| Tag | Content |
|---|
| CPLM ID | CPLM-023669 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Ubiquitin carboxyl-terminal hydrolase 20 |
Protein Synonyms/Alias | Deubiquitinating enzyme 20; Ubiquitin thioesterase 20; Ubiquitin-specific-processing protease 20; VHL-interacting deubiquitinating enzyme 2; hVDU2 |
Gene Name | USP20 |
Gene Synonyms/Alias | KIAA1003; LSFR3A; VDU2 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 19 | DSIGEVTKEDLLLKS | ubiquitination | [1] | | 194 | ALCKSYQKLVSEVWH | ubiquitination | [1] | | 203 | VSEVWHKKRPSYVVP | ubiquitination | [1] | | 331 | KERMKDRKFSWGQQR | ubiquitination | [1] | | 425 | APSYVLKKAQVLSAG | ubiquitination | [1, 2] | | 487 | PGKEDLAKLHSAIYQ | ubiquitination | [1] | | 803 | IEIDTFIKLNKAFQA | ubiquitination | [1] | | 835 | WEAFVKGKDNEPPGP | ubiquitination | [1] | | 906 | ENLHGEQKIEAETRA | ubiquitination | [1, 2] |
|
Reference | [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments. Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA. Mol Cell Proteomics. 2013 Mar;12(3):825-31. [ PMID: 23266961] [2] Integrated proteomic analysis of post-translational modifications by serial enrichment. Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA. Nat Methods. 2013 Jul;10(7):634-7. [ PMID: 23749302] |
Functional Description | Deubiquitinating enzyme involved in beta-2 adrenergic receptor (ADRB2) recycling. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination beta-2 adrenergic receptor (ADRB2). Plays a central role in ADRB2 recycling and resensitization after prolonged agonist stimulation by constitutively binding ADRB2, mediating deubiquitination of ADRB2 and inhibiting lysosomal trafficking of ADRB2. Upon dissociation, it is probably transferred to the translocated beta-arrestins, possibly leading to beta-arrestins deubiquitination and disengagement from ADRB2. This suggests the existence of a dynamic exchange between the ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating thyroid hormone regulation. Deubiquitinates HIF1A, leading to stabilize HIF1A and enhance HIF1A-mediated activity. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. |
Sequence Annotation | DOMAIN 687 780 DUSP 1.
DOMAIN 789 892 DUSP 2.
ZN_FING 28 92 UBP-type.
ACT_SITE 154 154 Nucleophile.
ACT_SITE 643 643 Proton acceptor (By similarity).
MOD_RES 132 132 Phosphoserine.
MOD_RES 134 134 Phosphoserine.
MOD_RES 258 258 Phosphothreonine.
MOD_RES 377 377 Phosphothreonine.
MOD_RES 413 413 Phosphoserine. |
Keyword | Complete proteome; Cytoplasm; Cytoskeleton; Endocytosis; Hydrolase; Metal-binding; Phosphoprotein; Polymorphism; Protease; Reference proteome; Repeat; Thiol protease; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 914 AA |
Protein Sequence | MGDSRDLCPH LDSIGEVTKE DLLLKSKGTC QSCGVTGPNL WACLQVACPY VGCGESFADH 60
STIHAQAKKH NLTVNLTTFR LWCYACEKEV FLEQRLAAPL LGSSSKFSEQ DSPPPSHPLK 120
AVPIAVADEG ESESEDDDLK PRGLTGMKNL GNSCYMNAAL QALSNCPPLT QFFLECGGLV 180
RTDKKPALCK SYQKLVSEVW HKKRPSYVVP TSLSHGIKLV NPMFRGYAQQ DTQEFLRCLM 240
DQLHEELKEP VVATVALTEA RDSDSSDTDE KREGDRSPSE DEFLSCDSSS DRGEGDGQGR 300
GGGSSQAETE LLIPDEAGRA ISEKERMKDR KFSWGQQRTN SEQVDEDADV DTAMAALDDQ 360
PAEAQPPSPR SSSPCRTPEP DNDAHLRSSS RPCSPVHHHE GHAKLSSSPP RASPVRMAPS 420
YVLKKAQVLS AGSRRRKEQR YRSVISDIFD GSILSLVQCL TCDRVSTTVE TFQDLSLPIP 480
GKEDLAKLHS AIYQNVPAKP GACGDSYAAQ GWLAFIVEYI RRFVVSCTPS WFWGPVVTLE 540
DCLAAFFAAD ELKGDNMYSC ERCKKLRNGV KYCKVLRLPE ILCIHLKRFR HEVMYSFKIN 600
SHVSFPLEGL DLRPFLAKEC TSQITTYDLL SVICHHGTAG SGHYIAYCQN VINGQWYEFD 660
DQYVTEVHET VVQNAEGYVL FYRKSSEEAM RERQQVVSLA AMREPSLLRF YVSREWLNKF 720
NTFAEPGPIT NQTFLCSHGG IPPHKYHYID DLVVILPQNV WEHLYNRFGG GPAVNHLYVC 780
SICQVEIEAL AKRRRIEIDT FIKLNKAFQA EESPGVIYCI SMQWFREWEA FVKGKDNEPP 840
GPIDNSRIAQ VKGSGHVQLK QGADYGQISE ETWTYLNSLY GGGPEIAIRQ SVAQPLGPEN 900
LHGEQKIEAE TRAV 914 |
Gene Ontology | GO:0005813; C:centrosome; IDA:UniProtKB. GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. GO:0004197; F:cysteine-type endopeptidase activity; IMP:UniProtKB. GO:0004221; F:ubiquitin thiolesterase activity; IDA:UniProtKB. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0006897; P:endocytosis; IEA:UniProtKB-KW. GO:0071108; P:protein K48-linked deubiquitination; IDA:UniProtKB. GO:0070536; P:protein K63-linked deubiquitination; IDA:UniProtKB. GO:0008277; P:regulation of G-protein coupled receptor protein signaling pathway; IMP:UniProtKB. GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. |
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PROSITE | |
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