| Tag | Content |
|---|
| CPLM ID | CPLM-018480 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Ubiquitin carboxyl-terminal hydrolase 3 |
Protein Synonyms/Alias | Deubiquitinating enzyme 3; Ubiquitin thioesterase 3; Ubiquitin-specific-processing protease 3 |
Gene Name | Usp3 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 135 | ADRHRKRKLLENSSL | ubiquitination | [1] | | 145 | ENSSLNSKLLKVNGS | ubiquitination | [1] | | 423 | WTAYLRNKVDTYVQF | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | Hydrolase that deubiquitinates monoubiquitinated target proteins such as histone H2A and H2B. Required for proper progression through S phase and subsequent mitotic entry. May regulate the DNA damage response (DDR) checkpoint through deubiquitination of H2A at DNA damage sites. Associates with the chromatin (By similarity). |
Sequence Annotation | ZN_FING 27 104 UBP-type.
ACT_SITE 168 168 Nucleophile (By similarity).
ACT_SITE 471 471 Proton acceptor (By similarity).
MOD_RES 1 1 N-acetylmethionine (By similarity). |
Keyword | Acetylation; Cell cycle; Chromatin regulator; Complete proteome; DNA damage; Hydrolase; Metal-binding; Nucleus; Protease; Reference proteome; Thiol protease; Ubl conjugation pathway; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 520 AA |
Protein Sequence | MECPHLSSSV CIAPDSAKFP NGSPSSWCCS VCRSNKSPWV CLTCSSVHCG RYVNGHAKKH 60
YEDAQIPLLN HKRSEKQEKA QHTVCMDCSS YSTYCYRCDD FVVNDTKLGL VQKVREHLQN 120
LENSAFTADR HRKRKLLENS SLNSKLLKVN GSTTAICATG LRNLGNTCFM NAILQSLSNI 180
EQFCCYFKEL PAVELRNGKT AGRRTYHTRS QGDSNVSLVE EFRKTLCALW QGSQTAFSPE 240
SLFYVVWKIM PNFRGYQQQD AHEFMRYLLD HLHLELQGGF NGVSRSAILQ ENSTLSASNK 300
CCINGASTVV TAIFGGILQN EVNCLICGTE SRKFDPFLDL SLDIPSQFRS KRSKNQENGP 360
VCSLRDCLRS FTDLEELDET ELYMCHKCKK KQKSTKKFWI QKLPKALCLH LKRFHWTAYL 420
RNKVDTYVQF PLRGLDMKCY LLEPENSGPD SCLYDLAAVV VHHGSGVGSG HYTAYAVHEG 480
RWFHFNDSTV TVTDEETVGK AKAYILFYVE RQARAGAEKL 520 |
Gene Ontology | GO:0000790; C:nuclear chromatin; IEA:Compara. GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW. GO:0004221; F:ubiquitin thiolesterase activity; IEA:InterPro. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0006281; P:DNA repair; IEA:Compara. GO:0016578; P:histone deubiquitination; IEA:Compara. GO:0000278; P:mitotic cell cycle; IEA:Compara. GO:0031647; P:regulation of protein stability; IEA:Compara. GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |