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Protein Page:
PANX1 (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
PANX1 Structural component of the gap junctions and the hemichannels. May play a role as a Ca(2+)-leak channel to regulate ER Ca(2+) homeostasis. Belongs to the pannexin family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Cell adhesion; Membrane protein, multi-pass; Membrane protein, integral
Chromosomal Location of Human Ortholog: 11q21
Cellular Component: endoplasmic reticulum; membrane; plasma membrane
Molecular Function: calcium channel activity; gap junction hemi-channel activity; leak channel activity; receptor binding
Biological Process: calcium ion transport; cation transport; cell-cell signaling; positive regulation of interleukin-1 beta secretion
Reference #:  Q96RD7 (UniProtKB)
Alt. Names/Synonyms: innexin; MGC21309; MRS1; pannexin 1; Pannexin-1; PANX1; PX1; UNQ2529
Gene Symbols: PANX1
Molecular weight: 48,050 Da
Basal Isoelectric point: 5.75  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PANX1

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

 
0 3 Y10‑p IAQLATEyVFSDFLL
0 1 Y150‑p MEELDKVyNRAIKAA
0 3 S182‑p VTENLGQsLWEVSEs
0 1 S189‑p sLWEVSEsHFKYPIV
0 1 Y193 VSEsHFKYPIVEQyL
0 2 Y199‑p KYPIVEQyLKTkkNS
0 1 K203‑ac VEQyLKTkkNSNNLI
0 1 K204‑ac EQyLKTkkNSNNLII
0 1 K212‑ac NSNNLIIkYISCRLL
0 1 K307‑ub RQKTDVLkVYEILPT
1 0 Y309 KTDVLkVYEILPTFD
0 2 K381‑ub KMDVVDGkTPMsAEM
0 1 S385‑p VDGkTPMsAEMREEQ
0 1 N394 EMREEQGNQTAELQG
0 1 K409‑ub MNIDSETkANNGEKN
0 2 S425‑p RQRLLDSsC______
  mouse

 
Y10‑p IAHLATEyVFSDFLL
Y150 MEELDKVYNRAIKAA
S181‑p VTENVGQsLWEISES
S188 sLWEISESHFKyPIV
Y192‑p ISESHFKyPIVEQyL
Y198‑p KyPIVEQyLKTKKNS
K202 VEQyLKTKKNSSHLI
K203 EQyLKTKKNSSHLIM
K211 NSSHLIMKYISCRLV
K306 RQKTDILKVYEILPT
Y308 KTDILKVYEILPTFD
K380 KMDIIDGKIPTSLQT
S384 IDGKIPTSLQTKGED
S394‑p TKGEDQGsQRVEFKD
A409 LDLSSEAAANNGEKN
S425 RQRLLNPSC______
  rat

 
Y10 IAHLATEYVFSDFLL
Y150 MEELDKVYNRAIKAA
S181 VTENVGQSLWEISES
S188 SLWEISESHFKYPIV
Y192 ISESHFKYPIVEQYL
Y198 KYPIVEQYLKTKKNS
K202 VEQYLKTKKNSSHLI
K203 EQYLKTKKNSSHLIM
K211 NSSHLIMKYISCRLV
K306 RQKTDVLKVyEILPT
Y308‑p KTDVLKVyEILPTFD
K380 KMDVIDGKVPMSLQT
S384 IDGKVPMSLQTKGED
S394 TKGEDQGSQRMDFKD
A409 LDLSSETAANNGEKN
S425 RQRLLNSSC______
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