ID IBP1_HUMAN Reviewed; 259 AA. AC P08833; A4D2F4; D3DVL9; Q8IYP5; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1988, sequence version 1. DT 02-SEP-2026, entry version 242. DE RecName: Full=Insulin-like growth factor-binding protein 1; DE Short=IBP-1; DE Short=IGF-binding protein 1; DE Short=IGFBP-1; DE AltName: Full=Placental protein 12; DE Short=PP12; DE Flags: Precursor; GN Name=IGFBP1; Synonyms=IBP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Placenta; RX PubMed=2461294; DOI=10.1002/j.1460-2075.1988.tb03087.x; RA Brinkman A., Groffen C., Kortleve D.J., Geurts A., Drop S.L.S.; RT "Isolation and characterization of a cDNA encoding the low molecular weight RT insulin-like growth factor binding protein (IBP-1)."; RL EMBO J. 7:2417-2423(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Decidua; RX PubMed=2454104; DOI=10.1016/s0006-291x(88)80425-x; RA Brewer M.T., Stetler G.L., Squires C.H., Thompson R.C., Busby W.H. Jr., RA Clemmons D.R.; RT "Cloning, characterization, and expression of a human insulin-like growth RT factor binding protein."; RL Biochem. Biophys. Res. Commun. 152:1289-1297(1988). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Placenta; RX PubMed=3419931; DOI=10.1093/nar/16.17.8711; RA Grundmann U., Nerlich C., Bohn H., Rein T.; RT "Cloning of cDNA encoding human placental protein 12 (PP12): binding RT protein for IGF I and somatomedin."; RL Nucleic Acids Res. 16:8711-8711(1988). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Decidua; RX PubMed=2457513; DOI=10.1016/0014-5793(88)80041-3; RA Julkunen M., Koistinen R., Aalto-Setala K., Seppala M., Janne O.A., RA Kontula K.; RT "Primary structure of human insulin-like growth factor-binding RT protein/placental protein 12 and tissue-specific expression of its mRNA."; RL FEBS Lett. 236:295-302(1988). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2458522; DOI=10.1210/mend-2-5-404; RA Lee Y.-L., Hintz R.L., James P.M., Lee P.D.K., Shively J.E., Powell D.R.; RT "Insulin-like growth factor (IGF) binding protein complementary RT deoxyribonucleic acid from human HEP G2 hepatoma cells: predicted protein RT sequence suggests an IGF binding domain different from those of the IGF-I RT and IGF-II receptors."; RL Mol. Endocrinol. 2:404-411(1988). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2474129; DOI=10.1210/mend-3-5-846; RA Cubbage M.L., Suwanichkul A., Powell D.R.; RT "Structure of the human chromosomal gene for the 25 kilodalton insulin-like RT growth factor binding protein."; RL Mol. Endocrinol. 3:846-851(1989). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2849945; DOI=10.1016/s0006-291x(88)80959-8; RA Brinkman A., Groffen C.A., Kortleve D.J., Drop S.L.; RT "Organization of the gene encoding the insulin-like growth factor binding RT protein IBP-1."; RL Biochem. Biophys. Res. Commun. 157:898-907(1988). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Liver; RX PubMed=1373120; DOI=10.1016/0888-7543(92)90440-4; RA Ehrenborg E., Larsson C., Stern I., Janson M., Powell D.R., Luthman H.; RT "Contiguous localization of the genes encoding human insulin-like growth RT factor binding proteins 1 (IGBP1) and 3 (IGBP3) on chromosome 7."; RL Genomics 12:497-502(1992). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-183 AND MET-253. RG NIEHS SNPs program; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., RA Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-253. RC TISSUE=Skin; 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [14] RP PROTEIN SEQUENCE OF 26-53; 95-152 AND 182-208, CLEAVAGE OF INITIATOR RP METHIONINE, PHOSPHORYLATION AT SER-120; SER-123; SER-126; SER-144 AND RP SER-194, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Amniotic fluid; RX PubMed=19765076; DOI=10.1111/j.1742-4658.2009.07318.x; RA Dolcini L., Sala A., Campagnoli M., Labo S., Valli M., Visai L., RA Minchiotti L., Monaco H.L., Galliano M.; RT "Identification of the amniotic fluid insulin-like growth factor binding RT protein-1 phosphorylation sites and propensity to proteolysis of the RT isoforms."; RL FEBS J. 276:6033-6046(2009). RN [15] RP NUCLEOTIDE SEQUENCE [MRNA] OF 141-259, AND PROTEIN SEQUENCE OF 26-259. RC TISSUE=Amniotic fluid; RX PubMed=2466665; DOI=10.1111/j.1432-1033.1989.tb14641.x; RA Luthman H., Soederling-Barros J., Persson B., Engberg C., Stern I., RA Lake M., Franzen S.A., Israelsson M., Raden B., Lindgren B., Hjelmqvist L., RA Enerbaeck S., Carlsson P., Bjursell G., Povoa G., Hall K., Joernvall H.; RT "Human insulin-like growth-factor-binding protein. Low-molecular-mass form: RT protein sequence and cDNA cloning."; RL Eur. J. Biochem. 180:259-265(1989). RN [16] RP PROTEIN SEQUENCE OF 26-53. RX PubMed=2971653; DOI=10.1016/s0021-9258(18)68206-7; RA Busby W.H. Jr., Klapper D.G., Clemmons D.R.; RT "Purification of a 31,000-dalton insulin-like growth factor binding protein RT from human amniotic fluid. Isolation of two forms with different biologic RT actions."; RL J. Biol. Chem. 263:14203-14210(1988). RN [17] RP MUTAGENESIS. RX PubMed=1718783; DOI=10.1016/0014-5793(91)81298-m; RA Brinkman A., Kortlrve D.J., Schuller A.G.P., Zwarthoff E.C., Drop S.L.S.; RT "Site-directed mutagenesis of the N-terminal region of IGF binding protein RT 1; analysis of IGF binding capability."; RL FEBS Lett. 291:264-268(1991). RN [18] RP FUNCTION, AND INTERACTION WITH IGF1 AND IGF2. RX PubMed=7679979; DOI=10.1210/endo.132.3.7679979; RA Oh Y., Mueller H.L., Lee D.Y., Fielder P.J., Rosenfeld R.G.; RT "Characterization of the affinities of insulin-like growth factor (IGF)- RT binding proteins 1-4 for IGF-I, IGF-II, IGF-I/insulin hybrid, and IGF-I RT analogs."; RL Endocrinology 132:1337-1344(1993). RN [19] RP PHOSPHORYLATION AT SER-126; SER-144 AND SER-194, AND PARTIAL PROTEIN RP SEQUENCE. RX PubMed=7678248; DOI=10.1016/s0021-9258(18)54050-3; RA Jones J.I., Busby W.H. Jr., Wright G., Smith C.E., Kimack N.M., RA Clemmons D.R.; RT "Identification of the sites of phosphorylation in insulin-like growth RT factor binding protein-1. Regulation of its affinity by phosphorylation of RT serine 101."; RL J. Biol. Chem. 268:1125-1131(1993). RN [20] RP FUNCTION, INTERACTION WITH ITGA5 AND ITGB1, AND MUTAGENESIS OF ARG-246. RX PubMed=7504269; DOI=10.1073/pnas.90.22.10553; RA Jones J.I., Gockerman A., Busby W.H. Jr., Wright G., Clemmons D.R.; RT "Insulin-like growth factor binding protein 1 stimulates cell migration and RT binds to the alpha 5 beta 1 integrin by means of its Arg-Gly-Asp RT sequence."; RL Proc. Natl. Acad. Sci. U.S.A. 90:10553-10557(1993). RN [21] RP DISULFIDE BONDS. RX PubMed=10329650; DOI=10.1074/jbc.274.21.14587; RA Neumann G.M., Bach L.A.; RT "The N-terminal disulfide linkages of human insulin-like growth factor- RT binding protein-6 (hIGFBP-6) and hIGFBP-1 are different as determined by RT mass spectrometry."; RL J. Biol. Chem. 274:14587-14594(1999). RN [22] RP FUNCTION. RX PubMed=11397844; DOI=10.1210/jcem.86.6.7532; RA Gleeson L.M., Chakraborty C., McKinnon T., Lala P.K.; RT "Insulin-like growth factor-binding protein 1 stimulates human trophoblast RT migration by signaling through alpha 5 beta 1 integrin via mitogen- RT activated protein Kinase pathway."; RL J. Clin. Endocrinol. Metab. 86:2484-2493(2001). RN [23] RP FUNCTION. RX PubMed=21892205; DOI=10.1038/onc.2011.357; RA Ammoun S., Schmid M.C., Zhou L., Ristic N., Ercolano E., Hilton D.A., RA Perks C.M., Hanemann C.O.; RT "Insulin-like growth factor-binding protein-1 (IGFBP-1) regulates human RT schwannoma proliferation, adhesion and survival."; RL Oncogene 31:1710-1722(2012). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [25] RP PHOSPHORYLATION AT SER-45; SER-156; THR-157; TYR-158; THR-193; SER-194; RP SER-199 AND SER-242. RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028; RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J., RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N., RA Pinna L.A., Pagliarini D.J., Dixon J.E.; RT "A single kinase generates the majority of the secreted phosphoproteome."; RL Cell 161:1619-1632(2015). RN [26] RP SUBCELLULAR LOCATION. RX PubMed=38246959; DOI=10.1038/s41598-024-52220-2; RA Huang B.L., Wei L.F., Lin Y.W., Huang L.S., Qu Q.Q., Li X.H., Chu L.Y., RA Xu Y.W., Wang W.D., Peng Y.H., Wu F.C.; RT "Serum IGFBP-1 as a promising diagnostic and prognostic biomarker for RT colorectal cancer."; RL Sci. Rep. 14:1839-1839(2024). RN [27] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 172-251, PARTIAL PROTEIN SEQUENCE, RP FUNCTION, PHOSPHORYLATION, AND DISULFIDE BONDS. RX PubMed=15972819; DOI=10.1074/jbc.m504304200; RA Sala A., Capaldi S., Campagnoli M., Faggion B., Labo S., Perduca M., RA Romano A., Carrizo M.E., Valli M., Visai L., Minchiotti L., Galliano M., RA Monaco H.L.; RT "Structure and properties of the C-terminal domain of insulin-like growth RT factor-binding protein-1 isolated from human amniotic fluid."; RL J. Biol. Chem. 280:29812-29819(2005). RN [28] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 166-259 IN COMPLEX WITH IGFBP4 AND RP IGF1, AND DISULFIDE BONDS. RX PubMed=16924115; DOI=10.1073/pnas.0605652103; RA Sitar T., Popowicz G.M., Siwanowicz I., Huber R., Holak T.A.; RT "Structural basis for the inhibition of insulin-like growth factors by RT insulin-like growth factor-binding proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 103:13028-13033(2006). CC -!- FUNCTION: Multifunctional protein that plays a critical role in CC regulating the availability of IGFs such as IGF1 and IGF2 to their CC receptors and thereby regulates IGF-mediated cellular processes CC including cell migration, proliferation, differentiation or apoptosis CC in a cell-type specific manner (PubMed:11397844, PubMed:15972819). Also CC plays a positive role in cell migration by interacting with integrin CC ITGA5:ITGB1 through its RGD motif (PubMed:7504269). Mechanistically, CC binding to integrins leads to activation of focal adhesion kinase/PTK2 CC and stimulation of the mitogen-activated protein kinase (MAPK) pathway CC (PubMed:11397844). Regulates cardiomyocyte apoptosis by suppressing CC HIF-1alpha/HIF1A ubiquitination and subsequent degradation (By CC similarity). {ECO:0000250|UniProtKB:P21743, CC ECO:0000269|PubMed:11397844, ECO:0000269|PubMed:15972819, CC ECO:0000269|PubMed:3419931, ECO:0000269|PubMed:7504269}. CC -!- SUBUNIT: Binds equally well IGF1 and IGF2 (PubMed:7679979). Interacts CC with integrin ITGA5:ITGB1 (PubMed:7504269). Interacts with VHL; this CC interaction inhibits HIF1A degradation (By similarity). CC {ECO:0000250|UniProtKB:P21743, ECO:0000269|PubMed:16924115, CC ECO:0000269|PubMed:7504269, ECO:0000269|PubMed:7679979}. CC -!- INTERACTION: CC P08833; P46379-2: BAG6; NbExp=3; IntAct=EBI-13646303, EBI-10988864; CC P08833; G5E9A7: DMWD; NbExp=3; IntAct=EBI-13646303, EBI-10976677; CC P08833; Q8IXL6: FAM20C; NbExp=2; IntAct=EBI-13646303, EBI-7147442; CC P08833; P05019: IGF1; NbExp=2; IntAct=EBI-13646303, EBI-7902275; CC P08833; O14901: KLF11; NbExp=3; IntAct=EBI-13646303, EBI-948266; CC P08833; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-13646303, EBI-5235340; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:38246959}. CC -!- PTM: Phosphorylated; probably by casein kinase II. Phosphorylation CC alters the affinity of the protein for IGFs. In amniotic fluid, the CC unmodified protein is the most abundant form, while mono-, bi-, CC tri- and tetraphosphorylated forms are present in decreasing amounts. CC The phosphorylation state may influence the propensity to proteolysis. CC {ECO:0000269|PubMed:15972819, ECO:0000269|PubMed:19765076, CC ECO:0000269|PubMed:7678248}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA52540.1; Type=Frameshift; Evidence={ECO:0000305}; 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; Y00856; CAA68770.1; -; mRNA. DR EMBL; M20841; AAA52540.1; ALT_FRAME; mRNA. DR EMBL; X12385; CAA30942.1; -; mRNA. DR EMBL; X13405; CAA31771.1; -; mRNA. DR EMBL; M31145; AAA52542.1; -; mRNA. DR EMBL; M59316; AAA52783.1; -; Genomic_DNA. DR EMBL; M23595; AAA52785.1; -; Genomic_DNA. DR EMBL; M23592; AAA52785.1; JOINED; Genomic_DNA. DR EMBL; M23593; AAA52785.1; JOINED; Genomic_DNA. DR EMBL; M23594; AAA52785.1; JOINED; Genomic_DNA. DR EMBL; M74587; AAA52784.1; -; Genomic_DNA. DR EMBL; BT019685; AAV38491.1; -; mRNA. DR EMBL; AY434089; AAQ96599.1; -; Genomic_DNA. DR EMBL; CH236958; EAL23800.1; -; Genomic_DNA. DR EMBL; CH471128; EAW61030.1; -; Genomic_DNA. DR EMBL; CH471128; EAW61031.1; -; Genomic_DNA. DR EMBL; BC035263; AAH35263.2; -; mRNA. DR EMBL; X15002; CAA33110.1; -; mRNA. DR CCDS; CCDS5504.1; -. DR PIR; A31867; IOHU1. DR RefSeq; NP_000587.1; NM_000596.4. DR PDB; 1ZT3; X-ray; 1.80 A; A=172-251. DR PDB; 1ZT5; X-ray; 1.82 A; A=172-251. DR PDB; 2DSQ; X-ray; 2.80 A; G/H=166-259. DR AlphaFoldDB; P08833; -. DR MDRepo; P08833; -. DR SMR; P08833; -. DR BioGRID; 109705; 31. DR DIP; DIP-59846N; -. DR FunCoup; P08833; 176. DR IntAct; P08833; 28. DR NDEx; IQUERY-CP-IGFBP1; 6 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000275525; -. DR BindingDB; P08833; -. DR ChEMBL; CHEMBL4178; -. DR DrugBank; DB01277; Mecasermin. DR MEROPS; I31.951; -. DR iPTMnet; P08833; -. DR PhosphoSitePlus; P08833; -. DR BioMuta; IGFBP1; -. DR DMDM; 124055; -. DR MassIVE; P08833; -. DR PaxDb; 9606-ENSP00000275525; -. DR PeptideAtlas; P08833; -. DR ProteomicsDB; 52167; -. DR Antibodypedia; 3841; 710 antibodies from 41 providers. DR DNASU; 3484; -. DR Ensembl; ENST00000275525.8; ENSP00000275525.3; ENSG00000146678.10. DR GeneID; 3484; -. DR KEGG; hsa:3484; -. DR MANE-Select; ENST00000275525.8; ENSP00000275525.3; NM_000596.4; NP_000587.1. DR UCSC; uc003tnp.4; human. DR AGR; HGNC:5469; -. DR ClinPGx; PA29703; -. DR CTD; 3484; -. DR DisGeNET; 3484; -. DR GeneCards; IGFBP1; -. DR HGNC; HGNC:5469; IGFBP1. DR HPA; ENSG00000146678; Tissue enriched (liver). DR MIM; 146730; gene. DR OpenTargets; ENSG00000146678; -. DR VEuPathDB; HostDB:ENSG00000146678; -. DR eggNOG; ENOG502QWRP; Eukaryota. DR GeneTree; ENSGT00940000157394; -. DR HOGENOM; CLU_070833_3_0_1; -. DR InParanoid; P08833; -. DR OMA; TRGDPNC; -. DR OrthoDB; 9926277at2759; -. DR PAN-GO; P08833; 4 GO annotations based on evolutionary models. DR PhylomeDB; P08833; -. DR PathwayCommons; P08833; -. DR Reactome; R-HSA-380994; ATF4 activates genes in response to endoplasmic reticulum stress. DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs). DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation. DR Reactome; R-HSA-9615017; FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes. DR SignaLink; P08833; -. DR SIGNOR; P08833; -. DR Agora; ENSG00000146678; -. DR BioGRID-ORCS; 3484; 15 hits in 1150 CRISPR screens. DR ChiTaRS; IGFBP1; human. DR EvolutionaryTrace; P08833; -. DR GeneWiki; IGFBP1; -. DR GenomeRNAi; 3484; -. DR Pharos; P08833; Tchem. DR PRO; PR:P08833; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; P08833; protein. DR Bgee; ENSG00000146678; Expressed in decidua and 99 other cell types or tissues. DR ExpressionAtlas; P08833; baseline and differential. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0005576; C:extracellular region; EXP:UniProtKB. DR GO; GO:0140144; C:non-collagenous component of basement membrane; TAS:GO_Central. DR GO; GO:0005520; F:insulin-like growth factor binding; TAS:ProtInc. DR GO; GO:0031994; F:insulin-like growth factor I binding; IDA:UniProtKB. DR GO; GO:0031995; F:insulin-like growth factor II binding; IDA:UniProtKB. DR GO; GO:0005102; F:signaling receptor binding; TAS:ParkinsonsUK-UCL. DR GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl. DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:ParkinsonsUK-UCL. DR GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl. DR GO; GO:0043567; P:regulation of insulin-like growth factor receptor signaling pathway; IBA:GO_Central. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0042246; P:tissue regeneration; IEA:Ensembl. DR CDD; cd00191; TY; 1. DR FunFam; 4.10.40.20:FF:000001; Insulin-like growth factor binding protein 5; 1. DR FunFam; 4.10.800.10:FF:000002; Insulin-like growth factor-binding protein 2; 1. DR Gene3D; 4.10.40.20; -; 1. DR Gene3D; 4.10.800.10; Thyroglobulin type-1; 1. DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf. DR InterPro; IPR000867; IGFBP-like. DR InterPro; IPR022322; IGFBP1. DR InterPro; IPR022321; IGFBP_1-6_chordata. DR InterPro; IPR017891; Insulin_GF-bd_Cys-rich_CS. DR InterPro; IPR000716; Thyroglobulin_1. DR InterPro; IPR036857; Thyroglobulin_1_sf. DR PANTHER; PTHR11551; INSULIN-LIKE GROWTH FACTOR BINDING PROTEIN; 1. DR PANTHER; PTHR11551:SF6; INSULIN-LIKE GROWTH FACTOR-BINDING PROTEIN 1; 1. DR Pfam; PF00219; IGFBP; 1. DR Pfam; PF00086; Thyroglobulin_1; 1. DR PRINTS; PR01976; IGFBPFAMILY. DR PRINTS; PR01977; IGFBPFAMILY1. DR SMART; SM00121; IB; 1. DR SMART; SM00211; TY; 1. DR SUPFAM; SSF57184; Growth factor receptor domain; 1. DR SUPFAM; SSF57610; Thyroglobulin type-1 domain; 1. DR PROSITE; PS00222; IGFBP_N_1; 1. DR PROSITE; PS51323; IGFBP_N_2; 1. DR PROSITE; PS00484; THYROGLOBULIN_1_1; 1. DR PROSITE; PS51162; THYROGLOBULIN_1_2; 1. DR PDBsum; 1ZT3; -. DR PDBsum; 1ZT5; -. DR PDBsum; 2DSQ; -. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disulfide bond; KW Growth factor binding; Phosphoprotein; Proteomics identification; KW Reference proteome; Secreted; Signal. FT SIGNAL 1..25 FT /evidence="ECO:0000269|PubMed:19765076, FT ECO:0000269|PubMed:2466665, ECO:0000269|PubMed:2971653" FT CHAIN 26..259 FT /note="Insulin-like growth factor-binding protein 1" FT /id="PRO_0000014365" FT DOMAIN 26..107 FT /note="IGFBP N-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DOMAIN 173..251 FT /note="Thyroglobulin type-1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00500" FT MOTIF 246..248 FT /note="Cell attachment site" FT /evidence="ECO:0000269|PubMed:7504269" FT MOD_RES 45 FT /note="Phosphoserine; by FAM20C" FT /evidence="ECO:0000269|PubMed:26091039" FT MOD_RES 120 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:19765076" FT MOD_RES 123 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:19765076" FT MOD_RES 126 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:19765076, FT ECO:0000269|PubMed:7678248" FT MOD_RES 144 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:19765076, FT ECO:0000269|PubMed:7678248, ECO:0007744|PubMed:24275569" FT MOD_RES 156 FT /note="Phosphoserine; by FAM20C" FT /evidence="ECO:0000269|PubMed:26091039" FT MOD_RES 157 FT /note="Phosphothreonine; by FAM20C" FT /evidence="ECO:0000269|PubMed:26091039" FT MOD_RES 158 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:26091039" FT MOD_RES 193 FT /note="Phosphothreonine; by FAM20C" FT /evidence="ECO:0000269|PubMed:26091039" FT MOD_RES 194 FT /note="Phosphoserine; by FAM20C" FT /evidence="ECO:0000269|PubMed:19765076, FT ECO:0000269|PubMed:26091039, ECO:0000269|PubMed:7678248" FT MOD_RES 199 FT /note="Phosphoserine; by FAM20C" FT /evidence="ECO:0000269|PubMed:26091039" FT MOD_RES 242 FT /note="Phosphoserine; by FAM20C" FT /evidence="ECO:0000269|PubMed:26091039" FT DISULFID 30..57 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 33..59 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 41..60 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 48..63 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 71..84 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 78..104 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00653" FT DISULFID 176..206 FT DISULFID 217..228 FT DISULFID 230..251 FT VARIANT 114 FT /note="H -> D (in dbSNP:rs41258845)" FT /id="VAR_049564" FT VARIANT 183 FT /note="V -> I (in dbSNP:rs1065782)" FT /evidence="ECO:0000269|Ref.10" FT /id="VAR_011905" FT VARIANT 253 FT /note="I -> M (in dbSNP:rs4619)" FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.10" FT /id="VAR_003821" FT MUTAGEN 246 FT /note="R->W: Loss of binding to ITGA5." FT /evidence="ECO:0000269|PubMed:7504269" FT CONFLICT 213 FT /note="H -> Q (in Ref. 2; AAA52540)" FT /evidence="ECO:0000305" FT HELIX 175..193 FT /evidence="ECO:0007829|PDB:1ZT3" FT STRAND 199..201 FT /evidence="ECO:0007829|PDB:1ZT3" FT STRAND 210..212 FT /evidence="ECO:0007829|PDB:1ZT3" FT STRAND 214..217 FT /evidence="ECO:0007829|PDB:1ZT3" FT STRAND 222..224 FT /evidence="ECO:0007829|PDB:1ZT3" FT HELIX 225..227 FT /evidence="ECO:0007829|PDB:1ZT3" FT STRAND 228..231 FT /evidence="ECO:0007829|PDB:1ZT3" FT TURN 233..235 FT /evidence="ECO:0007829|PDB:1ZT3" FT STRAND 245..247 FT /evidence="ECO:0007829|PDB:1ZT3" SQ SEQUENCE 259 AA; 27904 MW; 8AA75AF7DC966012 CRC64; MSEVPVARVW LVLLLLTVQV GVTAGAPWQC APCSAEKLAL CPPVSASCSE VTRSAGCGCC PMCALPLGAA CGVATARCAR GLSCRALPGE QQPLHALTRG QGACVQESDA SAPHAAEAGS PESPESTEIT EEELLDNFHL MAPSEEDHSI LWDAISTYDG SKALHVTNIK KWKEPCRIEL YRVVESLAKA QETSGEEISK FYLPNCNKNG FYHSRQCETS MDGEAGLCWC VYPWNGKRIP GSPEIRGDPN CQIYFNVQN //