CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016170
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ubiquitin carboxyl-terminal hydrolase 37 
Protein Synonyms/Alias
 Deubiquitinating enzyme 37; Ubiquitin thioesterase 37; Ubiquitin-specific-processing protease 37 
Gene Name
 USP37 
Gene Synonyms/Alias
 KIAA1594 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
68VLRPSGAKQSRLMLTubiquitination[1]
147SDNQASAKRGSLETKubiquitination[1]
315PVPLSVKKLRCNQDYubiquitination[1]
327QDYTGWNKPRVPLSSubiquitination[1, 2]
378KQGIPWKKIPLNALIubiquitination[3]
452EKLNKTWKTEPVSGEubiquitination[1, 3, 4]
540ELEYSCEKCGGKCALubiquitination[1]
544SCEKCGGKCALVRHKubiquitination[1]
635SPSTPSKKFTFKSKSubiquitination[1]
717AAVLEISKRDASPSLubiquitination[3]
785CDENKENKTPEGSQGubiquitination[3]
915ISDVYDIKKQAWFTYubiquitination[4]
916SDVYDIKKQAWFTYNubiquitination[1]
962DELLETEKNSQSLSTubiquitination[3]
973SLSTEVGKTTRQAL*ubiquitination[1, 2, 3]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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] 
Functional Description
 Deubiquitinase that antagonizes the anaphase-promoting complex (APC/C) during G1/S transition by mediating deubiquitination of cyclin-A (CCNA1 and CCNA2), thereby promoting S phase entry. Specifically mediates deubiquitination of 'Lys-11'- linked polyubiquitin chains, a specific ubiquitin-linkage type mediated by the APC/C complex. Also mediates deubiquitination of 'Lys-48'-linked polyubiquitin chains in vitro. Phosphorylation at Ser-628 during G1/S phase maximizes the deubiquitinase activity, leading to prevent degradation of cyclin-A (CCNA1 and CCNA2). 
Sequence Annotation
 REPEAT 704 723 UIM 1.
 REPEAT 806 825 UIM 2.
 REPEAT 828 847 UIM 3.
 MOTIF 32 34 KEN box 1.
 MOTIF 71 79 D-box 1.
 MOTIF 96 105 D-box 2.
 MOTIF 160 168 D-box 3.
 MOTIF 221 223 KEN box 2.
 MOTIF 782 784 KEN box 3.
 ACT_SITE 350 350 Nucleophile (Probable).
 ACT_SITE 906 906 Proton acceptor (By similarity).
 MOD_RES 213 213 Phosphoserine (By similarity).
 MOD_RES 628 628 Phosphoserine; by CDK2.
 MOD_RES 650 650 Phosphoserine.
 MOD_RES 652 652 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Cell cycle; Cell division; Complete proteome; Hydrolase; Mitosis; Phosphoprotein; Polymorphism; Protease; Reference proteome; Repeat; Thiol protease; Ubl conjugation; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 979 AA 
Protein Sequence
MSPLKIHGPI RIRSMQTGIT KWKEGSFEIV EKENKVSLVV HYNTGGIPRI FQLSHNIKNV 60
VLRPSGAKQS RLMLTLQDNS FLSIDKVPSK DAEEMRLFLD AVHQNRLPAA MKPSQGSGSF 120
GAILGSRTSQ KETSRQLSYS DNQASAKRGS LETKDDIPFR KVLGNPGRGS IKTVAGSGIA 180
RTIPSLTSTS TPLRSGLLEN RTEKRKRMIS TGSELNEDYP KENDSSSNNK AMTDPSRKYL 240
TSSREKQLSL KQSEENRTSG LLPLQSSSFY GSRAGSKEHS SGGTNLDRTN VSSQTPSAKR 300
SLGFLPQPVP LSVKKLRCNQ DYTGWNKPRV PLSSHQQQQL QGFSNLGNTC YMNAILQSLF 360
SLQSFANDLL KQGIPWKKIP LNALIRRFAH LLVKKDICNS ETKKDLLKKV KNAISATAER 420
FSGYMQNDAH EFLSQCLDQL KEDMEKLNKT WKTEPVSGEE NSPDISATRA YTCPVITNLE 480
FEVQHSIICK ACGEIIPKRE QFNDLSIDLP RRKKPLPPRS IQDSLDLFFR AEELEYSCEK 540
CGGKCALVRH KFNRLPRVLI LHLKRYSFNV ALSLNNKIGQ QVIIPRYLTL SSHCTENTKP 600
PFTLGWSAHM AISRPLKASQ MVNSCITSPS TPSKKFTFKS KSSLALCLDS DSEDELKRSV 660
ALSQRLCEML GNEQQQEDLE KDSKLCPIEP DKSELENSGF DRMSEEELLA AVLEISKRDA 720
SPSLSHEDDD KPTSSPDTGF AEDDIQEMPE NPDTMETEKP KTITELDPAS FTEITKDCDE 780
NKENKTPEGS QGEVDWLQQY DMEREREEQE LQQALAQSLQ EQEAWEQKED DDLKRATELS 840
LQEFNNSFVD ALGSDEDSGN EDVFDMEYTE AEAEELKRNA ETGNLPHSYR LISVVSHIGS 900
TSSSGHYISD VYDIKKQAWF TYNDLEVSKI QEAAVQSDRD RSGYIFFYMH KEIFDELLET 960
EKNSQSLSTE VGKTTRQAL 979 
Gene Ontology
 GO:0005634; C:nucleus; IDA:LIFEdb.
 GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
 GO:0004221; F:ubiquitin thiolesterase activity; IEA:InterPro.
 GO:0004843; F:ubiquitin-specific protease activity; IDA:UniProtKB.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0000082; P:G1/S transition of mitotic cell cycle; IDA:UniProtKB.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0035871; P:protein K11-linked deubiquitination; IDA:UniProtKB.
 GO:0071108; P:protein K48-linked deubiquitination; IDA:UniProtKB.
 GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. 
Interpro
 IPR018200; Pept_C19ubi-hydrolase_C_CS.
 IPR001394; Peptidase_C19.
 IPR003903; Ubiquitin-int_motif. 
Pfam
 PF00443; UCH
 PF02809; UIM 
SMART
 SM00726; UIM 
PROSITE
 PS00972; UCH_2_1
 PS00973; UCH_2_2
 PS50235; UCH_2_3
 PS50330; UIM 
PRINTS