dbPTM

GP1BA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GP1BA_HUMAN
UniProt AC	P07359
Protein Name	Platelet glycoprotein Ib alpha chain
Gene Name	GP1BA
Organism	Homo sapiens (Human).
Sequence Length	652
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 the A1 domain of vWF, which is already bound to the subendothelium..
Protein Sequence	MPLLLLLLLLPSPLHPHPICEVSKVASHLEVNCDKRNLTALPPDLPKDTTILHLSENLLYTFSLATLMPYTRLTQLNLDRCELTKLQVDGTLPVLGTLDLSHNQLQSLPLLGQTLPALTVLDVSFNRLTSLPLGALRGLGELQELYLKGNELKTLPPGLLTPTPKLEKLSLANNNLTELPAGLLNGLENLDTLLLQENSLYTIPKGFFGSHLLPFAFLHGNPWLCNCEILYFRRWLQDNAENVYVWKQGVDVKAMTSNVASVQCDNSDKFPVYKYPGKGCPTLGDEGDTDLYDYYPEEDTEGDKVRATRTVVKFPTKAHTTPWGLFYSWSTASLDSQMPSSLHPTQESTKEQTTFPPRWTPNFTLHMESITFSKTPKSTTEPTPSPTTSEPVPEPAPNMTTLEPTPSPTTPEPTSEPAPSPTTPEPTSEPAPSPTTPEPTSEPAPSPTTPEPTPIPTIATSPTILVSATSLITPKSTFLTTTKPVSLLESTKKTIPELDQPPKLRGVLQGHLESSRNDPFLHPDFCCLLPLGFYVLGLFWLLFASVVLILLLSWVGHVKPQALDSGQGAALTTATQTTHLELQRGRQVTVPRAWLLFLRGSLPTFRSSLFLWVRPNGRVGPLVAGRRPSALSQGRGQDLLSTVSIRYSGHSL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
37	N-linked_Glycosylation	EVNCDKRNLTALPPD EECCCCCCCCCCCCC	47.70	16263699
37	N-linked_Glycosylation	EVNCDKRNLTALPPD EECCCCCCCCCCCCC	47.70	16263699
129	Phosphorylation	DVSFNRLTSLPLGAL ECCCCCCCCCCHHHH	25.61	-
130	Phosphorylation	VSFNRLTSLPLGALR CCCCCCCCCCHHHHH	32.36	-
163	Phosphorylation	PPGLLTPTPKLEKLS CCCCCCCCCCHHHHH	28.02	18776048
175	N-linked_Glycosylation	KLSLANNNLTELPAG HHHCCCCCCCCCCHH	48.42	3497398
267	Phosphorylation	ASVQCDNSDKFPVYK EEEECCCCCCCCCCC	29.00	22210691
292	Sulfation	DEGDTDLYDYYPEED CCCCCCHHHCCCCCC	12.52	12087105
292	Sulfation	DEGDTDLYDYYPEED CCCCCCHHHCCCCCC	12.52	-
292	Phosphorylation	DEGDTDLYDYYPEED CCCCCCHHHCCCCCC	12.52	18088087
294	Sulfation	GDTDLYDYYPEEDTE CCCCHHHCCCCCCCC	13.83	12087105
294	Sulfation	GDTDLYDYYPEEDTE CCCCHHHCCCCCCCC	13.83	-
294	Phosphorylation	GDTDLYDYYPEEDTE CCCCHHHCCCCCCCC	13.83	18088087
295	Sulfation	DTDLYDYYPEEDTEG CCCHHHCCCCCCCCC	10.98	-
295	Sulfation	DTDLYDYYPEEDTEG CCCHHHCCCCCCCCC	10.98	12087105
295	Phosphorylation	DTDLYDYYPEEDTEG CCCHHHCCCCCCCCC	10.98	18088087
304	Acetylation	EEDTEGDKVRATRTV CCCCCCCEEEEEEEE	44.47	20167786
308	O-linked_Glycosylation	EGDKVRATRTVVKFP CCCEEEEEEEEEECC	19.13	UniProtKB CARBOHYD
353	Phosphorylation	QESTKEQTTFPPRWT CCCCCCCCCCCCCCC	31.34	27174698
354	Phosphorylation	ESTKEQTTFPPRWTP CCCCCCCCCCCCCCC	33.56	27174698
360	Phosphorylation	TTFPPRWTPNFTLHM CCCCCCCCCCEEEEE	15.05	29759185
364	O-linked_Glycosylation	PRWTPNFTLHMESIT CCCCCCEEEEEEEEE	23.53	OGP
476	Phosphorylation	TSLITPKSTFLTTTK CCCCCCCCCCCCCCC	42.55	29759185
477	Phosphorylation	SLITPKSTFLTTTKP CCCCCCCCCCCCCCC	58.46	29759185
494	O-linked_Glycosylation	LLESTKKTIPELDQP HHHHHCCCCCCCCCC	12.49	OGP
589	Phosphorylation	LQRGRQVTVPRAWLL ECCCCCCCCCHHHHH	37.70	24719451
601	Phosphorylation	WLLFLRGSLPTFRSS HHHHHHCCCCCCCCE	28.71	28060719
603	Phosphorylation	LFLRGSLPTFRSSLF HHHHCCCCCCCCEEE	39.78	18088087
604	Phosphorylation	FLRGSLPTFRSSLFL HHHCCCCCCCCEEEE	17.57	28270605
606	Phosphorylation	RGSLPTFRSSLFLWV HCCCCCCCCEEEEEE	30.24	18088087
607	Phosphorylation	GSLPTFRSSLFLWVR CCCCCCCCEEEEEEC	46.59	24719451
608	Phosphorylation	SLPTFRSSLFLWVRP CCCCCCCEEEEEECC	32.10	28270605
625	Phosphorylation	RVGPLVAGRRPSALS CCCCCCCCCCCCHHH	39.02	10559231
629	Phosphorylation	LVAGRRPSALSQGRG CCCCCCCCHHHCCCC		23401153
632	Phosphorylation	GRRPSALSQGRGQDL CCCCCHHHCCCCCCH		23401153
641	Phosphorylation	GRGQDLLSTVSIRYS CCCCCHHHEEEEEEC		28060719
642	Phosphorylation	RGQDLLSTVSIRYSG CCCCHHHEEEEEECC		28060719
644	Phosphorylation	QDLLSTVSIRYSGHS CCHHHEEEEEECCCC		29970186
647	Phosphorylation	LSTVSIRYSGHSL-- HHEEEEEECCCCC--		28270605
648	Phosphorylation	STVSIRYSGHSL--- HEEEEEECCCCC---		28270605
651	Phosphorylation	SIRYSGHSL------ EEEECCCCC------		10559231

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
Oops, there are no upstream regulatory protein records of GP1BA_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of GP1BA_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
163	Phosphorylation	161 (2)	T ⇒ M	rs6065	Platelet count	20139978 22139419

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
VWF_HUMAN	VWF	physical	12183630
FA12_HUMAN	F12	physical	10801853
1433Z_HUMAN	YWHAZ	physical	9454760
1433Z_HUMAN	YWHAZ	physical	8631758
FLNA_HUMAN	FLNA	physical	11700320
LYAM3_HUMAN	SELP	physical	10499919
FLNB_HUMAN	FLNB	physical	9651345
FLNA_HUMAN	FLNA	physical	25241761
FA12_HUMAN	F12	physical	25241761
GPIX_HUMAN	GP9	physical	12693941
GP1BB_HUMAN	GP1BB	physical	12693941
1433Z_HUMAN	YWHAZ	physical	22754302
VWF_HUMAN	VWF	physical	2690940

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
258660	Non-arteritic anterior ischemic optic neuropathy (NAION)
231200	Bernard-Soulier syndrome (BSS)
153670	Bernard-Soulier syndrome A2, autosomal dominant (BSSA2)
177820	Pseudo-von Willebrand disease (VWDP)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of GP1BA_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Elucidation of N-glycosylation sites on human platelet proteins: aglycoproteomic approach."; Lewandrowski U., Moebius J., Walter U., Sickmann A.; Mol. Cell. Proteomics 5:226-233(2006). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-37, AND MASS SPECTROMETRY.	16263699 [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 TYR-292; TYR-294; TYR-295;SER-603 AND SER-606, AND MASS SPECTROMETRY.	18088087 [Abstract]
Sulfation
Reference	PubMed
"Crystal structure of the platelet glycoprotein Ibalpha N-terminaldomain 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). Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 17-304, AND SULFATION ATTYR-292; TYR-294 AND TYR-295.	12087105 [Abstract]