IBP1_HUMAN
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 03-AUG-2022, entry version 223.
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 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 [19]
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 [20]
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 [21]
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 [22]
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 [23]
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: IGF-binding proteins prolong the half-life of the IGFs and
CC have been shown to either inhibit or stimulate the growth promoting
CC effects of the IGFs on cell culture. They alter the interaction of IGFs
CC with their cell surface receptors. Promotes cell migration.
CC {ECO:0000269|PubMed:15972819}.
CC -!- SUBUNIT: Binds equally well IGF1 and IGF2.
CC {ECO:0000269|PubMed:16924115}.
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.
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 -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/igfbp1/";
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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_000596.2.
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 PDBsum; 1ZT3; -.
DR PDBsum; 1ZT5; -.
DR PDBsum; 2DSQ; -.
DR AlphaFoldDB; P08833; -.
DR SMR; P08833; -.
DR BioGRID; 109705; 29.
DR DIP; DIP-59846N; -.
DR IntAct; P08833; 27.
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 MaxQB; P08833; -.
DR PaxDb; P08833; -.
DR PeptideAtlas; P08833; -.
DR PRIDE; P08833; -.
DR ProteomicsDB; 52167; -.
DR Antibodypedia; 3841; 685 antibodies from 39 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 CTD; 3484; -.
DR DisGeNET; 3484; -.
DR GeneCards; IGFBP1; -.
DR HGNC; HGNC:5469; IGFBP1.
DR HPA; ENSG00000146678; Tissue enriched (liver).
DR MIM; 146730; gene.
DR neXtProt; NX_P08833; -.
DR OpenTargets; ENSG00000146678; -.
DR PharmGKB; PA29703; -.
DR VEuPathDB; HostDB:ENSG00000146678; -.
DR eggNOG; ENOG502QWRP; Eukaryota.
DR GeneTree; ENSGT00940000157394; -.
DR HOGENOM; CLU_070833_3_0_1; -.
DR InParanoid; P08833; -.
DR OMA; HCAPCTE; -.
DR OrthoDB; 979270at2759; -.
DR PhylomeDB; P08833; -.
DR TreeFam; TF331211; -.
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 BioGRID-ORCS; 3484; 15 hits in 1072 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 97 other tissues.
DR ExpressionAtlas; P08833; baseline and differential.
DR Genevisible; P08833; HS.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
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:0007568; P:aging; IEA:Ensembl.
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 Gene3D; 4.10.800.10; -; 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 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; SSF57184; 1.
DR SUPFAM; SSF57610; SSF57610; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Growth factor binding; Phosphoprotein; Reference proteome; Secreted;
KW 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 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 71..84
FT DISULFID 78..104
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 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 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
