Variant position: 95 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 806 The length of the canonical sequence.
Location on the 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.
Human DTCSDEKIRMNRVVRNNLRV RLGDVISIQPCPDVKYGKRIH
Mouse DTCSDEKIRMNRVVRNNLRV RLGDVISIQPCPDVKYGKRIH
Rat DTCSDEKIRMNRVVRNNLRV RLGDVISIQPCPDVKYGKRIH
Pig DTCSDEKIRMNRVVRNNLRV HLGDVISIQPCPDVKYGKRIH
Bovine DTCSDEKIRMNRVVRNNLRV HLGDVISIQPCPDVKYGKRIH
Xenopus laevis DTCSDEKIRMNRVVRNNLRV RLGDVISIQPCPDVKYGKRVH
Xenopus tropicalis DTCSDEKIRMNRVVRNNLRV RLGDVISIQPCPDVKYGKRIH
Zebrafish DTCSDEKVRMNRVVRNNLRV RLGDVISIQPCPDVKYGKRIH
Drosophila DTCPDEKIRMNRVVRNNLCV HLSDVVSVQSCPDVKYGKRVR
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
2 – 806 Transitional endoplasmic reticulum ATPase
86 – 86 R -> A. Strongly increased affinity for ATP. Strongly reduced affinity for ADP.
110 – 110 Y -> A. Abolishes interaction with NPLOC4; when associated with 52-A--A-55.
93 – 95
Endolysosomal sorting of ubiquitylated caveolin-1 is regulated by VCP and UBXD1 and impaired by VCP disease mutations.
Ritz D.; Vuk M.; Kirchner P.; Bug M.; Schuetz S.; Hayer A.; Bremer S.; Lusk C.; Baloh R.H.; Lee H.; Glatter T.; Gstaiger M.; Aebersold R.; Weihl C.C.; Meyer H.;
Nat. Cell Biol. 13:1116-1123(2011)
Cited for: FUNCTION; INTERACTION WITH CAV1 AND UBXN6; CHARACTERIZATION OF VARIANTS IBMPFD1 GLY-95; HIS-155 AND GLU-232; MUTAGENESIS OF GLU-578;
A novel ATP-dependent conformation in p97 N-D1 fragment revealed by crystal structures of disease-related mutants.
Tang W.K.; Li D.; Li C.C.; Esser L.; Dai R.; Guo L.; Xia D.;
EMBO J. 29:2217-2229(2010)
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-481 IN COMPLEX WITH ATP ANALOG; CHARACTERIZATION OF VARIANTS IBMPFD1 GLY-95 AND HIS-155; MUTAGENESIS OF ARG-53 AND ARG-86; SUBUNIT;
Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein.
Watts G.D.J.; Wymer J.; Kovach M.J.; Mehta S.G.; Mumm S.; Darvish D.; Pestronk A.; Whyte M.P.; Kimonis V.E.;
Nat. Genet. 36:377-381(2004)
Cited for: VARIANTS IBMPFD1 GLY-95; CYS-155; HIS-155; PRO-155; GLN-191 AND GLU-232;
Inclusion body myopathy-associated mutations in p97/VCP impair endoplasmic reticulum-associated degradation.
Weihl C.C.; Dalal S.; Pestronk A.; Hanson P.I.;
Hum. Mol. Genet. 15:189-199(2006)
Cited for: CHARACTERIZATION OF VARIANTS IBMPFD1 GLY-95 AND HIS-155;
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