P13224 (GP1BB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Platelet glycoprotein Ib beta chain
Short name=GP-Ib beta
Short name=GPIb-beta
Short name=GPIbB

Alternative name(s):
Antigen CD42b-beta
CD_antigen=CD42c

Gene names

Name:

GP1BB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	206 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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 structure	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. Ref.9 Ref.13
Subcellular location	Membrane; Single-pass type I membrane protein.
Tissue specificity	Expressed in heart and brain. Ref.3
Involvement in disease	Bernard-Soulier syndrome (BSS) [MIM:231200]: A coagulation disorder characterized by a prolonged bleeding time, unusually large platelets, thrombocytopenia, and impaired prothrombin consumption. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5
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.
Sequence similarities	Contains 1 LRR (leucine-rich) repeat. Contains 1 LRRCT domain. Contains 1 LRRNT domain.

Ontologies

Keywords
Biological process	Blood coagulation Cell adhesion Hemostasis
Cellular component	Membrane
Coding sequence diversity	Alternative splicing
Disease	Bernard Soulier syndrome Disease mutation
Domain	Leucine-rich repeat Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	blood coagulation, intrinsic pathway Traceable author statement. Source: Reactome cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW cell surface receptor signaling pathway Non-traceable author statement Ref.1. Source: ProtInc platelet activation Non-traceable author statement PubMed 12871509. Source: UniProtKB
Cellular_component	integral to plasma membrane Non-traceable author statement Ref.1. Source: ProtInc
Molecular_function	transmembrane signaling receptor activity Non-traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P13224-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P13224-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-3: MGS → MIPSRHTMLR...RSAYCGASLA

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

26

Ref.6

Chain

27 – 206

180

Platelet glycoprotein Ib beta chain

PRO_0000021345

Regions

Topological domain

27 – 147

121

Extracellular Potential

Transmembrane

148 – 172

25

Helical; Potential

Topological domain

173 – 206

34

Cytoplasmic Potential

Domain

27 – 55

29

LRRNT

Repeat

60 – 83

24

LRR

Domain

89 – 143

55

LRRCT

Amino acid modifications

Modified residue

191

1

Phosphoserine; by PKA Ref.8 Ref.11 Ref.12

Modified residue

193

1

Phosphothreonine Ref.11

Glycosylation

66

1

N-linked (GlcNAc...) Ref.1 Ref.13

Disulfide bond

26 ↔ 32

Ref.9 Ref.13

Disulfide bond

30 ↔ 39

Ref.9 Ref.13

Disulfide bond

93 ↔ 118

Ref.9 Ref.13

Disulfide bond

95 ↔ 141

Ref.9 Ref.13

Disulfide bond

147

Interchain (with C-500 or C-501 in GP1BA) Ref.9 Ref.13

Natural variations

Alternative sequence

1 – 3

3

MGS → MIPSRHTMLRFLPVVNAASC PGDRRTMLVNVAAGVRVLRV PLRAGGSGSLSGLRPPAIVC YLPLQRASAASGLFLARPQH CGRCGRGRGGAALSLGSPAY ASRCRVSRAAVFSPWAPVSL ESGRAPGCSLGRPGLRGALV VWLQLGETWVRLRGDFQPAC GVVRVERLAGYRDAGHQGLD GAGPAVWVLRDVAQVPADRS AYCGASLA in isoform 2.

VSP_032671

Natural variant

113

1

Y → C in BSS. Ref.5

VAR_025000

Natural variant

133

1

A → P in BSS. Ref.5

VAR_025001

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

206

Helix Strand Turn

Details...

Beta strand

31 – 33

3

Beta strand

36 – 38

3

Turn

46 – 48

3

Beta strand

58 – 61

4

Turn

72 – 74

3

Helix

75 – 77

3

Beta strand

83 – 85

3

Helix

95 – 97

3

Helix

98 – 105

8

Helix

111 – 113

3

Beta strand

117 – 121

5

Turn

122 – 126

5

Helix

129 – 131

3

Helix

134 – 139

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: B5E81EB6F57DE0D9	FASTA	206	21,718
	10 20 30 40 50 60 MGSGPRGALS LLLLLLAPPS RPAAGCPAPC SCAGTLVDCG RRGLTWASLP TAFPVDTTEL 70 80 90 100 110 120 VLTGNNLTAL PPGLLDALPA LRTAHLGANP WRCDCRLVPL RAWLAGRPER APYRDLRCVA 130 140 150 160 170 180 PPALRGRLLP YLAEDELRAA CAPGPLCWGA LAAQLALLGL GLLHALLLVL LLCRLRRLRA 190 200 RARARAAARL SLTDPLVAER AGTDES
	Isoform 2 [UniParc]. Checksum: 7D84D76AA079DFCF	FASTA	411	43,158
	10 20 30 40 50 60 MIPSRHTMLR FLPVVNAASC PGDRRTMLVN VAAGVRVLRV PLRAGGSGSL SGLRPPAIVC 70 80 90 100 110 120 YLPLQRASAA SGLFLARPQH CGRCGRGRGG AALSLGSPAY ASRCRVSRAA VFSPWAPVSL 130 140 150 160 170 180 ESGRAPGCSL GRPGLRGALV VWLQLGETWV RLRGDFQPAC GVVRVERLAG YRDAGHQGLD 190 200 210 220 230 240 GAGPAVWVLR DVAQVPADRS AYCGASLAGP RGALSLLLLL LAPPSRPAAG CPAPCSCAGT 250 260 270 280 290 300 LVDCGRRGLT WASLPTAFPV DTTELVLTGN NLTALPPGLL DALPALRTAH LGANPWRCDC 310 320 330 340 350 360 RLVPLRAWLA GRPERAPYRD LRCVAPPALR GRLLPYLAED ELRAACAPGP LCWGALAAQL 370 380 390 400 410 ALLGLGLLHA LLLVLLLCRL RRLRARARAR AAARLSLTDP LVAERAGTDE S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The alpha and beta chains of human platelet glycoprotein Ib are both transmembrane proteins containing a leucine-rich amino acid sequence." Lopez J.A., Chung D.W., Fujikawa K., Hagen F.S., Davie E.W., Roth G.J. Proc. Natl. Acad. Sci. U.S.A. 85:2135-2139(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), GLYCOSYLATION AT ASN-66.
[2]	"Structural characterization and chromosomal location of the gene encoding human platelet glycoprotein Ib beta." Yagi M., Edelhoff S., Disteche C.M., Roth G.J. J. Biol. Chem. 269:17424-17427(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Brain.
[3]	"Complementary DNA cloning of the alternatively expressed endothelial cell glycoprotein Ib beta (GPIb beta) and localization of the GPIb beta gene to chromosome 22." Kelly M.D., Essex D.W., Shapiro S.S., Meloni F.J., Druck T., Huebner K., Konkle B.A. J. Clin. Invest. 93:2417-2424(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY. Tissue: Umbilical vein.
[4]	"Alternative expression of platelet glycoprotein Ib(beta) mRNA from an adjacent 5' gene with an imperfect polyadenylation signal sequence." Zieger B., Hashimoto Y., Ware J. J. Clin. Invest. 99:520-525(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]	"Missense mutations of the glycoprotein (GP) Ib beta gene impairing the GPIb alpha/beta disulfide linkage in a family with giant platelet disorder." Kunishima S., Lopez J.A., Kobayashi S., Imai N., Kamiya T., Saito H., Naoe T. Blood 89:2404-2412(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-206, VARIANTS BSS CYS-113 AND PRO-133.
[6]	"Isolation and characterization of the alpha and beta chains of human platelet glycoprotein Ib." Canfield V.A., Ozols J., Nugent D., Roth G.J. Biochem. Biophys. Res. Commun. 147:526-534(1987) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-40.
[7]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 83-92 AND 190-200. Tissue: Platelet.
[8]	"Platelet glycoprotein Ib beta is phosphorylated on serine 166 by cyclic AMP-dependent protein kinase." Wardell M.R., Reynolds C.C., Berndt M.C., Wallace R.W., Fox J.E.B. J. Biol. Chem. 264:15656-15661(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-191, PROTEIN SEQUENCE OF 186-200.
[9]	"Glycoprotein Ibalpha forms disulfide bonds with 2 glycoprotein Ibbeta subunits in the resting platelet." Luo S.Z., Mo X., Afshar-Kharghan V., Srinivasan S., Lopez J.A., Li R. Blood 109:603-609(2007) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, INTERCHAIN DISULFIDE BOND.
[10]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: T-cell.
[11]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191 AND THR-193, MASS SPECTROMETRY. Tissue: Platelet.
[12]	Carrascal M., Abian J. Submitted (JAN-2008) to UniProtKB Cited for: PHOSPHORYLATION AT SER-191, MASS SPECTROMETRY.
[13]	"Quaternary organization of GPIb-IX complex and insights into Bernard-Soulier syndrome revealed by the structures of GPIbbeta and a GPIbbeta/GPIX chimera." McEwan P.A., Yang W., Carr K.H., Mo X., Zheng X., Li R., Emsley J. Blood 118:5292-5301(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.24 ANGSTROMS) OF 26-146, GLYCOSYLATION AT ASN-66, DISULFIDE BONDS.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J03259 mRNA. Translation: AAA52594.1.
AF006988 Genomic DNA. Translation: AAC39781.1.
L20860 mRNA. Translation: AAA20398.1.
U59632 mRNA. Translation: AAB93437.1.
AB086231 Genomic DNA. Translation: BAC00777.1.

IPI

IPI00464990.
IPI00889679.

PIR

NBHUIB. A54137.
I55604.

RefSeq

NP_000398.1. NM_000407.4.

UniGene

Hs.283743.
Hs.728762.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3REZ	X-ray	2.35	A/B/C/D	26-146	[»]
3RFE	X-ray	1.24	A/B	26-146	[»]

ProteinModelPortal

P13224.

ModBase

Search...

Protein-protein interaction databases

IntAct

P13224. 2 interactions.

MINT

MINT-1530456.

STRING

9606.ENSP00000383382.

PTM databases

PhosphoSite

P13224.

Polymorphism databases

DMDM

121532.

2D gel databases

OGP

P13224.

Proteomic databases

PaxDb

P13224.

PRIDE

P13224.

Protocols and materials databases

DNASU

2812.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000366425; ENSP00000383382; ENSG00000203618.

GeneID

2812.

KEGG

hsa:2812.

UCSC

uc002zpz.2. human.

Organism-specific databases

CTD

2812.

GeneCards

GC22P019710.

HGNC

HGNC:4440. GP1BB.

MIM

138720. gene.
231200. phenotype.

neXtProt

NX_P13224.

Orphanet

274. Bernard-Soulier syndrome.

PharmGKB

PA179.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG266400.

HOGENOM

HOG000060136.

HOVERGEN

HBG051791.

InParanoid

P13224.

KO

K06262.

OrthoDB

EOG4SBF03.

Enzyme and pathway databases

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P13224.

Genevestigator

P13224.

Family and domain databases

InterPro

IPR000483. Cys-rich_flank_reg_C.
IPR000372. LRR-contain_N.
[Graphical view]

Pfam

PF01463. LRRCT. 1 hit.
PF01462. LRRNT. 1 hit.
[Graphical view]

SMART

SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

GenomeRNAi

2812.

NextBio

11079.

SOURCE

Search...

Entry information

Entry name

GP1BB_HUMAN

Accession

Primary (citable) accession number: P13224
Secondary accession number(s): Q14422, Q8NG40

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	May 1, 2013
This is version 126 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.