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UniProtKB/Swiss-Prot Q99572: Variant p.Ile568Asn

P2X purinoceptor 7
Gene: P2RX7
Variant information

Variant position:  568
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Polymorphism
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Isoleucine (I) to Asparagine (N) at position 568 (I568N, p.Ile568Asn).
Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.

Physico-chemical properties:  Change from medium size and hydrophobic (I) to medium size and polar (N)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -3
The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page

Variant description:  Polymorphism; results in trafficking defect and around 50% loss of function.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.

Sequence information

Variant position:  568
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  595
The length of the canonical sequence.

The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.

Residue conservation: 
The multiple alignment of the region surrounding the variant against various orthologous sequences.




Sequence annotation in neighborhood:  
The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
  • Type: the type of sequence feature.
  • Positions: endpoints of the sequence feature.
  • Description: contains additional information about the feature.

Chain 1 – 595 P2X purinoceptor 7
Topological domain 356 – 595 Cytoplasmic
Alternative sequence 129 – 595 Missing. In isoform C.
Alternative sequence 365 – 595 Missing. In isoform B, isoform E and isoform G.

Literature citations

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)

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)

A rare functional haplotype of the P2RX4 and P2RX7 genes leads to loss of innate phagocytosis and confers increased risk of age-related macular degeneration.
Gu B.J.; Baird P.N.; Vessey K.A.; Skarratt K.K.; Fletcher E.L.; Fuller S.J.; Richardson A.J.; Guymer R.H.; Wiley J.S.;
FASEB J. 27:1479-1487(2013)

Purinergic receptors P2RX4 and P2RX7 in familial multiple sclerosis.
Sadovnick A.D.; Gu B.J.; Traboulsee A.L.; Bernales C.Q.; Encarnacion M.; Yee I.M.; Criscuoli M.G.; Huang X.; Ou A.; Milligan C.J.; Petrou S.; Wiley J.S.; Vilarino-Gueell C.;
Hum. Mutat. 38:736-744(2017)
Cited for: VARIANTS ALA-76; TRP-117; LEU-125; ARG-148; ARG-150; HIS-155; MET-205; HIS-264; HIS-270; HIS-276; HIS-288; GLN-307; THR-348; SER-357; SER-361; VAL-433; ARG-460; ALA-496; GLN-521; ILE-522; VAL-535; GLN-544 AND ASN-568; CHARACTERIZATION OF VARIANTS MET-205 AND SER-361; SUBCELLULAR LOCATION; FUNCTION;

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