Variant position: 488 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 1014 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 SLQELFLAHILSPWGAEVKA EPVEVVAPRGKSGAALSKKSK
Mouse SLQDLLSAHSLSPWGAEVKA EPGEVVAPRGKS-AAPSKKSK
Rat SLQELLSAHSLSSWGAEVKV EPGEVVVPKGKS-AAPSKKSK
Bovine SLQELLSTHLLSPWGAEVKV EPVEAVGPKGKSGAAPSKKSK
Chicken GFQELLSLHAISPWGAEVKT EHQEVAV-DGKCSKPANMKSA
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 – 1014 Poly [ADP-ribose] polymerase 1
373 – 524 Automodification domain
471 – 471 PolyADP-ribosyl glutamic acid
484 – 484 PolyADP-ribosyl glutamic acid
488 – 488 PolyADP-ribosyl glutamic acid
491 – 491 PolyADP-ribosyl glutamic acid
499 – 499 ADP-ribosylserine
507 – 507 ADP-ribosylserine
486 – 486 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)
486 – 486 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
499 – 499 S -> A. Abolishes automodification on serine following interaction with HPF1; when associated with A-507 and A-519.
507 – 507 S -> A. Abolishes automodification on serine following interaction with HPF1; when associated with A-499 and A-519.
The consensus coding sequences of human breast and colorectal cancers.
Sjoeblom T.; Jones S.; Wood L.D.; Parsons D.W.; Lin J.; Barber T.D.; Mandelker D.; Leary R.J.; Ptak J.; Silliman N.; Szabo S.; Buckhaults P.; Farrell C.; Meeh P.; Markowitz S.D.; Willis J.; Dawson D.; Willson J.K.V.; Gazdar A.F.; Hartigan J.; Wu L.; Liu C.; Parmigiani G.; Park B.H.; Bachman K.E.; Papadopoulos N.; Vogelstein B.; Kinzler K.W.; Velculescu V.E.;
Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-488;
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