CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017693
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ubiquitin carboxyl-terminal hydrolase 32 
Protein Synonyms/Alias
 Deubiquitinating enzyme 32; Renal carcinoma antigen NY-REN-60; Ubiquitin thioesterase 32; Ubiquitin-specific-processing protease 32 
Gene Name
 USP32 
Gene Synonyms/Alias
 USP10 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
589RPVIKNSKTDIPELEubiquitination[1, 2, 3]
951EKYTGLKKQLSDLCGubiquitination[4, 5]
1162FTLRVVQKDGNSCAWubiquitination[2]
1537YAKNPNCKWYCYNDSubiquitination[1, 3]
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] 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] 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]
 [5] 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
Functional Description
  
Sequence Annotation
 DOMAIN 91 126 EF-hand 1.
 DOMAIN 228 263 EF-hand 2.
 DOMAIN 264 299 EF-hand 3.
 DOMAIN 369 585 DUSP.
 ACT_SITE 743 743 Nucleophile (By similarity).
 ACT_SITE 1526 1526 Proton acceptor (By similarity).
 MOD_RES 1173 1173 Phosphotyrosine.
 MOD_RES 1372 1372 Phosphoserine.
 MOD_RES 1601 1601 Cysteine methyl ester (Potential).
 LIPID 1601 1601 S-farnesyl cysteine (Potential).  
Keyword
 Calcium; Complete proteome; Golgi apparatus; Hydrolase; Lipoprotein; Membrane; Metal-binding; Methylation; Phosphoprotein; Polymorphism; Prenylation; Protease; Reference proteome; Repeat; Thiol protease; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1604 AA 
Protein Sequence
MGAKESRIGF LSYEEALRRV TDVELKRLKD AFKRTCGLSY YMGQHCFIRE VLGDGVPPKV 60
AEVIYCSFGG TSKGLHFNNL IVGLVLLTRG KDEEKAKYIF SLFSSESGNY VIREEMERML 120
HVVDGKVPDT LRKCFSEGEK VNYEKFRNWL FLNKDAFTFS RWLLSGGVYV TLTDDSDTPT 180
FYQTLAGVTH LEESDIIDLE KRYWLLKAQS RTGRFDLETF GPLVSPPIRP SLSEGLFNAF 240
DENRDNHIDF KEISCGLSAC CRGPLAERQK FCFKVFDVDR DGVLSRVELR DMVVALLEVW 300
KDNRTDDIPE LHMDLSDIVE GILNAHDTTK MGHLTLEDYQ IWSVKNVLAN EFLNLLFQVC 360
HIVLGLRPAT PEEEGQIIRG WLERESRYGL QAGHNWFIIS MQWWQQWKEY VKYDANPVVI 420
EPSSVLNGGK YSFGTAAHPM EQVEDRIGSS LSYVNTTEEK FSDNISTASE ASETAGSGFL 480
YSATPGADVC FARQHNTSDN NNQCLLGANG NILLHLNPQK PGAIDNQPLV TQEPVKATSL 540
TLEGGRLKRT PQLIHGRDYE MVPEPVWRAL YHWYGANLAL PRPVIKNSKT DIPELELFPR 600
YLLFLRQQPA TRTQQSNIWV NMGNVPSPNA PLKRVLAYTG CFSRMQTIKE IHEYLSQRLR 660
IKEEDMRLWL YNSENYLTLL DDEDHKLEYL KIQDEQHLVI EVRNKDMSWP EEMSFIANSS 720
KIDRHKVPTE KGATGLSNLG NTCFMNSSIQ CVSNTQPLTQ YFISGRHLYE LNRTNPIGMK 780
GHMAKCYGDL VQELWSGTQK NVAPLKLRWT IAKYAPRFNG FQQQDSQELL AFLLDGLHED 840
LNRVHEKPYV ELKDSDGRPD WEVAAEAWDN HLRRNRSIVV DLFHGQLRSQ VKCKTCGHIS 900
VRFDPFNFLS LPLPMDSYMH LEITVIKLDG TTPVRYGLRL NMDEKYTGLK KQLSDLCGLN 960
SEQILLAEVH GSNIKNFPQD NQKVRLSVSG FLCAFEIPVP VSPISASSPT QTDFSSSPST 1020
NEMFTLTTNG DLPRPIFIPN GMPNTVVPCG TEKNFTNGMV NGHMPSLPDS PFTGYIIAVH 1080
RKMMRTELYF LSSQKNRPSL FGMPLIVPCT VHTRKKDLYD AVWIQVSRLA SPLPPQEASN 1140
HAQDCDDSMG YQYPFTLRVV QKDGNSCAWC PWYRFCRGCK IDCGEDRAFI GNAYIAVDWD 1200
PTALHLRYQT SQERVVDEHE SVEQSRRAQA EPINLDSCLR AFTSEEELGE NEMYYCSKCK 1260
THCLATKKLD LWRLPPILII HLKRFQFVNG RWIKSQKIVK FPRESFDPSA FLVPRDPALC 1320
QHKPLTPQGD ELSEPRILAR EVKKVDAQSS AGEEDVLLSK SPSSLSANII SSPKGSPSSS 1380
RKSGTSCPSS KNSSPNSSPR TLGRSKGRLR LPQIGSKNKL SSSKENLDAS KENGAGQICE 1440
LADALSRGHV LGGSQPELVT PQDHEVALAN GFLYEHEACG NGYSNGQLGN HSEEDSTDDQ 1500
REDTRIKPIY NLYAISCHSG ILGGGHYVTY AKNPNCKWYC YNDSSCKELH PDEIDTDSAY 1560
ILFYEQQGID YAQFLPKTDG KKMADTSSMD EDFESDYKKY CVLQ 1604 
Gene Ontology
 GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
 GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
 GO:0004221; F:ubiquitin thiolesterase activity; IDA:UniProtKB.
 GO:0016579; P:protein deubiquitination; TAS:UniProtKB.
 GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. 
Interpro
 IPR011992; EF-hand-like_dom.
 IPR018247; EF_Hand_1_Ca_BS.
 IPR002048; EF_hand_dom.
 IPR006615; Pept_C19_DUSP.
 IPR018200; Pept_C19ubi-hydrolase_C_CS.
 IPR001394; Peptidase_C19.
 IPR001125; Recoverin. 
Pfam
 PF06337; DUSP
 PF13202; EF_hand_3
 PF00443; UCH 
SMART
 SM00695; DUSP
 SM00054; EFh 
PROSITE
 PS51283; DUSP
 PS00018; EF_HAND_1
 PS50222; EF_HAND_2
 PS00972; UCH_2_1
 PS00973; UCH_2_2
 PS50235; UCH_2_3 
PRINTS
 PR00450; RECOVERIN.