977.
IPI00940065.

PIR

IGHU2. B23614.
I67610.
S02423.

RefSeq

NP_000603.1. NM_000612.4.
NP_001007140.2. NM_001007139.4.

UniGene

Hs.272259.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P01344.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29508N.

MINT

MINT-6380943.

STRING

9606.ENSP00000338297.

PTM databases

PhosphoSite

P01344.

Polymorphism databases

DMDM

124255.

Proteomic databases

PaxDb

P01344.

PRIDE

P01344.

Protocols and materials databases

DNASU

3481.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000300632; ENSP00000300632; ENSG00000167244.
ENST00000337883; ENSP00000338297; ENSG00000167244.
ENST00000381319; ENSP00000370720; ENSG00000167244.
ENST00000381379; ENSP00000370786; ENSG00000167244.
ENST00000381389; ENSP00000370796; ENSG00000167244.
ENST00000381392; ENSP00000370799; ENSG00000167244.
ENST00000381395; ENSP00000370802; ENSG00000167244.
ENST00000381406; ENSP00000370813; ENSG00000167244.
ENST00000416167; ENSP00000414497; ENSG00000167244.
ENST00000418738; ENSP00000402047; ENSG00000167244.

GeneID

3481.

KEGG

hsa:3481.

UCSC

uc001lvg.3. human.

Organism-specific databases

CTD

3481.

GeneCards

GC11M002113.

H-InvDB

HIX0128667.

HGNC

HGNC:5466. IGF2.

HPA

CAB024999.
HPA007993.

MIM

147470. gene+phenotype.
180860. phenotype.

neXtProt

NX_P01344.

Orphanet

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.

PharmGKB

PA29699.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG44017.

HOVERGEN

HBG006137.

KO

K13769.

OrthoDB

EOG4HMJBH.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_116125. Disease.

Gene expression databases

ArrayExpress

P01344.

Bgee

P01344.

CleanEx

HS_IGF2.

Genevestigator

P01344.

GermOnline

ENSG00000167244. Homo sapiens.

Family and domain databases

Gene3D

1.10.100.10. 1 hit.

InterPro

IPR022334. IGF2.
IPR013576. IGF2_C.
IPR016179. Insulin-like.
IPR022350. Insulin-like_growth_factor.
IPR022353. Insulin_CS.
IPR022352. Insulin_family.
[Graphical view]

Pfam

PF08365. IGF2_C. 1 hit.
PF00049. Insulin. 2 hits.
[Graphical view]

PRINTS

PR02002. INSLNLIKEGF.
PR02006. INSLNLIKEGF2.
PR00276. INSULINFAMLY.

ProDom

PD005188. IGF2_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00078. IlGF. 1 hit.
[Graphical view]

SUPFAM

SSF56994. Insulin-like. 1 hit.

PROSITE

PS00262. INSULIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

IGF2. human.

EvolutionaryTrace

P01344.

GenomeRNAi

3481.

NextBio

13686.

PMAP-CutDB

P01344.

SOURCE

Search...

Entry information

Entry name

IGF2_HUMAN

Accession

Primary (citable) accession number: P01344
Secondary accession number(s): B3KX48 , 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:	May 1, 2013
This is version 175 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.