CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023289
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ubiquitin carboxyl-terminal hydrolase 22 
Protein Synonyms/Alias
 Deubiquitinating enzyme 22; Ubiquitin thioesterase 22; Ubiquitin-specific-processing protease 22 
Gene Name
 USP22 
Gene Synonyms/Alias
 KIAA1063; USP3L 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
35SFKVDNWKQNLRAIYubiquitination[1, 2, 3]
59EARKRKAKSCICHVCubiquitination[3]
129KDMEIIAKEEQRKAWacetylation[4]
137EEQRKAWKMQGVGEKubiquitination[2, 5, 6]
144KMQGVGEKFSTWEPTubiquitination[2, 6, 7, 8]
152FSTWEPTKRELELLKubiquitination[2, 5]
159KRELELLKHNPKRRKubiquitination[2]
166KHNPKRRKITSNCTIubiquitination[2, 5, 6]
380EHLGSSAKIKCSGCHubiquitination[2]
382LGSSAKIKCSGCHSYubiquitination[2, 3]
394HSYQESTKQLTMKKLubiquitination[2, 3, 9]
410IVACFHLKRFEHSAKubiquitination[2]
417KRFEHSAKLRRKITTacetylation[3]
417KRFEHSAKLRRKITTubiquitination[2, 3, 10]
442TPFMASSKESRMNGQubiquitination[2, 9]
462DSLNNDNKYSLFAVVubiquitination[2, 9]
488TSFIRQHKDQWFKCDubiquitination[2]
493QHKDQWFKCDDAIITubiquitination[2, 7, 8, 9]
501CDDAIITKASIKDVLubiquitination[2, 3, 9]
505IITKASIKDVLDSEGubiquitination[2, 7, 8]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] 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]
 [3] 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]
 [4] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [6] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [7] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [8] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [9] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [10] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 
Functional Description
 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. 
Sequence Annotation
 ZN_FING 61 121 UBP-type.
 ACT_SITE 185 185 Nucleophile (By similarity).
 ACT_SITE 479 479 Proton acceptor (By similarity).
 MOD_RES 129 129 N6-acetyllysine.  
Keyword
 Acetylation; Activator; Alternative splicing; Cell cycle; Chromatin regulator; Complete proteome; Hydrolase; Metal-binding; Nucleus; Protease; Reference proteome; Thiol protease; Transcription; Transcription regulation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 525 AA 
Protein Sequence
MVSRPEPEGE AMDAELAVAP PGCSHLGSFK VDNWKQNLRA IYQCFVWSGT AEARKRKAKS 60
CICHVCGVHL NRLHSCLYCV FFGCFTKKHI HEHAKAKRHN LAIDLMYGGI YCFLCQDYIY 120
DKDMEIIAKE EQRKAWKMQG VGEKFSTWEP TKRELELLKH NPKRRKITSN CTIGLRGLIN 180
LGNTCFMNCI VQALTHTPLL RDFFLSDRHR CEMQSPSSCL VCEMSSLFQE FYSGHRSPHI 240
PYKLLHLVWT HARHLAGYEQ QDAHEFLIAA LDVLHRHCKG DDNGKKANNP NHCNCIIDQI 300
FTGGLQSDVT CQVCHGVSTT IDPFWDISLD LPGSSTPFWP LSPGSEGNVV NGESHVSGTT 360
TLTDCLRRFT RPEHLGSSAK IKCSGCHSYQ ESTKQLTMKK LPIVACFHLK RFEHSAKLRR 420
KITTYVSFPL ELDMTPFMAS SKESRMNGQY QQPTDSLNND NKYSLFAVVN HQGTLESGHY 480
TSFIRQHKDQ WFKCDDAIIT KASIKDVLDS EGYLLFYHKQ FLEYE 525 
Gene Ontology
 GO:0000124; C:SAGA complex; IDA:UniProtKB.
 GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IMP:UniProtKB.
 GO:0004221; F:ubiquitin thiolesterase activity; IEA:InterPro.
 GO:0004843; F:ubiquitin-specific protease activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0009790; P:embryo development; NAS:UniProtKB.
 GO:0016578; P:histone deubiquitination; IDA:UniProtKB.
 GO:0043967; P:histone H4 acetylation; IDA:GOC.
 GO:0016574; P:histone ubiquitination; IDA:UniProtKB.
 GO:0045931; P:positive regulation of mitotic cell cycle; IMP:UniProtKB.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IMP:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. 
Interpro
 IPR018200; Pept_C19ubi-hydrolase_C_CS.
 IPR001394; Peptidase_C19.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR001607; Znf_UBP. 
Pfam
 PF00443; UCH
 PF02148; zf-UBP 
SMART
  
PROSITE
 PS00972; UCH_2_1
 PS00973; UCH_2_2
 PS50235; UCH_2_3
 PS50271; ZF_UBP 
PRINTS