CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018087
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; hVDU1 
Gene Name
 USP33 
Gene Synonyms/Alias
 KIAA1097; VDU1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
227TTLFQGIKTVNPTFRubiquitination[1]
352NSEGEFDKDRDSISEubiquitination[1]
832REWESFVKGKDGDPPubiquitination[1]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 
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 717 810 DUSP 1.
 DOMAIN 818 921 DUSP 2.
 ZN_FING 59 123 UBP-type.
 ACT_SITE 194 194 Nucleophile.
 ACT_SITE 673 673 Proton acceptor (By similarity).
 MOD_RES 439 439 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton; Endocytosis; Golgi apparatus; 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
 942 AA 
Protein Sequence
MSAFRNHCPH LDSVGEITKE DLIQKSLGTC QDCKVQGPNL WACLENRCSY VGCGESQVDH 60
STIHSQETKH YLTVNLTTLR VWCYACSKEV FLDRKLGTQP SLPHVRQPHQ IQENSVQDFK 120
IPSNTTLKTP LVAVFDDLDI EADEEDELRA RGLTGLKNIG NTCYMNAALQ ALSNCPPLTQ 180
FFLDCGGLAR TDKKPAICKS YLKLMTELWH KSRPGSVVPT TLFQGIKTVN PTFRGYSQQD 240
AQEFLRCLMD LLHEELKEQV MEVEEDPQTI TTEETMEEDK SQSDVDFQSC ESCSNSDRAE 300
NENGSRCFSE DNNETTMLIQ DDENNSEMSK DWQKEKMCNK INKVNSEGEF DKDRDSISET 360
VDLNNQETVK VQIHSRASEY ITDVHSNDLS TPQILPSNEG VNPRLSASPP KSGNLWPGLA 420
PPHKKAQSAS PKRKKQHKKY RSVISDIFDG TIISSVQCLT CDRVSVTLET FQDLSLPIPG 480
KEDLAKLHSS SHPTSIVKAG SCGEAYAPQG WIAFFMEYVK RFVVSCVPSW FWGPVVTLQD 540
CLAAFFARDE LKGDNMYSCE KCKKLRNGVK FCKVQNFPEI LCIHLKRFRH ELMFSTKIST 600
HVSFPLEGLD LQPFLAKDSP AQIVTYDLLS VICHHGTASS GHYIAYCRNN LNNLWYEFDD 660
QSVTEVSEST VQNAEAYVLF YRKSSEEAQK ERRRISNLLN IMEPSLLQFY ISRQWLNKFK 720
TFAEPGPISN NDFLCIHGGV PPRKAGYIED LVLMLPQNIW DNLYSRYGGG PAVNHLYICH 780
TCQIEAEKIE KRRKTELEIF IRLNRAFQKE DSPATFYCIS MQWFREWESF VKGKDGDPPG 840
PIDNTKIAVT KCGNVMLRQG ADSGQISEET WNFLQSIYGG GPEVILRPPV VHVDPDILQA 900
EEKIEVETRS L 911 
Gene Ontology
 GO:0044297; C:cell body; IEA:Compara.
 GO:0005813; C:centrosome; IDA:UniProtKB.
 GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
 GO:0030891; C:VCB complex; TAS:UniProtKB.
 GO:0004197; F:cysteine-type endopeptidase activity; IMP:UniProtKB.
 GO:0004221; F:ubiquitin thiolesterase activity; IDA:UniProtKB.
 GO:0004843; F:ubiquitin-specific protease activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IDA:UniProtKB.
 GO:0007411; P:axon guidance; ISS:UniProtKB.
 GO:0016477; P:cell migration; ISS:UniProtKB.
 GO:0051298; P:centrosome duplication; IMP:UniProtKB.
 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; TAS:UniProtKB. 
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