Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q99572 (P2RX7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
P2X purinoceptor 7

Short name=P2X7
Alternative name(s):
ATP receptor
P2Z receptor
Purinergic receptor
Gene names
Name:P2RX7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length595 AA.
Sequence statusComplete.
Protein existenceEvidence 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.7

Subcellular location

Cell membrane; Multi-pass membrane protein.

Tissue specificity

Widely expressed with highest levels in brain and immune tissues. Ref.3

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.8

Sequence similarities

Belongs to the P2X receptor family.

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransmembrane
Transmembrane helix
   Molecular functionIon channel
Ligand-gated ion channel
Receptor
   PTMADP-ribosylation
Disulfide bond
Glycoprotein
Lipoprotein
Palmitate
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processNAD transport

Inferred from electronic annotation. Source: Ensembl

T cell homeostasis

Inferred from electronic annotation. Source: Ensembl

T cell proliferation

Inferred from electronic annotation. Source: Ensembl

activation of MAPK activity

Inferred from electronic annotation. Source: Ensembl

apoptotic signaling pathway

Inferred from sequence or structural similarity. Source: BHF-UCL

bleb assembly

Inferred from sequence or structural similarity. Source: BHF-UCL

cell morphogenesis

Inferred from electronic annotation. Source: Ensembl

cell volume homeostasis

Inferred from electronic annotation. Source: Ensembl

cellular response to extracellular stimulus

Inferred from electronic annotation. Source: Ensembl

ceramide biosynthetic process

Inferred from electronic annotation. Source: Ensembl

collagen metabolic process

Inferred from electronic annotation. Source: Ensembl

cytolysis

Inferred from electronic annotation. Source: Ensembl

defense response to Gram-positive bacterium

Inferred from electronic annotation. Source: Ensembl

homeostasis of number of cells within a tissue

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

membrane budding

Inferred from electronic annotation. Source: Ensembl

membrane depolarization

Inferred from direct assay Ref.1. Source: BHF-UCL

membrane protein ectodomain proteolysis

Inferred from electronic annotation. Source: Ensembl

mitochondrion organization

Inferred from electronic annotation. Source: Ensembl

multicellular organismal protein catabolic process

Inferred from electronic annotation. Source: Ensembl

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

neuronal action potential

Inferred from electronic annotation. Source: Ensembl

nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway

Traceable author statement. Source: Reactome

phagolysosome assembly

Inferred from electronic annotation. Source: Ensembl

phospholipid transfer to membrane

Inferred from electronic annotation. Source: Ensembl

phospholipid translocation

Inferred from electronic annotation. Source: Ensembl

plasma membrane organization

Inferred from electronic annotation. Source: Ensembl

pore complex assembly

Inferred from direct assay Ref.1. Source: BHF-UCL

positive regulation of T cell mediated cytotoxicity

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

positive regulation of glutamate secretion

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-1 alpha secretion

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

positive regulation of lymphocyte apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of mitochondrial depolarization

Inferred from electronic annotation. Source: Ensembl

positive regulation of prostaglandin secretion

Inferred from electronic annotation. Source: Ensembl

protein oligomerization

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

protein processing

Inferred from electronic annotation. Source: Ensembl

reactive oxygen species metabolic process

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

response to ATP

Inferred from direct assay Ref.1. Source: BHF-UCL

response to calcium ion

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to electrical stimulus

Inferred from electronic annotation. Source: Ensembl

response to fluid shear stress

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

response to zinc ion

Inferred from electronic annotation. Source: Ensembl

sensory perception of pain

Inferred from sequence or structural similarity. Source: BHF-UCL

skeletal system morphogenesis

Inferred from electronic annotation. Source: Ensembl

synaptic vesicle exocytosis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentbleb

Inferred from sequence or structural similarity. Source: BHF-UCL

cell-cell junction

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from sequence or structural similarity. Source: BHF-UCL

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

integral component of nuclear inner membrane

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred by curator Ref.1. Source: BHF-UCL

membrane raft

Inferred from electronic annotation. Source: Ensembl

neuromuscular junction

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from electronic annotation. Source: Ensembl

terminal bouton

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred by curator Ref.1. Source: BHF-UCL

copper ion binding

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

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: Ensembl

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: Q99572-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform B (identifier: Q99572-2)

Also known as: Delta-C; cytoplasmic tail deleted;

The sequence of this isoform differs from the canonical sequence as follows:
     347-364: AAVFIDFLIDTYSSNCCR → VRDSLFHALGKWFGEGSD
     365-595: Missing.
Note: Predominant form in many tissues.
Isoform C (identifier: Q99572-3)

The sequence of this isoform differs from the canonical sequence as follows:
     122-128: YPTRRTL → EFRPEGV
     129-595: Missing.
Isoform D (identifier: Q99572-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: MPACCSC → MDGPAEQ
     8-177: Missing.
Isoform E (identifier: Q99572-5)

The sequence of this isoform differs from the canonical sequence as follows:
     206-294: Missing.
     347-364: AAVFIDFLIDTYSSNCCR → VRDSLFHALGKWFGEGSD
     365-595: Missing.
Isoform F (identifier: Q99572-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-3: MPA → MWQ
     4-292: Missing.
Isoform G (identifier: Q99572-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-98: MPACCSCSDV...DTADYTFPLQ → MTPGDHSW
     347-364: AAVFIDFLIDTYSSNCCR → VRDSLFHALGKWFGEGSD
     365-595: Missing.
Isoform H (identifier: Q99572-8)

Also known as: Delta-TM1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-98: MPACCSCSDV...DTADYTFPLQ → MTPGDHSW
Note: Non-functional channel.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 595595P2X purinoceptor 7
PRO_0000161560

Regions

Topological domain1 – 2525Cytoplasmic Potential
Transmembrane26 – 4621Helical; Name=1; Potential
Topological domain47 – 334288Extracellular Potential
Transmembrane335 – 35521Helical; Name=2; Potential
Topological domain356 – 595240Cytoplasmic Potential

Amino acid modifications

Modified residue1251ADP-ribosylarginine By similarity
Modified residue1331ADP-ribosylarginine By similarity
Modified residue3431Phosphotyrosine Ref.7
Glycosylation1871N-linked (GlcNAc...) Ref.9
Glycosylation2021N-linked (GlcNAc...) Ref.9
Glycosylation2131N-linked (GlcNAc...) Ref.9
Glycosylation2411N-linked (GlcNAc...) Ref.9
Glycosylation2841N-linked (GlcNAc...) Ref.9
Disulfide bond119 ↔ 168 By similarity
Disulfide bond129 ↔ 152 By similarity
Disulfide bond135 ↔ 162 By similarity
Disulfide bond216 ↔ 226 By similarity
Disulfide bond260 ↔ 269 By similarity

Natural variations

Alternative sequence1 – 9898MPACC…TFPLQ → MTPGDHSW in isoform G and isoform H.
VSP_047776
Alternative sequence1 – 77MPACCSC → MDGPAEQ in isoform D.
VSP_047777
Alternative sequence1 – 33MPA → MWQ in isoform F.
VSP_047778
Alternative sequence4 – 292289Missing in isoform F.
VSP_047779
Alternative sequence8 – 177170Missing in isoform D.
VSP_047780
Alternative sequence122 – 1287YPTRRTL → EFRPEGV in isoform C.
VSP_047781
Alternative sequence129 – 595467Missing in isoform C.
VSP_047782
Alternative sequence206 – 29489Missing in isoform E.
VSP_047783
Alternative sequence347 – 36418AAVFI…SNCCR → VRDSLFHALGKWFGEGSD in isoform B, isoform E and isoform G.
VSP_047784
Alternative sequence365 – 595231Missing in isoform B, isoform E and isoform G.
VSP_047785
Natural variant251N → S in a colorectal cancer sample; somatic mutation. Ref.13
VAR_036444
Natural variant761V → A.
Corresponds to variant rs17525809 [ dbSNP | Ensembl ].
VAR_057665
Natural variant1501G → R.
Corresponds to variant rs28360447 [ dbSNP | Ensembl ].
VAR_057666
Natural variant1551Y → H. Ref.1 Ref.2 Ref.3 Ref.6
Corresponds to variant rs208294 [ dbSNP | Ensembl ].
VAR_019649
Natural variant2701R → C.
Corresponds to variant rs16950860 [ dbSNP | Ensembl ].
VAR_057667
Natural variant2701R → H. Ref.1 Ref.3 Ref.6
Corresponds to variant rs7958311 [ dbSNP | Ensembl ].
VAR_019648
Natural variant2761R → H.
Corresponds to variant rs7958316 [ dbSNP | Ensembl ].
VAR_057668
Natural variant3071R → Q Polymorphism that results in a loss of function. Ref.12
Corresponds to variant rs28360457 [ dbSNP | Ensembl ].
VAR_057669
Natural variant3481A → T. Ref.2
Corresponds to variant rs1718119 [ dbSNP | Ensembl ].
VAR_057670
Natural variant3571T → S. Ref.4
Corresponds to variant rs2230911 [ dbSNP | Ensembl ].
VAR_019650
Natural variant4301P → R.
Corresponds to variant rs10160951 [ dbSNP | Ensembl ].
VAR_057671
Natural variant4331A → V.
Corresponds to variant rs28360459 [ dbSNP | Ensembl ].
VAR_057672
Natural variant4601Q → R.
Corresponds to variant rs2230912 [ dbSNP | Ensembl ].
VAR_019651
Natural variant4961E → A Polymorphism that results in a loss of function. Ref.6 Ref.10
Corresponds to variant rs3751143 [ dbSNP | Ensembl ].
VAR_019652
Natural variant5211H → Q.
Corresponds to variant rs2230913 [ dbSNP | Ensembl ].
VAR_057673
Natural variant5221V → I.
Corresponds to variant rs34219304 [ dbSNP | Ensembl ].
VAR_057674
Natural variant5681I → N Polymorphism that results in trafficking defect and around 50% loss of function. Ref.5 Ref.11
Corresponds to variant rs1653624 [ dbSNP | Ensembl ].
VAR_068011
Natural variant5741R → L in a colorectal cancer sample; somatic mutation. Ref.13
VAR_036445
Natural variant5781R → Q.
Corresponds to variant rs28360460 [ dbSNP | Ensembl ].
VAR_057675

Experimental info

Mutagenesis1871N → A: Alters cell surface expression. Ref.9
Sequence conflict4811S → R in CAA73360. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform A [UniParc].

Last modified July 11, 2012. Version 4.
Checksum: 584C17EF6D5EC899

FASTA59568,585
        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 

« Hide

Isoform B (Delta-C) (cytoplasmic tail deleted) [UniParc].

Checksum: 3A9C0F1D110543FC
Show »

FASTA36441,792
Isoform C [UniParc].

Checksum: DBBA1D99D97E108E
Show »

FASTA12814,749
Isoform D [UniParc].

Checksum: 9245A1363145ABD7
Show »

FASTA42549,165
Isoform E [UniParc].

Checksum: 6AE04D318BEB617C
Show »

FASTA27531,294
Isoform F [UniParc].

Checksum: 28004164298DC12A
Show »

FASTA30635,544
Isoform G [UniParc].

Checksum: 48E9BBD37BFEFDA1
Show »

FASTA27431,446
Isoform H (Delta-TM1) [UniParc].

Checksum: D65D70EADCE5702A
Show »

FASTA50558,239

References

« Hide '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] (ISOFORM A), 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]"Identification and characterization of splice variants of the human P2X7 ATP channel."
Cheewatrakoolpong B., Gilchrest H., Anthes J.C., Greenfeder S.
Biochem. Biophys. Res. Commun. 332:17-27(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B; C; D; E; F; G AND H), ALTERNATIVE SPLICING, TISSUE SPECIFICITY, VARIANTS HIS-155 AND HIS-270.
Tissue: Brain.
[4]"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. expand/collapse author list , 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] (ISOFORMS A AND C), VARIANT SER-357.
Tissue: Brain and Umbilical cord blood.
[5]"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. expand/collapse author list , 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.
[6]"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] (ISOFORMS A AND D), VARIANTS HIS-155; HIS-270 AND ALA-496.
Tissue: Brain and Skin.
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y09561 mRNA. Translation: CAA70755.1.
Y12851 expand/collapse EMBL AC list , Y12852, Y12853, Y12854, Y12855 Genomic DNA. Translation: CAA73360.1.
AY847298 mRNA. Translation: AAX82087.1.
AY847299 mRNA. Translation: AAX82088.1.
AY847300 mRNA. Translation: AAX82089.1.
AY847301 mRNA. Translation: AAX82090.1.
AY847302 mRNA. Translation: AAX82091.1.
AY847303 mRNA. Translation: AAX82092.1.
AY847304 mRNA. Translation: AAX82093.1.
AK290405 mRNA. Translation: BAF83094.1.
AK294126 mRNA. Translation: BAH11678.1.
AC069209 Genomic DNA. No translation available.
AC079602 Genomic DNA. No translation available.
Z98941 Genomic DNA. No translation available.
BC007679 mRNA. Translation: AAH07679.1.
BC011913 mRNA. Translation: AAH11913.1.
RefSeqNP_002553.3. NM_002562.5.
UniGeneHs.729169.

3D structure databases

ProteinModelPortalQ99572.
SMRQ99572. Positions 32-354.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ99572. 6 interactions.
MINTMINT-3972963.
STRING9606.ENSP00000261826.

Chemistry

BindingDBQ99572.
ChEMBLCHEMBL4805.
GuidetoPHARMACOLOGY484.

Protein family/group databases

TCDB1.A.7.1.3. the atp-gated p2x receptor cation channel (p2x receptor) family.

PTM databases

PhosphoSiteQ99572.

Polymorphism databases

DMDM296439282.

Proteomic databases

PaxDbQ99572.
PRIDEQ99572.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000377162; ENSP00000366367; ENSG00000089041. [Q99572-5]
ENST00000535600; ENSP00000442470; ENSG00000089041. [Q99572-5]
ENST00000541022; ENSP00000441230; ENSG00000089041. [Q99572-3]
ENST00000541716; ENSP00000437729; ENSG00000089041. [Q99572-3]
GeneID5027.
KEGGhsa:5027.
UCSCuc001tzm.3. human. [Q99572-1]

Organism-specific databases

CTD5027.
GeneCardsGC12P121570.
HGNCHGNC:8537. P2RX7.
HPAHPA034968.
HPA044141.
MIM602566. gene.
neXtProtNX_Q99572.
PharmGKBPA32866.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG38999.
HOGENOMHOG000232042.
HOVERGENHBG053086.
InParanoidQ99572.
KOK05220.
OrthoDBEOG78PV92.
TreeFamTF328633.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkQ99572.

Gene expression databases

ArrayExpressQ99572.
BgeeQ99572.
CleanExHS_P2RX7.
GenevestigatorQ99572.

Family and domain databases

Gene3D2.60.490.10. 1 hit.
InterProIPR003050. P2X7_purnocptor.
IPR027309. P2X_extracellular_dom.
IPR001429. P2X_purnocptor.
[Graphical view]
PANTHERPTHR10125. PTHR10125. 1 hit.
PTHR10125:SF13. PTHR10125:SF13. 1 hit.
PfamPF00864. P2X_receptor. 1 hit.
[Graphical view]
PRINTSPR01314. P2X7RECEPTOR.
PR01307. P2XRECEPTOR.
TIGRFAMsTIGR00863. P2X. 1 hit.
PROSITEPS01212. P2X_RECEPTOR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSP2RX7. human.
GeneWikiP2RX7.
GenomeRNAi5027.
NextBio13635968.
PROQ99572.
SOURCESearch...

Entry information

Entry nameP2RX7_HUMAN
AccessionPrimary (citable) accession number: Q99572
Secondary accession number(s): A8K2Z0 expand/collapse secondary AC list , E7EMK6, F5H6P2, F5H7E8, F8W951, O14991, Q4VKH8, Q4VKH9, Q4VKI0, Q4VKI1, Q4VKI2, Q4VKI3, Q4VKI4, Q7Z771, Q96EV7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 11, 2012
Last modified: March 19, 2014
This is version 139 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM