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Protein Page:
P2X1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
P2X1 Ligand-gated ion channel with relatively high calcium permeability. Binding to ATP mediates synaptic transmission between neurons and from neurons to smooth muscle. Seems to be linked to apoptosis, by increasing the intracellular concentration of calcium in the presence of ATP, leading to programmed cell death. Belongs to the P2X receptor family. Note: This description may include information from UniProtKB.
Protein type: Membrane protein, integral; Channel, ligand-gated; Membrane protein, multi-pass
Chromosomal Location of Human Ortholog: 17p13.3
Cellular Component: integral to nuclear inner membrane; plasma membrane
Molecular Function: cation channel activity; purinergic nucleotide receptor activity
Biological Process: blood coagulation; ion transport; signal transduction; transport
Disease: Bleeding Disorder, Platelet-type, 8
Reference #:  P51575 (UniProtKB)
Alt. Names/Synonyms: P2RX1; P2X purinoceptor 1; P2X receptor, subunit 1; P2X1; P2X1 receptor; purinergic receptor P2X, ligand-gated ion channel, 1
Gene Symbols: P2RX1
Molecular weight: 44,980 Da
Basal Isoelectric point: 8.75  Predict pI for various phosphorylation states
Select Structure to View Below

P2X1

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment



 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
1 0 T18 AFLFEYDTPRMVLVR
0 1 S130‑p GGICKEDsGCTPGKA
0 1 K138‑ac GCTPGKAkRKAQGIR
0 1 Y274‑p VRHCRPIyEFHGLYE
0 1 S286‑p LYEEKNLsPGFNFRF
0 1 Y370‑p YKQKKFKyAEDMGPG
1 1 S387‑p ERDLAATsstLGLQE
1 1 S388‑p RDLAATsstLGLQEN
1 1 T389‑p DLAATsstLGLQENM
  mouse

 
T18 AFFFEYDTPRMVLVR
S130 GGICQDDSGCTPGKA
E138 GCTPGKAERKAQGIR
Y274 VRHCKPIYQFHGLYG
S286 LYGEKNLSPGFNFRF
Y370 YKQKKFKYAEDMGPG
S387 ERDPAATSSTLGLQE
S388 RDPAATSSTLGLQEN
T389 DPAATSSTLGLQENM
  rat

 
T18‑p AFFFEYDtPRMVLVR
S130 GGICQDDSGCTPGKA
E138 GCTPGKAERKAQGIR
Y274 VRHCKPIYQFHGLYG
S286 LYGEKNLSPGFNFRF
Y370 YKQKKFKYAEDMGPG
S387 EHDPVATSSTLGLQE
S388 HDPVATSSTLGLQEN
T389 DPVATSSTLGLQENM
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