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Survey
Identification
HMDB Protein ID HMDBP10114
Secondary Accession Numbers
  • 16067
Name Ubiquitin carboxyl-terminal hydrolase 33
Synonyms
  1. Deubiquitinating enzyme 33
  2. Ubiquitin thiolesterase 33
  3. Ubiquitin-specific-processing protease 33
  4. VHL-interacting deubiquitinating enzyme 1
  5. hVDU1
Gene Name USP33
Protein Type Enzyme
Biological Properties
General Function Involved in ubiquitin thiolesterase activity
Specific Function Deubiquitinating enzyme involved in various processes such as cellular migration and beta-2 adrenergic receptor/ADRB2 recycling. 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
Pathways Not Available
Reactions Not Available
GO Classification
Function
ion binding
cation binding
metal ion binding
hydrolase activity, acting on ester bonds
binding
catalytic activity
hydrolase activity
transition metal ion binding
zinc ion binding
ubiquitin thiolesterase activity
thiolester hydrolase activity
Process
metabolic process
catabolic process
macromolecule catabolic process
cellular macromolecule catabolic process
modification-dependent macromolecule catabolic process
modification-dependent protein catabolic process
ubiquitin-dependent protein catabolic process
Cellular Location
  1. Cytoplasm
  2. perinuclear region
Gene Properties
Chromosome Location Chromosome:1
Locus 1p31.1
SNPs USP33
Gene Sequence
>2829 bp
ATGACAGGATCAAATTCACACATAACGATATTAACCTTAAAGGTGTTACCTCATTTTGAA
AGTCTTGGGAAACAGGAAAAAATTCCTAACAAAATGTCAGCTTTTCGAAATCATTGTCCA
CATTTGGATTCAGTTGGTGAAATAACAAAAGAAGATTTGATACAAAAATCCCTTGGTACT
TGTCAGGATTGTAAAGTCCAAGGACCAAATCTTTGGGCATGTCTGGAGAATAGATGTTCA
TATGTTGGCTGTGGTGAATCACAAGTAGATCACAGCACCATACATTCTCAGGAGACAAAG
CATTATCTAACTGTGAACCTTACCACTCTTCGAGTATGGTGTTATGCTTGCAGCAAAGAA
GTATTTTTGGATAGGAAATTAGGAACTCAGCCTTCATTGCCTCATGTAAGACAACCTCAC
CAAATACAAGAAAACAGTGTCCAGGATTTTAAAATACCCAGTAATACAACATTAAAAACT
CCTCTGGTTGCCGTATTTGATGATCTGGATATAGAAGCGGATGAAGAAGATGAACTTAGG
GCCAGAGGTCTTACAGGTTTGAAAAATATTGGAAATACTTGTTACATGAATGCAGCTTTG
CAGGCTCTTTCTAATTGCCCACCTTTGACACAGTTTTTTCTTGATTGTGGAGGACTAGCT
CGAACAGATAAGAAACCTGCCATTTGTAAAAGTTATCTCAAACTAATGACAGAGCTGTGG
CATAAAAGCAGGCCAGGATCTGTTGTGCCTACTACTCTGTTTCAAGGAATTAAAACTGTA
AATCCAACATTTCGGGGGTATTCTCAGCAGGATGCTCAAGAATTCCTTCGATGTTTAATG
GATTTGCTTCATGAAGAATTGAAAGAGCAAGTCATGGAAGTAGAAGAAGATCCGCAAACC
ATAACCACTGAGGAGACAATGGAAGAAGACAAGAGCCAGTCGGATGTAGATTTTCAGTCT
TGTGAATCTTGTAGCAACAGTGATAGAGCAGAAAATGAAAATGGCTCTAGATGCTTTTCT
GAAGATAATAATGAAACAACAATGTTAATTCAGGATGATGAAAACAATTCAGAAATGTCA
AAGGATTGGCAAAAAGAGAAGATGTGCAATAAGATTAATAAAGTAAATTCTGAAGGCGAA
TTTGATAAAGATAGAGACTCTATATCTGAAACAGTCGACTTAAACAACCAGGAAACTGTC
AAAGTGCAAATACACAGCAGAGCTTCAGAATATATCACTGATGTCCATTCGAATGACCTG
TCTACACCACAGATCCTTCCATCAAATGAAGGTGTTAATCCACGTTTATCGGCAAGCCCT
CCTAAATCAGGCAATTTGTGGCCAGGATTGGCACCACCACACAAAAAAGCTCAGTCTGCA
TCTCCAAAGAGAAAAAAACAGCACAAGAAATACAGAAGTGTTATTTCAGACATATTTGAT
GGAACAATCATTAGTTCAGTGCAGTGTCTGACTTGTGACAGGGTGTCTGTAACCCTCGAG
ACCTTTCAAGATCTGTCCTTGCCAATTCCTGGCAAGGAAGACCTTGCTAAGCTGCATTCA
TCAAGTCATCCAACTTCTATAGTCAAAGCAGGATCATGTGGCGAAGCATATGCTCCACAA
GGGTGGATAGCTTTTTTCATGGAATATGTGAAGAGGTTTGTTGTCTCATGTGTCCCTAGC
TGGTTTTGGGGTCCAGTAGTAACCTTGCAAGATTGTCTTGCTGCCTTCTTTGCCAGAGAT
GAACTAAAAGGTGACAATATGTACAGTTGTGAAAAATGCAAAAAGTTGAGAAATGGAGTG
AAGTTTTGTAAAGTACAAAACTTTCCTGAGATTTTGTGCATCCACCTTAAAAGATTCAGA
CATGAACTAATGTTTTCCACCAAAATCAGTACCCATGTTTCATTTCCGCTAGAAGGCTTG
GATCTTCAGCCATTTCTTGCTAAGGATAGTCCAGCTCAAATTGTGACATATGATCTTCTG
TCAGTCATTTGCCATCATGGAACTGCAAGTAGTGGACACTATATAGCCTACTGCCGAAAC
AATCTAAATAATCTCTGGTATGAATTTGATGATCAGAGTGTCACTGAAGTTTCAGAATCT
ACTGTACAAAATGCAGAAGCTTACGTTCTTTTCTATAGGAAGAGCAGCGAAGAGGCACAA
AAAGAGAGGAGAAGGATATCAAATTTATTGAACATAATGGAACCAAGCCTCCTTCAGTTT
TATATTTCTCGACAGTGGCTTAATAAATTTAAGACCTTTGCCGAACCTGGCCCTATTTCA
AATAATGACTTTCTTTGTATTCATGGAGGTGTTCCTCCAAGAAAAGCTGGTTATATTGAA
GACCTGGTTTTGATGCTGCCTCAGAACATTTGGGATAACCTATATAGCAGGTATGGTGGA
GGACCAGCTGTCAACCATCTGTACATTTGTCATACTTGCCAAATTGAGGCGGAGAAAATT
GAAAAAAGAAGAAAAACTGAATTGGAAATTTTTATTCGGCTTAACAGAGCGTTCCAAAAA
GAGGACTCTCCAGCTACTTTTTATTGCATCAGTATGCAGTGGTTTAGAGAATGGGAAAGT
TTTGTGAAGGGTAAAGATGGAGATCCTCCAGGTCCTATTGACAATACTAAGATTGCAGTC
ACTAAATGTGGTAATGTGATGCTTAGGCAAGGAGCAGATTCTGGCCAGATTTCTGAAGAA
ACATGGAATTTTCTGCAGTCTATTTATGGTGGAGGGCCTGAAGTTATCCTGCGACCTCCG
GTTGTTCATGTTGATCCAGATATACTTCAAGCAGAAGAAAAAATTGAAGTAGAAACTCGG
TCTTTGTAA
Protein Properties
Number of Residues 942
Molecular Weight 106726.0
Theoretical pI 5.91
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Ubiquitin carboxyl-terminal hydrolase 33
MTGSNSHITILTLKVLPHFESLGKQEKIPNKMSAFRNHCPHLDSVGEITKEDLIQKSLGT
CQDCKVQGPNLWACLENRCSYVGCGESQVDHSTIHSQETKHYLTVNLTTLRVWCYACSKE
VFLDRKLGTQPSLPHVRQPHQIQENSVQDFKIPSNTTLKTPLVAVFDDLDIEADEEDELR
ARGLTGLKNIGNTCYMNAALQALSNCPPLTQFFLDCGGLARTDKKPAICKSYLKLMTELW
HKSRPGSVVPTTLFQGIKTVNPTFRGYSQQDAQEFLRCLMDLLHEELKEQVMEVEEDPQT
ITTEETMEEDKSQSDVDFQSCESCSNSDRAENENGSRCFSEDNNETTMLIQDDENNSEMS
KDWQKEKMCNKINKVNSEGEFDKDRDSISETVDLNNQETVKVQIHSRASEYITDVHSNDL
STPQILPSNEGVNPRLSASPPKSGNLWPGLAPPHKKAQSASPKRKKQHKKYRSVISDIFD
GTIISSVQCLTCDRVSVTLETFQDLSLPIPGKEDLAKLHSSSHPTSIVKAGSCGEAYAPQ
GWIAFFMEYVKRFVVSCVPSWFWGPVVTLQDCLAAFFARDELKGDNMYSCEKCKKLRNGV
KFCKVQNFPEILCIHLKRFRHELMFSTKISTHVSFPLEGLDLQPFLAKDSPAQIVTYDLL
SVICHHGTASSGHYIAYCRNNLNNLWYEFDDQSVTEVSESTVQNAEAYVLFYRKSSEEAQ
KERRRISNLLNIMEPSLLQFYISRQWLNKFKTFAEPGPISNNDFLCIHGGVPPRKAGYIE
DLVLMLPQNIWDNLYSRYGGGPAVNHLYICHTCQIEAEKIEKRRKTELEIFIRLNRAFQK
EDSPATFYCISMQWFREWESFVKGKDGDPPGPIDNTKIAVTKCGNVMLRQGADSGQISEE
TWNFLQSIYGGGPEVILRPPVVHVDPDILQAEEKIEVETRSL
GenBank ID Protein 42516567
UniProtKB/Swiss-Prot ID Q8TEY7
UniProtKB/Swiss-Prot Entry Name UBP33_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_015017.3
GeneCard ID USP33
GenAtlas ID USP33
HGNC ID HGNC:20059
References
General References
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  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  3. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  4. Kikuno R, Nagase T, Ishikawa K, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Jun 30;6(3):197-205. [PubMed:10470851 ]
  5. Curcio-Morelli C, Zavacki AM, Christofollete M, Gereben B, de Freitas BC, Harney JW, Li Z, Wu G, Bianco AC: Deubiquitination of type 2 iodothyronine deiodinase by von Hippel-Lindau protein-interacting deubiquitinating enzymes regulates thyroid hormone activation. J Clin Invest. 2003 Jul;112(2):189-96. [PubMed:12865408 ]
  6. Berthouze M, Venkataramanan V, Li Y, Shenoy SK: The deubiquitinases USP33 and USP20 coordinate beta2 adrenergic receptor recycling and resensitization. EMBO J. 2009 Jun 17;28(12):1684-96. doi: 10.1038/emboj.2009.128. Epub 2009 May 7. [PubMed:19424180 ]
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  8. Jeong JY, Wang Y, Sytkowski AJ: Human selenium binding protein-1 (hSP56) interacts with VDU1 in a selenium-dependent manner. Biochem Biophys Res Commun. 2009 Feb 6;379(2):583-8. doi: 10.1016/j.bbrc.2008.12.110. Epub 2008 Dec 30. [PubMed:19118533 ]
  9. Shenoy SK, Modi AS, Shukla AK, Xiao K, Berthouze M, Ahn S, Wilkinson KD, Miller WE, Lefkowitz RJ: Beta-arrestin-dependent signaling and trafficking of 7-transmembrane receptors is reciprocally regulated by the deubiquitinase USP33 and the E3 ligase Mdm2. Proc Natl Acad Sci U S A. 2009 Apr 21;106(16):6650-5. doi: 10.1073/pnas.0901083106. Epub 2009 Apr 10. [PubMed:19363159 ]
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