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Identification
HMDB Protein ID HMDBP10115
Secondary Accession Numbers
  • 16068
Name Ubiquitin carboxyl-terminal hydrolase 22
Synonyms
  1. Deubiquitinating enzyme 22
  2. Ubiquitin thiolesterase 22
  3. Ubiquitin-specific-processing protease 22
Gene Name USP22
Protein Type Enzyme
Biological Properties
General Function Involved in ubiquitin thiolesterase activity
Specific Function Histone deubiquitinating component of the transcription regulatory histone acetylation (HAT) complex SAGA. Catalyzes the deubiquitination of both histones H2A and H2B, thereby acting as a coactivator. Recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Required for nuclear receptor-mediated transactivation and cell cycle progression
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. Nucleus (Probable)
Gene Properties
Chromosome Location Chromosome:1
Locus 17p11.2
SNPs USP22
Gene Sequence
>1578 bp
ATGGTGTCCCGGCCAGAGCCCGAGGGCGAGGCCATGGACGCCGAGCTGGCGGTAGCGCCG
CCGGGCTGCTCGCACCTGGGCAGCTTCAAGGTGGACAACTGGAAGCAGAACCTGCGGGCC
ATCTACCAGTGCTTCGTGTGGAGCGGCACGGCTGAGGCCCGCAAGCGCAAGGCCAAGTCC
TGTATCTGCCATGTCTGTGGCGTCCACCTCAACAGGCTGCATTCCTGCCTCTACTGTGTC
TTCTTCGGCTGTTTCACAAAGAAGCATATTCACGAGCATGCGAAGGCGAAGCGGCACAAC
CTGGCCATTGATCTGATGTACGGAGGCATCTACTGTTTTCTGTGCCAGGACTACATCTAT
GACAAAGACATGGAAATAATCGCCAAGGAGGAGCAGCGAAAAGCTTGGAAAATGCAAGGC
GTTGGAGAGAAGTTTTCAACTTGGGAACCAACCAAACGGGAGCTTGAACTGCTGAAGCAC
AACCCGAAAAGGAGAAAGATCACCTCGAACTGCACCATAGGTCTGCGTGGGCTGATCAAC
CTTGGGAACACATGCTTCATGAACTGCATCGTGCAGGCCCTGACCCACACGCCACTTCTG
CGGGACTTCTTCCTGTCTGACAGGCACCGCTGTGAGATGCAGAGCCCCAGCTCCTGTCTG
GTCTGTGAGATGTCCTCACTGTTTCAGGAGTTTTACTCTGGACACCGGTCCCCTCACATC
CCGTATAAGTTGCTGCACCTGGTGTGGACCCACGCGAGGCACCTAGCAGGCTACGAGCAG
CAGGACGCCCACGAGTTCCTCATCGCGGCCCTGGACGTGCTCCACCGACACTGCAAAGGT
GATGACAATGGGAAGAAGGCCAACAACCCCAACCACTGCAACTGCATCATAGACCAGATC
TTCACAGGCGGGTTGCAGTCAGACGTCACCTGCCAAGTCTGCCATGGAGTCTCCACCACC
ATCGACCCCTTCTGGGACATCAGCTTGGATCTCCCCGGCTCTTCCACCCCATTCTGGCCC
CTGAGCCCAGGGAGCGAGGGCAACGTGGTAAACGGGGAAAGCCACGTGTCGGGAACCACC
ACGCTCACGGACTGCCTGCGACGATTCACCAGACCAGAGCACTTGGGCAGCAGCGCCAAG
ATCAAGTGCAGCGGTTGCCATAGCTACCAGGAGTCCACAAAGCAGCTCACTATGAAGAAA
CTGCCCATCGTAGCCTGTTTTCATCTCAAACGATTTGAACACTCAGCCAAGCTGCGGCGG
AAGATCACCACGTATGTGTCCTTCCCCCTGGAGCTGGACATGACCCCTTTCATGGCCTCC
AGCAAAGAGAGCAGGATGAATGGACAGTACCAGCAGCCCACGGACAGTCTCAACAATGAC
AACAAGTATTCCCTGTTTGCTGTTGTTAACCATCAAGGGACCTTGGAGAGTGGCCACTAC
ACCAGCTTTATCCGGCAGCACAAAGACCAGTGGTTCAAGTGTGACGATGCCATCATCACC
AAGGCCAGCATCAAGGACGTCCTGGACAGCGAAGGGTACTTGCTGTTCTATCACAAACAG
TTCCTGGAATACGAGTAG
Protein Properties
Number of Residues 525
Molecular Weight 59960.1
Theoretical pI 8.09
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Ubiquitin carboxyl-terminal hydrolase 22
MVSRPEPEGEAMDAELAVAPPGCSHLGSFKVDNWKQNLRAIYQCFVWSGTAEARKRKAKS
CICHVCGVHLNRLHSCLYCVFFGCFTKKHIHEHAKAKRHNLAIDLMYGGIYCFLCQDYIY
DKDMEIIAKEEQRKAWKMQGVGEKFSTWEPTKRELELLKHNPKRRKITSNCTIGLRGLIN
LGNTCFMNCIVQALTHTPLLRDFFLSDRHRCEMQSPSSCLVCEMSSLFQEFYSGHRSPHI
PYKLLHLVWTHARHLAGYEQQDAHEFLIAALDVLHRHCKGDDNGKKANNPNHCNCIIDQI
FTGGLQSDVTCQVCHGVSTTIDPFWDISLDLPGSSTPFWPLSPGSEGNVVNGESHVSGTT
TLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHLKRFEHSAKLRR
KITTYVSFPLELDMTPFMASSKESRMNGQYQQPTDSLNNDNKYSLFAVVNHQGTLESGHY
TSFIRQHKDQWFKCDDAIITKASIKDVLDSEGYLLFYHKQFLEYE
GenBank ID Protein 150010639
UniProtKB/Swiss-Prot ID Q9UPT9
UniProtKB/Swiss-Prot Entry Name UBP22_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_015276.1
GeneCard ID USP22
GenAtlas ID USP22
HGNC ID HGNC:12621
References
General References
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  2. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed:17974005 ]
  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. Zhao Y, Lang G, Ito S, Bonnet J, Metzger E, Sawatsubashi S, Suzuki E, Le Guezennec X, Stunnenberg HG, Krasnov A, Georgieva SG, Schule R, Takeyama K, Kato S, Tora L, Devys D: A TFTC/STAGA module mediates histone H2A and H2B deubiquitination, coactivates nuclear receptors, and counteracts heterochromatin silencing. Mol Cell. 2008 Jan 18;29(1):92-101. doi: 10.1016/j.molcel.2007.12.011. [PubMed:18206972 ]
  6. Lee HJ, Kim MS, Shin JM, Park TJ, Chung HM, Baek KH: The expression patterns of deubiquitinating enzymes, USP22 and Usp22. Gene Expr Patterns. 2006 Mar;6(3):277-84. Epub 2005 Dec 27. [PubMed:16378762 ]
  7. Zhang XY, Varthi M, Sykes SM, Phillips C, Warzecha C, Zhu W, Wyce A, Thorne AW, Berger SL, McMahon SB: The putative cancer stem cell marker USP22 is a subunit of the human SAGA complex required for activated transcription and cell-cycle progression. Mol Cell. 2008 Jan 18;29(1):102-11. doi: 10.1016/j.molcel.2007.12.015. [PubMed:18206973 ]
  8. Zhang XY, Pfeiffer HK, Thorne AW, McMahon SB: USP22, an hSAGA subunit and potential cancer stem cell marker, reverses the polycomb-catalyzed ubiquitylation of histone H2A. Cell Cycle. 2008 Jun 1;7(11):1522-4. Epub 2008 Mar 18. [PubMed:18469533 ]