CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-041970
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ubiquitin carboxyl-terminal hydrolase 
Protein Synonyms/Alias
  
Gene Name
 USP11 
Gene Synonyms/Alias
 hCG_17279 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
64ESWFLVEKHWYKQWEubiquitination[1, 2, 3]
139GQPPIERKVIELPNIubiquitination[2]
148IELPNIQKVEVYPVEubiquitination[2]
202EDTRLWAKNSEGSLDubiquitination[1, 2, 3, 4, 5, 6, 7]
312FRNPLGMKGEIAEAYubiquitination[1, 2, 3, 4, 5, 6, 7]
324EAYADLVKQAWSGHHubiquitination[1, 2, 3]
340SIVPHVFKNKVGHFAubiquitination[2]
342VPHVFKNKVGHFASQubiquitination[2]
404QEAWQNHKRRNDSVIubiquitination[2, 6, 7]
450VPLPISHKRVLEVFFubiquitination[2]
476HRLVVPKKGKISDLCubiquitination[2]
488DLCVALSKHTGISPEubiquitination[1, 2, 5, 6, 7]
671WPPRRRRKQLFTLQTubiquitination[1, 2, 3, 7]
709IDWEPEMKKRYYDEVubiquitination[2, 3]
710DWEPEMKKRYYDEVEubiquitination[2]
723VEAEGYVKHDCVGYVubiquitination[2, 6, 7]
733CVGYVMKKAPVRLQEubiquitination[2]
763PWYCPSCKQHQLATKubiquitination[1]
770KQHQLATKKLDLWMLubiquitination[2]
792LKRFSYTKFSREKLDubiquitination[1, 2, 3, 6, 7]
797YTKFSREKLDTLVEFubiquitination[1, 2, 3, 4, 7]
853YTTFACNKDSGQWHYubiquitination[2]
877NENQIESKAAYVLFYubiquitination[6]
Reference
 [1] 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]
 [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] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Hydrolase; Protease; Reference proteome; Thiol protease; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 920 AA 
Protein Sequence
MATVAANPAA AAAAVAAAAA VTEDREPQHE ELPGLDSQWR QIENGESGRE RPLRAGESWF 60
LVEKHWYKQW EAYVQGGDQD SSTFPGCINN ATLFQDEINW RLKEGLVEGE DYVLLPAAAW 120
HYLVSWYGLE HGQPPIERKV IELPNIQKVE VYPVELLLVR HNDLGKSHTV QFSHTDSIGL 180
VLRTARERFL VEPQEDTRLW AKNSEGSLDR LYDTHITVLD AALETGQLII METRKKDGTW 240
PSAQLHVMNN NMSEEDEDFK GQPGICGLTN LGNTCFMNSA LQCLSNVPQL TEYFLNNCYL 300
EELNFRNPLG MKGEIAEAYA DLVKQAWSGH HRSIVPHVFK NKVGHFASQF LGYQQHDSQE 360
LLSFLLDGLH EDLNRVKKKE YVELCDAAGR PDQEVAQEAW QNHKRRNDSV IVDTFHGLFK 420
STLVCPDCGN VSVTFDPFCY LSVPLPISHK RVLEVFFIPM DPRRKPEQHR LVVPKKGKIS 480
DLCVALSKHT GISPERMMVA DVFSHRFYKL YQLEEPLSSI LDRDDIFVYE VSGRIEAIEG 540
SREDIVVPVY LRERTPARDY NNSYYGLMLF GHPLLVSVPR DRFTWEGLYN VLMYRLSRYV 600
TKPNSDDEDD GDEKEDDEED KDDVPGPSTG GSLRDPEPEQ AGPSSGVTNR CPFLLDNCLG 660
TSQWPPRRRR KQLFTLQTVN SNGTSDRTTS PEEVHAQPYI AIDWEPEMKK RYYDEVEAEG 720
YVKHDCVGYV MKKAPVRLQE CIELFTTVET LEKENPWYCP SCKQHQLATK KLDLWMLPEI 780
LIIHLKRFSY TKFSREKLDT LVEFPIRDLD FSEFVIQPQN ESNPELYKYD LIAVSNHYGG 840
MRDGHYTTFA CNKDSGQWHY FDDNSVSPVN ENQIESKAAY VLFYQRQDVA RRLLSPAGSS 900
GAPASPACSS PPSSEFMDVN 920 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
 GO:0004221; F:ubiquitin thiolesterase activity; IEA:InterPro.
 GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. 
Interpro
 IPR006615; Pept_C19_DUSP.
 IPR018200; Pept_C19ubi-hydrolase_C_CS.
 IPR001394; Peptidase_C19. 
Pfam
 PF06337; DUSP
 PF00443; UCH 
SMART
 SM00695; DUSP 
PROSITE
 PS51283; DUSP
 PS00972; UCH_2_1
 PS00973; UCH_2_2
 PS50235; UCH_2_3 
PRINTS