Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O15547

- P2RX6_HUMAN

UniProt

O15547 - P2RX6_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

P2X purinoceptor 6

Gene

P2RX6

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

Functioni

Receptor for ATP that acts as a ligand-gated ion channel.By similarity

GO - Molecular functioni

  1. ATP binding Source: BHF-UCL
  2. channel activity Source: ProtInc
  3. extracellular ATP-gated cation channel activity Source: BHF-UCL
  4. identical protein binding Source: BHF-UCL
  5. purinergic nucleotide receptor activity Source: BHF-UCL
  6. transmembrane signaling receptor activity Source: ProtInc

GO - Biological processi

  1. cation transmembrane transport Source: GOC
  2. cation transport Source: RefGenome
  3. muscle contraction Source: ProtInc
  4. protein heterooligomerization Source: Ensembl
  5. protein homooligomerization Source: BHF-UCL
  6. purinergic nucleotide receptor signaling pathway Source: GOC
  7. signal transduction Source: ProtInc
  8. transmembrane transport Source: GOC
  9. transport Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Ion transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
P2X purinoceptor 6
Short name:
P2X6
Alternative name(s):
ATP receptor
P2XM
Purinergic receptor
Purinergic receptor P2X-like 1
Gene namesi
Name:P2RX6
Synonyms:P2RXL1, P2X6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:8538. P2RX6.

Subcellular locationi

GO - Cellular componenti

  1. cell junction Source: BHF-UCL
  2. cytoplasm Source: BHF-UCL
  3. dendritic spine Source: Ensembl
  4. integral component of nuclear inner membrane Source: RefGenome
  5. integral component of plasma membrane Source: ProtInc
  6. neuronal cell body Source: Ensembl
  7. postsynaptic density Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162398523.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 441441P2X purinoceptor 6PRO_0000161557Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei64 – 641Phosphotyrosine1 Publication
Disulfide bondi127 ↔ 177By similarity
Disulfide bondi138 ↔ 161By similarity
Disulfide bondi144 ↔ 171By similarity
Glycosylationi165 – 1651N-linked (GlcNAc...)Sequence Analysis
Glycosylationi195 – 1951N-linked (GlcNAc...)Sequence Analysis
Glycosylationi210 – 2101N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi228 ↔ 238By similarity
Disulfide bondi272 ↔ 281By similarity

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiO15547.
PRIDEiO15547.

PTM databases

PhosphoSiteiO15547.

Expressioni

Tissue specificityi

Expressed predominantly in skeletal muscle.

Gene expression databases

BgeeiO15547.
CleanExiHS_P2RX6.
ExpressionAtlasiO15547. baseline and differential.
GenevestigatoriO15547.

Organism-specific databases

HPAiHPA028776.
HPA028777.

Interactioni

Subunit structurei

Unlike most P2XRs, P2RX6 does not seem to form homotrimers or heterotrimers.1 Publication

Protein-protein interaction databases

BioGridi114575. 4 interactions.
IntActiO15547. 1 interaction.
STRINGi9606.ENSP00000416193.

Structurei

3D structure databases

ProteinModelPortaliO15547.
SMRiO15547. Positions 41-356.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini11 – 3929CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini61 – 333273ExtracellularSequence AnalysisAdd
BLAST
Topological domaini355 – 44187CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei40 – 6021Helical; Name=1Sequence AnalysisAdd
BLAST
Transmembranei334 – 35421Helical; Name=2Sequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Belongs to the P2X receptor family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG47843.
GeneTreeiENSGT00390000016028.
HOGENOMiHOG000232042.
HOVERGENiHBG053086.
InParanoidiO15547.
KOiK05221.
OMAiRCPEHPS.
OrthoDBiEOG78PV92.
PhylomeDBiO15547.
TreeFamiTF328633.

Family and domain databases

Gene3Di2.60.490.10. 1 hit.
InterProiIPR003049. P2X6_purnocptor.
IPR027309. P2X_extracellular_dom.
IPR001429. P2X_purnocptor.
[Graphical view]
PANTHERiPTHR10125. PTHR10125. 1 hit.
PfamiPF00864. P2X_receptor. 1 hit.
[Graphical view]
PRINTSiPR01313. P2X6RECEPTOR.
PR01307. P2XRECEPTOR.
TIGRFAMsiTIGR00863. P2X. 1 hit.
PROSITEiPS01212. P2X_RECEPTOR. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O15547-1) [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
MCPQLAGAGS MGSPGATTGW GLLDYKTEKY VMTRNWRVGA LQRLLQFGIV
60 70 80 90 100
VYVVGWALLA KKGYQERDLE PQFSIITKLK GVSVTQIKEL GNRLWDVADF
110 120 130 140 150
VKPPQGENVF FLVTNFLVTP AQVQGRCPEH PSVPLANCWV DEDCPEGEGG
160 170 180 190 200
THSHGVKTGQ CVVFNGTHRT CEIWSWCPVE SGVVPSRPLL AQAQNFTLFI
210 220 230 240 250
KNTVTFSKFN FSKSNALETW DPTYFKHCRY EPQFSPYCPV FRIGDLVAKA
260 270 280 290 300
GGTFEDLALL GGSVGIRVHW DCDLDTGDSG CWPHYSFQLQ EKSYNFRTAT
310 320 330 340 350
HWWEQPGVEA RTLLKLYGIR FDILVTGQAG KFGLIPTAVT LGTGAAWLGV
360 370 380 390 400
VTFFCDLLLL YVDREAHFYW RTKYEEAKAP KATANSVWRE LALASQARLA
410 420 430 440
ECLRRSSAPA PTATAAGSQT QTPGWPCPSS DTHLPTHSGS L
Length:441
Mass (Da):48,829
Last modified:November 2, 2010 - v2
Checksum:iEFD45BDC81234A64
GO
Isoform 2 (identifier: O15547-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     30-55: Missing.

Note: No experimental confirmation available.

Show »
Length:415
Mass (Da):45,808
Checksum:i3E32A59741527671
GO

Sequence cautioni

The sequence AAF13303.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.
The sequence AAF13303.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAH33488.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence AAI09210.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAA22046.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
The sequence BAA22047.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti393 – 3931L → F in AAF13303. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti38 – 381V → G.
Corresponds to variant rs2006846 [ dbSNP | Ensembl ].
VAR_057664
Natural varianti242 – 2421R → H.1 Publication
Corresponds to variant rs2277838 [ dbSNP | Ensembl ].
VAR_020338

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei30 – 5526Missing in isoform 2. 1 PublicationVSP_044799Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB002059 Genomic DNA. Translation: BAA22047.1. Different initiation.
AB002058 mRNA. Translation: BAA22046.1. Different initiation.
CR456535 mRNA. Translation: CAG30421.1.
AC002472 Genomic DNA. No translation available.
BC033488 mRNA. Translation: AAH33488.1. Different initiation.
BC109209 mRNA. Translation: AAI09210.1. Different initiation.
AF065385 mRNA. Translation: AAF13303.1. Sequence problems.
CCDSiCCDS13788.2. [O15547-1]
CCDS54504.1. [O15547-2]
RefSeqiNP_001153026.1. NM_001159554.1. [O15547-2]
NP_005437.2. NM_005446.3. [O15547-1]
UniGeneiHs.113275.

Genome annotation databases

EnsembliENST00000401443; ENSP00000385309; ENSG00000099957. [O15547-2]
ENST00000413302; ENSP00000416193; ENSG00000099957. [O15547-1]
GeneIDi9127.
KEGGihsa:9127.
UCSCiuc010gsu.1. human. [O15547-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

P2X receptor entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB002059 Genomic DNA. Translation: BAA22047.1 . Different initiation.
AB002058 mRNA. Translation: BAA22046.1 . Different initiation.
CR456535 mRNA. Translation: CAG30421.1 .
AC002472 Genomic DNA. No translation available.
BC033488 mRNA. Translation: AAH33488.1 . Different initiation.
BC109209 mRNA. Translation: AAI09210.1 . Different initiation.
AF065385 mRNA. Translation: AAF13303.1 . Sequence problems.
CCDSi CCDS13788.2. [O15547-1 ]
CCDS54504.1. [O15547-2 ]
RefSeqi NP_001153026.1. NM_001159554.1. [O15547-2 ]
NP_005437.2. NM_005446.3. [O15547-1 ]
UniGenei Hs.113275.

3D structure databases

ProteinModelPortali O15547.
SMRi O15547. Positions 41-356.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114575. 4 interactions.
IntActi O15547. 1 interaction.
STRINGi 9606.ENSP00000416193.

Chemistry

BindingDBi O15547.
ChEMBLi CHEMBL2670.
GuidetoPHARMACOLOGYi 483.

PTM databases

PhosphoSitei O15547.

Proteomic databases

PaxDbi O15547.
PRIDEi O15547.

Protocols and materials databases

DNASUi 9127.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000401443 ; ENSP00000385309 ; ENSG00000099957 . [O15547-2 ]
ENST00000413302 ; ENSP00000416193 ; ENSG00000099957 . [O15547-1 ]
GeneIDi 9127.
KEGGi hsa:9127.
UCSCi uc010gsu.1. human. [O15547-1 ]

Organism-specific databases

CTDi 9127.
GeneCardsi GC22P021364.
HGNCi HGNC:8538. P2RX6.
HPAi HPA028776.
HPA028777.
MIMi 608077. gene.
neXtProti NX_O15547.
PharmGKBi PA162398523.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG47843.
GeneTreei ENSGT00390000016028.
HOGENOMi HOG000232042.
HOVERGENi HBG053086.
InParanoidi O15547.
KOi K05221.
OMAi RCPEHPS.
OrthoDBi EOG78PV92.
PhylomeDBi O15547.
TreeFami TF328633.

Miscellaneous databases

GeneWikii P2RX6.
GenomeRNAii 9127.
NextBioi 34213.
PROi O15547.
SOURCEi Search...

Gene expression databases

Bgeei O15547.
CleanExi HS_P2RX6.
ExpressionAtlasi O15547. baseline and differential.
Genevestigatori O15547.

Family and domain databases

Gene3Di 2.60.490.10. 1 hit.
InterProi IPR003049. P2X6_purnocptor.
IPR027309. P2X_extracellular_dom.
IPR001429. P2X_purnocptor.
[Graphical view ]
PANTHERi PTHR10125. PTHR10125. 1 hit.
Pfami PF00864. P2X_receptor. 1 hit.
[Graphical view ]
PRINTSi PR01313. P2X6RECEPTOR.
PR01307. P2XRECEPTOR.
TIGRFAMsi TIGR00863. P2X. 1 hit.
PROSITEi PS01212. P2X_RECEPTOR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of P2XM, a novel human P2X receptor gene regulated by p53."
    Urano T., Nishimori H., Han H., Furuhata T., Kimura Y., Nakamura Y., Tokino T.
    Cancer Res. 57:3281-3287(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-441 (ISOFORM 1), VARIANT HIS-242.
    Tissue: Brain.
  5. "Cloning and tissue distribution of a human cDNA encoding P2X6 purinoceptor."
    Cheng X., Jin H., Huang C.-C.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-441 (ISOFORM 1).
    Tissue: Skeletal muscle.
  6. "Identification of the phosphotyrosine proteome from thrombin activated platelets."
    Maguire P.B., Wynne K.J., Harney D.F., O'Donoghue N.M., Stephens G., Fitzgerald D.J.
    Proteomics 2:642-648(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-64.
  7. "Atomic force microscopy imaging demonstrates that P2X2 receptors are trimers but that P2X6 receptor subunits do not oligomerize."
    Barrera N.P., Ormond S.J., Henderson R.M., Murrell-Lagnado R.D., Edwardson J.M.
    J. Biol. Chem. 280:10759-10765(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, GLYCOSYLATION.

Entry informationi

Entry nameiP2RX6_HUMAN
AccessioniPrimary (citable) accession number: O15547
Secondary accession number(s): F6V3D7
, Q32MB6, Q58F04, Q6IC33, Q9UL50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 2, 2010
Last modified: October 29, 2014
This is version 133 of the entry and version 2 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 22
    Human chromosome 22: 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