dbPTM

GP1BB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GP1BB_HUMAN
UniProt AC	P13224
Protein Name	Platelet glycoprotein Ib beta chain
Gene Name	GP1BB
Organism	Homo sapiens (Human).
Sequence Length	206
Subcellular Localization	Membrane Single-pass type I membrane protein.
Protein Description	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..
Protein Sequence	MGSGPRGALSLLLLLLAPPSRPAAGCPAPCSCAGTLVDCGRRGLTWASLPTAFPVDTTELVLTGNNLTALPPGLLDALPALRTAHLGANPWRCDCRLVPLRAWLAGRPERAPYRDLRCVAPPALRGRLLPYLAEDELRAACAPGPLCWGALAAQLALLGLGLLHALLLVLLLCRLRRLRARARARAAARLSLTDPLVAERAGTDES

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
66	N-linked_Glycosylation	ELVLTGNNLTALPPG EEEEECCCCCCCCCC	39.86	3353370
83	O-linked_Glycosylation	DALPALRTAHLGANP HHHHHHHHCCCCCCC	21.19	55829007
191	Phosphorylation	ARAAARLSLTDPLVA HHHHHHHCCCCHHHH	24.54	23401153
193	Phosphorylation	AAARLSLTDPLVAER HHHHHCCCCHHHHHH	31.99	3353370
203	Phosphorylation	LVAERAGTDES---- HHHHHHCCCCC----	35.29	28270605
206	Phosphorylation	ERAGTDES------- HHHCCCCC-------	48.62	25262027

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
191	S	Phosphorylation	Kinase	PRKACA	P00517	GPS
191	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
191	S	Phosphorylation	Kinase	PKA	-	Uniprot
191	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of GP1BB_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of GP1BB_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
1433Z_HUMAN	YWHAZ	physical	9454760
TRAF4_HUMAN	TRAF4	physical	20946164
TGFI1_HUMAN	TGFB1I1	physical	20946164
NCF1_HUMAN	NCF1	physical	20946164
FAK2_HUMAN	PTK2B	physical	20946164
LYN_HUMAN	LYN	physical	20946164

Drug and Disease Associations

Kegg Disease
H00224	Bernard-Soulier syndrome; Giant platelet syndrome
OMIM Disease
231200	Bernard-Soulier syndrome (BSS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of GP1BB_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Quaternary organization of GPIb-IX complex and insights into Bernard-Soulier syndrome revealed by the structures of GPIbbeta and aGPIbbeta/GPIX chimera."; McEwan P.A., Yang W., Carr K.H., Mo X., Zheng X., Li R., Emsley J.; Blood 118:5292-5301(2011). Cited for: X-RAY CRYSTALLOGRAPHY (1.24 ANGSTROMS) OF 26-146, GLYCOSYLATION ATASN-66, AND DISULFIDE BONDS.	21908432 [Abstract]
"The alpha and beta chains of human platelet glycoprotein Ib are bothtransmembrane proteins containing a leucine-rich amino acidsequence."; 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). Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND GLYCOSYLATION AT ASN-66.	3353370 [Abstract]
Phosphorylation
Reference	PubMed
"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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191 AND THR-193, ANDMASS SPECTROMETRY.	18088087 [Abstract]
"Platelet glycoprotein Ib beta is phosphorylated on serine 166 bycyclic 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). Cited for: PHOSPHORYLATION AT SER-191, AND PROTEIN SEQUENCE OF 186-200.	2504723 [Abstract]