CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017895
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ubiquitin carboxyl-terminal hydrolase 33 
Protein Synonyms/Alias
 Deubiquitinating enzyme 33; Ubiquitin thioesterase 33; Ubiquitin-specific-processing protease 33; VHL-interacting deubiquitinating enzyme 1 
Gene Name
 Usp33 
Gene Synonyms/Alias
 Vdu1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
34LGACQDCKVRGPNLWubiquitination[1]
227ANLFQGIKTVNPTFRubiquitination[1]
342KVCNKINKANADVELubiquitination[1]
849NTKIAVTKCGSVMLKubiquitination[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
 Deubiquitinating enzyme involved in various processes such as centrosome duplication, cellular migration and beta-2 adrenergic receptor/ADRB2 recycling. Involved in regulation of centrosome duplication by mediating deubiquitination of CCP110 in S and G2/M phase, leading to stabilize CCP110 during the period which centrioles duplicate and elongate. Involved in cell migration via its interaction with intracellular domain of ROBO1, leading to regulate the Slit signaling. Plays a role in commissural axon guidance cross the ventral midline of the neural tube in a Slit-dependent manner, possibly by mediating the deubiquitination of ROBO1. Acts as a regulator of G-protein coupled receptor (GPCR) signaling by mediating the deubiquitination of beta-arrestins (ARRB1 and ARRB2) and 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, 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. Mediates deubiquitination of both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. 
Sequence Annotation
 DOMAIN 684 777 DUSP 1.
 DOMAIN 785 888 DUSP 2.
 ZN_FING 28 92 UBP-type.
 ACT_SITE 163 163 Nucleophile (By similarity).
 ACT_SITE 640 640 Proton acceptor (By similarity).
 MOD_RES 407 407 Phosphoserine (By similarity).  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton; Endocytosis; Hydrolase; Metal-binding; Phosphoprotein; Protease; Reference proteome; Repeat; Thiol protease; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 909 AA 
Protein Sequence
MTTFRNHCPH LDSVGEITKE DLIQKSLGAC QDCKVRGPNL WACLENRCSY VGCGESQVDH 60
STIHSQETKH YLTVNLTTLR VWCYACSKEV FLDRKLGTPP SLPHVRQPQQ TQENSVQDFK 120
IPSNPALKTP MVAVSEDLDI EVEEEDELKA RGLTGLKNIG NTCYMNAALQ ALSNCPPLTQ 180
FFLDCGGLAR TDKKPAICKS YLKLMTELWH KSRPGSVVPA NLFQGIKTVN PTFRGYSQQD 240
AQEFLRCLMD LLHEELKEQV MEMEEEPQTL TSEETVEEEK SQSDVDFQSC ESCSSSEKAE 300
NESGSKGFPE DSNETTMLIQ DEDDLEMAKD WQKEKVCNKI NKANADVELD KDRDTVCETV 360
DLNSQETVKV QIHGRASESI TDVHLNDLAT SQILPSNESV SPRLSASPPK LGSLWPGLSP 420
PHKKAQSTSA KRKKQHKKYR SVISDIFDGT VISSVQCLTC DRVSITLETF QDLSLPIPGK 480
EDLAKLHSSS HPTIVKAGSC GEAYAPQGWI AFFMEYVKRF VVSCVPSWFW GPVVTLQDCL 540
AAFFARDELK GDNMYSCEKC KKLRNGVKFC KVQKFPEILC IHLKRFRHEL MFSTKISTHV 600
SFPLEGLDLQ PFLAKDSPAQ IVTYDLLSVI CHHGTASSGH YIAYCRNNLN NLWYEFDDQS 660
VTEVSESTVQ NAEAYVLFYR KSSEEAQKER RRISNLLNIM EPSLLQFYIS RQWLNKFKTF 720
AEPGPISNND FLCIHGGIPP RKASYIEDLV LMLPQNIWDN LYSRYGGGPA VNHLYICHTC 780
QIELEKIEKR RKTELEIFIR LNRAFQEEDS PATFYCISMQ WFREWESFVK GKDGDPPGPI 840
DNTKIAVTKC GSVMLKQGAD SGQISEETWN FLQSIYGGGP EVILRPPVVH VDPDVLQAEE 900
KIEVETRSL 909 
Gene Ontology
 GO:0044297; C:cell body; IDA:MGI.
 GO:0005813; C:centrosome; ISS:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
 GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
 GO:0004221; F:ubiquitin thiolesterase activity; ISS:UniProtKB.
 GO:0004843; F:ubiquitin-specific protease activity; ISS:UniProtKB.
 GO:0008270; F:zinc ion binding; ISS:UniProtKB.
 GO:0007411; P:axon guidance; IMP:UniProtKB.
 GO:0016477; P:cell migration; IMP:UniProtKB.
 GO:0051298; P:centrosome duplication; ISS:UniProtKB.
 GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
 GO:0071108; P:protein K48-linked deubiquitination; ISS:UniProtKB.
 GO:0070536; P:protein K63-linked deubiquitination; ISS:UniProtKB.
 GO:0008277; P:regulation of G-protein coupled receptor protein signaling pathway; ISS:UniProtKB.
 GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. 
Interpro
 IPR006615; Pept_C19_DUSP.
 IPR018200; Pept_C19ubi-hydrolase_C_CS.
 IPR001394; Peptidase_C19.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR001607; Znf_UBP. 
Pfam
 PF06337; DUSP
 PF00443; UCH
 PF02148; zf-UBP 
SMART
 SM00695; DUSP 
PROSITE
 PS51283; DUSP
 PS00972; UCH_2_1
 PS00973; UCH_2_2
 PS50235; UCH_2_3
 PS50271; ZF_UBP 
PRINTS