Sequence information
Variant position: 64 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 531 The length of the canonical sequence.
Location on the sequence:
GTGKEGQPREYYTLDSILFL
L NNVHLSHPVYVRRAATENIP
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.
Human GTGK--EGQPREYYTLDSILFLL NNVHLSHPVYVRRAATENIP
Mouse GTGK--EGQPREYYTLDSILFLL NNVHLSHPVYVRRAATEN
Rat GTGK--EGQPREYYTLDSILFLL NNVHLSHPVYVRRAATEN
Chicken GTGK--EGQPREYYTLDSILFLL NNVHLSHPVYVRRAATEN
Caenorhabditis elegans G-------KSDEFYSLESLVVFL KYSHENHGVYVKEAAAAG
Baker's yeast EETE--IEIDGSLVQLRIIVHCW MNKDSSAADYLADCQNKQ
Fission yeast EPTKFIKLENDSHFSLRSVYFAW LLRDTSIAEYIQQCSELG
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.
Literature citations
The parafibromin tumor suppressor protein is part of a human Paf1 complex.
Rozenblatt-Rosen O.; Hughes C.M.; Nannepaga S.J.; Shanmugam K.S.; Copeland T.D.; Guszczynski T.; Resau J.H.; Meyerson M.;
Mol. Cell. Biol. 25:612-620(2005)
Cited for: FUNCTION; INTERACTION WITH PAF1; LEO1 AND POLR2A; INTERACTION WITH SET1-LIKE COMPLEX; SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANT HRPT1 PRO-64;
HRPT2, encoding parafibromin, is mutated in hyperparathyroidism-jaw tumor syndrome.
Carpten J.D.; Robbins C.M.; Villablanca A.; Forsberg L.; Presciuttini S.; Bailey-Wilson J.; Simonds W.F.; Gillanders E.M.; Kennedy A.M.; Chen J.D.; Agarwal S.K.; Sood R.; Jones M.P.; Moses T.Y.; Haven C.; Petillo D.; Leotlela P.D.; Harding B.; Cameron D.; Pannett A.A.; Hoeoeg A.; Heath H. III; James-Newton L.A.; Robinson B.; Zarbo R.J.; Cavaco B.M.; Wassif W.; Perrier N.D.; Rosen I.B.; Kristoffersson U.; Turnpenny P.D.; Farnebo L.-O.; Besser G.M.; Jackson C.E.; Morreau H.; Trent J.M.; Thakker R.V.; Marx S.J.; Teh B.T.; Larsson C.; Hobbs M.R.;
Nat. Genet. 32:676-680(2002)
Cited for: INVOLVEMENT IN HRPT2; INVOLVEMENT IN HRPT1; VARIANT HRPT1 PRO-64;
HRPT2 mutations are associated with malignancy in sporadic parathyroid tumours.
Howell V.M.; Haven C.J.; Kahnoski K.; Khoo S.K.; Petillo D.; Chen J.; Fleuren G.J.; Robinson B.G.; Delbridge L.W.; Philips J.; Nelson A.E.; Krause U.; Hammje K.; Dralle H.; Hoang-Vu C.; Gimm O.; Marsh D.J.; Morreau H.; Teh B.T.;
J. Med. Genet. 40:657-663(2003)
Cited for: VARIANT HRPT1 PRO-64;
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.