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Insulin-like growth factor-binding protein 1 (IBP-1) (IGF-binding protein 1) (IGFBP-1) (Placental protein 12) (PP12)

 IBP1_HUMAN              Reviewed;         259 AA.
P08833; A4D2F4; D3DVL9; Q8IYP5;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1988, sequence version 1.
20-JUN-2018, entry version 201.
RecName: Full=Insulin-like growth factor-binding protein 1;
Short=IBP-1;
Short=IGF-binding protein 1;
Short=IGFBP-1;
AltName: Full=Placental protein 12;
Short=PP12;
Flags: Precursor;
Name=IGFBP1; Synonyms=IBP1;
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=Placenta;
PubMed=2461294;
Brinkman A., Groffen C., Kortleve D.J., Geurts A., Drop S.L.S.;
"Isolation and characterization of a cDNA encoding the low molecular
weight insulin-like growth factor binding protein (IBP-1).";
EMBO J. 7:2417-2423(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Decidua;
PubMed=2454104; DOI=10.1016/S0006-291X(88)80425-X;
Brewer M.T., Stetler G.L., Squires C.H., Thompson R.C.,
Busby W.H. Jr., Clemmons D.R.;
"Cloning, characterization, and expression of a human insulin-like
growth factor binding protein.";
Biochem. Biophys. Res. Commun. 152:1289-1297(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=3419931; DOI=10.1093/nar/16.17.8711;
Grundmann U., Nerlich C., Bohn H., Rein T.;
"Cloning of cDNA encoding human placental protein 12 (PP12): binding
protein for IGF I and somatomedin.";
Nucleic Acids Res. 16:8711-8711(1988).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Decidua;
PubMed=2457513; DOI=10.1016/0014-5793(88)80041-3;
Julkunen M., Koistinen R., Aalto-Setala K., Seppala M., Janne O.A.,
Kontula K.;
"Primary structure of human insulin-like growth factor-binding
protein/placental protein 12 and tissue-specific expression of its
mRNA.";
FEBS Lett. 236:295-302(1988).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2458522; DOI=10.1210/mend-2-5-404;
Lee Y.-L., Hintz R.L., James P.M., Lee P.D.K., Shively J.E.,
Powell D.R.;
"Insulin-like growth factor (IGF) binding protein complementary
deoxyribonucleic acid from human HEP G2 hepatoma cells: predicted
protein sequence suggests an IGF binding domain different from those
of the IGF-I and IGF-II receptors.";
Mol. Endocrinol. 2:404-411(1988).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2474129; DOI=10.1210/mend-3-5-846;
Cubbage M.L., Suwanichkul A., Powell D.R.;
"Structure of the human chromosomal gene for the 25 kilodalton
insulin-like growth factor binding protein.";
Mol. Endocrinol. 3:846-851(1989).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2849945; DOI=10.1016/S0006-291X(88)80959-8;
Brinkman A., Groffen C.A., Kortleve D.J., Drop S.L.;
"Organization of the gene encoding the insulin-like growth factor
binding protein IBP-1.";
Biochem. Biophys. Res. Commun. 157:898-907(1988).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Liver;
PubMed=1373120; DOI=10.1016/0888-7543(92)90440-4;
Ehrenborg E., Larsson C., Stern I., Janson M., Powell D.R.,
Luthman H.;
"Contiguous localization of the genes encoding human insulin-like
growth factor binding proteins 1 (IGBP1) and 3 (IGBP3) on chromosome
7.";
Genomics 12:497-502(1992).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-183 AND MET-253.
NIEHS SNPs program;
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[11]
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).
[12]
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.
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-253.
TISSUE=Skin;
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).
[14]
PROTEIN SEQUENCE OF 26-53; 95-152 AND 182-208, CLEAVAGE OF INITIATOR
METHIONINE, PHOSPHORYLATION AT SER-120; SER-123; SER-126; SER-144 AND
SER-194, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Amniotic fluid;
PubMed=19765076; DOI=10.1111/j.1742-4658.2009.07318.x;
Dolcini L., Sala A., Campagnoli M., Labo S., Valli M., Visai L.,
Minchiotti L., Monaco H.L., Galliano M.;
"Identification of the amniotic fluid insulin-like growth factor
binding protein-1 phosphorylation sites and propensity to proteolysis
of the isoforms.";
FEBS J. 276:6033-6046(2009).
[15]
NUCLEOTIDE SEQUENCE [MRNA] OF 141-259, AND PROTEIN SEQUENCE OF 26-259.
TISSUE=Amniotic fluid;
PubMed=2466665; DOI=10.1111/j.1432-1033.1989.tb14641.x;
Luthman H., Soederling-Barros J., Persson B., Engberg C., Stern I.,
Lake M., Franzen S.A., Israelsson M., Raden B., Lindgren B.,
Hjelmqvist L., Enerbaeck S., Carlsson P., Bjursell G., Povoa G.,
Hall K., Joernvall H.;
"Human insulin-like growth-factor-binding protein. Low-molecular-mass
form: protein sequence and cDNA cloning.";
Eur. J. Biochem. 180:259-265(1989).
[16]
PROTEIN SEQUENCE OF 26-53.
PubMed=2971653;
Busby W.H. Jr., Klapper D.G., Clemmons D.R.;
"Purification of a 31,000-dalton insulin-like growth factor binding
protein from human amniotic fluid. Isolation of two forms with
different biologic actions.";
J. Biol. Chem. 263:14203-14210(1988).
[17]
MUTAGENESIS.
PubMed=1718783; DOI=10.1016/0014-5793(91)81298-M;
Brinkman A., Kortlrve D.J., Schuller A.G.P., Zwarthoff E.C.,
Drop S.L.S.;
"Site-directed mutagenesis of the N-terminal region of IGF binding
protein 1; analysis of IGF binding capability.";
FEBS Lett. 291:264-268(1991).
[18]
PHOSPHORYLATION AT SER-126; SER-144 AND SER-194, AND PARTIAL PROTEIN
SEQUENCE.
PubMed=7678248;
Jones J.I., Busby W.H. Jr., Wright G., Smith C.E., Kimack N.M.,
Clemmons D.R.;
"Identification of the sites of phosphorylation in insulin-like growth
factor binding protein-1. Regulation of its affinity by
phosphorylation of serine 101.";
J. Biol. Chem. 268:1125-1131(1993).
[19]
DISULFIDE BONDS.
PubMed=10329650; DOI=10.1074/jbc.274.21.14587;
Neumann G.M., Bach L.A.;
"The N-terminal disulfide linkages of human insulin-like growth
factor-binding protein-6 (hIGFBP-6) and hIGFBP-1 are different as
determined by mass spectrometry.";
J. Biol. Chem. 274:14587-14594(1999).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, AND 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).
[21]
PHOSPHORYLATION AT SER-45; SER-156; THR-157; TYR-158; THR-193;
SER-194; SER-199 AND SER-242.
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).
[22]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 172-251, PARTIAL PROTEIN
SEQUENCE, FUNCTION, PHOSPHORYLATION, AND DISULFIDE BONDS.
PubMed=15972819; DOI=10.1074/jbc.M504304200;
Sala A., Capaldi S., Campagnoli M., Faggion B., Labo S., Perduca M.,
Romano A., Carrizo M.E., Valli M., Visai L., Minchiotti L.,
Galliano M., Monaco H.L.;
"Structure and properties of the C-terminal domain of insulin-like
growth factor-binding protein-1 isolated from human amniotic fluid.";
J. Biol. Chem. 280:29812-29819(2005).
[23]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 166-259 IN COMPLEX WITH
IGFBP4 AND IGF1, AND DISULFIDE BONDS.
PubMed=16924115; DOI=10.1073/pnas.0605652103;
Sitar T., Popowicz G.M., Siwanowicz I., Huber R., Holak T.A.;
"Structural basis for the inhibition of insulin-like growth factors by
insulin-like growth factor-binding proteins.";
Proc. Natl. Acad. Sci. U.S.A. 103:13028-13033(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. Promotes
cell migration. {ECO:0000269|PubMed:15972819}.
-!- SUBUNIT: Binds equally well IGF1 and IGF2.
{ECO:0000269|PubMed:16924115}.
-!- INTERACTION:
Q8IXL6:FAM20C; NbExp=2; IntAct=EBI-13646303, EBI-7147442;
P05019:IGF1; NbExp=2; IntAct=EBI-13646303, EBI-7902275;
-!- SUBCELLULAR LOCATION: Secreted.
-!- PTM: Phosphorylated; probably by casein kinase II. Phosphorylation
alters the affinity of the protein for IGFs. In amniotic fluid,
the unmodified protein is the most abundant form, while mono-,
bi-, tri- and tetraphosphorylated forms are present in decreasing
amounts. The phosphorylation state may influence the propensity to
proteolysis. {ECO:0000269|PubMed:15972819,
ECO:0000269|PubMed:19765076, ECO:0000269|PubMed:7678248}.
-!- SEQUENCE CAUTION:
Sequence=AAA52540.1; Type=Frameshift; Positions=55, 71; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/igfbp1/";
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EMBL; Y00856; CAA68770.1; -; mRNA.
EMBL; M20841; AAA52540.1; ALT_FRAME; mRNA.
EMBL; X12385; CAA30942.1; -; mRNA.
EMBL; X13405; CAA31771.1; -; mRNA.
EMBL; M31145; AAA52542.1; -; mRNA.
EMBL; M59316; AAA52783.1; -; Genomic_DNA.
EMBL; M23595; AAA52785.1; -; Genomic_DNA.
EMBL; M23592; AAA52785.1; JOINED; Genomic_DNA.
EMBL; M23593; AAA52785.1; JOINED; Genomic_DNA.
EMBL; M23594; AAA52785.1; JOINED; Genomic_DNA.
EMBL; M74587; AAA52784.1; -; Genomic_DNA.
EMBL; BT019685; AAV38491.1; -; mRNA.
EMBL; AY434089; AAQ96599.1; -; Genomic_DNA.
EMBL; CH236958; EAL23800.1; -; Genomic_DNA.
EMBL; CH471128; EAW61030.1; -; Genomic_DNA.
EMBL; CH471128; EAW61031.1; -; Genomic_DNA.
EMBL; BC035263; AAH35263.2; -; mRNA.
EMBL; X15002; CAA33110.1; -; mRNA.
CCDS; CCDS5504.1; -.
PIR; A31867; IOHU1.
RefSeq; NP_000587.1; NM_000596.2.
UniGene; Hs.642938; -.
PDB; 1ZT3; X-ray; 1.80 A; A=172-251.
PDB; 1ZT5; X-ray; 1.82 A; A=172-251.
PDB; 2DSQ; X-ray; 2.80 A; G/H=166-259.
PDBsum; 1ZT3; -.
PDBsum; 1ZT5; -.
PDBsum; 2DSQ; -.
ProteinModelPortal; P08833; -.
SMR; P08833; -.
BioGrid; 109705; 20.
DIP; DIP-59846N; -.
IntAct; P08833; 4.
STRING; 9606.ENSP00000275525; -.
BindingDB; P08833; -.
ChEMBL; CHEMBL4178; -.
MEROPS; I31.951; -.
iPTMnet; P08833; -.
PhosphoSitePlus; P08833; -.
BioMuta; IGFBP1; -.
DMDM; 124055; -.
MaxQB; P08833; -.
PaxDb; P08833; -.
PeptideAtlas; P08833; -.
PRIDE; P08833; -.
ProteomicsDB; 52167; -.
DNASU; 3484; -.
Ensembl; ENST00000275525; ENSP00000275525; ENSG00000146678.
GeneID; 3484; -.
KEGG; hsa:3484; -.
UCSC; uc003tnp.4; human.
CTD; 3484; -.
DisGeNET; 3484; -.
EuPathDB; HostDB:ENSG00000146678.9; -.
GeneCards; IGFBP1; -.
HGNC; HGNC:5469; IGFBP1.
HPA; CAB004445; -.
HPA; HPA046972; -.
HPA; HPA050640; -.
MIM; 146730; gene.
neXtProt; NX_P08833; -.
OpenTargets; ENSG00000146678; -.
PharmGKB; PA29703; -.
eggNOG; ENOG410IITJ; Eukaryota.
eggNOG; ENOG4111H9A; LUCA.
GeneTree; ENSGT00550000074457; -.
HOGENOM; HOG000253012; -.
HOVERGEN; HBG002631; -.
InParanoid; P08833; -.
OMA; GLCWCVY; -.
OrthoDB; EOG091G0EIN; -.
PhylomeDB; P08833; -.
TreeFam; TF331211; -.
Reactome; R-HSA-380994; ATF4 activates genes.
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-8957275; Post-translational protein phosphorylation.
SignaLink; P08833; -.
SIGNOR; P08833; -.
ChiTaRS; IGFBP1; human.
EvolutionaryTrace; P08833; -.
GeneWiki; IGFBP1; -.
GenomeRNAi; 3484; -.
PMAP-CutDB; P08833; -.
PRO; PR:P08833; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000146678; -.
CleanEx; HS_IGFBP1; -.
ExpressionAtlas; P08833; baseline and differential.
Genevisible; P08833; HS.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0005520; F:insulin-like growth factor binding; TAS:ProtInc.
GO; GO:0031994; F:insulin-like growth factor I binding; IDA:UniProtKB.
GO; GO:0031995; F:insulin-like growth factor II binding; IDA:UniProtKB.
GO; GO:0005102; F:signaling receptor binding; TAS:ParkinsonsUK-UCL.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:ParkinsonsUK-UCL.
GO; GO:0036499; P:PERK-mediated unfolded protein response; TAS:Reactome.
GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0043567; P:regulation of insulin-like growth factor receptor signaling pathway; IBA:GO_Central.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0042246; P:tissue regeneration; IEA:Ensembl.
CDD; cd00191; TY; 1.
Gene3D; 4.10.800.10; -; 1.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR000867; IGFBP-like.
InterPro; IPR022322; IGFBP1.
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; PR01977; IGFBPFAMILY1.
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; Growth factor binding; Phosphoprotein; Polymorphism;
Reference proteome; Secreted; Signal.
SIGNAL 1 25 {ECO:0000269|PubMed:19765076,
ECO:0000269|PubMed:2466665,
ECO:0000269|PubMed:2971653}.
CHAIN 26 259 Insulin-like growth factor-binding
protein 1.
/FTId=PRO_0000014365.
DOMAIN 26 107 IGFBP N-terminal. {ECO:0000255|PROSITE-
ProRule:PRU00653}.
DOMAIN 173 251 Thyroglobulin type-1.
{ECO:0000255|PROSITE-ProRule:PRU00500}.
MOTIF 246 248 Cell attachment site.
MOD_RES 45 45 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 120 120 Phosphoserine.
{ECO:0000269|PubMed:19765076}.
MOD_RES 123 123 Phosphoserine.
{ECO:0000269|PubMed:19765076}.
MOD_RES 126 126 Phosphoserine.
{ECO:0000269|PubMed:19765076,
ECO:0000269|PubMed:7678248}.
MOD_RES 144 144 Phosphoserine.
{ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:19765076,
ECO:0000269|PubMed:7678248}.
MOD_RES 156 156 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 157 157 Phosphothreonine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 158 158 Phosphotyrosine.
{ECO:0000269|PubMed:26091039}.
MOD_RES 193 193 Phosphothreonine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 194 194 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:19765076,
ECO:0000269|PubMed:26091039,
ECO:0000269|PubMed:7678248}.
MOD_RES 199 199 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 242 242 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
DISULFID 71 84
DISULFID 78 104
DISULFID 176 206
DISULFID 217 228
DISULFID 230 251
VARIANT 114 114 H -> D (in dbSNP:rs41258845).
/FTId=VAR_049564.
VARIANT 183 183 V -> I (in dbSNP:rs1065782).
{ECO:0000269|Ref.10}.
/FTId=VAR_011905.
VARIANT 253 253 I -> M (in dbSNP:rs4619).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.10}.
/FTId=VAR_003821.
CONFLICT 213 213 H -> Q (in Ref. 2; AAA52540).
{ECO:0000305}.
HELIX 175 193 {ECO:0000244|PDB:1ZT3}.
STRAND 199 201 {ECO:0000244|PDB:1ZT3}.
STRAND 210 212 {ECO:0000244|PDB:1ZT3}.
STRAND 214 217 {ECO:0000244|PDB:1ZT3}.
STRAND 222 224 {ECO:0000244|PDB:1ZT3}.
STRAND 228 231 {ECO:0000244|PDB:1ZT3}.
TURN 233 235 {ECO:0000244|PDB:1ZT3}.
STRAND 245 247 {ECO:0000244|PDB:1ZT3}.
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


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