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Platelet glycoprotein Ib beta chain (GP-Ib beta) (GPIb-beta) (GPIbB) (Antigen CD42b-beta) (CD antigen CD42c)

 GP1BB_HUMAN             Reviewed;         206 AA.
P13224; Q14422; Q8NG40;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 1.
22-NOV-2017, entry version 168.
RecName: Full=Platelet glycoprotein Ib beta chain;
Short=GP-Ib beta;
Short=GPIb-beta;
Short=GPIbB;
AltName: Full=Antigen CD42b-beta;
AltName: CD_antigen=CD42c;
Flags: Precursor;
Name=GP1BB;
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 GLYCOSYLATION AT ASN-66.
PubMed=3353370; DOI=10.1073/pnas.85.7.2135;
Lopez J.A., Chung D.W., Fujikawa K., Hagen F.S., Davie E.W.,
Roth G.J.;
"The alpha and beta chains of human platelet glycoprotein Ib are both
transmembrane proteins containing a leucine-rich amino acid
sequence.";
Proc. Natl. Acad. Sci. U.S.A. 85:2135-2139(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Brain;
PubMed=8021244;
Yagi M., Edelhoff S., Disteche C.M., Roth G.J.;
"Structural characterization and chromosomal location of the gene
encoding human platelet glycoprotein Ib beta.";
J. Biol. Chem. 269:17424-17427(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
TISSUE=Umbilical vein;
PubMed=8200976; DOI=10.1172/JCI117249;
Kelly M.D., Essex D.W., Shapiro S.S., Meloni F.J., Druck T.,
Huebner K., Konkle B.A.;
"Complementary DNA cloning of the alternatively expressed endothelial
cell glycoprotein Ib beta (GPIb beta) and localization of the GPIb
beta gene to chromosome 22.";
J. Clin. Invest. 93:2417-2424(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9022087; DOI=10.1172/JCI119188;
Zieger B., Hashimoto Y., Ware J.;
"Alternative expression of platelet glycoprotein Ib(beta) mRNA from an
adjacent 5' gene with an imperfect polyadenylation signal sequence.";
J. Clin. Invest. 99:520-525(1997).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-206, AND VARIANTS BSS CYS-113
AND PRO-133.
PubMed=9116284;
Kunishima S., Lopez J.A., Kobayashi S., Imai N., Kamiya T., Saito H.,
Naoe T.;
"Missense mutations of the glycoprotein (GP) Ib beta gene impairing
the GPIb alpha/beta disulfide linkage in a family with giant platelet
disorder.";
Blood 89:2404-2412(1997).
[6]
PROTEIN SEQUENCE OF 27-40, AND SIGNAL SEQUENCE CLEAVAGE SITE.
PubMed=3632685; DOI=10.1016/0006-291X(87)90963-6;
Canfield V.A., Ozols J., Nugent D., Roth G.J.;
"Isolation and characterization of the alpha and beta chains of human
platelet glycoprotein Ib.";
Biochem. Biophys. Res. Commun. 147:526-534(1987).
[7]
PROTEIN SEQUENCE OF 83-92 AND 190-200.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[8]
PHOSPHORYLATION AT SER-191, AND PROTEIN SEQUENCE OF 186-200.
PubMed=2504723;
Wardell M.R., Reynolds C.C., Berndt M.C., Wallace R.W., Fox J.E.B.;
"Platelet glycoprotein Ib beta is phosphorylated on serine 166 by
cyclic AMP-dependent protein kinase.";
J. Biol. Chem. 264:15656-15661(1989).
[9]
SUBUNIT, AND INTERCHAIN DISULFIDE BOND.
PubMed=17008541; DOI=10.1182/blood-2006-05-024091;
Luo S.Z., Mo X., Afshar-Kharghan V., Srinivasan S., Lopez J.A., Li R.;
"Glycoprotein Ibalpha forms disulfide bonds with 2 glycoprotein Ibbeta
subunits in the resting platelet.";
Blood 109:603-609(2007).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191 AND THR-193, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191 AND THR-193, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191 AND THR-193, 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).
[14]
X-RAY CRYSTALLOGRAPHY (1.24 ANGSTROMS) OF 26-146, GLYCOSYLATION AT
ASN-66, AND DISULFIDE BONDS.
PubMed=21908432; DOI=10.1182/blood-2011-05-356253;
McEwan P.A., Yang W., Carr K.H., Mo X., Zheng X., Li R., Emsley J.;
"Quaternary organization of GPIb-IX complex and insights into Bernard-
Soulier syndrome revealed by the structures of GPIbbeta and a
GPIbbeta/GPIX chimera.";
Blood 118:5292-5301(2011).
-!- FUNCTION: Gp-Ib, a surface membrane protein of platelets,
participates in the formation of platelet plugs by binding to von
Willebrand factor, which is already bound to the subendothelium.
-!- SUBUNIT: Two GP-Ib beta are disulfide-linked to one GP-Ib alpha.
GP-IX is complexed with the GP-Ib heterodimer via a non covalent
linkage. {ECO:0000269|PubMed:17008541,
ECO:0000269|PubMed:21908432}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-2833037, EBI-2833037;
P07359:GP1BA; NbExp=6; IntAct=EBI-2833037, EBI-297082;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P13224-1; Sequence=Displayed;
Name=2;
IsoId=P13224-2; Sequence=VSP_032671;
-!- TISSUE SPECIFICITY: Expressed in heart and brain.
{ECO:0000269|PubMed:8200976}.
-!- DISEASE: Bernard-Soulier syndrome (BSS) [MIM:231200]: A
coagulation disorder characterized by a prolonged bleeding time,
unusually large platelets, thrombocytopenia, and impaired
prothrombin consumption. {ECO:0000269|PubMed:9116284}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- MISCELLANEOUS: Platelet activation apparently involves disruption
of the macromolecular complex of GP-Ib with the platelet
glycoprotein IX (GP-IX) and dissociation of GP-Ib from the actin-
binding protein.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; J03259; AAA52594.1; -; mRNA.
EMBL; AF006988; AAC39781.1; -; Genomic_DNA.
EMBL; L20860; AAA20398.1; -; mRNA.
EMBL; U59632; AAB93437.1; -; mRNA.
EMBL; AB086231; BAC00777.1; -; Genomic_DNA.
CCDS; CCDS42980.1; -. [P13224-1]
PIR; A54137; NBHUIB.
PIR; I55604; I55604.
RefSeq; NP_000398.1; NM_000407.4. [P13224-1]
UniGene; Hs.283743; -.
UniGene; Hs.728762; -.
PDB; 3REZ; X-ray; 2.35 A; A/B/C/D=26-146.
PDB; 3RFE; X-ray; 1.24 A; A/B=26-146.
PDBsum; 3REZ; -.
PDBsum; 3RFE; -.
ProteinModelPortal; P13224; -.
SMR; P13224; -.
BioGrid; 109074; 43.
IntAct; P13224; 4.
MINT; MINT-1530456; -.
STRING; 9606.ENSP00000383382; -.
iPTMnet; P13224; -.
PhosphoSitePlus; P13224; -.
DMDM; 121532; -.
OGP; P13224; -.
MaxQB; P13224; -.
PaxDb; P13224; -.
PeptideAtlas; P13224; -.
PRIDE; P13224; -.
DNASU; 2812; -.
Ensembl; ENST00000366425; ENSP00000383382; ENSG00000203618. [P13224-1]
GeneID; 2812; -.
KEGG; hsa:2812; -.
UCSC; uc062bnf.1; human. [P13224-1]
CTD; 2812; -.
DisGeNET; 2812; -.
EuPathDB; HostDB:ENSG00000203618.5; -.
GeneCards; GP1BB; -.
HGNC; HGNC:4440; GP1BB.
MalaCards; GP1BB; -.
MIM; 138720; gene.
MIM; 231200; phenotype.
neXtProt; NX_P13224; -.
OpenTargets; ENSG00000203618; -.
Orphanet; 567; 22q11.2 deletion syndrome.
Orphanet; 274; Bernard-Soulier syndrome.
Orphanet; 853; Fetal and neonatal alloimmune thrombocytopenia.
PharmGKB; PA179; -.
eggNOG; KOG0619; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00530000064244; -.
HOGENOM; HOG000060136; -.
HOVERGEN; HBG051791; -.
InParanoid; P13224; -.
KO; K06262; -.
OMA; YRDLRCA; -.
OrthoDB; EOG091G0XGH; -.
PhylomeDB; P13224; -.
Reactome; R-HSA-140837; Intrinsic Pathway of Fibrin Clot Formation.
Reactome; R-HSA-430116; GP1b-IX-V activation signalling.
Reactome; R-HSA-75892; Platelet Adhesion to exposed collagen.
Reactome; R-HSA-76009; Platelet Aggregation (Plug Formation).
SignaLink; P13224; -.
SIGNOR; P13224; -.
GeneWiki; GP1BB; -.
GenomeRNAi; 2812; -.
PRO; PR:P13224; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000203618; -.
Genevisible; P13224; HS.
GO; GO:0005887; C:integral component of plasma membrane; NAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004888; F:transmembrane signaling receptor activity; NAS:ProtInc.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0007597; P:blood coagulation, intrinsic pathway; TAS:Reactome.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0007166; P:cell surface receptor signaling pathway; NAS:ProtInc.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
Gene3D; 3.80.10.10; -; 2.
InterPro; IPR000483; Cys-rich_flank_reg_C.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR000372; LRRNT.
Pfam; PF01463; LRRCT; 1.
SMART; SM00082; LRRCT; 1.
SMART; SM00013; LRRNT; 1.
SUPFAM; SSF52058; SSF52058; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Bernard Soulier syndrome;
Blood coagulation; Cell adhesion; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; Hemostasis; Leucine-rich repeat; Membrane;
Phosphoprotein; Reference proteome; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 25 {ECO:0000269|PubMed:3632685}.
CHAIN 26 206 Platelet glycoprotein Ib beta chain.
/FTId=PRO_0000021345.
TOPO_DOM 27 147 Extracellular. {ECO:0000255}.
TRANSMEM 148 172 Helical. {ECO:0000255}.
TOPO_DOM 173 206 Cytoplasmic. {ECO:0000255}.
DOMAIN 27 55 LRRNT.
REPEAT 60 83 LRR.
DOMAIN 89 143 LRRCT.
MOD_RES 191 191 Phosphoserine; by PKA.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:2504723}.
MOD_RES 193 193 Phosphothreonine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
CARBOHYD 66 66 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:21908432,
ECO:0000269|PubMed:3353370}.
DISULFID 26 32 {ECO:0000269|PubMed:21908432}.
DISULFID 30 39 {ECO:0000269|PubMed:21908432}.
DISULFID 93 118 {ECO:0000269|PubMed:21908432}.
DISULFID 95 141 {ECO:0000269|PubMed:21908432}.
DISULFID 147 147 Interchain (with C-500 or C-501 in
GP1BA). {ECO:0000269|PubMed:21908432}.
VAR_SEQ 1 3 MGS -> MIPSRHTMLRFLPVVNAASCPGDRRTMLVNVAAG
VRVLRVPLRAGGSGSLSGLRPPAIVCYLPLQRASAASGLFL
ARPQHCGRCGRGRGGAALSLGSPAYASRCRVSRAAVFSPWA
PVSLESGRAPGCSLGRPGLRGALVVWLQLGETWVRLRGDFQ
PACGVVRVERLAGYRDAGHQGLDGAGPAVWVLRDVAQVPAD
RSAYCGASLA (in isoform 2).
{ECO:0000303|PubMed:8200976}.
/FTId=VSP_032671.
VARIANT 113 113 Y -> C (in BSS; dbSNP:rs121909750).
{ECO:0000269|PubMed:9116284}.
/FTId=VAR_025000.
VARIANT 133 133 A -> P (in BSS; dbSNP:rs121909751).
{ECO:0000269|PubMed:9116284}.
/FTId=VAR_025001.
STRAND 31 33 {ECO:0000244|PDB:3RFE}.
STRAND 36 38 {ECO:0000244|PDB:3RFE}.
TURN 46 48 {ECO:0000244|PDB:3RFE}.
STRAND 58 61 {ECO:0000244|PDB:3RFE}.
TURN 72 74 {ECO:0000244|PDB:3RFE}.
HELIX 75 77 {ECO:0000244|PDB:3RFE}.
STRAND 83 85 {ECO:0000244|PDB:3RFE}.
HELIX 95 97 {ECO:0000244|PDB:3RFE}.
HELIX 98 105 {ECO:0000244|PDB:3RFE}.
HELIX 111 113 {ECO:0000244|PDB:3RFE}.
STRAND 117 121 {ECO:0000244|PDB:3REZ}.
TURN 122 126 {ECO:0000244|PDB:3RFE}.
HELIX 129 131 {ECO:0000244|PDB:3RFE}.
HELIX 134 139 {ECO:0000244|PDB:3RFE}.
SEQUENCE 206 AA; 21718 MW; B5E81EB6F57DE0D9 CRC64;
MGSGPRGALS LLLLLLAPPS RPAAGCPAPC SCAGTLVDCG RRGLTWASLP TAFPVDTTEL
VLTGNNLTAL PPGLLDALPA LRTAHLGANP WRCDCRLVPL RAWLAGRPER APYRDLRCVA
PPALRGRLLP YLAEDELRAA CAPGPLCWGA LAAQLALLGL GLLHALLLVL LLCRLRRLRA
RARARAAARL SLTDPLVAER AGTDES


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