ID IGF2_HUMAN Reviewed; 180 AA. AC P01344; B3KX48; B7WP08; C9JAF2; E3UN45; P78449; Q14299; Q1WM26; AC Q9UC68; Q9UC69; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 11-NOV-2015, entry version 202. DE RecName: Full=Insulin-like growth factor II; DE Short=IGF-II; DE AltName: Full=Somatomedin-A; DE AltName: Full=T3M-11-derived growth factor; DE Contains: DE RecName: Full=Insulin-like growth factor II; DE Contains: DE RecName: Full=Insulin-like growth factor II Ala-25 Del; DE Contains: DE RecName: Full=Preptin; DE Flags: Precursor; GN Name=IGF2; ORFNames=PP1446; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). RX PubMed=6382022; DOI=10.1038/310777a0; RA Dull T.J., Gray A., Hayflick J.S., Ullrich A.; RT "Insulin-like growth factor II precursor gene organization in relation RT to insulin gene family."; RL Nature 310:777-781(1984). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=6382021; DOI=10.1038/310775a0; RA Bell G.I., Merryweather J.P., Sanchez-Pescador R., Stempien M.M., RA Priestley L., Scott J., Rall L.B.; RT "Sequence of a cDNA clone encoding human preproinsulin-like growth RT factor II."; RL Nature 310:775-777(1984). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2450353; DOI=10.1073/pnas.85.6.1947; RA Shen S.-J., Daimon M., Wang C.-Y., Jansen M., Ilan J.; RT "Isolation of an insulin-like growth factor II cDNA with a unique 5' RT untranslated region from human placenta."; RL Proc. Natl. Acad. Sci. U.S.A. 85:1947-1951(1988). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). RX PubMed=3002851; DOI=10.1016/0014-5793(86)80156-9; RA de Pagter-Holthuizen P., van Schaik F.M.A., Verduijn G.M., RA van Ommen G.J.B., Bouma B.N., Jansen M., Sussenbach J.S.; RT "Organization of the human genes for insulin-like growth factors I and RT II."; RL FEBS Lett. 195:179-184(1986). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=3476948; DOI=10.1073/pnas.84.18.6330; RA Irminger J.C., Rosen K.M., Humbel R.E., Villa-Komaroff L.; RT "Tissue-specific expression of insulin-like growth factor II mRNAs RT with distinct 5' untranslated regions."; RL Proc. Natl. Acad. Sci. U.S.A. 84:6330-6334(1987). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=3683205; RA Rall L.B., Scott J., Bell G.I.; RT "Human insulin-like growth factor I and II messenger RNA: isolation of RT complementary DNA and analysis of expression."; RL Methods Enzymol. 146:239-248(1987). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RX PubMed=3881277; DOI=10.1016/0014-5793(85)80527-5; RA Jansen M., van Schaik F.M.A., van Tol H., van den Brande J.L., RA Sussenbach J.S.; RT "Nucleotide sequences of cDNAs encoding precursors of human insulin- RT like growth factor II (IGF-II) and an IGF-II variant."; RL FEBS Lett. 179:243-246(1985). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=7730145; RA Hagiwara K., Kobayashi T., Tobita M., Kikyo N., Yazaki Y., Okabe T.; RT "Isolation of a cDNA for a growth factor of vascular endothelial cells RT from human lung cancer cells: its identity with insulin-like growth RT factor II."; RL Jpn. J. Cancer Res. 86:202-207(1995). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=16531418; DOI=10.1093/hmg/ddl041; RA Monk D., Sanches R., Arnaud P., Apostolidou S., Hills F.A., RA Abu-Amero S., Murrell A., Friess H., Reik W., Stanier P., RA Constancia M., Moore G.E.; RT "Imprinting of IGF2 P0 transcript and novel alternatively spliced INS- RT IGF2 isoforms show differences between mouse and human."; RL Hum. Mol. Genet. 15:1259-1269(2006). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-165 (ISOFORM 3), AND ALTERNATIVE RP SPLICING. RX PubMed=20842449; DOI=10.1007/s11033-010-0259-z; RA Li J., Neumann I., Volkmer I., Staege M.S.; RT "Down-regulation of achaete-scute complex homolog 1 (ASCL1) in RT neuroblastoma cells induces up-regulation of insulin-like growth RT factor 2 (IGF2)."; RL Mol. Biol. Rep. 38:1515-1521(2011). RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15498874; DOI=10.1073/pnas.0404089101; RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., RA Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., RA Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., RA Gu J.; RT "Large-scale cDNA transfection screening for genes related to cancer RT development and progression."; RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004). RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG SeattleSNPs variation discovery resource; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. RN [14] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Cerebellum; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [15] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S., RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., RA Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [16] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [17] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Muscle; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [18] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 103-180. RX PubMed=3167054; DOI=10.1016/0167-4781(88)90124-8; RA de Pagter-Holthuizen P., van der Kammen R.A., Jansen M., RA van Schaik F.M.A., Sussenbach J.S.; RT "Differential expression of the human insulin-like growth factor II RT gene. Characterization of the IGF-II mRNAs and an mRNA encoding a RT putative IGF-II-associated protein."; RL Biochim. Biophys. Acta 950:282-295(1988). RN [19] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-161 (ISOFORM 2). RX PubMed=3653397; DOI=10.1016/0014-5793(87)80216-8; RA le Bouc Y., Noguiez P., Sondermeijer P., Dreyer D., Girard F., RA Binoux M.; RT "A new 5'-non-coding region for human placental insulin-like growth RT factor II mRNA expression."; RL FEBS Lett. 222:181-185(1987). RN [20] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52. RC TISSUE=Liver; RX PubMed=3652904; DOI=10.1089/dna.1987.6.283; RA Gray A., Tam A.W., Dull T.J., Hayflick J.S., Pintar J., Cavenee W.K., RA Koufos A., Ullrich A.; RT "Tissue-specific and developmentally regulated transcription of the RT insulin-like growth factor 2 gene."; RL DNA 6:283-295(1987). RN [21] RP PROTEIN SEQUENCE OF 25-91. RX PubMed=658418; DOI=10.1016/0014-5793(78)80237-3; RA Rinderknecht E., Humbel R.E.; RT "Primary structure of human insulin-like growth factor II."; RL FEBS Lett. 89:283-286(1978). RN [22] RP PARTIAL PROTEIN SEQUENCE, AND DISULFIDE BONDS. RX PubMed=2722836; RA Smith M.C., Cook J.A., Furman T.C., Occolowitz J.L.; RT "Structure and activity dependence of recombinant human insulin-like RT growth factor II on disulfide bond pairing."; RL J. Biol. Chem. 264:9314-9321(1989). RN [23] RP PROTEIN SEQUENCE OF 25-68. RX PubMed=7633596; DOI=10.1016/0378-4347(94)00576-Q; RA De Ceuninck F., Willeput J., Corvol M.; RT "Purification and characterization of insulin-like growth factor II RT (IGF II) and an IGF II variant from human placenta."; RL J. Chromatogr. B 666:203-214(1995). RN [24] RP POLYMORPHISM, AND ASSOCIATION WITH WITH BODY MASS INDEX. RX PubMed=11448941; DOI=10.1093/hmg/10.14.1491; RA Gaunt T.R., Cooper J.A., Miller G.J., Day I.N.M., O'Dell S.D.; RT "Positive associations between single nucleotide polymorphisms in the RT IGF2 gene region and body mass index in adult males."; RL Hum. Mol. Genet. 10:1491-1501(2001). RN [25] RP MASS SPECTROMETRY, AND PROTEOLYTIC PROCESSING. RX PubMed=12586351; DOI=10.1016/S0014-5793(03)00042-5; RA Nedelkov D., Nelson R.W., Kiernan U.A., Niederkofler E.E., Tubbs K.A.; RT "Detection of bound and free IGF-1 and IGF-2 in human plasma via RT biomolecular interaction analysis mass spectrometry."; RL FEBS Lett. 536:130-134(2003). RN [26] RP MASS SPECTROMETRY, AND PROTEOLYTIC PROCESSING. RX PubMed=15359740; DOI=10.1021/pr0499388; RA Nelson R.W., Nedelkov D., Tubbs K.A., Kiernan U.A.; RT "Quantitative mass spectrometric immunoassay of insulin like growth RT factor 1."; RL J. Proteome Res. 3:851-855(2004). RN [27] RP GLYCOSYLATION AT THR-99. RX PubMed=1569071; RA Hudgins W.R., Hampton B., Burgess W.H., Perdue J.F.; RT "The identification of O-glycosylated precursors of insulin-like RT growth factor II."; RL J. Biol. Chem. 267:8153-8160(1992). RN [28] RP OSTEOGENIC FUNCTION OF PREPTIN. RX PubMed=16912056; DOI=10.1152/ajpendo.00642.2005; RA Cornish J., Callon K.E., Bava U., Watson M., Xu X., Lin J.M., RA Chan V.A., Grey A.B., Naot D., Buchanan C.M., Cooper G.J., Reid I.R.; RT "Preptin, another peptide product of the pancreatic beta-cell, is RT osteogenic in vitro and in vivo."; RL Am. J. Physiol. 292:E117-E122(2007). RN [29] RP INVOLVEMENT IN SRS. RX PubMed=19066168; DOI=10.1136/jmg.2008.061820; RA Bartholdi D., Krajewska-Walasek M., Ounap K., Gaspar H., RA Chrzanowska K.H., Ilyana H., Kayserili H., Lurie I.W., Schinzel A., RA Baumer A.; RT "Epigenetic mutations of the imprinted IGF2-H19 domain in Silver- RT Russell syndrome (SRS): results from a large cohort of patients with RT SRS and SRS-like phenotypes."; RL J. Med. Genet. 46:192-197(2009). RN [30] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-163, AND STRUCTURE OF RP CARBOHYDRATES. RC TISSUE=Cerebrospinal fluid; RX PubMed=19838169; DOI=10.1038/nmeth.1392; RA Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., RA Brinkmalm G., Larson G.; RT "Enrichment of glycopeptides for glycan structure and attachment site RT identification."; RL Nat. Methods 6:809-811(2009). RN [31] RP GLYCOSYLATION AT THR-96; THR-99 AND THR-163, STRUCTURE OF RP CARBOHYDRATES, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=22171320; DOI=10.1074/mcp.M111.013649; RA Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.; RT "Human urinary glycoproteomics; attachment site specific analysis of RT N-and O-linked glycosylations by CID and ECD."; RL Mol. Cell. Proteomics 0:0-0(2011). RN [32] RP GLYCOSYLATION AT THR-96, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=23234360; DOI=10.1021/pr300963h; RA Halim A., Ruetschi U., Larson G., Nilsson J.; RT "LC-MS/MS characterization of O-glycosylation sites and glycan RT structures of human cerebrospinal fluid glycoproteins."; RL J. Proteome Res. 12:573-584(2013). RN [33] RP INVOLVEMENT IN GRDF. RX PubMed=26154720; DOI=10.1056/NEJMoa1415227; RA Begemann M., Zirn B., Santen G., Wirthgen E., Soellner L., RA Buettel H.M., Schweizer R., van Workum W., Binder G., Eggermann T.; RT "Paternally inherited IGF2 mutation and growth restriction."; RL N. Engl. J. Med. 373:349-356(2015). RN [34] RP 3D-STRUCTURE MODELING. RX PubMed=6189745; RA Blundell T.L., Bedarkar S., Humbel R.E.; RT "Tertiary structures, receptor binding, and antigenicity of RT insulinlike growth factors."; RL Fed. Proc. 42:2592-2597(1983). RN [35] RP STRUCTURE BY NMR. RX PubMed=7527339; RA Terasawa H., Kohda D., Hatanaka H., Nagata K., Higashihashi N., RA Fujiwara H., Sakano K., Inagaki F.; RT "Solution structure of human insulin-like growth factor II; RT recognition sites for receptors and binding proteins."; RL EMBO J. 13:5590-5597(1994). RN [36] RP X-RAY CRYSTALLOGRAPHY (4.1 ANGSTROMS) OF 25-91 IN COMPLEX WITH IGF2R, RP AND DISULFIDE BONDS. RX PubMed=18046459; DOI=10.1038/sj.emboj.7601938; RA Brown J., Delaine C., Zaccheo O.J., Siebold C., Gilbert R.J., RA van Boxel G., Denley A., Wallace J.C., Hassan A.B., Forbes B.E., RA Jones E.Y.; RT "Structure and functional analysis of the IGF-II/IGF2R interaction."; RL EMBO J. 27:265-276(2008). CC -!- FUNCTION: The insulin-like growth factors possess growth-promoting CC activity. In vitro, they are potent mitogens for cultured cells. CC IGF-II is influenced by placental lactogen and may play a role in CC fetal development. CC -!- FUNCTION: Preptin undergoes glucose-mediated co-secretion with CC insulin, and acts as physiological amplifier of glucose-mediated CC insulin secretion. Exhibits osteogenic properties by increasing CC osteoblast mitogenic activity through phosphoactivation of MAPK1 CC and MAPK3. CC -!- INTERACTION: CC P11717:IGF2R; NbExp=17; IntAct=EBI-7178764, EBI-1048580; CC Q93062:RBPMS; NbExp=3; IntAct=EBI-7178764, EBI-740322; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P01344-1; Sequence=Displayed; CC Name=2; CC IsoId=P01344-2; Sequence=VSP_002708; CC Name=3; CC IsoId=P01344-3; Sequence=VSP_045624; CC Note=Gene prediction based on EST data.; CC -!- PTM: O-glycosylated with core 1 or possibly core 8 glycans. Thr-96 CC is a minor glycosylation site compared to Thr-99. CC {ECO:0000269|PubMed:1569071, ECO:0000269|PubMed:19838169, CC ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:23234360}. CC -!- MASS SPECTROMETRY: Mass=7469.4; Method=MALDI; Range=25-91; CC Evidence={ECO:0000269|PubMed:12586351, CC ECO:0000269|PubMed:15359740}; CC -!- MASS SPECTROMETRY: Mass=7398.3; Method=MALDI; Range=26-91; CC Evidence={ECO:0000269|PubMed:12586351, CC ECO:0000269|PubMed:15359740}; CC -!- POLYMORPHISM: Genetic variations in IGF2 are associated with body CC mass index (BMI). The BMI is a statistical measurement which CC compares a person's weight and height. CC -!- DISEASE: Silver-Russell syndrome (SRS) [MIM:180860]: A clinically CC heterogeneous condition characterized by severe intrauterine CC growth retardation, poor postnatal growth, craniofacial features CC such as a triangular shaped face and a broad forehead, body CC asymmetry, and a variety of minor malformations. The phenotypic CC expression changes during childhood and adolescence, with the CC facial features and asymmetry usually becoming more subtle with CC age. {ECO:0000269|PubMed:19066168}. Note=The gene represented in CC this entry is involved in disease pathogenesis. Most of the cases CC of Silver-Russell syndrome are caused by the epigenetic changes of CC DNA hypomethylation at the telomeric imprinting control region CC (ICR1) on chromosome 11p15, involving the H19 and IGF2 genes. CC -!- DISEASE: Growth restriction, severe, with distinctive facies CC (GRDF) [MIM:616489]: A disease characterized by severe prenatal CC and postnatal growth restriction, facial dysmorphism, and short CC stature in the presence of normal or slightly elevated growth CC hormone levels. {ECO:0000269|PubMed:26154720}. Note=The disease is CC caused by mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Insulin-like growth factor 2 CC entry; CC URL="https://en.wikipedia.org/wiki/Insulin-like_growth_factor_2"; CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/igf2/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X03562; CAA27249.1; -; Genomic_DNA. DR EMBL; X00910; CAA25426.1; -; mRNA. DR EMBL; J03242; AAA52545.1; -; mRNA. DR EMBL; X03425; CAA27155.1; -; Genomic_DNA. DR EMBL; X03426; CAA27156.1; -; Genomic_DNA. DR EMBL; X03427; CAA27157.1; -; Genomic_DNA. DR EMBL; M17426; AAA60088.1; -; mRNA. DR EMBL; M29645; AAA52544.1; -; mRNA. DR EMBL; M17863; AAA52443.1; ALT_SEQ; mRNA. DR EMBL; S77035; AAB34155.1; -; mRNA. DR EMBL; DQ104203; ABD93451.1; -; mRNA. DR EMBL; HM481219; ADO21454.1; -; mRNA. DR EMBL; AF217977; AAG17220.1; -; mRNA. DR EMBL; BT007013; AAP35659.1; -; mRNA. DR EMBL; AF517226; AAM51825.1; -; Genomic_DNA. DR EMBL; AC132217; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK126688; BAG54360.1; -; mRNA. DR EMBL; CH471158; EAX02485.1; -; Genomic_DNA. DR EMBL; BC000531; AAH00531.1; -; mRNA. DR EMBL; X07868; CAA30717.1; -; Genomic_DNA. DR EMBL; X06159; CAA29516.1; -; mRNA. DR EMBL; X06160; CAA29517.1; -; Transcribed_RNA. DR EMBL; X06161; CAA29518.1; -; mRNA. DR EMBL; M22373; AAA52536.1; -; Genomic_DNA. DR CCDS; CCDS44517.1; -. [P01344-3] DR CCDS; CCDS7728.1; -. [P01344-1] DR PIR; B23614; IGHU2. DR PIR; I67610; I67610. DR PIR; S02423; S02423. DR RefSeq; NP_000603.1; NM_000612.5. [P01344-1] DR RefSeq; NP_001007140.2; NM_001007139.5. [P01344-1] DR RefSeq; NP_001121070.1; NM_001127598.2. [P01344-3] DR RefSeq; NP_001278790.1; NM_001291861.2. [P01344-1] DR RefSeq; NP_001278791.1; NM_001291862.2. [P01344-1] DR UniGene; Hs.272259; -. DR PDB; 1GF2; Model; -; A=25-91. DR PDB; 1IGL; NMR; -; A=25-91. DR PDB; 2L29; NMR; -; B=25-91. DR PDB; 2V5P; X-ray; 4.10 A; C/D=25-91. DR PDB; 3E4Z; X-ray; 2.28 A; C/D=25-91. DR PDB; 3KR3; X-ray; 2.20 A; D=25-91. DR PDBsum; 1GF2; -. DR PDBsum; 1IGL; -. DR PDBsum; 2L29; -. DR PDBsum; 2V5P; -. DR PDBsum; 3E4Z; -. DR PDBsum; 3KR3; -. DR ProteinModelPortal; P01344; -. DR SMR; P01344; 29-88. DR BioGrid; 109702; 15. DR DIP; DIP-29508N; -. DR IntAct; P01344; 6. DR MINT; MINT-6380943; -. DR STRING; 9606.ENSP00000391826; -. DR PhosphoSite; P01344; -. DR BioMuta; IGF2; -. DR DMDM; 124255; -. DR MaxQB; P01344; -. DR PaxDb; P01344; -. DR PRIDE; P01344; -. DR DNASU; 3481; -. DR Ensembl; ENST00000300632; ENSP00000300632; ENSG00000167244. [P01344-1] DR Ensembl; ENST00000381389; ENSP00000370796; ENSG00000167244. [P01344-1] DR Ensembl; ENST00000381392; ENSP00000370799; ENSG00000167244. [P01344-2] DR Ensembl; ENST00000381395; ENSP00000370802; ENSG00000167244. [P01344-1] DR Ensembl; ENST00000381406; ENSP00000370813; ENSG00000167244. [P01344-2] DR Ensembl; ENST00000416167; ENSP00000414497; ENSG00000167244. [P01344-1] DR Ensembl; ENST00000418738; ENSP00000402047; ENSG00000167244. [P01344-1] DR Ensembl; ENST00000434045; ENSP00000391826; ENSG00000167244. [P01344-3] DR GeneID; 3481; -. DR KEGG; hsa:3481; -. DR UCSC; uc001lvg.3; human. [P01344-1] DR CTD; 3481; -. DR GeneCards; IGF2; -. DR GeneReviews; IGF2; -. DR H-InvDB; HIX0128667; -. DR HGNC; HGNC:5466; IGF2. DR HPA; CAB024999; -. DR HPA; HPA007993; -. DR MIM; 147470; gene+phenotype. DR MIM; 180860; phenotype. DR MIM; 616489; phenotype. DR neXtProt; NX_P01344; -. DR Orphanet; 231117; Beckwith-Wiedemann syndrome due to imprinting defect of 11p15. DR Orphanet; 2128; Hemihypertrophy. DR Orphanet; 231144; Silver-Russell syndrome due to 11p15 microduplication. DR Orphanet; 231140; Silver-Russell syndrome due to imprinting defect of 11p15. DR PharmGKB; PA29699; -. DR eggNOG; ENOG410IY3P; Eukaryota. DR eggNOG; ENOG4111KP2; LUCA. DR GeneTree; ENSGT00530000063856; -. DR HOGENOM; HOG000233362; -. DR HOVERGEN; HBG006137; -. DR InParanoid; P01344; -. DR KO; K13769; -. DR OMA; FFQYDTW; -. DR OrthoDB; EOG7TF7CG; -. DR PhylomeDB; P01344; -. DR TreeFam; TF332820; -. DR Reactome; R-HSA-114608; Platelet degranulation. DR Reactome; R-HSA-2404192; Signaling by Type 1 Insulin-like Growth Factor 1 Receptor (IGF1R). DR Reactome; R-HSA-2428928; IRS-related events triggered by IGF1R. DR Reactome; R-HSA-2428933; SHC-related events triggered by IGF1R. DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs). DR SignaLink; P01344; -. DR ChiTaRS; IGF2; human. DR EvolutionaryTrace; P01344; -. DR GeneWiki; Insulin-like_growth_factor_2; -. DR GenomeRNAi; 3481; -. DR NextBio; 13686; -. DR PMAP-CutDB; P01344; -. DR PRO; PR:P01344; -. DR Proteomes; UP000005640; Chromosome 11. DR Bgee; P01344; -. DR CleanEx; HS_IGF2; -. DR Genevisible; P01344; HS. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome. DR GO; GO:0008083; F:growth factor activity; IDA:BHF-UCL. DR GO; GO:0005158; F:insulin receptor binding; IPI:BHF-UCL. DR GO; GO:0005159; F:insulin-like growth factor receptor binding; IMP:AgBase. DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; ISS:BHF-UCL. DR GO; GO:0030546; F:receptor activator activity; ISS:BHF-UCL. DR GO; GO:0007596; P:blood coagulation; TAS:Reactome. DR GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome. DR GO; GO:0031017; P:exocrine pancreas development; IEA:Ensembl. DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW. DR GO; GO:0008286; P:insulin receptor signaling pathway; TAS:ProtInc. DR GO; GO:0038028; P:insulin receptor signaling pathway via phosphatidylinositol 3-kinase; ISS:BHF-UCL. DR GO; GO:0007275; P:multicellular organismal development; TAS:ProtInc. DR GO; GO:0009887; P:organ morphogenesis; IEA:Ensembl. DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW. DR GO; GO:0030168; P:platelet activation; TAS:Reactome. DR GO; GO:0002576; P:platelet degranulation; TAS:Reactome. DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; IDA:BHF-UCL. DR GO; GO:0043085; P:positive regulation of catalytic activity; ISS:BHF-UCL. DR GO; GO:0008284; P:positive regulation of cell proliferation; IC:BHF-UCL. DR GO; GO:2000467; P:positive regulation of glycogen (starch) synthase activity; ISS:BHF-UCL. DR GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; ISS:BHF-UCL. DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IDA:BHF-UCL. DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:BHF-UCL. DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; IDA:BHF-UCL. DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISS:BHF-UCL. DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:BHF-UCL. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:BHF-UCL. DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISS:GOC. DR GO; GO:2000273; P:positive regulation of receptor activity; ISS:GOC. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl. DR GO; GO:0006349; P:regulation of gene expression by genetic imprinting; TAS:ProtInc. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:BHF-UCL. DR GO; GO:0001501; P:skeletal system development; TAS:ProtInc. DR GO; GO:0051146; P:striated muscle cell differentiation; IEA:Ensembl. DR Gene3D; 1.10.100.10; -; 1. DR InterPro; IPR022334; IGF2. DR InterPro; IPR013576; IGF2_C. DR InterPro; IPR016179; Insulin-like. DR InterPro; IPR022350; Insulin-like_growth_factor. DR InterPro; IPR022353; Insulin_CS. DR InterPro; IPR022352; Insulin_family. DR Pfam; PF08365; IGF2_C; 1. DR Pfam; PF00049; Insulin; 2. DR PRINTS; PR02002; INSLNLIKEGF. DR PRINTS; PR02006; INSLNLIKEGF2. DR PRINTS; PR00276; INSULINFAMLY. DR ProDom; PD005188; IGF2_C; 1. DR SMART; SM00078; IlGF; 1. DR SUPFAM; SSF56994; SSF56994; 1. DR PROSITE; PS00262; INSULIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Carbohydrate metabolism; KW Cleavage on pair of basic residues; Complete proteome; KW Direct protein sequencing; Disulfide bond; Dwarfism; KW Glucose metabolism; Glycoprotein; Growth factor; Hormone; Mitogen; KW Osteogenesis; Polymorphism; Reference proteome; Secreted; Signal. FT SIGNAL 1 24 {ECO:0000269|PubMed:658418, FT ECO:0000269|PubMed:7633596}. FT CHAIN 25 91 Insulin-like growth factor II. FT /FTId=PRO_0000015717. FT CHAIN 26 91 Insulin-like growth factor II Ala-25 Del. FT /FTId=PRO_0000015718. FT PROPEP 92 180 E peptide. FT /FTId=PRO_0000015719. FT PEPTIDE 93 126 Preptin. FT /FTId=PRO_0000370376. FT REGION 25 52 B. FT REGION 53 64 C. FT REGION 65 85 A. FT REGION 86 91 D. FT CARBOHYD 96 96 O-linked (GalNAc...). FT {ECO:0000269|PubMed:22171320, FT ECO:0000269|PubMed:23234360}. FT CARBOHYD 99 99 O-linked (GalNAc...). FT {ECO:0000269|PubMed:1569071, FT ECO:0000269|PubMed:22171320}. FT CARBOHYD 163 163 O-linked (GalNAc...). FT {ECO:0000269|PubMed:19838169, FT ECO:0000269|PubMed:22171320}. FT DISULFID 33 71 {ECO:0000269|PubMed:2722836}. FT DISULFID 45 84 {ECO:0000269|PubMed:2722836}. FT DISULFID 70 75 {ECO:0000269|PubMed:2722836}. FT VAR_SEQ 1 1 M -> MVSPDPQIIVVAPETELASMQVQRTEDGVTIIQIFW FT VGRKGELLRRTPVSSAMQTPM (in isoform 3). FT {ECO:0000303|PubMed:20842449}. FT /FTId=VSP_045624. FT VAR_SEQ 53 53 S -> RLPG (in isoform 2). FT {ECO:0000303|PubMed:3653397, FT ECO:0000303|PubMed:3881277}. FT /FTId=VSP_002708. FT VARIANT 120 120 K -> N (in dbSNP:rs14367). FT /FTId=VAR_011959. FT VARIANT 173 173 P -> Q (in dbSNP:rs1050342). FT /FTId=VAR_011960. FT VARIANT 180 180 K -> N (in dbSNP:rs12993). FT /FTId=VAR_011961. FT CONFLICT 3 3 I -> M (in Ref. 6; AAA52544). FT {ECO:0000305}. FT CONFLICT 107 110 RYPV -> EIPL (in Ref. 1; CAA27249). FT {ECO:0000305}. FT CONFLICT 147 147 E -> ELE (in Ref. 5; AAA60088). FT {ECO:0000305}. FT HELIX 34 44 {ECO:0000244|PDB:3KR3}. FT TURN 45 48 {ECO:0000244|PDB:3KR3}. FT STRAND 50 52 {ECO:0000244|PDB:3KR3}. FT HELIX 55 58 {ECO:0000244|PDB:3KR3}. FT HELIX 61 72 {ECO:0000244|PDB:3KR3}. FT HELIX 77 82 {ECO:0000244|PDB:3KR3}. FT STRAND 86 88 {ECO:0000244|PDB:1IGL}. SQ SEQUENCE 180 AA; 20140 MW; C1B0EB1E016BA37A CRC64; MGIPMGKSML VLLTFLAFAS CCIAAYRPSE TLCGGELVDT LQFVCGDRGF YFSRPASRVS RRSRGIVEEC CFRSCDLALL ETYCATPAKS ERDVSTPPTV LPDNFPRYPV GKFFQYDTWK QSTQRLRRGL PALLRARRGH VLAKELEAFR EAKRHRPLIA LPTQDPAHGG APPEMASNRK //