Q99572 (P2RX7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
P2X purinoceptor 7
Short name=P2X7

Alternative name(s):
ATP receptor
P2Z receptor
Purinergic receptor

Gene names

Name:

P2RX7

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	595 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	Functional P2XRs are organized as homomeric and heteromeric trimers. Interacts with LAMA3, ITGB2, ACTB, ACTN4, SVIL, MPP3, HSPA1, HSPCB, HSPA8, PIK230 and PTPRB. Ref.6
Subcellular location	Cell membrane; Multi-pass membrane protein.
Post-translational modification	Phosphorylation results in its inactivation. ADP-ribosylation at Arg-125 is necessary and sufficient to activate P2RX7 and gate the channel By similarity. Palmitoylation of several cysteines in the C-terminal cytoplasmic tail is required for efficient localization to cell surface. Ref.7
Sequence similarities	Belongs to the P2X receptor family.

Ontologies

Keywords
Biological process	Ion transport Transport
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
Molecular function	Ion channel Ligand-gated ion channel Receptor
PTM	ADP-ribosylation Disulfide bond Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	NAD transport Inferred from electronic annotation. Source: Compara T cell homeostasis Inferred from electronic annotation. Source: Compara T cell proliferation Inferred from electronic annotation. Source: Compara activation of MAPK activity Inferred from electronic annotation. Source: Compara bleb assembly Inferred from sequence or structural similarity. Source: BHF-UCL cell morphogenesis Inferred from electronic annotation. Source: Compara cell volume homeostasis Inferred from electronic annotation. Source: Compara cellular response to extracellular stimulus Inferred from electronic annotation. Source: Compara ceramide biosynthetic process Inferred from electronic annotation. Source: Compara collagen metabolic process Inferred from electronic annotation. Source: Compara cytolysis Inferred from electronic annotation. Source: Compara defense response to Gram-positive bacterium Inferred from electronic annotation. Source: Compara homeostasis of number of cells within a tissue Inferred from electronic annotation. Source: Compara inflammatory response Inferred from electronic annotation. Source: Compara innate immune response Traceable author statement. Source: Reactome membrane budding Inferred from electronic annotation. Source: Compara membrane depolarization Inferred from direct assay Ref.1. Source: BHF-UCL membrane protein ectodomain proteolysis Inferred from electronic annotation. Source: Compara mitochondrion organization Inferred from electronic annotation. Source: Compara multicellular organismal protein catabolic process Inferred from electronic annotation. Source: Compara negative regulation of MAPK cascade Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of bone resorption Inferred from sequence or structural similarity. Source: BHF-UCL nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Traceable author statement. Source: Reactome phagolysosome assembly Inferred from electronic annotation. Source: Compara phospholipid transfer to membrane Inferred from electronic annotation. Source: Compara phospholipid translocation Inferred from electronic annotation. Source: Compara plasma membrane organization Inferred from electronic annotation. Source: Compara pore complex assembly Inferred from direct assay Ref.1. Source: BHF-UCL positive regulation of T cell mediated cytotoxicity Inferred from electronic annotation. Source: Compara positive regulation of apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of bone mineralization Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of calcium ion transport into cytosol Inferred from direct assay Ref.1. Source: BHF-UCL positive regulation of cytolysis Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of cytoskeleton organization Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of gamma-aminobutyric acid secretion Inferred from electronic annotation. Source: Compara positive regulation of glutamate secretion Inferred from electronic annotation. Source: Compara positive regulation of interleukin-1 alpha secretion Inferred from electronic annotation. Source: Compara positive regulation of interleukin-1 beta secretion Inferred from direct assay PubMed 17036048PubMed 18089587. Source: BHF-UCL positive regulation of interleukin-6 production Inferred from electronic annotation. Source: Compara positive regulation of mitochondrial depolarization Inferred from electronic annotation. Source: Compara positive regulation of prostaglandin secretion Inferred from electronic annotation. Source: Compara protein oligomerization Inferred from electronic annotation. Source: Compara protein processing Inferred from electronic annotation. Source: Compara reactive oxygen species metabolic process Inferred from electronic annotation. Source: Compara regulation of action potential in neuron Inferred from electronic annotation. Source: Compara regulation of apoptotic process Inferred from sequence or structural similarity. Source: BHF-UCL regulation of killing of cells of other organism Non-traceable author statement PubMed 17785580. Source: BHF-UCL regulation of sodium ion transport Inferred from sequence or structural similarity PubMed 17785580. Source: BHF-UCL release of sequestered calcium ion into cytosol Inferred from electronic annotation. Source: Compara response to ATP Inferred from direct assay Ref.1. Source: BHF-UCL response to calcium ion Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to electrical stimulus Inferred from electronic annotation. Source: Compara response to fluid shear stress Inferred from electronic annotation. Source: Compara response to lipopolysaccharide Inferred from electronic annotation. Source: Compara response to mechanical stimulus Inferred from electronic annotation. Source: Compara response to zinc ion Inferred from electronic annotation. Source: Compara sensory perception of pain Inferred from sequence or structural similarity. Source: BHF-UCL skeletal system morphogenesis Inferred from electronic annotation. Source: Compara synaptic vesicle exocytosis Inferred from electronic annotation. Source: Compara
Cellular_component	bleb Inferred from sequence or structural similarity. Source: BHF-UCL cell-cell junction Inferred from electronic annotation. Source: Compara cytoplasm Inferred from sequence or structural similarity. Source: BHF-UCL external side of plasma membrane Inferred from electronic annotation. Source: Compara integral to nuclear inner membrane Inferred from electronic annotation. Source: Compara integral to plasma membrane Inferred by curator Ref.1. Source: BHF-UCL membrane raft Inferred from electronic annotation. Source: Compara neuromuscular junction Inferred from electronic annotation. Source: Compara neuronal cell body Inferred from electronic annotation. Source: Compara protein complex Inferred from electronic annotation. Source: Compara terminal bouton Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred by curator Ref.1. Source: BHF-UCL copper ion binding Inferred from electronic annotation. Source: Compara extracellular ATP-gated cation channel activity Inferred from direct assay Ref.1. Source: BHF-UCL lipopolysaccharide binding Inferred from sequence or structural similarity. Source: BHF-UCL magnesium ion binding Inferred from electronic annotation. Source: Compara protein homodimerization activity Non-traceable author statement PubMed 17895406. Source: BHF-UCL purinergic nucleotide receptor activity Inferred from direct assay Ref.1. Source: BHF-UCL receptor binding Inferred from sequence or structural similarity PubMed 17785580. Source: BHF-UCL zinc ion binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ABL1	P00519	1	EBI-1753251,EBI-375543
GRB2	P62993	1	EBI-1753251,EBI-401755
NCK1	P16333	1	EBI-1753251,EBI-389883

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 595	595	P2X purinoceptor 7		PRO_0000161560
Regions
	Topological domain	1 – 25	25	Cytoplasmic Potential
	Transmembrane	26 – 46	21	Helical; Name=1; Potential
	Topological domain	47 – 334	288	Extracellular Potential
	Transmembrane	335 – 355	21	Helical; Name=2; Potential
	Topological domain	356 – 595	240	Cytoplasmic Potential
Amino acid modifications
	Modified residue	125	1	ADP-ribosylarginine By similarity
	Modified residue	133	1	ADP-ribosylarginine By similarity
	Modified residue	343	1	Phosphotyrosine Ref.6
	Glycosylation	187	1	N-linked (GlcNAc...) Ref.8
	Glycosylation	202	1	N-linked (GlcNAc...) Ref.8
	Glycosylation	213	1	N-linked (GlcNAc...) Ref.8
	Glycosylation	241	1	N-linked (GlcNAc...) Ref.8
	Glycosylation	284	1	N-linked (GlcNAc...) Ref.8
	Disulfide bond	119 ↔ 168		By similarity
	Disulfide bond	129 ↔ 152		By similarity
	Disulfide bond	135 ↔ 162		By similarity
	Disulfide bond	216 ↔ 226		By similarity
	Disulfide bond	260 ↔ 269		By similarity
Natural variations
	Natural variant	25	1	N → S in a colorectal cancer sample; somatic mutation. Ref.12		VAR_036444
	Natural variant	76	1	V → A. Corresponds to variant rs17525809 [ dbSNP | Ensembl ].		VAR_057665
	Natural variant	150	1	G → R. Corresponds to variant rs28360447 [ dbSNP | Ensembl ].		VAR_057666
	Natural variant	155	1	Y → H. Ref.1 Ref.2 Ref.5 Corresponds to variant rs208294 [ dbSNP | Ensembl ].		VAR_019649
	Natural variant	270	1	R → C. Corresponds to variant rs16950860 [ dbSNP | Ensembl ].		VAR_057667
	Natural variant	270	1	R → H. Ref.1 Ref.5 Corresponds to variant rs7958311 [ dbSNP | Ensembl ].		VAR_019648
	Natural variant	276	1	R → H. Corresponds to variant rs7958316 [ dbSNP | Ensembl ].		VAR_057668
	Natural variant	307	1	R → Q Polymorphism that results in a loss of function. Ref.11 Corresponds to variant rs28360457 [ dbSNP | Ensembl ].		VAR_057669
	Natural variant	348	1	A → T. Ref.2 Corresponds to variant rs1718119 [ dbSNP | Ensembl ].		VAR_057670
	Natural variant	357	1	T → S. Ref.3 Corresponds to variant rs2230911 [ dbSNP | Ensembl ].		VAR_019650
	Natural variant	430	1	P → R. Corresponds to variant rs10160951 [ dbSNP | Ensembl ].		VAR_057671
	Natural variant	433	1	A → V. Corresponds to variant rs28360459 [ dbSNP | Ensembl ].		VAR_057672
	Natural variant	460	1	Q → R. Corresponds to variant rs2230912 [ dbSNP | Ensembl ].		VAR_019651
	Natural variant	496	1	E → A Polymorphism that results in a loss of function. Ref.9 Corresponds to variant rs3751143 [ dbSNP | Ensembl ].		VAR_019652
	Natural variant	521	1	H → Q. Corresponds to variant rs2230913 [ dbSNP | Ensembl ].		VAR_057673
	Natural variant	522	1	V → I. Corresponds to variant rs34219304 [ dbSNP | Ensembl ].		VAR_057674
	Natural variant	568	1	I → N Polymorphism that results in trafficking defect and around 50% loss of function. Ref.4 Ref.10 Corresponds to variant rs1653624 [ dbSNP | Ensembl ].		VAR_068011
	Natural variant	574	1	R → L in a colorectal cancer sample; somatic mutation. Ref.12		VAR_036445
	Natural variant	578	1	R → Q. Corresponds to variant rs28360460 [ dbSNP | Ensembl ].		VAR_057675
Experimental info
	Mutagenesis	187	1	N → A: Alters cell surface expression. Ref.8
	Sequence conflict	481	1	S → R in CAA73360. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q99572 [UniParc]. Last modified July 11, 2012. Version 4. Checksum: 584C17EF6D5EC899	FASTA	595	68,585
	10 20 30 40 50 60 MPACCSCSDV FQYETNKVTR IQSMNYGTIK WFFHVIIFSY VCFALVSDKL YQRKEPVISS 70 80 90 100 110 120 VHTKVKGIAE VKEEIVENGV KKLVHSVFDT ADYTFPLQGN SFFVMTNFLK TEGQEQRLCP 130 140 150 160 170 180 EYPTRRTLCS SDRGCKKGWM DPQSKGIQTG RCVVYEGNQK TCEVSAWCPI EAVEEAPRPA 190 200 210 220 230 240 LLNSAENFTV LIKNNIDFPG HNYTTRNILP GLNITCTFHK TQNPQCPIFR LGDIFRETGD 250 260 270 280 290 300 NFSDVAIQGG IMGIEIYWDC NLDRWFHHCR PKYSFRRLDD KTTNVSLYPG YNFRYAKYYK 310 320 330 340 350 360 ENNVEKRTLI KVFGIRFDIL VFGTGGKFDI IQLVVYIGST LSYFGLAAVF IDFLIDTYSS 370 380 390 400 410 420 NCCRSHIYPW CKCCQPCVVN EYYYRKKCES IVEPKPTLKY VSFVDESHIR MVNQQLLGRS 430 440 450 460 470 480 LQDVKGQEVP RPAMDFTDLS RLPLALHDTP PIPGQPEEIQ LLRKEATPRS RDSPVWCQCG 490 500 510 520 530 540 SCLPSQLPES HRCLEELCCR KKPGACITTS ELFRKLVLSR HVLQFLLLYQ EPLLALDVDS 550 560 570 580 590 TNSRLRHCAY RCYATWRFGS QDMADFAILP SCCRWRIRKE FPKSEGQYSG FKSPY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The permeabilizing ATP receptor, P2X7. Cloning and expression of a human cDNA." Rassendren F., Buell G.N., Virginio C., Collo G., North R.A., Surprenant A. J. Biol. Chem. 272:5482-5486(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS HIS-155 AND HIS-270. Tissue: Brain.
[2]	"Gene structure and chromosomal localization of the human P2X7 receptor." Buell G.N., Talabot F., Gos A., Lorenz J., Lai E., Morris M.A., Antonarakis S.E. Recept. Channels 5:347-354(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-155 AND THR-348.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-357. Tissue: Umbilical cord blood.
[4]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASN-568.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS HIS-155 AND HIS-270. Tissue: Skin.
[6]	"Proteomic and functional evidence for a P2X7 receptor signalling complex." Kim M., Jiang L.H., Wilson H.L., North R.A., Surprenant A. EMBO J. 20:6347-6358(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-343, INTERACTION WITH LAMA3; ITGB2; ACTB; ACTN4; SVIL; MPP3; HSPA1; HSPCB; HSPA8; PIK230 AND PTPRB.
[7]	"Palmitoylation of the P2X7 receptor, an ATP-gated channel, controls its expression and association with lipid rafts." Gonnord P., Delarasse C., Auger R., Benihoud K., Prigent M., Cuif M.H., Lamaze C., Kanellopoulos J.M. FASEB J. 23:795-805(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PALMITOYLATION.
[8]	"Mutation of putative N-linked glycosylation sites on the human nucleotide receptor P2X7 reveals a key residue important for receptor function." Lenertz L.Y., Wang Z., Guadarrama A., Hill L.M., Gavala M.L., Bertics P.J. Biochemistry 49:4611-4619(2010) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-187; ASN-202; ASN-213; ASN-241 AND ASN-284, MUTAGENESIS OF ASN-187.
[9]	"A Glu-496 to Ala polymorphism leads to loss of function of the human P2X7 receptor." Gu B.J., Zhang W., Worthington R.A., Sluyter R., Dao-Ung P., Petrou S., Barden J.A., Wiley J.S. J. Biol. Chem. 276:11135-11142(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ALA-496.
[10]	"An Ile-568 to Asn polymorphism prevents normal trafficking and function of the human P2X7 receptor." Wiley J.S., Dao-Ung L.P., Li C., Shemon A.N., Gu B.J., Smart M.L., Fuller S.J., Barden J.A., Petrou S., Sluyter R. J. Biol. Chem. 278:17108-17113(2003) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANT ASN-568.
[11]	"An Arg307 to Gln polymorphism within the ATP-binding site causes loss of function of the human P2X7 receptor." Gu B.J., Sluyter R., Skarratt K.K., Shemon A.N., Dao-Ung L.P., Fuller S.J., Barden J.A., Clarke A.L., Petrou S., Wiley J.S. J. Biol. Chem. 279:31287-31295(2004) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANT GLN-307.
[12]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-25 AND LEU-574.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Wikipedia

P2X receptor entry

Wikipedia

P2RX7 entry

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y09561 mRNA. Translation: CAA70755.1. Y12851 , Y12852, Y12853, Y12854, Y12855 Genomic DNA. Translation: CAA73360.1. AK290405 mRNA. Translation: BAF83094.1. Z98941 Genomic DNA. No translation available. BC011913 mRNA. Translation: AAH11913.1.
IPI	IPI00293328.
RefSeq	NP_002553.3. NM_002562.5.
UniGene	Hs.729169.
3D structure databases
ProteinModelPortal	Q99572.
SMR	Q99572. Positions 32-354.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q99572. 3 interactions.
MINT	MINT-3972963.
STRING	9606.ENSP00000261826.
Protein family/group databases
TCDB	1.A.7.1.3. ATP-gated P2X receptor cation channel (P2X Receptor) family.
PTM databases
PhosphoSite	Q99572.
Polymorphism databases
DMDM	296439282.
Proteomic databases
PaxDb	Q99572.
PRIDE	Q99572.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000546057; ENSP00000442349; ENSG00000089041.
GeneID	5027.
KEGG	hsa:5027.
UCSC	uc001tzm.3. human.
Organism-specific databases
CTD	5027.
GeneCards	GC12P121570.
HGNC	HGNC:8537. P2RX7.
HPA	HPA034968. HPA044141.
MIM	602566. gene.
neXtProt	NX_Q99572.
PharmGKB	PA32866.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG38999.
HOGENOM	HOG000232042.
HOVERGEN	HBG053086.
InParanoid	Q99572.
KO	K05220.
OrthoDB	EOG4DJJWD.
Enzyme and pathway databases
Reactome	REACT_6900. Immune System.
Gene expression databases
ArrayExpress	Q99572.
Bgee	Q99572.
CleanEx	HS_P2RX7.
Genevestigator	Q99572.
GermOnline	ENSG00000089041. Homo sapiens.
Family and domain databases
Gene3D	2.60.490.10. 1 hit.
InterPro	IPR003050. P2X7_purnocptor. IPR027309. P2X_extracellular_dom. IPR001429. P2X_purnocptor. [Graphical view]
PANTHER	PTHR10125. PTHR10125. 1 hit. PTHR10125:SF13. PTHR10125:SF13. 1 hit.
Pfam	PF00864. P2X_receptor. 1 hit. [Graphical view]
PRINTS	PR01314. P2X7RECEPTOR. PR01307. P2XRECEPTOR.
TIGRFAMs	TIGR00863. P2X. 1 hit.
PROSITE	PS01212. P2X_RECEPTOR. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q99572.
ChEMBL	CHEMBL4805.
ChiTaRS	P2RX7. human.
GenomeRNAi	5027.
NextBio	19358.
SOURCE	Search...

Entry information

Entry name

P2RX7_HUMAN

Accession

Primary (citable) accession number: Q99572
Secondary accession number(s): A8K2Z0, O14991, Q96EV7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 11, 2012
Last modified:	May 1, 2013
This is version 129 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.