Tag | Content |
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CPLM ID | CPLM-023425 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Ubiquitin thioesterase OTU1 |
Protein Synonyms/Alias | |
Gene Name | CG4603 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Drosophila melanogaster (Fruit fly) |
NCBI Taxa ID | 7227 |
Lysine Modification | Position | Peptide | Type | References |
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314 | RQYTNVDKFTLRCMQ | acetylation | [1] |
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Reference | [1] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation. Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C. Sci Signal. 2011 Jul 26;4(183):ra48. [ PMID: 21791702] |
Functional Description | Hydrolase that can remove conjugated ubiquitin from proteins and may therefore play an important regulatory role at the level of protein turnover by preventing degradation (By similarity). |
Sequence Annotation | DOMAIN 5 87 Ubiquitin-like. DOMAIN 150 274 OTU. ZN_FING 317 341 C2H2-type. ACT_SITE 158 158 By similarity. ACT_SITE 161 161 Nucleophile (By similarity). ACT_SITE 341 341 By similarity. |
Keyword | Complete proteome; Hydrolase; Metal-binding; Protease; Reference proteome; Thiol protease; Ubl conjugation pathway; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 347 AA |
Protein Sequence | MTGSFSVKLK SKKGQFIVND LNEHTTLGEL KTKIVQATDI EATQLHVLVG YPPKPLDLSQ 60 QQEQRALKAV GINSGETLIV EEKAAPAPAA PVPGGTTVED DEALARRLQA EEEAQLLQET 120 AGGPVAQAAD YQLPVAPTES GPNGDFNGIL LKKVVPADNS CLFTSIRFVL NGKVDNEGSE 180 MMRHIIAQEV AADPQSYNDA VLGKSNAEYC AWIQKADSWG GAIEVSILSN YYGIEIDVVD 240 IQNAIINRFG EDKNFGLRVF LLFDGIHYDP LYMETSPSAA PATIFPVEEL GVYQQAEQLA 300 NEAQSSRQYT NVDKFTLRCM QCDVRLVGQV QAQEHAKQTG HKNFGEI 347 |
Gene Ontology | GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW. GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. GO:0006520; P:cellular amino acid metabolic process; ISS:UniProtKB. GO:0006508; P:proteolysis; IEA:UniProtKB-KW. |
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PRINTS | |