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Insulin-like growth factor-binding protein 2 (IBP-2) (IGF-binding protein 2) (IGFBP-2)

 IBP2_HUMAN              Reviewed;         325 AA.
P18065; Q14619; Q9UCL3;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
02-MAR-2010, sequence version 2.
25-OCT-2017, entry version 182.
RecName: Full=Insulin-like growth factor-binding protein 2;
Short=IBP-2;
Short=IGF-binding protein 2;
Short=IGFBP-2;
Flags: Precursor;
Name=IGFBP2; Synonyms=BP2, IBP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fetal liver;
PubMed=2479552;
Binkert C., Landwehr J., Mary J.L., Schwander J., Heinrich G.;
"Cloning, sequence analysis and expression of a cDNA encoding a novel
insulin-like growth factor binding protein (IGFBP-2).";
EMBO J. 8:2497-2502(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 37-74.
PubMed=1697583;
Zapf J., Kiefer M., Merryweather J., Musiarz F., Bauer D., Born W.,
Fischer J.A., Froesch E.R.;
"Isolation from adult human serum of four insulin-like growth factor
(IGF) binding proteins and molecular cloning of one of them that is
increased by IGF I administration and in extrapancreatic tumor
hypoglycemia.";
J. Biol. Chem. 265:14892-14898(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=1710112; DOI=10.1016/0006-291X(91)90420-C;
Ehrenborg E., Vilhelmsdotter S., Bajalica S., Larsson C., Sterm I.,
Koch J., Brondum-Nielsen K., Luthman H.;
"Structure and localization of the human insulin-like growth factor-
binding protein 2 gene.";
Biochem. Biophys. Res. Commun. 176:1250-1255(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Retina;
PubMed=1712312; DOI=10.1016/0014-4835(91)90056-K;
Agarwal N., Hsieh C.L., Sills D., Swaroop M., Desai B., Francke U.,
Swaroop A.;
"Sequence analysis, expression and chromosomal localization of a gene,
isolated from a subtracted human retina cDNA library, that encodes an
insulin-like growth factor binding protein (IGFBP2).";
Exp. Eye Res. 52:549-561(1991).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=1376411; DOI=10.1210/mend.6.5.1376411;
Binkert C., Margot J.B., Landwehr J., Heinrich G., Schwander J.;
"Structure of the human insulin-like growth factor binding protein-2
gene.";
Mol. Endocrinol. 6:826-836(1992).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
Li W.B., Gruber C., Jessee J., Polayes D.;
"Full-length cDNA libraries and normalization.";
Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASP-137.
NIEHS SNPs program;
Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Ovary, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PROTEIN SEQUENCE OF 40-58, INTERACTION WITH IGF2, AND GLYCOSYLATION.
TISSUE=Cerebrospinal fluid;
PubMed=1726837;
Roghani M., Segovia B., Whitechurch O., Binoux M.;
"Purification from human cerebrospinal fluid of insulin-like growth
factor binding proteins (IGFBPs). Isolation of IGFBP-2, an altered
form of IGFBP-3 and a new IGFBP species.";
Growth Regul. 1:125-130(1991).
[11]
FUNCTION, IGF1-BINDING, DOMAIN, AND MUTAGENESIS OF 216-LYS--ARG-219
AND ASP-303.
PubMed=19081843; DOI=10.1371/journal.pone.0003926;
Zhou J., Li W., Kamei H., Duan C.;
"Duplication of the IGFBP-2 gene in teleost fish: protein structure
and functionality conservation and gene expression divergence.";
PLoS ONE 3:E3926-E3926(2008).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
STRUCTURE BY NMR OF 220-325, AND DISULFIDE BONDS.
PubMed=17020769; DOI=10.1016/j.jmb.2006.09.006;
Kuang Z., Yao S., Keizer D.W., Wang C.C., Bach L.A., Forbes B.E.,
Wallace J.C., Norton R.S.;
"Structure, dynamics and heparin binding of the C-terminal domain of
insulin-like growth factor-binding protein-2 (IGFBP-2).";
J. Mol. Biol. 364:690-704(2006).
-!- FUNCTION: Inhibits IGF-mediated growth and developmental rates.
IGF-binding proteins prolong the half-life of the IGFs and have
been shown to either inhibit or stimulate the growth promoting
effects of the IGFs on cell culture. They alter the interaction of
IGFs with their cell surface receptors.
{ECO:0000269|PubMed:19081843}.
-!- SUBUNIT: Binds IGF2 more than IGF1.
-!- INTERACTION:
Q9C086:INO80B; NbExp=4; IntAct=EBI-2504392, EBI-715611;
-!- SUBCELLULAR LOCATION: Secreted.
-!- DOMAIN: The C-terminus is required for IGF-binding and growth
inhibition. {ECO:0000269|PubMed:19081843}.
-!- PTM: O-glycosylated. {ECO:0000269|PubMed:1726837}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/igfbp2/";
-----------------------------------------------------------------------
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EMBL; X16302; CAA34373.1; -; mRNA.
EMBL; M69241; AAA36048.1; -; Genomic_DNA.
EMBL; M69237; AAA36048.1; JOINED; Genomic_DNA.
EMBL; M69239; AAA36048.1; JOINED; Genomic_DNA.
EMBL; M69240; AAA36048.1; JOINED; Genomic_DNA.
EMBL; M35410; AAA03246.1; -; mRNA.
EMBL; S37730; AAB22308.1; -; Genomic_DNA.
EMBL; S37712; AAB22308.1; JOINED; Genomic_DNA.
EMBL; S37722; AAB22308.1; JOINED; Genomic_DNA.
EMBL; S37726; AAB22308.1; JOINED; Genomic_DNA.
EMBL; CR610845; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AY398667; AAQ87876.1; -; Genomic_DNA.
EMBL; AC073321; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC007563; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC004312; AAH04312.1; -; mRNA.
EMBL; BC009902; AAH09902.1; -; mRNA.
EMBL; BC012769; AAH12769.1; -; mRNA.
EMBL; BC071967; AAH71967.1; -; mRNA.
PIR; A41927; A41927.
RefSeq; NP_000588.2; NM_000597.2.
RefSeq; NP_001300919.1; NM_001313990.1.
RefSeq; NP_001300921.1; NM_001313992.1.
RefSeq; NP_001300922.1; NM_001313993.1.
UniGene; Hs.438102; -.
PDB; 2H7T; NMR; -; A=220-325.
PDBsum; 2H7T; -.
ProteinModelPortal; P18065; -.
SMR; P18065; -.
BioGrid; 109706; 6.
CORUM; P18065; -.
IntAct; P18065; 3.
STRING; 9606.ENSP00000233809; -.
BindingDB; P18065; -.
ChEMBL; CHEMBL3088; -.
MEROPS; I31.953; -.
iPTMnet; P18065; -.
PhosphoSitePlus; P18065; -.
BioMuta; IGFBP2; -.
DMDM; 290457647; -.
EPD; P18065; -.
PaxDb; P18065; -.
PeptideAtlas; P18065; -.
PRIDE; P18065; -.
DNASU; 3485; -.
Ensembl; ENST00000233809; ENSP00000233809; ENSG00000115457.
GeneID; 3485; -.
KEGG; hsa:3485; -.
UCSC; uc061sgd.1; human.
CTD; 3485; -.
DisGeNET; 3485; -.
EuPathDB; HostDB:ENSG00000115457.9; -.
GeneCards; IGFBP2; -.
HGNC; HGNC:5471; IGFBP2.
HPA; HPA077723; -.
MIM; 146731; gene.
neXtProt; NX_P18065; -.
OpenTargets; ENSG00000115457; -.
PharmGKB; PA29704; -.
eggNOG; ENOG410IHUR; Eukaryota.
eggNOG; ENOG4111GWQ; LUCA.
GeneTree; ENSGT00550000074457; -.
HOGENOM; HOG000253012; -.
HOVERGEN; HBG002631; -.
InParanoid; P18065; -.
OMA; DGTMNML; -.
OrthoDB; EOG091G0EIN; -.
PhylomeDB; P18065; -.
TreeFam; TF331211; -.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
ChiTaRS; IGFBP2; human.
EvolutionaryTrace; P18065; -.
GeneWiki; IGFBP2; -.
GenomeRNAi; 3485; -.
PMAP-CutDB; P18065; -.
PRO; PR:P18065; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115457; -.
CleanEx; HS_IGFBP2; -.
ExpressionAtlas; P18065; baseline and differential.
Genevisible; P18065; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0031994; F:insulin-like growth factor I binding; IDA:UniProtKB.
GO; GO:0031995; F:insulin-like growth factor II binding; ISS:UniProtKB.
GO; GO:0005102; F:receptor binding; TAS:ParkinsonsUK-UCL.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0032870; P:cellular response to hormone stimulus; IEA:Ensembl.
GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:ParkinsonsUK-UCL.
GO; GO:0042104; P:positive regulation of activated T cell proliferation; IDA:BHF-UCL.
GO; GO:0001558; P:regulation of cell growth; IEA:InterPro.
GO; GO:0043567; P:regulation of insulin-like growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
GO; GO:0010226; P:response to lithium ion; IEA:Ensembl.
GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; IEA:Ensembl.
Gene3D; 4.10.800.10; -; 1.
InterPro; IPR009030; Growth_fac_rcpt_.
InterPro; IPR012210; IGFBP-2.
InterPro; IPR000867; IGFBP-like.
InterPro; IPR009168; IGFBP1-6.
InterPro; IPR022321; IGFBP_1-6_chordata.
InterPro; IPR017891; Insulin_GF-bd_Cys-rich_CS.
InterPro; IPR000716; Thyroglobulin_1.
InterPro; IPR036857; Thyroglobulin_1_sf.
PANTHER; PTHR11551; PTHR11551; 1.
Pfam; PF00219; IGFBP; 1.
Pfam; PF00086; Thyroglobulin_1; 1.
PRINTS; PR01976; IGFBPFAMILY.
PRINTS; PR01978; IGFBPFAMILY2.
SMART; SM00121; IB; 1.
SMART; SM00211; TY; 1.
SUPFAM; SSF57184; SSF57184; 1.
SUPFAM; SSF57610; SSF57610; 1.
PROSITE; PS00222; IGFBP_N_1; 1.
PROSITE; PS51323; IGFBP_N_2; 1.
PROSITE; PS00484; THYROGLOBULIN_1_1; 1.
PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Growth factor binding;
Growth regulation; Polymorphism; Reference proteome; Secreted; Signal.
SIGNAL 1 35
CHAIN 36 325 Insulin-like growth factor-binding
protein 2.
/FTId=PRO_0000014370.
DOMAIN 38 134 IGFBP N-terminal. {ECO:0000255|PROSITE-
ProRule:PRU00653}.
DOMAIN 224 306 Thyroglobulin type-1.
{ECO:0000255|PROSITE-ProRule:PRU00500}.
MOTIF 301 303 Cell attachment site.
DISULFID 227 261 {ECO:0000255|PROSITE-ProRule:PRU00500,
ECO:0000269|PubMed:17020769}.
DISULFID 272 283 {ECO:0000255|PROSITE-ProRule:PRU00500,
ECO:0000269|PubMed:17020769}.
DISULFID 285 306 {ECO:0000255|PROSITE-ProRule:PRU00500,
ECO:0000269|PubMed:17020769}.
VARIANT 137 137 A -> D (in dbSNP:rs9341096).
{ECO:0000269|Ref.7}.
/FTId=VAR_018871.
MUTAGEN 216 219 KKLR->NNLA: Does not disrupt growth-
inhibiting activity.
{ECO:0000269|PubMed:19081843}.
MUTAGEN 303 303 D->E: Does not disrupt growth-inhibiting
activity. {ECO:0000269|PubMed:19081843}.
CONFLICT 15 15 P -> PPLL (in Ref. 1; CAA34373, 3;
AAA36048, 4; AAA03246, 5; AAB22308, 7;
AAQ87876 and 9; AAH04312/AAH09902/
AAH12769/AAH71967). {ECO:0000305}.
CONFLICT 57 57 P -> R (in Ref. 3; AAA36048).
{ECO:0000305}.
CONFLICT 317 317 R -> C (in Ref. 1; CAA34373).
{ECO:0000305}.
CONFLICT 320 320 H -> D (in Ref. 3; AAA36048).
{ECO:0000305}.
HELIX 226 240 {ECO:0000244|PDB:2H7T}.
STRAND 247 249 {ECO:0000244|PDB:2H7T}.
STRAND 269 276 {ECO:0000244|PDB:2H7T}.
TURN 277 279 {ECO:0000244|PDB:2H7T}.
STRAND 282 285 {ECO:0000244|PDB:2H7T}.
SEQUENCE 325 AA; 34814 MW; 9E1436DBCCC6EA2A CRC64;
MLPRVGCPAL PLPPPPLLPL LLLLLGASGG GGGARAEVLF RCPPCTPERL AACGPPPVAP
PAAVAAVAGG ARMPCAELVR EPGCGCCSVC ARLEGEACGV YTPRCGQGLR CYPHPGSELP
LQALVMGEGT CEKRRDAEYG ASPEQVADNG DDHSEGGLVE NHVDSTMNML GGGGSAGRKP
LKSGMKELAV FREKVTEQHR QMGKGGKHHL GLEEPKKLRP PPARTPCQQE LDQVLERIST
MRLPDERGPL EHLYSLHIPN CDKHGLYNLK QCKMSLNGQR GECWCVNPNT GKLIQGAPTI
RGDPECHLFY NEQQEARGVH TQRMQ


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