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Q9UBL9 (P2RX2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
P2X purinoceptor 2

Short name=P2X2
Alternative name(s):
ATP receptor
Purinergic receptor
Gene names
Name:P2RX2
Synonyms:P2X2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length471 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Binding of this ligand-gated ion channel to ATP mediates synaptic transmission between neurons and from neurons to smooth muscle.

Subunit structure

Functional P2XRs are organized as homomeric and heteromeric trimers.

Subcellular location

Membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the P2X receptor family.

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   Molecular functionIon channel
Ligand-gated ion channel
Receptor
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbehavioral response to pain

Inferred from electronic annotation. Source: Compara

detection of hypoxic conditions in blood by carotid body chemoreceptor signaling

Inferred from electronic annotation. Source: Compara

neuromuscular junction development

Inferred from electronic annotation. Source: Compara

neuromuscular synaptic transmission

Inferred from electronic annotation. Source: Compara

peristalsis

Inferred from electronic annotation. Source: Compara

positive regulation of calcium ion transport into cytosol

Non-traceable author statement PubMed 17895406. Source: BHF-UCL

positive regulation of calcium-mediated signaling

Non-traceable author statement PubMed 17895406. Source: BHF-UCL

protein heterooligomerization

Inferred from electronic annotation. Source: Compara

protein homooligomerization

Inferred from physical interaction PubMed 15313628. Source: BHF-UCL

regulation of action potential in neuron

Inferred from electronic annotation. Source: Compara

response to ATP

Inferred from electronic annotation. Source: Compara

response to carbohydrate stimulus

Inferred from electronic annotation. Source: Compara

response to hypoxia

Inferred from electronic annotation. Source: Compara

sensory perception of taste

Inferred from electronic annotation. Source: Compara

urinary bladder smooth muscle contraction

Inferred from electronic annotation. Source: Compara

   Cellular_componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

neuronal cell body

Inferred from electronic annotation. Source: Compara

plasma membrane

Inferred from electronic annotation. Source: Compara

postsynaptic density

Inferred from electronic annotation. Source: Compara

presynaptic membrane

Inferred from electronic annotation. Source: Compara

terminal bouton

Inferred from electronic annotation. Source: Compara

   Molecular_functionATP binding

Non-traceable author statement PubMed 17895406. Source: BHF-UCL

cadmium ion binding

Inferred from electronic annotation. Source: Compara

cobalt ion binding

Inferred from electronic annotation. Source: Compara

copper ion binding

Inferred from electronic annotation. Source: Compara

drug binding

Inferred from electronic annotation. Source: Compara

extracellular ATP-gated cation channel activity

Non-traceable author statement PubMed 17895406. Source: BHF-UCL

mercury ion binding

Inferred from electronic annotation. Source: Compara

nickel cation binding

Inferred from electronic annotation. Source: Compara

phosphatidylinositol binding

Inferred from electronic annotation. Source: Compara

purinergic nucleotide receptor activity

Non-traceable author statement PubMed 17895406. Source: BHF-UCL

zinc ion binding

Inferred from electronic annotation. Source: Compara

Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform A (identifier: Q9UBL9-1)

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: Q9UBL9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     381-447: Missing.
Isoform C (identifier: Q9UBL9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     104-127: Missing.
Isoform D (identifier: Q9UBL9-4)

The sequence of this isoform differs from the canonical sequence as follows:
     354-354: V → VVRNPLWGPSGCGGSTRPLHTGLCWPQ
Isoform H (identifier: Q9UBL9-5)

The sequence of this isoform differs from the canonical sequence as follows:
     36-127: Missing.
Isoform I (identifier: Q9UBL9-6)

The sequence of this isoform differs from the canonical sequence as follows:
     38-152: NRRLGVLYRA...VAGELDMLGN → IHRAEKLPGE...GRGGVREAPR
Isoform K (identifier: Q9UBL9-7)

The sequence of this isoform differs from the canonical sequence as follows:
     104-127: Missing.
     154-258: LRTGRCVPYY...GESFTELAHK → ALQDLRGVRL...ELHRARTQGR
     381-447: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 471471P2X purinoceptor 2
PRO_0000161549

Regions

Topological domain1 – 4242Cytoplasmic Potential
Transmembrane43 – 6321Helical; Name=1; Potential
Topological domain64 – 337274Extracellular Potential
Transmembrane338 – 35821Helical; Name=2; Potential
Topological domain359 – 471113Cytoplasmic Potential
Region320 – 33314Pore-forming motif Potential

Amino acid modifications

Glycosylation1331N-linked (GlcNAc...) Potential
Glycosylation1941N-linked (GlcNAc...) Potential
Glycosylation3101N-linked (GlcNAc...) Potential
Disulfide bond21 ↔ 439 By similarity
Disulfide bond125 ↔ 176 By similarity
Disulfide bond136 ↔ 159 By similarity
Disulfide bond142 ↔ 170 By similarity
Disulfide bond226 ↔ 236 By similarity
Disulfide bond270 ↔ 279 By similarity

Natural variations

Alternative sequence36 – 12792Missing in isoform H.
VSP_004495
Alternative sequence38 – 152115NRRLG…DMLGN → IHRAEKLPGERDGPRELHHH QGQGDHHVRAQSVGRGGVRE APR in isoform I.
VSP_004496
Alternative sequence104 – 12724Missing in isoform C and isoform K.
VSP_004497
Alternative sequence154 – 258105LRTGR…ELAHK → ALQDLRGVRLVPGGRWGLCQ PISGYDGPKFHHPHQEQHPL PQIPLLQGQHRRPHRRVPEA LHVPRGLRPLLPHLQAGLYR GEGWGELHRARTQGR in isoform K.
VSP_014135
Alternative sequence3541V → VVRNPLWGPSGCGGSTRPLH TGLCWPQ in isoform D.
VSP_004498
Alternative sequence381 – 44767Missing in isoform B and isoform K.
VSP_004499

Experimental info

Sequence conflict1 – 1414MAAAQ…AGATA → MV in AAD42947. Ref.3
Sequence conflict1 – 1414MAAAQ…AGATA → MV in AAD42948. Ref.3
Sequence conflict481V → A in AAQ54329. Ref.4

Sequences

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

Last modified May 1, 2000. Version 1.
Checksum: 84CD61DA136EF420

FASTA47151,754
        10         20         30         40         50         60 
MAAAQPKYPA GATARRLARG CWSALWDYET PKVIVVRNRR LGVLYRAVQL LILLYFVWYV 

        70         80         90        100        110        120 
FIVQKSYQES ETGPESSIIT KVKGITTSEH KVWDVEEYVK PPEGGSVFSI ITRVEATHSQ 

       130        140        150        160        170        180 
TQGTCPESIR VHNATCLSDA DCVAGELDML GNGLRTGRCV PYYQGPSKTC EVFGWCPVED 

       190        200        210        220        230        240 
GASVSQFLGT MAPNFTILIK NSIHYPKFHF SKGNIADRTD GYLKRCTFHE ASDLYCPIFK 

       250        260        270        280        290        300 
LGFIVEKAGE SFTELAHKGG VIGVIINWDC DLDLPASECN PKYSFRRLDP KHVPASSGYN 

       310        320        330        340        350        360 
FRFAKYYKIN GTTTRTLIKA YGIRIDVIVH GQAGKFSLIP TIINLATALT SVGVGSFLCD 

       370        380        390        400        410        420 
WILLTFMNKN KVYSHKKFDK VCTPSHPSGS WPVTLARVLG QAPPEPGHRS EDQHPSPPSG 

       430        440        450        460        470 
QEGQQGAECG PAFPPLRPCP ISAPSEQMVD TPASEPAQAS TPTDPKGLAQ L 

« Hide

Isoform B [UniParc].

Checksum: 695AC6C1655DB952
Show »

FASTA40444,842
Isoform C [UniParc].

Checksum: BAF5513A27314D1D
Show »

FASTA44749,266
Isoform D [UniParc].

Checksum: FC4007F5BDD46E0E
Show »

FASTA49754,513
Isoform H [UniParc].

Checksum: 8D1AA9A069D7F008
Show »

FASTA37941,254
Isoform I [UniParc].

Checksum: 8B55562C9BAEAE5E
Show »

FASTA39943,726
Isoform K [UniParc].

Checksum: 36FC1F15D45624DC
Show »

FASTA37041,370

References

« Hide 'large scale' references
[1]"Molecular and functional characterization of human P2X(2) receptors."
Lynch K.J., Touma E., Niforatos W., Kage K.L., Burgard E.C., van Biesen T., Kowaluk E.A., Jarvis M.F.
Mol. Pharmacol. 56:1171-1181(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS A; B; C AND D).
Tissue: Pituitary.
[2]"Cloning of the human P2X2 receptor cDNA and multiple splice variants."
McMahon R.A., Egan T.M., Hurley P.T., Nelson A., Rogers M., Martin F.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
Tissue: Placenta.
[3]"Cloning and molecular characterization of human P2X2 and its splice variants."
Chang T.K., Kosaka A.H., Oglesby I.B., Gever J.R., Lachnit W.G., Ford A.P.D.W., Chang D.J.
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; C; H AND I).
Tissue: Prostate.
[4]Lin L., Zheng G., Yu R., Li H., Shen C., Zhou G., Zhong G., Li M., Xiao W., Ke R., Yang S.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM K).
[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].
+Additional computationally mapped references.

Web resources

Wikipedia

P2X receptor entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF190822 mRNA. Translation: AAF19170.1.
AF190823 mRNA. Translation: AAF19171.1.
AF190824 mRNA. Translation: AAF19172.1.
AF190825 mRNA. Translation: AAF19173.1.
AF190826 Genomic DNA. Translation: AAF19174.1.
AF109387 mRNA. Translation: AAD42947.1.
AF109388 mRNA. Translation: AAD42948.1.
AF260426 mRNA. Translation: AAF74201.1.
AF260427 mRNA. Translation: AAF74202.1.
AF260428 mRNA. Translation: AAF74203.1.
AF260429 mRNA. Translation: AAF74204.1.
AY346374 mRNA. Translation: AAQ54329.1.
AC131212 Genomic DNA. No translation available.
IPIIPI00219278.
IPI00219279.
IPI00219280.
IPI00219281.
IPI00298586.
IPI00329494.
IPI00433338.
RefSeqNP_036358.2. NM_012226.3.
NP_057402.1. NM_016318.2.
NP_733782.1. NM_170682.2.
NP_733783.1. NM_170683.2.
NP_777361.1. NM_174872.1.
NP_777362.1. NM_174873.1.
UniGeneHs.258580.

3D structure databases

ProteinModelPortalQ9UBL9.
ModBaseSearch...

PTM databases

PhosphoSiteQ9UBL9.

Polymorphism databases

DMDM12643353.

Proteomic databases

PaxDbQ9UBL9.
PRIDEQ9UBL9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000343948; ENSP00000343339; ENSG00000187848.
ENST00000348800; ENSP00000345095; ENSG00000187848.
ENST00000350048; ENSP00000343904; ENSG00000187848.
ENST00000351222; ENSP00000344502; ENSG00000187848.
ENST00000352418; ENSP00000341419; ENSG00000187848.
ENST00000389110; ENSP00000373762; ENSG00000187848.
ENST00000449132; ENSP00000405531; ENSG00000187848.
GeneID22953.
KEGGhsa:22953.
UCSCuc001uki.1. human.
uc001ukj.1. human.
uc001ukk.1. human.
uc001ukl.1. human.
uc001ukm.1. human.
uc001ukn.1. human.
uc001uko.1. human.

Organism-specific databases

CTD22953.
GeneCardsGC12P133195.
HGNCHGNC:15459. P2RX2.
HPAHPA014025.
MIM600844. gene.
neXtProtNX_Q9UBL9.
PharmGKBPA32862.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG68669.
HOVERGENHBG053086.
KOK05216.
OMAILLYFVW.

Gene expression databases

BgeeQ9UBL9.
GenevestigatorQ9UBL9.
GermOnlineENSG00000187848. Homo sapiens.

Family and domain databases

Gene3D2.60.490.10. 1 hit.
InterProIPR003045. P2X2_purnocptor.
IPR027309. P2X_extracellular_dom.
IPR001429. P2X_purnocptor.
[Graphical view]
PANTHERPTHR10125. PTHR10125. 1 hit.
PTHR10125:SF4. PTHR10125:SF4. 1 hit.
PfamPF00864. P2X_receptor. 1 hit.
[Graphical view]
PRINTSPR01309. P2X2RECEPTOR.
PR01307. P2XRECEPTOR.
TIGRFAMsTIGR00863. P2X. 1 hit.
PROSITEPS01212. P2X_RECEPTOR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBQ9UBL9.
ChEMBLCHEMBL2531.
GenomeRNAi22953.
NextBio43725.
SOURCESearch...

Entry information

Entry nameP2RX2_HUMAN
AccessionPrimary (citable) accession number: Q9UBL9
Secondary accession number(s): A6NGB4 expand/collapse secondary AC list , A6NH93, A6NHC2, A6NHU3, A6NIG9, Q6V9R6, Q9NR37, Q9NR38, Q9UHD5, Q9UHD6, Q9UHD7, Q9Y637, Q9Y638
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: May 1, 2000
Last modified: May 1, 2013
This is version 108 of the entry and version 1 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

Human chromosome 12

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

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families