Reviewed, UniProtKB/Swiss-Prot P07359 (GP1BA_HUMAN)

Names and origin

Protein names

Recommended name:
    Platelet glycoprotein Ib alpha chain
      Short name=Glycoprotein Ibalpha
      Short name=GP-Ib alpha
      Short name=GPIb-alpha
      Short name=GPIbA
Alternative name(s):
    Antigen CD42b-alpha
    CD_antigen=CD42b
Cleaved into the following chain:
    1- Recommended name:
            Glycocalicin

Gene names

Name:

GP1BA

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	626 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 the A1 domain of vWF, which is already bound to the subendothelium.
Subunit structure	Heterodimer composed of GP-Ib alpha and beta; disulfide linked. GP-IX is complexed with the GP-Ib heterodimer via a non covalent linkage. Interacts with FLNB. Ref.11
Subcellular location	Membrane; Single-pass type I membrane protein.
Post-translational modification	Glycocalicin, which is approximately coextensive with the extracellular part of the molecule, is cleaved off by calpain during platelet lysis.
Polymorphism	Position 161 is associated with platelet-specific alloantigen Siba. Siba- has Thr-161 and Siba+ has Met-161. Siba is involved in neonatal alloimmune thrombocytopenia (NATP). Polymorphisms arise from a variable number of tandem 13-amino acid repeats of S-E-P-A-P-S-P-T-T-P-E-P-T in the mucin-like macroglycopeptide (Pro/Thr-rich) domain. Allele D (shown here) contains one repeat starting at position 415, allele C contains two repeats, allele B contains three repeats and allele A contains four repeats. Allele B is associated with susceptibility to nonarteritic anterior ischemic optic neuropathy.
Involvement in disease	Genetic variations in GP1BA may be a cause of susceptibility to nonarteritic anterior ischemic optic neuropathy (NAION) [MIM:258660]; also known as susceptibility to anterior ishcemic optic neuropathy (AION). AION involves loss of vision due to damage to the optic nerve from insufficient blood supply. AION is generally divided into two types: arteritic AION and NAION. NAION probably results from minute infarctions of the optic nerve caused by occlusion of the posterior ciliary arteries. Hypercholesterolemia, diabetes mellitus, ischemic heart disease, hyperhomocysteinemia, hypertension, and crowded disk have been implicated as predisposing conditions. Ref.32 Defects in GP1BA are a cause of Bernard-Soulier syndrome (BSS) [MIM:231200]; also known as giant platelet disease (GPD). BSS patients have unusually large platelets and have a clinical bleeding tendency. Ref.18 Ref.20 Ref.21 Ref.26 Ref.27 Ref.30 Defects in GP1BA are the cause of benign mediterranean macrothrombocytopenia [MIM:153670]; also known as autosomal dominant benign Bernard-Soulier syndrome. Benign mediterranean macrothrombocytopenia is characterized by mild or no clinical symptoms, normal platelet function, and normal megakaryocyte count. Ref.31 Defects in GP1BA are a cause of von Willebrand disease (vWD) [MIM:177820]; also known as platelet-type von Willebrand disease or pseudo-von Willebrand disease (pseudo-vWD). This autosomal dominant bleeding disorder is caused by an increased affinity of GP-Ib for soluble vWF resulting in impaired hemostatic function due to the removal of vWF from the circulation.
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. Binding sites for vWF and thrombin (the latter site with unknown function) are in the N-terminal part of the molecule.
Sequence similarities	Contains 6 LRR (leucine-rich) repeats.

Ontologies

Keywords
Biological process	Blood coagulation Cell adhesion Hemostasis
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Disease	Bernard Soulier syndrome Disease mutation von Willebrand disease
Domain	Leucine-rich repeat Repeat Signal Transmembrane
PTM	Disulfide bond Glycoprotein Phosphoprotein Sulfation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cell adhesion Inferred from direct assay. Source: MGI cell surface receptor linked signal transduction Traceable author statement. Source: ProtInc fibrinolysis Inferred from direct assay. Source: UniProtKB platelet activation Traceable author statement. Source: UniProtKB
Cellular component	integral to plasma membrane Traceable author statement. Source: ProtInc membrane fraction Inferred from direct assay. Source: MGI platelet alpha granule membrane Inferred from Experiment. Source: Reactome
Molecular function	protein binding Ref.15 Inferred from physical interaction. Source: UniProtKB thrombin receptor activity Traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
VWF	P04275	2	EBI-297082,EBI-981819

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 16

16

Ref.7

Chain

17 – 626

610

Platelet glycoprotein Ib alpha chain

PRO_0000021343

Chain

17 – ?

Glycocalicin

PRO_0000021344

Regions

Topological domain

17 – 505

489

Extracellular Potential

Transmembrane

506 – 526

21

Potential

Topological domain

527 – 626

100

Cytoplasmic Potential

Repeat

70 – 92

23

LRR 1

Repeat

93 – 117

25

LRR 2

Repeat

119 – 138

20

LRR 3

Repeat

139 – 162

24

LRR 4

Repeat

164 – 186

23

LRR 5

Repeat

188 – 210

23

LRR 6

Compositional bias

345 – 456

112

Pro/Thr-rich

Amino acid modifications

Modified residue

292

1

Phosphotyrosine Ref.13

Modified residue

292

1

Sulfotyrosine

Modified residue

294

1

Phosphotyrosine Ref.13

Modified residue

294

1

Sulfotyrosine

Modified residue

295

1

Phosphotyrosine Ref.13

Modified residue

295

1

Sulfotyrosine

Modified residue

603

1

Phosphoserine Ref.13

Modified residue

606

1

Phosphoserine Ref.13

Glycosylation

37

1

N-linked (GlcNAc...) Ref.12

Glycosylation

175

1

N-linked (GlcNAc...)

Glycosylation

308

1

O-linked (GalNAc...)

Disulfide bond

20 ↔ 33

Ref.10

Disulfide bond

225 ↔ 264

Ref.10

Disulfide bond

227 ↔ 280

Ref.10

Natural variations

Natural variant

72

1

R → H: dbSNP rs6068. Ref.28

VAR_011909

Natural variant

73

1

L → F in BSS. Ref.18

VAR_014206

Natural variant

81

1

C → R in BSS. Ref.27

VAR_005256

Natural variant

86

1

L → F: dbSNP rs13306411. Ref.3

VAR_013511

Natural variant

145

1

L → P in BSS. Ref.30

VAR_014207

Natural variant

161

1

T → M in Siba(+). dbSNP rs6065.

VAR_005257

Natural variant

172

1

A → V in BSS and benign mediterranean macrothrombocytopenia.

VAR_005258

Natural variant

195

1

Missing in BSS. Ref.26

VAR_005259

Natural variant

225

1

C → S in BSS. Ref.21

VAR_005260

Natural variant

249

1

G → S in pseudo-vWD. Ref.4 Ref.22 Ref.23

VAR_019657

Natural variant

249

1

G → V in pseudo-vWD. Ref.4 Ref.22 Ref.23

VAR_005261

Natural variant

254

1

A → S: dbSNP rs382524.

VAR_011910

Natural variant

255

1

M → V in pseudo-vWD; increased binding to vWF. Ref.4 Ref.24

VAR_005262

Experimental info

Mutagenesis

249

1

G → A: No change. Ref.4

Mutagenesis

249

1

G → K or D: Decreased binding to vWF. Ref.4

Mutagenesis

249

1

G → S or V: Increased binding to vWF. Ref.4

Sequence conflict

593

1

V → L in AAH27955. Ref.6

Secondary structure

1

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626

Helix Strand Turn

Details...

Beta strand

19 – 23

5

Beta strand

30 – 32

3

Beta strand

51 – 53

3

Beta strand

60 – 63

4

Helix

64 – 67

4

Beta strand

75 – 77

3

Beta strand

84 – 87

4

Beta strand

97 – 99

3

Turn

112 – 114

3

Beta strand

120 – 122

3

Turn

133 – 138

6

Beta strand

144 – 146

3

Turn

157 – 162

6

Beta strand

168 – 170

3

Turn

181 – 186

6

Beta strand

192 – 194

3

Turn

205 – 210

6

Beta strand

214 – 217

4

Helix

227 – 229

3

Helix

230 – 238

9

Helix

240 – 242

3

Helix

259 – 261

3

Beta strand

262 – 264

3

Turn

265 – 268

4

Helix

272 – 274

3

Beta strand

283 – 287

5

Beta strand

579 – 587

9

Sequences

	Sequence		Length	Mass (Da)
	P07359-1 [UniParc]. Last modified April 1, 1988. Version 1. Checksum: 19514119B45DF573	FASTA	626	68,955
	10 20 30 40 50 60 MPLLLLLLLL PSPLHPHPIC EVSKVASHLE VNCDKRNLTA LPPDLPKDTT ILHLSENLLY 70 80 90 100 110 120 TFSLATLMPY TRLTQLNLDR CELTKLQVDG TLPVLGTLDL SHNQLQSLPL LGQTLPALTV 130 140 150 160 170 180 LDVSFNRLTS LPLGALRGLG ELQELYLKGN ELKTLPPGLL TPTPKLEKLS LANNNLTELP 190 200 210 220 230 240 AGLLNGLENL DTLLLQENSL YTIPKGFFGS HLLPFAFLHG NPWLCNCEIL YFRRWLQDNA 250 260 270 280 290 300 ENVYVWKQGV DVKAMTSNVA SVQCDNSDKF PVYKYPGKGC PTLGDEGDTD LYDYYPEEDT 310 320 330 340 350 360 EGDKVRATRT VVKFPTKAHT TPWGLFYSWS TASLDSQMPS SLHPTQESTK EQTTFPPRWT 370 380 390 400 410 420 PNFTLHMESI TFSKTPKSTT EPTPSPTTSE PVPEPAPNMT TLEPTPSPTT PEPTSEPAPS 430 440 450 460 470 480 PTTPEPTPIP TIATSPTILV SATSLITPKS TFLTTTKPVS LLESTKKTIP ELDQPPKLRG 490 500 510 520 530 540 VLQGHLESSR NDPFLHPDFC CLLPLGFYVL GLFWLLFASV VLILLLSWVG HVKPQALDSG 550 560 570 580 590 600 QGAALTTATQ TTHLELQRGR QVTVPRAWLL FLRGSLPTFR SSLFLWVRPN GRVGPLVAGR 610 620 RPSALSQGRG QDLLSTVSIR YSGHSL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of the alpha chain of human platelet glycoprotein Ib: a transmembrane protein with homology to leucine-rich alpha 2-glycoprotein." Lopez J.A., Chung D.W., Fujikawa K., Hagen F.S., Papayannopoulou T., Roth G.J. Proc. Natl. Acad. Sci. U.S.A. 84:5615-5619(1987) [PubMed: 3303030] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]	"Structure of the human blood platelet membrane glycoprotein Ib alpha gene." Wenger R.H., Kieffer N., Wicki A.N., Clemetson K.J. Biochem. Biophys. Res. Commun. 156:389-395(1988) [PubMed: 2845978] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"A novel polymorphism, 70Leu/Phe, disrupts a consensus Leu residue within the leucine-rich repeat sequence of platelet glycoprotein Ibalpha." Matsubara Y., Murata M., Moriki T., Yokoyama K., Watanabe N., Nakajima H., Handa M., Kawano K., Aoki N., Yoshino H., Ikeda Y. Thromb. Haemost. 87:867-872(2002) [PubMed: 12038791] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PHE-86.
[4]	"Identification of a novel point mutation in platelet glycoprotein Ibalpha, Gly to Ser at residue 233, in a Japanese family with platelet-type von Willebrand disease." Matsubara Y., Murata M., Sugita K., Ikeda Y. J. Thromb. Haemost. 1:2198-2205(2003) [PubMed: 14521605] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PSEUDO-VWD SER-249, CHARACTERIZATION OF VARIANT PSEUDO-VWD VAL-255, MUTAGENESIS OF GLY-249.
[5]	SeattleSNPs variation discovery resource Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-161.
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[7]	"Amino acid sequence of the von Willebrand factor-binding domain of platelet membrane glycoprotein Ib." Titani K., Takio K., Handa M., Ruggeri Z.M. Proc. Natl. Acad. Sci. U.S.A. 84:5610-5614(1987) [PubMed: 3497398] [Abstract] Cited for: PROTEIN SEQUENCE OF 17-315, STRUCTURE OF CARBOHYDRATE.
[8]	"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: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 128-137. Tissue: Platelet.
[9]	"StyI polymorphism at nucleotide 1610 in the human platelet glycoprotein Ib alpha gene." Suzuki K., Hayashi T., Akiba J., Yahagi A., Tajima K., Satoh S., Sasaki H. Jpn. J. Hum. Genet. 41:419-421(1996) [PubMed: 9088113] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 305-397.
[10]	"Identification of the disulphide bonds in human platelet glycocalicin." Hess D., Schaller J., Rickli E.E., Clemetson K.J. Eur. J. Biochem. 199:389-393(1991) [PubMed: 2070794] [Abstract] Cited for: DISULFIDE BONDS.
[11]	"Human beta-filamin is a new protein that interacts with the cytoplasmic tail of glycoprotein Ibalpha." Takafuta T., Wu G., Murphy G.F., Shapiro S.S. J. Biol. Chem. 273:17531-17538(1998) [PubMed: 9651345] [Abstract] Cited for: INTERACTION WITH FLNB. Tissue: Endothelial cell and Placenta.
[12]	"Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach." Lewandrowski U., Moebius J., Walter U., Sickmann A. Mol. Cell. Proteomics 5:226-233(2006) [PubMed: 16263699] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-37, MASS SPECTROMETRY. Tissue: Platelet.
[13]	"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: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-292; TYR-294; TYR-295; SER-603 AND SER-606, MASS SPECTROMETRY. Tissue: Platelet.
[14]	"Crystal structure of the platelet glycoprotein Ibalpha N-terminal domain reveals an unmasking mechanism for receptor activation." Uff S., Clemetson J.M., Harrison T., Clemetson K.J., Emsley J. J. Biol. Chem. 277:35657-35663(2002) [PubMed: 12087105] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 17-304, SULFATION AT TYR-292; TYR-294 AND TYR-295.
[15]	"Structures of glycoprotein Ibalpha and its complex with von Willebrand factor A1 domain." Huizinga E.G., Tsuji S., Romijn R.A., Schiphorst M.E., de Groot P.G., Sixma J.J., Gros P. Science 297:1176-1179(2002) [PubMed: 12183630] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
[16]	"Molecular modeling of the seven tandem leucine-rich repeats within the ligand-binding region of platelet glycoprotein Ib alpha." Whisstock J.C., Shen Y., Lopez J.A., Andrews R.K., Berndt M.C. Thromb. Haemost. 87:329-333(2002) [PubMed: 11858495] [Abstract] Cited for: 3D-STRUCTURE MODELING OF 52-216.
[17]	"Genetic and structural characterization of an amino acid dimorphism in glycoprotein Ib alpha involved in platelet transfusion refractoriness." Murata M., Furihata K., Ishida F., Russell S.R., Ware J., Ruggeri Z.M. Blood 79:3086-3090(1992) [PubMed: 1586750] [Abstract] Cited for: VARIANT SIBA MET-161.
[18]	"Mutation of leucine-57 to phenylalanine in a platelet glycoprotein Ib alpha leucine tandem repeat occurring in patients with an autosomal dominant variant of Bernard-Soulier disease." Miller J.L., Lyle V.A., Cunningham D. Blood 79:439-446(1992) [PubMed: 1730088] [Abstract] Cited for: VARIANT BSS PHE-73.
[19]	"Polymorphism of human glycoprotein Ib alpha results from a variable number of tandem repeats of a 13-amino acid sequence in the mucin-like macroglycopeptide region. Structure/function implications." Lopez J.A., Ludwig E.H., McCarthy B.J. J. Biol. Chem. 267:10055-10061(1992) [PubMed: 1577776] [Abstract] Cited for: POLYMORPHISM OF PRO/THR-RICH DOMAIN.
[20]	"Point mutation in a leucine-rich repeat of platelet glycoprotein Ib alpha resulting in the Bernard-Soulier syndrome." Ware J., Russell S.R., Marchese P., Murata M., Mazzucato M., de Marco L., Ruggeri Z.M. J. Clin. Invest. 92:1213-1220(1993) [PubMed: 7690774] [Abstract] Cited for: VARIANT BSS VAL-172.
[21]	"Cys209 Ser mutation in the platelet membrane glycoprotein Ib alpha gene is associated with Bernard-Soulier syndrome." Simsek S., Noris P., Lozano M., Pico M., von Dem Borne A.E.G.K., Ribera A., Gallardo D. Br. J. Haematol. 88:839-844(1994) [PubMed: 7819107] [Abstract] Cited for: VARIANT BSS SER-225.
[22]	"Mutation in the gene encoding the alpha chain of platelet glycoprotein Ib in platelet-type von Willebrand disease." Miller J.L., Cunningham D., Lyle V.A., Finch C.N. Proc. Natl. Acad. Sci. U.S.A. 88:4761-4765(1991) [PubMed: 2052556] [Abstract] Cited for: VARIANT PSEUDO-VWD VAL-249.
[23]	"Expression of the phenotypic abnormality of platelet-type von Willebrand disease in a recombinant glycoprotein Ib alpha fragment." Murata M., Russell S.R., Ruggeri Z.M., Ware J. J. Clin. Invest. 91:2133-2137(1993) [PubMed: 8486780] [Abstract] Cited for: VARIANT PSEUDO-VWD VAL-249.
[24]	"Pseudo-von Willebrand disease: a mutation in the platelet glycoprotein Ib alpha gene associated with a hyperactive surface receptor." Russell S.D., Roth G.J. Blood 81:1787-1791(1993) [PubMed: 8384898] [Abstract] Cited for: VARIANT PSEUDO-VWD VAL-255.
[25]	"The largest variant of platelet glycoprotein Ib alpha has four tandem repeats of 13 amino acids in the macroglycopeptide region and a genetic linkage with methionine145." Ishida F., Furihata K., Ishida K., Yan J., Kitano K., Kiyosawa K., Furuta S. Blood 86:1357-1360(1995) [PubMed: 7632942] [Abstract] Cited for: VARIANT SIBA MET-161, POLYMORPHISM OF PRO/THR-RICH DOMAIN.
[26]	"A three-base deletion removing a leucine residue in a leucine-rich repeat of platelet glycoprotein Ib alpha associated with a variant of Bernard-Soulier syndrome (Nancy I)." de la Salle C., Baas M.-J., Lanza F., Schwartz A., Hanau D., Chevalier J., Gachet C., Briquel M.-E., Cazenave J.-P. Br. J. Haematol. 89:386-396(1995) [PubMed: 7873390] [Abstract] Cited for: VARIANT BSS LEU-195 DEL.
[27]	"Naturally occurring mutations in glycoprotein Ibalpha that result in defective ligand binding and synthesis of a truncated protein." Kenny D., Jonsson O.G., Morateck P.A., Montgomery R.R. Blood 92:175-183(1998) [PubMed: 9639514] [Abstract] Cited for: VARIANT BSS ARG-81.
[28]	"Characterization of single-nucleotide polymorphisms in coding regions of human genes." Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S. Nat. Genet. 22:231-238(1999) [PubMed: 10391209] [Abstract] Cited for: VARIANTS HIS-72 AND MET-161.
[29]	Erratum Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S. Nat. Genet. 23:373-373(1999)
[30]	"Molecular characterization of two mutations in platelet glycoprotein (GP) Ib alpha in two Finnish Bernard-Soulier syndrome families." Koskela S., Partanen J., Salmi T.T., Kekomaki R. Eur. J. Haematol. 62:160-168(1999) [PubMed: 10089893] [Abstract] Cited for: VARIANT BSS PRO-145.
[31]	"Autosomal dominant macrothrombocytopenia in Italy is most frequently a type of heterozygous Bernard-Soulier syndrome." Savoia A., Balduini C.L., Savino M., Noris P., Del Vecchio M., Perrotta S., Belletti S., Poggi V., Iolascon A. Blood 97:1330-1335(2001) [PubMed: 11222377] [Abstract] Cited for: VARIANT BENIGN MEDITERRANEAN MACROTHROMBOCYTOPENIA VAL-172.
[32]	"Nonarteritic anterior ischemic optic neuropathy is associated with a specific platelet polymorphism located on the glycoprotein Ibalpha gene." Salomon O., Rosenberg N., Steinberg D.M., Huna-Baron R., Moisseiev J., Dardik R., Goldan O., Kurtz S., Ifrah A., Seligsohn U. Ophthalmology 111:184-188(2004) [PubMed: 14711733] [Abstract] Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO NAION.
+	Additional computationally mapped references.

Web resources

GeneReviews

SeattleSNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

J02940 mRNA. Translation: AAA52595.1.
M22403 Genomic DNA. Translation: AAA52596.1.
AB038516 Genomic DNA. Translation: BAB12038.1.
AB086948 Genomic DNA. Translation: BAC10305.1.
AF395009 Genomic DNA. Translation: AAK71325.1.
BC027955 mRNA. Translation: AAH27955.1.
D85894 Genomic DNA. Translation: BAA12911.1.
S34436 Genomic DNA. Translation: AAB22152.1.
S34439 Genomic DNA. Translation: AAB22153.1.
L39103 Genomic DNA. Translation: AAA69491.1.

IPI

IPI00748955.

PIR

NBHUIA. A94174.
I70082.

RefSeq

NP_000164.4.

UniGene

Hs.1472

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GWB	X-ray	2.80	A/B	16-296	[»]
1K13	model	-	A	52-216	[»]
1M0Z	X-ray	1.85	A/B	17-306	[»]
1M10	X-ray	3.10	B	17-306	[»]
1OOK	X-ray	2.30	G	17-306	[»]
1P8V	X-ray	2.60	A	17-294	[»]
1P9A	X-ray	1.70	G	17-306	[»]
1QYY	X-ray	2.80	A/G	17-306	[»]
1SQ0	X-ray	2.60	B	17-304	[»]
1U0N	X-ray	2.95	D	17-281	[»]
2BP3	X-ray	2.32	S/T	572-593	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P07359. 2 interactions.

PTM databases

GlycoSuiteDB

P07359.

PhosphoSite

P07359.

Proteomic databases

PRIDE

P07359.

Genome annotation databases

Ensembl

ENSG00000185245. Homo sapiens. [Contig view]

GeneID

2811.

KEGG

hsa:2811.

Organism-specific databases

GeneCards

GC17P004776.

H-InvDB

HIX0013453.

HGNC

HGNC:4439. GP1BA.

HPA

CAB002496.
HPA013316.

MIM

153670. phenotype.
177820. phenotype.
231200. phenotype.
258660. phenotype.
606672. gene.

Orphanet

274. Bernard-Soulier syndrome.
52530. Pseudo-Von Willebrand disease.

PharmGKB

PA178.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

P07359.

Enzyme and pathway databases

Pathway_Interaction_DB

amb2_neutrophils_pathway. amb2 Integrin signaling.

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P07359.

Bgee

P07359.

CleanEx

HS_GP1BA.

GermOnline

ENSG00000185245. Homo sapiens.

Family and domain databases

InterPro

IPR001611. Leu-rich_rpt.
IPR000372. Leu-rich_rpt_Cys-rich-reg_N.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR000483. LRR_C.
[Graphical view]

Pfam

PF00560. LRR_1. 3 hits.
PF01462. LRRNT. 1 hit.
[Graphical view]

SMART

SM00369. LRR_TYP. 2 hits.
SM00082. LRRCT. 1 hit.
SM00013. LRRNT. 1 hit.
[Graphical view]

ProtoNet

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Other Resources

NextBio

11075.

PMAP-CutDB

P07359.

SOURCE

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Entry information

Entry name

GP1BA_HUMAN

Accession

Primary (citable) accession number: P07359
Secondary accession number(s): Q14441 , Q16469, Q8N1F3, Q8NG39, Q9HDC7, Q9UEK1, Q9UQS4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	April 1, 1988
Last modified:	June 16, 2009
This is version 136 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)