P2RX4_HUMAN - dbPTM
P2RX4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID P2RX4_HUMAN
UniProt AC Q99571
Protein Name P2X purinoceptor 4
Gene Name P2RX4
Organism Homo sapiens (Human).
Sequence Length 388
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description Receptor for ATP that acts as a ligand-gated ion channel. This receptor is insensitive to the antagonists PPADS and suramin..
Protein Sequence MAGCCAALAAFLFEYDTPRIVLIRSRKVGLMNRAVQLLILAYVIGWVFVWEKGYQETDSVVSSVTTKVKGVAVTNTSKLGFRIWDVADYVIPAQEENSLFVMTNVILTMNQTQGLCPEIPDATTVCKSDASCTAGSAGTHSNGVSTGRCVAFNGSVKTCEVAAWCPVEDDTHVPQPAFLKAAENFTLLVKNNIWYPKFNFSKRNILPNITTTYLKSCIYDAKTDPFCPIFRLGKIVENAGHSFQDMAVEGGIMGIQVNWDCNLDRAASLCLPRYSFRRLDTRDVEHNVSPGYNFRFAKYYRDLAGNEQRTLIKAYGIRFDIIVFGKAGKFDIIPTMINIGSGLALLGMATVLCDIIVLYCMKKRLYYREKKYKYVEDYEQGLASELDQ
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
75N-linked_GlycosylationVKGVAVTNTSKLGFR
EEEEEEECCCCCCCE		35.44UniProtKB CARBOHYD
110N-linked_GlycosylationTNVILTMNQTQGLCP
EEEEEEECCCCCCCC		36.19UniProtKB CARBOHYD
128PhosphorylationDATTVCKSDASCTAG
CCCEEECCCCCCCCC		33.03-
141PhosphorylationAGSAGTHSNGVSTGR
CCCCCCCCCCCCCCC		34.81-
146PhosphorylationTHSNGVSTGRCVAFN
CCCCCCCCCCEEEEC		26.66-
153N-linked_GlycosylationTGRCVAFNGSVKTCE
CCCEEEECCCEEEEE		31.90UniProtKB CARBOHYD
184N-linked_GlycosylationAFLKAAENFTLLVKN
HHHHHHHCEEEEEEC		30.4019522481
184N-linked_GlycosylationAFLKAAENFTLLVKN
HHHHHHHCEEEEEEC		30.4019522481
199N-linked_GlycosylationNIWYPKFNFSKRNIL
CCEECCCCCCCCCCC		46.54UniProtKB CARBOHYD
201PhosphorylationWYPKFNFSKRNILPN
EECCCCCCCCCCCCC		31.6328961369
208N-linked_GlycosylationSKRNILPNITTTYLK
CCCCCCCCCCHHHHH		40.57UniProtKB CARBOHYD
275PhosphorylationSLCLPRYSFRRLDTR
HHHCCCHHCCCCCCC		17.3529496963
289PhosphorylationRDVEHNVSPGYNFRF
CCCCCCCCCCCCHHH		20.23-
292PhosphorylationEHNVSPGYNFRFAKY
CCCCCCCCCHHHHHH		17.9522817900
299PhosphorylationYNFRFAKYYRDLAGN
CCHHHHHHHHHHCCH		10.5822817900
300PhosphorylationNFRFAKYYRDLAGNE
CHHHHHHHHHHCCHH		9.2822817900
384PhosphorylationDYEQGLASELDQ---
HHHHHHHHHHCC---		43.6730108239
400Phosphorylation-------------------
-------------------		27251275
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 P2RX4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of P2RX4_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 P2RX4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CADH5_HUMANCDH5physical
12088286
WNT4_HUMANWNT4physical
21988832
PIHD3_HUMANPIH1D3physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
CQ062_HUMANC17orf62physical
26186194
EI2BE_HUMANEIF2B5physical
26186194
EMC1_HUMANEMC1physical
26186194
FDFT_HUMANFDFT1physical
26186194
ARMX3_HUMANARMCX3physical
26186194
XYLK_HUMANFAM20Bphysical
26186194
EI2BA_HUMANEIF2B1physical
26186194
GALT1_HUMANGALNT1physical
26186194
SPTC2_HUMANSPTLC2physical
26186194
TM246_HUMANTMEM246physical
26186194
HS2ST_HUMANHS2ST1physical
26186194
PIGH_HUMANPIGHphysical
26186194
TNPO3_HUMANTNPO3physical
26186194
COQ8B_HUMANADCK4physical
26186194
EI2BG_HUMANEIF2B3physical
26186194
EI2BD_HUMANEIF2B4physical
26186194
SAAL1_HUMANSAAL1physical
26186194
EI2BB_HUMANEIF2B2physical
26186194
TIM14_HUMANDNAJC19physical
26186194
KCNJ8_HUMANKCNJ8physical
26186194
EMC7_HUMANEMC7physical
26186194
PLD6_HUMANPLD6physical
26186194
CQ062_HUMANC17orf62physical
28514442
XYLK_HUMANFAM20Bphysical
28514442
PIGH_HUMANPIGHphysical
28514442
EI2BG_HUMANEIF2B3physical
28514442
EI2BE_HUMANEIF2B5physical
28514442
TNPO3_HUMANTNPO3physical
28514442
EI2BD_HUMANEIF2B4physical
28514442
TIM14_HUMANDNAJC19physical
28514442
EMC7_HUMANEMC7physical
28514442
GL8D1_HUMANGLT8D1physical
28514442
GALT1_HUMANGALNT1physical
28514442
COQ8B_HUMANADCK4physical
28514442
EI2BA_HUMANEIF2B1physical
28514442
KCNJ8_HUMANKCNJ8physical
28514442
ORC4_HUMANORC4physical
28514442
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 P2RX4_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-184, AND MASSSPECTROMETRY.

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