| Tag | Content |
|---|
| CPLM ID | CPLM-006008 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Poly [ADP-ribose] polymerase 1 |
Protein Synonyms/Alias | PARP-1; ADP-ribosyltransferase diphtheria toxin-like 1; ARTD1; NAD(+) ADP-ribosyltransferase 1; ADPRT 1; Poly[ADP-ribose] synthase 1 |
Gene Name | parp1 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Xenopus laevis (African clawed frog) |
NCBI Taxa ID | 8355 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 469 | SSWGAEIKQEAVQPT | sumoylation | [1] |
|
Reference | [1] PIASy mediates SUMO-2/3 conjugation of poly(ADP-ribose) polymerase 1 (PARP1) on mitotic chromosomes. Ryu H, Al-Ani G, Deckert K, Kirkpatrick D, Gygi SP, Dasso M, Azuma Y. J Biol Chem. 2010 May 7;285(19):14415-23. [ PMID: 20228053] |
Functional Description | Poly[ADP-ribose] polymerase modifies various nuclear proteins by poly(ADP-ribosyl)ation. The modification is dependent on DNA and is involved in the regulation of various important cellular processes such as differentiation, proliferation, and tumor transformation and also in the regulation of the molecular events involved in the recovery of cell from DNA damage. |
Sequence Annotation | DOMAIN 369 460 BRCT.
DOMAIN 645 762 PARP alpha-helical.
DOMAIN 771 997 PARP catalytic.
DNA_BIND <1 356
ZN_FING <1 78 PARP-type 1.
ZN_FING 99 189 PARP-type 2.
REGION 357 507 Automodification domain.
MOTIF 193 195 Nuclear localization signal.
MOTIF 207 212 Nuclear localization signal.
MOD_RES 391 391 PolyADP-ribosyl glutamic acid
MOD_RES 397 397 PolyADP-ribosyl glutamic acid
MOD_RES 419 419 PolyADP-ribosyl glutamic acid
MOD_RES 428 428 PolyADP-ribosyl glutamic acid
MOD_RES 429 429 PolyADP-ribosyl glutamic acid
MOD_RES 445 445 PolyADP-ribosyl glutamic acid
MOD_RES 447 447 PolyADP-ribosyl glutamic acid
MOD_RES 454 454 PolyADP-ribosyl glutamic acid
MOD_RES 467 467 PolyADP-ribosyl glutamic acid
MOD_RES 471 471 PolyADP-ribosyl glutamic acid
MOD_RES 477 477 PolyADP-ribosyl glutamic acid
MOD_RES 495 495 PolyADP-ribosyl glutamic acid
MOD_RES 496 496 PolyADP-ribosyl glutamic acid
MOD_RES 503 503 PolyADP-ribosyl glutamic acid |
Keyword | ADP-ribosylation; DNA-binding; Glycosyltransferase; Metal-binding; NAD; Nucleus; Repeat; Transferase; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 998 AA |
Protein Sequence | AKSGRASCKK CGDNIAKESL GLAIMVQSPM FDGKVPHWHH YSCFWKRARV LSQGDIYGYT 60
ELRWEDQEMI KKAIETGGAA AGAGGDSKGG KGEMTLNDFA AEYAKSNRSA CKGCEQKIEK 120
GQIRISKKSV DVERPQLGMI DRWYHPDCFV SSREELDFLP SYSASQLKGF TILSAEDKDS 180
LKKKLPAVKN EGKRKADEVD GHSAATKKKI KKEKEKESKL EKLLKEQTEL IWHIKDELKK 240
VCSTNDLKEL LIANKQQVPS GETNIVDRVS DGMAFGALLP CEECSGQFVF KGDAYYCTGD 300
LSAWTKCVAK TQTPNRKDWV TPKEFHEIPY LKKFKFKRHD RAFPPCAAPT PISPPAAPEP 360
KPTVEETFPE GKPLTNTKVL LIGKLSKNKD EVKTLIEGLG GKVAGSAHKA NLCISTNKEV 420
KKMSKKMEEV KAANVRVVSD DFLKEVESGK SVQELLSQFG ISSWGAEIKQ EAVQPTEKQP 480
SSGPVAGKSS GKVKEEKGSN KSEKKMKLTV KGGAAIDPDS ELEDSCHVLE TGGKIFSATL 540
GLVDITRGTN SYYKLQLIEH DRDSRYWVFR SWGRVGTVIG SKKLEEMSSK EDAIEHFLNL 600
YQDKTGNAWH SPNFTKYPKK FYPLEIDYGQ EEDVVKKLSV GAGTKSKLAK PVQELIKLIF 660
DVESMKKAMV EFEIDLQKMP LGKLSKRQIQ SAYSILSQVQ QAVSESLSEA RLLDLSNQFY 720
TLIPHDFGMK KPPLLNNLEY IQAKVQMLDN LLDIEVAYSL LRGGADDGEK DPIDVKYEKI 780
KTDIKVVAKD SEESRIICDY VKNTHADTHN AYDLEVLEIF KIDREGEYQR YKPFKQLHNR 840
QLLWHGSRTT NFAGILSQGL RIAPPEAPVT GYMFGKGIYF ADMVSKSANY CHAMPGSPIG 900
LILLGEVALG NMHELKAASQ ITKLPKGKHS VKGLGRTAPD PSATVQLDGV DVPLGKGTSA 960
NISDTSLLYN EYIVYDIAQV NLKYLLKLKF NYKGGMMW 998 |
Gene Ontology | |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |