P2RX7_HUMAN - dbPTM
P2RX7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID P2RX7_HUMAN
UniProt AC Q99572
Protein Name P2X purinoceptor 7
Gene Name P2RX7
Organism Homo sapiens (Human).
Sequence Length 595
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description Receptor for ATP that acts as a ligand-gated ion channel. Responsible for ATP-dependent lysis of macrophages through the formation of membrane pores permeable to large molecules. Could function in both fast synaptic transmission and the ATP-mediated lysis of antigen-presenting cells. In the absence of its natural ligand, ATP, functions as a scavenger receptor in the recognition and engulfment of apoptotic cells. [PubMed: 21821797]
Protein Sequence MPACCSCSDVFQYETNKVTRIQSMNYGTIKWFFHVIIFSYVCFALVSDKLYQRKEPVISSVHTKVKGIAEVKEEIVENGVKKLVHSVFDTADYTFPLQGNSFFVMTNFLKTEGQEQRLCPEYPTRRTLCSSDRGCKKGWMDPQSKGIQTGRCVVYEGNQKTCEVSAWCPIEAVEEAPRPALLNSAENFTVLIKNNIDFPGHNYTTRNILPGLNITCTFHKTQNPQCPIFRLGDIFRETGDNFSDVAIQGGIMGIEIYWDCNLDRWFHHCRPKYSFRRLDDKTTNVSLYPGYNFRYAKYYKENNVEKRTLIKVFGIRFDILVFGTGGKFDIIQLVVYIGSTLSYFGLAAVFIDFLIDTYSSNCCRSHIYPWCKCCQPCVVNEYYYRKKCESIVEPKPTLKYVSFVDESHIRMVNQQLLGRSLQDVKGQEVPRPAMDFTDLSRLPLALHDTPPIPGQPEEIQLLRKEATPRSRDSPVWCQCGSCLPSQLPESHRCLEELCCRKKPGACITTSELFRKLVLSRHVLQFLLLYQEPLLALDVDSTNSRLRHCAYRCYATWRFGSQDMADFAILPSCCRWRIRKEFPKSEGQYSGFKSPY
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
13PhosphorylationSCSDVFQYETNKVTR
CCCCEEEEECCCEEE		17.16-
59PhosphorylationQRKEPVISSVHTKVK
CCCCCCCCCHHHHCC		26.9229083192
60PhosphorylationRKEPVISSVHTKVKG
CCCCCCCCHHHHCCC		13.5429083192
63PhosphorylationPVISSVHTKVKGIAE
CCCCCHHHHCCCHHH		35.0629083192
125ADP-ribosylationLCPEYPTRRTLCSSD
CCCCCCCCCEEECCC		25.69-
125ADP-ribosylationLCPEYPTRRTLCSSD
CCCCCCCCCEEECCC		25.69-
133ADP-ribosylationRTLCSSDRGCKKGWM
CEEECCCCCCCCCCC		55.12-
133ADP-ribosylationRTLCSSDRGCKKGWM
CEEECCCCCCCCCCC		55.12-
144PhosphorylationKGWMDPQSKGIQTGR
CCCCCCCCCCCCCCC		37.9323663014
149PhosphorylationPQSKGIQTGRCVVYE
CCCCCCCCCCEEEEE		25.3623663014
187N-linked_GlycosylationALLNSAENFTVLIKN
HHHCCCCCEEEEEEC		37.2920450227
202N-linked_GlycosylationNIDFPGHNYTTRNIL
CCCCCCCCCCCCCCC		41.5820450227
213N-linked_GlycosylationRNILPGLNITCTFHK
CCCCCCCEEEEEEEC		33.1820450227
241N-linked_GlycosylationIFRETGDNFSDVAIQ
HHHHHCCCHHHHEEE		39.4020450227
284N-linked_GlycosylationRLDDKTTNVSLYPGY
CCCCCCCCEEECCCC		26.9820450227
343PhosphorylationYIGSTLSYFGLAAVF
HHHCHHHHHHHHHHH		12.5511707406
362S-palmitoylationIDTYSSNCCRSHIYP
HHHCCCCCCHHHCCC		1.8928920575
363S-palmitoylationDTYSSNCCRSHIYPW
HHCCCCCCHHHCCCC		6.1428920575
371S-palmitoylationRSHIYPWCKCCQPCV
HHHCCCCHHCCCCEE		1.7728920575
390PhosphorylationYYRKKCESIVEPKPT
EHHHCCCCCCCCCCC		41.2128326637
449PhosphorylationLPLALHDTPPIPGQP
CCCCCCCCCCCCCCH		21.8829255136
467PhosphorylationQLLRKEATPRSRDSP
HHHHHCCCCCCCCCC		21.9624702127
470PhosphorylationRKEATPRSRDSPVWC
HHCCCCCCCCCCEEE		41.4624702127
519PhosphorylationLFRKLVLSRHVLQFL
HHHHHHHHHHHHHHH		16.9224719451
529PhosphorylationVLQFLLLYQEPLLAL
HHHHHHHHCCCEEEC		15.7029083192
540PhosphorylationLLALDVDSTNSRLRH
EEECCCCCCCHHHHH		29.3629083192
541PhosphorylationLALDVDSTNSRLRHC
EECCCCCCCHHHHHH		32.5229083192
543PhosphorylationLDVDSTNSRLRHCAY
CCCCCCCHHHHHHHH		32.5529083192
588PhosphorylationFPKSEGQYSGFKSPY
CCCCCCCCCCCCCCC		22.94-
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 P2RX7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of P2RX7_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 P2RX7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TM9S1_HUMANTM9SF1physical
21988832
KR108_HUMANKRTAP10-8physical
25416956
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
D00808 Suramin hexasodium (USAN); Bayer 205 (TN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of P2RX7_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mutation of putative N-linked GLycosylation sites on the humannucleotide receptor P2X7 reveals a key residue important for receptorfunction.";
Lenertz L.Y., Wang Z., Guadarrama A., Hill L.M., Gavala M.L.,Bertics P.J.;
Biochemistry 49:4611-4619(2010).
Cited for: GLYCOSYLATION AT ASN-187; ASN-202; ASN-213; ASN-241 AND ASN-284, ANDMUTAGENESIS OF ASN-187.
Phosphorylation
ReferencePubMed
"Proteomic and functional evidence for a P2X7 receptor signallingcomplex.";
Kim M., Jiang L.H., Wilson H.L., North R.A., Surprenant A.;
EMBO J. 20:6347-6358(2001).
Cited for: PHOSPHORYLATION AT TYR-343, AND INTERACTION WITH LAMA3; ITGB2; ACTB;ACTN4; SVIL; MPP3; HSPA1; HSPCB; HSPA8; PIK230 AND PTPRB.

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