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Insulin-like growth factor-binding protein 3 (IBP-3) (IGF-binding protein 3) (IGFBP-3)

 IBP3_HUMAN              Reviewed;         291 AA.
P17936; A4D2F5; D3DVM0; Q2V509; Q6P1M6; Q9UCL4;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
06-MAR-2007, sequence version 2.
05-JUL-2017, entry version 198.
RecName: Full=Insulin-like growth factor-binding protein 3;
Short=IBP-3;
Short=IGF-binding protein 3;
Short=IGFBP-3;
Flags: Precursor;
Name=IGFBP3; Synonyms=IBP3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLY-32.
PubMed=2464130; DOI=10.1210/mend-2-12-1176;
Wood W.I., Cachianes G., Henzel W.J., Winslow G.A., Spencer S.A.,
Hellmiss R., Martin J.L., Baxter R.C.;
"Cloning and expression of the growth hormone-dependent insulin-like
growth factor-binding protein.";
Mol. Endocrinol. 2:1176-1185(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANT GLY-32.
PubMed=1695633;
Cubbage M.L., Suwanichkul A., Powell D.R.;
"Insulin-like growth factor binding protein-3. Organization of the
human chromosomal gene and demonstration of promoter activity.";
J. Biol. Chem. 265:12642-12649(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT GLY-32.
TISSUE=Skin;
PubMed=7508771; DOI=10.3109/10425179309015621;
Thweatt R., Fleischmann R., Goldstein S.;
"Analysis of the primary structure of insulin-like growth factor
binding protein-3 cDNA from Werner syndrome fibroblasts.";
DNA Seq. 4:43-46(1993).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), AND VARIANTS THR-56 AND
SER-234.
NIEHS SNPs program;
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Kidney, and Spleen;
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).
[9]
PROTEIN SEQUENCE OF 28-65.
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).
[10]
PROTEIN SEQUENCE OF 28-45, INTERACTION WITH IGF2, AND VARIANT GLY-32.
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]
PROTEIN SEQUENCE OF 28-42.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[12]
INTERACTION WITH HN.
PubMed=14561895; DOI=10.1073/pnas.2135111100;
Ikonen M., Liu B., Hashimoto Y., Ma L., Lee K.W., Niikura T.,
Nishimoto I., Cohen P.;
"Interaction between the Alzheimer's survival peptide humanin and
insulin-like growth factor-binding protein 3 regulates cell survival
and apoptosis.";
Proc. Natl. Acad. Sci. U.S.A. 100:13042-13047(2003).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-136.
TISSUE=Plasma;
PubMed=14760718; DOI=10.1002/pmic.200300556;
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
"Screening for N-glycosylated proteins by liquid chromatography mass
spectrometry.";
Proteomics 4:454-465(2004).
[14]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-136 AND ASN-199.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[15]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-136.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[16]
GLYCOSYLATION AT ASN-116; ASN-136 AND ASN-199.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[17]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TMEM219.
PubMed=20353938; DOI=10.1074/jbc.M110.122226;
Ingermann A.R., Yang Y.F., Han J., Mikami A., Garza A.E., Mohanraj L.,
Fan L., Idowu M., Ware J.L., Kim H.S., Lee D.Y., Oh Y.;
"Identification of a novel cell death receptor mediating IGFBP-3-
induced anti-tumor effects in breast and prostate cancer.";
J. Biol. Chem. 285:30233-30246(2010).
[18]
PHOSPHORYLATION AT SER-148 AND SER-201.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[19]
VARIANTS [LARGE SCALE ANALYSIS] MET-7 AND CYS-252.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: 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. Also
exhibits IGF-independent antiproliferative and apoptotic effects
mediated by its receptor TMEM219/IGFBP-3R.
{ECO:0000269|PubMed:20353938}.
-!- SUBUNIT: Interacts with XLKD1 (By similarity). Binds IGF2 more
than IGF1. Forms a ternary complex of about 140 to 150 kDa with
IGF1 or IGF2 and a 85 kDa glycoprotein (ALS). Interacts with HN.
Interacts with TMEM219. {ECO:0000250, ECO:0000269|PubMed:14561895,
ECO:0000269|PubMed:1726837, ECO:0000269|PubMed:20353938}.
-!- INTERACTION:
P00533:EGFR; NbExp=3; IntAct=EBI-715709, EBI-297353;
P78527:PRKDC; NbExp=2; IntAct=EBI-715709, EBI-352053;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20353938}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P17936-1; Sequence=Displayed;
Name=2;
IsoId=P17936-2; Sequence=VSP_047293;
Note=Gene prediction based on EST data.;
-!- TISSUE SPECIFICITY: Expressed by most tissues. Present in plasma.
-!- DEVELOPMENTAL STAGE: IGFBP3 levels are higher during extrauterine
life and peak during puberty.
-!- INDUCTION: Up-regulated in the presence of IGF1, insulin and other
growth-stimulating factors such as growth hormone, EGF and phorbol
esters.
-!- DOMAIN: The thyroglobulin type-1 domain mediates interaction with
HN.
-!- PTM: Phosphorylated by FAM20C in the extracellular medium.
{ECO:0000269|PubMed:26091039}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/igfbp3/";
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=IGFBP3";
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EMBL; M31159; AAA52541.1; -; mRNA.
EMBL; M35878; AAA52706.1; -; Genomic_DNA.
EMBL; X64875; CAA46087.1; -; mRNA.
EMBL; DQ301819; ABB96247.1; -; Genomic_DNA.
EMBL; AC091524; AAS07554.1; -; Genomic_DNA.
EMBL; CH236958; EAL23801.1; -; Genomic_DNA.
EMBL; CH471128; EAW61028.1; -; Genomic_DNA.
EMBL; CH471128; EAW61029.1; -; Genomic_DNA.
EMBL; BC000013; AAH00013.1; -; mRNA.
EMBL; BC018962; AAH18962.1; -; mRNA.
EMBL; BC064987; AAH64987.1; -; mRNA.
CCDS; CCDS34632.1; -. [P17936-2]
CCDS; CCDS5505.1; -. [P17936-1]
PIR; A36578; IOHU3.
RefSeq; NP_000589.2; NM_000598.4. [P17936-1]
RefSeq; NP_001013416.1; NM_001013398.1. [P17936-2]
RefSeq; XP_016867641.1; XM_017012152.1. [P17936-1]
UniGene; Hs.450230; -.
ProteinModelPortal; P17936; -.
SMR; P17936; -.
BioGrid; 109707; 18.
DIP; DIP-40786N; -.
IntAct; P17936; 16.
MINT; MINT-142445; -.
STRING; 9606.ENSP00000370473; -.
BindingDB; P17936; -.
ChEMBL; CHEMBL3997; -.
DrugBank; DB01277; Mecasermin.
MEROPS; I31.952; -.
iPTMnet; P17936; -.
PhosphoSitePlus; P17936; -.
BioMuta; IGFBP3; -.
DMDM; 146327827; -.
MaxQB; P17936; -.
PaxDb; P17936; -.
PeptideAtlas; P17936; -.
PRIDE; P17936; -.
DNASU; 3486; -.
Ensembl; ENST00000275521; ENSP00000275521; ENSG00000146674. [P17936-1]
Ensembl; ENST00000381083; ENSP00000370473; ENSG00000146674. [P17936-2]
GeneID; 3486; -.
KEGG; hsa:3486; -.
UCSC; uc003tnr.4; human. [P17936-1]
CTD; 3486; -.
DisGeNET; 3486; -.
GeneCards; IGFBP3; -.
HGNC; HGNC:5472; IGFBP3.
HPA; CAB010360; -.
MIM; 146732; gene.
neXtProt; NX_P17936; -.
OpenTargets; ENSG00000146674; -.
PharmGKB; PA29705; -.
eggNOG; ENOG410IHZU; Eukaryota.
eggNOG; ENOG4111MF3; LUCA.
GeneTree; ENSGT00550000074457; -.
HOGENOM; HOG000253012; -.
HOVERGEN; HBG002631; -.
InParanoid; P17936; -.
KO; K10138; -.
OMA; KGDVHCY; -.
OrthoDB; EOG091G0EIN; -.
PhylomeDB; P17936; -.
TreeFam; TF331211; -.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-6803211; TP53 Regulates Transcription of Death Receptors and Ligands.
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
SIGNOR; P17936; -.
ChiTaRS; IGFBP3; human.
GeneWiki; IGFBP3; -.
GenomeRNAi; 3486; -.
PMAP-CutDB; P17936; -.
PRO; PR:P17936; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000146674; -.
CleanEx; HS_IGFBP3; -.
ExpressionAtlas; P17936; baseline and differential.
Genevisible; P17936; HS.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0016942; C:insulin-like growth factor binding protein complex; IC:BHF-UCL.
GO; GO:0042567; C:insulin-like growth factor ternary complex; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0001968; F:fibronectin binding; IBA:GO_Central.
GO; GO:0005520; F:insulin-like growth factor binding; NAS:UniProtKB.
GO; GO:0031994; F:insulin-like growth factor I binding; IPI:BHF-UCL.
GO; GO:0031995; F:insulin-like growth factor II binding; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; NAS:UniProtKB.
GO; GO:0008160; F:protein tyrosine phosphatase activator activity; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0008285; P:negative regulation of cell proliferation; IGI:MGI.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:MGI.
GO; GO:0009968; P:negative regulation of signal transduction; NAS:UniProtKB.
GO; GO:0014912; P:negative regulation of smooth muscle cell migration; IDA:BHF-UCL.
GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IDA:BHF-UCL.
GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
GO; GO:0045663; P:positive regulation of myoblast differentiation; IDA:UniProtKB.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0042981; P:regulation of apoptotic process; TAS:Reactome.
GO; GO:0001558; P:regulation of cell growth; IEA:Ensembl.
GO; GO:0010906; P:regulation of glucose metabolic process; IEA:Ensembl.
GO; GO:0043567; P:regulation of insulin-like growth factor receptor signaling pathway; IBA:GO_Central.
GO; GO:0044342; P:type B pancreatic cell proliferation; IEA:Ensembl.
Gene3D; 4.10.800.10; -; 1.
InterPro; IPR009030; Growth_fac_rcpt_.
InterPro; IPR012211; IGFBP-3.
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.
PANTHER; PTHR11551; PTHR11551; 1.
PANTHER; PTHR11551:SF22; PTHR11551:SF22; 1.
Pfam; PF00219; IGFBP; 1.
Pfam; PF00086; Thyroglobulin_1; 1.
PRINTS; PR01976; IGFBPFAMILY.
PRINTS; PR01979; IGFBPFAMILY3.
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;
Alternative splicing; Apoptosis; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Growth factor binding; Phosphoprotein; Polymorphism;
Reference proteome; Secreted; Signal.
SIGNAL 1 27 {ECO:0000269|PubMed:15340161,
ECO:0000269|PubMed:1697583,
ECO:0000269|PubMed:1726837}.
CHAIN 28 291 Insulin-like growth factor-binding
protein 3.
/FTId=PRO_0000014378.
DOMAIN 36 117 IGFBP N-terminal. {ECO:0000255|PROSITE-
ProRule:PRU00653}.
DOMAIN 210 285 Thyroglobulin type-1.
{ECO:0000255|PROSITE-ProRule:PRU00500}.
REGION 28 134 IGF-binding. {ECO:0000255}.
COMPBIAS 138 161 Ser/Thr-rich.
COMPBIAS 192 208 Ser/Thr-rich.
MOD_RES 148 148 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 201 201 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
CARBOHYD 116 116 N-linked (GlcNAc...) (complex)
asparagine.
{ECO:0000269|PubMed:19139490}.
CARBOHYD 136 136 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218}.
CARBOHYD 199 199 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490}.
DISULFID 213 240 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 251 262 {ECO:0000255|PROSITE-ProRule:PRU00500}.
DISULFID 264 285 {ECO:0000255|PROSITE-ProRule:PRU00500}.
VAR_SEQ 135 135 G -> GEPPAPG (in isoform 2).
{ECO:0000305}.
/FTId=VSP_047293.
VARIANT 7 7 T -> M (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036279.
VARIANT 32 32 A -> G (in dbSNP:rs2854746).
{ECO:0000269|PubMed:1695633,
ECO:0000269|PubMed:1726837,
ECO:0000269|PubMed:2464130,
ECO:0000269|PubMed:7508771}.
/FTId=VAR_025262.
VARIANT 56 56 A -> T (in dbSNP:rs34257987).
{ECO:0000269|Ref.4}.
/FTId=VAR_025263.
VARIANT 158 158 H -> P (in dbSNP:rs9282734).
/FTId=VAR_021974.
VARIANT 234 234 G -> S (in dbSNP:rs35712717).
{ECO:0000269|Ref.4}.
/FTId=VAR_025264.
VARIANT 252 252 R -> C (in a colorectal cancer sample;
somatic mutation; dbSNP:rs538312081).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036280.
SEQUENCE 291 AA; 31674 MW; A9682065AB266586 CRC64;
MQRARPTLWA AALTLLVLLR GPPVARAGAS SAGLGPVVRC EPCDARALAQ CAPPPAVCAE
LVREPGCGCC LTCALSEGQP CGIYTERCGS GLRCQPSPDE ARPLQALLDG RGLCVNASAV
SRLRAYLLPA PPAPGNASES EEDRSAGSVE SPSVSSTHRV SDPKFHPLHS KIIIIKKGHA
KDSQRYKVDY ESQSTDTQNF SSESKRETEY GPCRREMEDT LNHLKFLNVL SPRGVHIPNC
DKKGFYKKKQ CRPSKGRKRG FCWCVDKYGQ PLPGYTTKGK EDVHCYSMQS K


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