dbPTM

PANX1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PANX1_HUMAN
UniProt AC	Q96RD7
Protein Name	Pannexin-1
Gene Name	PANX1
Organism	Homo sapiens (Human).
Sequence Length	426
Subcellular Localization	Cell membrane Multi-pass membrane protein . Cell junction, gap junction . Endoplasmic reticulum membrane Multi-pass membrane protein .
Protein Description	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..
Protein Sequence	MAIAQLATEYVFSDFLLKEPTEPKFKGLRLELAVDKMVTCIAVGLPLLLISLAFAQEISIGTQISCFSPSSFSWRQAAFVDSYCWAAVQQKNSLQSESGNLPLWLHKFFPYILLLFAILLYLPPLFWRFAAAPHICSDLKFIMEELDKVYNRAIKAAKSARDLDMRDGACSVPGVTENLGQSLWEVSESHFKYPIVEQYLKTKKNSNNLIIKYISCRLLTLIIILLACIYLGYYFSLSSLSDEFVCSIKSGILRNDSTVPDQFQCKLIAVGIFQLLSVINLVVYVLLAPVVVYTLFVPFRQKTDVLKVYEILPTFDVLHFKSEGYNDLSLYNLFLEENISEVKSYKCLKVLENIKSSGQGIDPMLLLTNLGMIKMDVVDGKTPMSAEMREEQGNQTAELQGMNIDSETKANNGEKNARQRLLDSSC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
10	Phosphorylation	IAQLATEYVFSDFLL HHHHHHHHHHHHHHC	11.48	25884760
40	S-nitrosocysteine	AVDKMVTCIAVGLPL HHHHHHHHHHHHHHH	0.97	-
40	S-nitrosylation	AVDKMVTCIAVGLPL HHHHHHHHHHHHHHH	0.97	-
150	Phosphorylation	MEELDKVYNRAIKAA HHHHHHHHHHHHHHH	12.50	-
171	Phosphorylation	DMRDGACSVPGVTEN CCCCCCCCCCCCHHC	30.71	30266825
176	Phosphorylation	ACSVPGVTENLGQSL CCCCCCCHHCHHHHH	25.68	30266825
182	Phosphorylation	VTENLGQSLWEVSES CHHCHHHHHHHCCHH	33.38	30266825
187	Phosphorylation	GQSLWEVSESHFKYP HHHHHHCCHHHCCCH	23.13	30266825
189	Phosphorylation	SLWEVSESHFKYPIV HHHHCCHHHCCCHHH	27.07	30108239
199	Phosphorylation	KYPIVEQYLKTKKNS CCHHHHHHHHCCCCC	9.17	23403867
201	Ubiquitination	PIVEQYLKTKKNSNN HHHHHHHHCCCCCCC	54.05	-
203	Acetylation	VEQYLKTKKNSNNLI HHHHHHCCCCCCCHH	48.66	7226459
204	Acetylation	EQYLKTKKNSNNLII HHHHHCCCCCCCHHH	71.49	7226469
212	Acetylation	NSNNLIIKYISCRLL CCCCHHHHHHHHHHH	29.54	7226479
255	N-linked_Glycosylation	IKSGILRNDSTVPDQ ECCCCCCCCCCCCCH	44.11	17715132
307	Ubiquitination	RQKTDVLKVYEILPT CCCCCHHHHEECCCC	42.49	-
309	Phosphorylation	KTDVLKVYEILPTFD CCCHHHHEECCCCCC	8.82	-
343	Ubiquitination	EENISEVKSYKCLKV HCCHHHHHHHHHHHH	43.97	-
347	S-nitrosylation	SEVKSYKCLKVLENI HHHHHHHHHHHHHHH	3.18	-
347	S-nitrosocysteine	SEVKSYKCLKVLENI HHHHHHHHHHHHHHH	3.18	-
355	Ubiquitination	LKVLENIKSSGQGID HHHHHHHHHCCCCCC	50.58	-
381 (in isoform 1)	Ubiquitination	-	45.02	21906983
381 (in isoform 2)	Ubiquitination	-	45.02	21906983
381	Ubiquitination	KMDVVDGKTPMSAEM EEEECCCCCCCCHHH	45.02	21906983
385	Phosphorylation	VDGKTPMSAEMREEQ CCCCCCCCHHHHHHH	23.45	-
406	Phosphorylation	LQGMNIDSETKANNG HCCCCCCCCCCCCCC	43.28	25627689
408	Phosphorylation	GMNIDSETKANNGEK CCCCCCCCCCCCCCC	39.13	21815630
409	Ubiquitination	MNIDSETKANNGEKN CCCCCCCCCCCCCCH	45.10	2190698
409 (in isoform 1)	Ubiquitination	-	45.10	21906983
424	Phosphorylation	ARQRLLDSSC----- HHHHHHHCCC-----	33.31	28450419
425	Phosphorylation	RQRLLDSSC------ HHHHHHCCC------	24.42	28450419

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
199	Y	Phosphorylation	Kinase	SRC	P12931	PSP
309	Y	Phosphorylation	Kinase	SRC	P12931	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PANX1_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 PANX1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GNAS3_HUMAN	GNAS	physical	16293724
GNAS2_HUMAN	GNAS	physical	16293724
ALEX_HUMAN	GNAS	physical	16293724
GNAS1_HUMAN	GNAS	physical	16293724

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB01032	Probenecid

Regulatory Network of PANX1_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Pannexin1 channels contain a glycosylation site that targets thehexamer to the plasma membrane."; Boassa D., Ambrosi C., Qiu F., Dahl G., Gaietta G., Sosinsky G.; J. Biol. Chem. 282:31733-31743(2007). Cited for: GLYCOSYLATION AT ASN-255, HOMOHEXAMERIZATION, SUBCELLULAR LOCATION,AND MUTAGENESIS OF ASN-255.	17715132 [Abstract]