Sequence information
Variant position: 144 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 1689 The length of the canonical sequence.
Location on the sequence:
KSYYKPDSPEYKAACKLWDL
Y LRTRNEFVQKGEADDEDDDE
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 KSYYKPDSPEYKAACKLWDLY LRTRNEFVQKGEADDEDDDE
Mouse KAYYKPDSPEYKAACKLWDLY LRTRNEFVQKGEADDEDDDE
Pig ----------------LW--- --------------------
Chicken KAYYKPDSPEYKAACKLWELY LRTKNEFVQKGDAEEEDEDE
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.
Type Positions Description
Chain
1 – 1689
Protein polybromo-1
Modified residue
131 – 131
Phosphoserine
Modified residue
134 – 134
Phosphotyrosine
Cross
154 – 154
Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Helix
132 – 152
Literature citations
Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma.
Varela I.; Tarpey P.; Raine K.; Huang D.; Ong C.K.; Stephens P.; Davies H.; Jones D.; Lin M.L.; Teague J.; Bignell G.; Butler A.; Cho J.; Dalgliesh G.L.; Galappaththige D.; Greenman C.; Hardy C.; Jia M.; Latimer C.; Lau K.W.; Marshall J.; McLaren S.; Menzies A.; Mudie L.; Stebbings L.; Largaespada D.A.; Wessels L.F.A.; Richard S.; Kahnoski R.J.; Anema J.; Tuveson D.A.; Perez-Mancera P.A.; Mustonen V.; Fischer A.; Adams D.J.; Rust A.; Chan-On W.; Subimerb C.; Dykema K.; Furge K.; Campbell P.J.; Teh B.T.; Stratton M.R.; Futreal P.A.;
Nature 469:539-542(2011)
Cited for: FUNCTION AS NEGATIVE REGULATOR OF CELL PROLIFERATION; INVOLVEMENT IN RCC; VARIANTS LEU-49; ALA-56; ILE-57 DEL; GLY-66; GLU-90; PHE-144; ALA-160; CYS-202; LYS-206; GLY-226; VAL-228; PRO-232; THR-233; THR-256; ALA-340; ILE-523; SER-540; ASP-597; GLU-621; ASN-661; GLU-674; CYS-678; CYS-893; SER-895; GLN-922; GLN-925; TYR-1079; SER-1098; GLN-1120; SER-1177; PRO-1204; 1209-MET--GLU-1214 DEL; GLN-1287; GLU-1414; CYS-1503; HIS-1560; ASN-1614 AND CYS-1647;
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.