Tag | Content |
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CPLM ID | CPLM-014184 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | ADP-ribose pyrophosphatase, mitochondrial |
Protein Synonyms/Alias | ADP-ribose diphosphatase; ADP-ribose phosphohydrolase; Adenosine diphosphoribose pyrophosphatase; ADPR-PPase; Nucleoside diphosphate-linked moiety X motif 9; Nudix motif 9 |
Gene Name | Nudt9 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
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310 | GDDAGKVKWVDISDQ | acetylation | [1] | 319 | VDISDQLKLYASHSQ | acetylation | [1] |
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Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | Hydrolyzes ADP-ribose (ADPR) to AMP and ribose 5'- phosphate. |
Sequence Annotation | DOMAIN 178 334 Nudix hydrolase. MOTIF 215 237 Nudix box. MOD_RES 121 121 Phosphoserine (By similarity). |
Keyword | Complete proteome; Hydrolase; Magnesium; Manganese; Mitochondrion; Phosphoprotein; Reference proteome; Transit peptide. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 350 AA |
Protein Sequence | MAGRSLGKAV ATVSLSVALA SVTVRSSGCR AIPAPRNPFP SCGFHLKANI MSGSNGVKDN 60 SHNKARTSPY PGSKVERSKV PNEKVGWLVE WQDYNPVEYT AVSVLAGPQW ADPQISESSF 120 SPRFNEKDGH VERKSQNGLY EIENGRPRNP AGRTGLVGRG LLGRWGPNHA ADPIITRWKR 180 DESGNKITHP VSGKCILQFV AIKRKDCGEW AIPGGMVDPG EKISATLKRE FGEEALNSLQ 240 KSSAEKREIE EKLHALFSQE HLVIYKGYVD DPRNTDNAWM ETEAVNYHDE TGETMDNLTL 300 EAGDDAGKVK WVDISDQLKL YASHSQFIKL VAEKRDAHWS EDCAADSHGL 350 |
Gene Ontology | GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. GO:0043262; F:adenosine-diphosphatase activity; IEA:Compara. GO:0047631; F:ADP-ribose diphosphatase activity; IEA:EC. GO:0046032; P:ADP catabolic process; IEA:Compara. GO:0046709; P:IDP catabolic process; IEA:Compara. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |