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Protein

P2X purinoceptor 7

Gene

P2RX7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. ATP binding Source: BHF-UCL
  2. extracellular ATP-gated cation channel activity Source: BHF-UCL
  3. lipopolysaccharide binding Source: BHF-UCL
  4. protein homodimerization activity Source: BHF-UCL
  5. purinergic nucleotide receptor activity Source: BHF-UCL
  6. receptor binding Source: BHF-UCL

GO - Biological processi

  1. apoptotic signaling pathway Source: BHF-UCL
  2. bleb assembly Source: UniProtKB
  3. cation transmembrane transport Source: GOC
  4. cation transport Source: GOC
  5. cell surface receptor signaling pathway Source: BHF-UCL
  6. innate immune response Source: Reactome
  7. membrane depolarization Source: BHF-UCL
  8. negative regulation of bone resorption Source: BHF-UCL
  9. negative regulation of MAPK cascade Source: BHF-UCL
  10. nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Source: Reactome
  11. pore complex assembly Source: BHF-UCL
  12. positive regulation of bone mineralization Source: BHF-UCL
  13. positive regulation of calcium ion transport into cytosol Source: BHF-UCL
  14. positive regulation of cytolysis Source: BHF-UCL
  15. positive regulation of cytoskeleton organization Source: BHF-UCL
  16. positive regulation of interleukin-1 beta secretion Source: BHF-UCL
  17. purinergic nucleotide receptor signaling pathway Source: GOC
  18. regulation of killing of cells of other organism Source: BHF-UCL
  19. regulation of sodium ion transport Source: BHF-UCL
  20. response to ATP Source: BHF-UCL
  21. sensory perception of pain Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Ion transport, Transport

Enzyme and pathway databases

ReactomeiREACT_75808. The NLRP3 inflammasome.
SignaLinkiQ99572.

Protein family/group databases

TCDBi1.A.7.1.3. the atp-gated p2x receptor cation channel (p2x receptor) family.

Names & Taxonomyi

Protein namesi
Recommended name:
P2X purinoceptor 7
Short name:
P2X7
Alternative name(s):
ATP receptor
P2Z receptor
Purinergic receptor
Gene namesi
Name:P2RX7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:8537. P2RX7.

Subcellular locationi

Cell membrane 1 Publication; Multi-pass membrane protein

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2525CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei26 – 4621Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini47 – 334288ExtracellularSequence AnalysisAdd
BLAST
Transmembranei335 – 35521Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini356 – 595240CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. bleb Source: BHF-UCL
  2. cytoplasm Source: BHF-UCL
  3. integral component of nuclear inner membrane Source: GO_Central
  4. integral component of plasma membrane Source: BHF-UCL
  5. membrane Source: BHF-UCL
  6. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi187 – 1871N → A: Alters cell surface expression. 1 Publication

Organism-specific databases

PharmGKBiPA32866.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 595595P2X purinoceptor 7PRO_0000161560Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi119 ↔ 168By similarity
Modified residuei125 – 1251ADP-ribosylarginineBy similarity
Disulfide bondi129 ↔ 152By similarity
Modified residuei133 – 1331ADP-ribosylarginineBy similarity
Disulfide bondi135 ↔ 162By similarity
Glycosylationi187 – 1871N-linked (GlcNAc...)1 Publication
Glycosylationi202 – 2021N-linked (GlcNAc...)1 Publication
Glycosylationi213 – 2131N-linked (GlcNAc...)1 Publication
Disulfide bondi216 ↔ 226By similarity
Glycosylationi241 – 2411N-linked (GlcNAc...)1 Publication
Disulfide bondi260 ↔ 269By similarity
Glycosylationi284 – 2841N-linked (GlcNAc...)1 Publication
Modified residuei343 – 3431Phosphotyrosine1 Publication

Post-translational modificationi

Phosphorylation results in its inactivation.1 Publication
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.1 Publication

Keywords - PTMi

ADP-ribosylation, Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiQ99572.
PRIDEiQ99572.

PTM databases

PhosphoSiteiQ99572.

Expressioni

Tissue specificityi

Widely expressed with highest levels in brain and immune tissues.1 Publication

Gene expression databases

BgeeiQ99572.
CleanExiHS_P2RX7.
ExpressionAtlasiQ99572. baseline and differential.
GenevestigatoriQ99572.

Organism-specific databases

HPAiHPA034968.
HPA044141.

Interactioni

Subunit structurei

Functional P2XRs are organized as homomeric and heteromeric trimers. Interacts with LAMA3, ITGB2, ACTB, ACTN4, SVIL, MPP3, HSPA1, HSPCB, HSPA8, PIK230 and PTPRB. Interacts (via C-terminus) with EMP2 (PubMed:12107182).2 Publications

Protein-protein interaction databases

IntActiQ99572. 6 interactions.
MINTiMINT-3972963.
STRINGi9606.ENSP00000261826.

Structurei

3D structure databases

ProteinModelPortaliQ99572.
SMRiQ99572. Positions 32-354.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the P2X receptor family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG38999.
GeneTreeiENSGT00390000016028.
HOGENOMiHOG000232042.
HOVERGENiHBG053086.
InParanoidiQ99572.
KOiK05220.
OrthoDBiEOG78PV92.
TreeFamiTF328633.

Family and domain databases

Gene3Di2.60.490.10. 1 hit.
InterProiIPR003050. P2X7_purnocptor.
IPR027309. P2X_extracellular_dom.
IPR001429. P2X_purnocptor.
[Graphical view]
PANTHERiPTHR10125. PTHR10125. 1 hit.
PTHR10125:SF13. PTHR10125:SF13. 1 hit.
PfamiPF00864. P2X_receptor. 1 hit.
[Graphical view]
PRINTSiPR01314. P2X7RECEPTOR.
PR01307. P2XRECEPTOR.
TIGRFAMsiTIGR00863. P2X. 1 hit.
PROSITEiPS01212. P2X_RECEPTOR. 1 hit.
[Graphical view]

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. Align

Isoform A (identifier: Q99572-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MPACCSCSDV FQYETNKVTR IQSMNYGTIK WFFHVIIFSY VCFALVSDKL
60 70 80 90 100
YQRKEPVISS VHTKVKGIAE VKEEIVENGV KKLVHSVFDT ADYTFPLQGN
110 120 130 140 150
SFFVMTNFLK TEGQEQRLCP EYPTRRTLCS SDRGCKKGWM DPQSKGIQTG
160 170 180 190 200
RCVVYEGNQK TCEVSAWCPI EAVEEAPRPA LLNSAENFTV LIKNNIDFPG
210 220 230 240 250
HNYTTRNILP GLNITCTFHK TQNPQCPIFR LGDIFRETGD NFSDVAIQGG
260 270 280 290 300
IMGIEIYWDC NLDRWFHHCR PKYSFRRLDD KTTNVSLYPG YNFRYAKYYK
310 320 330 340 350
ENNVEKRTLI KVFGIRFDIL VFGTGGKFDI IQLVVYIGST LSYFGLAAVF
360 370 380 390 400
IDFLIDTYSS NCCRSHIYPW CKCCQPCVVN EYYYRKKCES IVEPKPTLKY
410 420 430 440 450
VSFVDESHIR MVNQQLLGRS LQDVKGQEVP RPAMDFTDLS RLPLALHDTP
460 470 480 490 500
PIPGQPEEIQ LLRKEATPRS RDSPVWCQCG SCLPSQLPES HRCLEELCCR
510 520 530 540 550
KKPGACITTS ELFRKLVLSR HVLQFLLLYQ EPLLALDVDS TNSRLRHCAY
560 570 580 590
RCYATWRFGS QDMADFAILP SCCRWRIRKE FPKSEGQYSG FKSPY
Length:595
Mass (Da):68,585
Last modified:July 11, 2012 - v4
Checksum:i584C17EF6D5EC899
GO
Isoform B (identifier: Q99572-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:364
Mass (Da):41,792
Checksum:i3A9C0F1D110543FC
GO
Isoform C (identifier: Q99572-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     122-128: YPTRRTL → EFRPEGV
     129-595: Missing.

Show »
Length:128
Mass (Da):14,749
Checksum:iDBBA1D99D97E108E
GO
Isoform D (identifier: Q99572-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: MPACCSC → MDGPAEQ
     8-177: Missing.

Show »
Length:425
Mass (Da):49,165
Checksum:i9245A1363145ABD7
GO
Isoform E (identifier: Q99572-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     206-294: Missing.
     347-364: AAVFIDFLIDTYSSNCCR → VRDSLFHALGKWFGEGSD
     365-595: Missing.

Show »
Length:275
Mass (Da):31,294
Checksum:i6AE04D318BEB617C
GO
Isoform F (identifier: Q99572-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-3: MPA → MWQ
     4-292: Missing.

Show »
Length:306
Mass (Da):35,544
Checksum:i28004164298DC12A
GO
Isoform G (identifier: Q99572-7) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-98: MPACCSCSDV...DTADYTFPLQ → MTPGDHSW
     347-364: AAVFIDFLIDTYSSNCCR → VRDSLFHALGKWFGEGSD
     365-595: Missing.

Show »
Length:274
Mass (Da):31,446
Checksum:i48E9BBD37BFEFDA1
GO
Isoform H (identifier: Q99572-8) [UniParc]FASTAAdd to Basket

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.

Show »
Length:505
Mass (Da):58,239
Checksum:iD65D70EADCE5702A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti481 – 4811S → R in CAA73360. (PubMed:9826911)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti25 – 251N → S in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036444
Natural varianti76 – 761V → A.
Corresponds to variant rs17525809 [ dbSNP | Ensembl ].
VAR_057665
Natural varianti150 – 1501G → R.
Corresponds to variant rs28360447 [ dbSNP | Ensembl ].
VAR_057666
Natural varianti155 – 1551Y → H.4 Publications
Corresponds to variant rs208294 [ dbSNP | Ensembl ].
VAR_019649
Natural varianti270 – 2701R → C.
Corresponds to variant rs16950860 [ dbSNP | Ensembl ].
VAR_057667
Natural varianti270 – 2701R → H.3 Publications
Corresponds to variant rs7958311 [ dbSNP | Ensembl ].
VAR_019648
Natural varianti276 – 2761R → H.
Corresponds to variant rs7958316 [ dbSNP | Ensembl ].
VAR_057668
Natural varianti307 – 3071R → Q Polymorphism that results in a loss of function. 1 Publication
Corresponds to variant rs28360457 [ dbSNP | Ensembl ].
VAR_057669
Natural varianti348 – 3481A → T.1 Publication
Corresponds to variant rs1718119 [ dbSNP | Ensembl ].
VAR_057670
Natural varianti357 – 3571T → S.1 Publication
Corresponds to variant rs2230911 [ dbSNP | Ensembl ].
VAR_019650
Natural varianti430 – 4301P → R.
Corresponds to variant rs10160951 [ dbSNP | Ensembl ].
VAR_057671
Natural varianti433 – 4331A → V.
Corresponds to variant rs28360459 [ dbSNP | Ensembl ].
VAR_057672
Natural varianti460 – 4601Q → R.
Corresponds to variant rs2230912 [ dbSNP | Ensembl ].
VAR_019651
Natural varianti496 – 4961E → A Polymorphism that results in a loss of function. 2 Publications
Corresponds to variant rs3751143 [ dbSNP | Ensembl ].
VAR_019652
Natural varianti521 – 5211H → Q.
Corresponds to variant rs2230913 [ dbSNP | Ensembl ].
VAR_057673
Natural varianti522 – 5221V → I.
Corresponds to variant rs34219304 [ dbSNP | Ensembl ].
VAR_057674
Natural varianti568 – 5681I → N Polymorphism that results in trafficking defect and around 50% loss of function. 2 Publications
Corresponds to variant rs1653624 [ dbSNP | Ensembl ].
VAR_068011
Natural varianti574 – 5741R → L in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036445
Natural varianti578 – 5781R → Q.
Corresponds to variant rs28360460 [ dbSNP | Ensembl ].
VAR_057675

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9898MPACC…TFPLQ → MTPGDHSW in isoform G and isoform H. 1 PublicationVSP_047776Add
BLAST
Alternative sequencei1 – 77MPACCSC → MDGPAEQ in isoform D. 2 PublicationsVSP_047777
Alternative sequencei1 – 33MPA → MWQ in isoform F. 1 PublicationVSP_047778
Alternative sequencei4 – 292289Missing in isoform F. 1 PublicationVSP_047779Add
BLAST
Alternative sequencei8 – 177170Missing in isoform D. 2 PublicationsVSP_047780Add
BLAST
Alternative sequencei122 – 1287YPTRRTL → EFRPEGV in isoform C. 2 PublicationsVSP_047781
Alternative sequencei129 – 595467Missing in isoform C. 2 PublicationsVSP_047782Add
BLAST
Alternative sequencei206 – 29489Missing in isoform E. 1 PublicationVSP_047783Add
BLAST
Alternative sequencei347 – 36418AAVFI…SNCCR → VRDSLFHALGKWFGEGSD in isoform B, isoform E and isoform G. 1 PublicationVSP_047784Add
BLAST
Alternative sequencei365 – 595231Missing in isoform B, isoform E and isoform G. 1 PublicationVSP_047785Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09561 mRNA. Translation: CAA70755.1.
Y12851
, 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.
CCDSiCCDS9213.1. [Q99572-1]
RefSeqiNP_002553.3. NM_002562.5. [Q99572-1]
UniGeneiHs.729169.

Genome annotation databases

EnsembliENST00000328963; ENSP00000330696; ENSG00000089041. [Q99572-1]
ENST00000535250; ENSP00000442572; ENSG00000089041. [Q99572-2]
ENST00000535600; ENSP00000442470; ENSG00000089041. [Q99572-5]
ENST00000541022; ENSP00000441230; ENSG00000089041. [Q99572-3]
ENST00000541716; ENSP00000437729; ENSG00000089041. [Q99572-3]
GeneIDi5027.
KEGGihsa:5027.
UCSCiuc001tzm.3. human. [Q99572-1]

Polymorphism databases

DMDMi395398617.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
Wikipedia

P2X receptor entry

Wikipedia

P2RX7 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09561 mRNA. Translation: CAA70755.1.
Y12851
, 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.
CCDSiCCDS9213.1. [Q99572-1]
RefSeqiNP_002553.3. NM_002562.5. [Q99572-1]
UniGeneiHs.729169.

3D structure databases

ProteinModelPortaliQ99572.
SMRiQ99572. Positions 32-354.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ99572. 6 interactions.
MINTiMINT-3972963.
STRINGi9606.ENSP00000261826.

Chemistry

BindingDBiQ99572.
ChEMBLiCHEMBL4805.
GuidetoPHARMACOLOGYi484.

Protein family/group databases

TCDBi1.A.7.1.3. the atp-gated p2x receptor cation channel (p2x receptor) family.

PTM databases

PhosphoSiteiQ99572.

Polymorphism databases

DMDMi395398617.

Proteomic databases

PaxDbiQ99572.
PRIDEiQ99572.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000328963; ENSP00000330696; ENSG00000089041. [Q99572-1]
ENST00000535250; ENSP00000442572; ENSG00000089041. [Q99572-2]
ENST00000535600; ENSP00000442470; ENSG00000089041. [Q99572-5]
ENST00000541022; ENSP00000441230; ENSG00000089041. [Q99572-3]
ENST00000541716; ENSP00000437729; ENSG00000089041. [Q99572-3]
GeneIDi5027.
KEGGihsa:5027.
UCSCiuc001tzm.3. human. [Q99572-1]

Organism-specific databases

CTDi5027.
GeneCardsiGC12P121570.
HGNCiHGNC:8537. P2RX7.
HPAiHPA034968.
HPA044141.
MIMi602566. gene.
neXtProtiNX_Q99572.
PharmGKBiPA32866.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG38999.
GeneTreeiENSGT00390000016028.
HOGENOMiHOG000232042.
HOVERGENiHBG053086.
InParanoidiQ99572.
KOiK05220.
OrthoDBiEOG78PV92.
TreeFamiTF328633.

Enzyme and pathway databases

ReactomeiREACT_75808. The NLRP3 inflammasome.
SignaLinkiQ99572.

Miscellaneous databases

ChiTaRSiP2RX7. human.
GeneWikiiP2RX7.
GenomeRNAii5027.
NextBioi13635968.
PROiQ99572.
SOURCEiSearch...

Gene expression databases

BgeeiQ99572.
CleanExiHS_P2RX7.
ExpressionAtlasiQ99572. baseline and differential.
GenevestigatoriQ99572.

Family and domain databases

Gene3Di2.60.490.10. 1 hit.
InterProiIPR003050. P2X7_purnocptor.
IPR027309. P2X_extracellular_dom.
IPR001429. P2X_purnocptor.
[Graphical view]
PANTHERiPTHR10125. PTHR10125. 1 hit.
PTHR10125:SF13. PTHR10125:SF13. 1 hit.
PfamiPF00864. P2X_receptor. 1 hit.
[Graphical view]
PRINTSiPR01314. P2X7RECEPTOR.
PR01307. P2XRECEPTOR.
TIGRFAMsiTIGR00863. P2X. 1 hit.
PROSITEiPS01212. P2X_RECEPTOR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. "Epithelial membrane proteins induce membrane blebbing and interact with the P2X7 receptor C terminus."
    Wilson H.L., Wilson S.A., Surprenant A., North R.A.
    J. Biol. Chem. 277:34017-34023(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EMP2, SUBCELLULAR LOCATION.
  9. "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.
  10. "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.
  11. "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.
  12. "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.
  13. "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.
  14. Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-25 AND LEU-574.

Entry informationi

Entry nameiP2RX7_HUMAN
AccessioniPrimary (citable) accession number: Q99572
Secondary accession number(s): A8K2Z0
, E7EMK6, F5H6P2, F5H7E8, F8W951, O14991, Q4VKH8, Q4VKH9, Q4VKI0, Q4VKI1, Q4VKI2, Q4VKI3, Q4VKI4, Q7Z771, Q96EV7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 11, 2012
Last modified: February 4, 2015
This is version 147 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.