CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-032268
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 USP48 protein 
Protein Synonyms/Alias
 Ubiquitin carboxyl-terminal hydrolase 48 
Gene Name
 USP48 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
9APRLQLEKAAWRWAEubiquitination[1]
170IDPSGFVKALGLDTGubiquitination[1, 2, 3, 4, 5, 6, 7]
199LLEDTLSKQKNPDVRubiquitination[1, 3, 5]
201EDTLSKQKNPDVRNIubiquitination[1]
258DCISEFLKEEKLEGDubiquitination[1, 7]
276FCENCQSKQNATRKIubiquitination[1, 4, 7]
368PQSGEWYKFNDEDIEubiquitination[3]
467SVDKGKAKHEEVKELubiquitination[1]
550GGPRLTVKALCKECVubiquitination[1, 8]
554LTVKALCKECVVERCubiquitination[1]
586NLLKAAVKGSDGFWVubiquitination[2, 5, 6, 7, 8]
595SDGFWVGKSSLRSWRubiquitination[1]
681NERRLVSKEAWSKLQubiquitination[1, 8]
686VSKEAWSKLQQYFPKubiquitination[1]
693KLQQYFPKAPEFPSYubiquitination[2, 3, 6, 8]
701APEFPSYKECCSQCKubiquitination[1, 4, 7]
708KECCSQCKILEREGEubiquitination[1, 7]
802FTFASMTKEDSKLIAubiquitination[5]
880QATIYVHKVVDNKKVubiquitination[1, 2, 6]
886HKVVDNKKVMKDSAPubiquitination[1]
957HRKVRGEKALLVSANubiquitination[2, 6]
968VSANQTLKELKIQIMubiquitination[1, 2, 6, 7, 8]
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] 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]
 [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] 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]
 [5] 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]
 [6] 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]
 [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]
 [8] 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
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1047 AA 
Protein Sequence
MAPRLQLEKA AWRWAETVRP EEVSQEHIET AYRIWLEPCI RGVCRRNCKG NPNCLVGIGE 60
HIWLGEIDEN SFHNIDDPNC ERRKKNSFVG LTNLGATCYV NTFLQVWFLN LELRQALYLC 120
PSTCSDYMLG DGIQEEKDYE PQTICEHLQY LFALLQNSNR RYIDPSGFVK ALGLDTGQQQ 180
DAQEFSKLFM SLLEDTLSKQ KNPDVRNIVQ QQFCGEYAYV TVCNQCGRES KLLSKFYELE 240
LNIQGHKQLT DCISEFLKEE KLEGDNRYFC ENCQSKQNAT RKIRLLSLPC TLNLQLMRFV 300
FDRQTGHKKK LNTYIGFSEI LDMEPYVEHK GGSYVYELSA VLIHRGVSAY SGHYIAHVKD 360
PQSGEWYKFN DEDIEKMEGK KLQLGIEEDL EPSKSQTRKP KCGKGTHCSR NAYMLVYRLQ 420
TQEKPNTTVQ VPAFLQELVD RDNSKFEEWC IEMAEMRKQS VDKGKAKHEE VKELYQRLPA 480
GAEPYEFVSL EWLQKWLDES TPTKPIDNHA CLCSHDKLHP DKISIMKRIS EYAADIFYSR 540
YGGGPRLTVK ALCKECVVER CRILRLKNQL NEDYKTVNNL LKAAVKGSDG FWVGKSSLRS 600
WRQLALEQLD EQDGDAEQSN GKMNGSTLNK DESKEERKEE EELNFNEDIL CPHAVFFFSK 660
YIFLNSGELC ISENERRLVS KEAWSKLQQY FPKAPEFPSY KECCSQCKIL EREGEENEAL 720
HKMIANEQKT SLPNLFQDKN RPCLSNWPED TDVLYIVSQF FVEEWRKFVR KPTRCSPVSS 780
VGNSALLCPH GGLMFTFASM TKEDSKLIAL IWPSEWQMIQ KLFVVDHVIK ITRIEVGDVN 840
PSETQYISEP KLCPECREGL LCQQQRDLRE YTQATIYVHK VVDNKKVMKD SAPELNVSSS 900
ETEEDKEEAK PDGEKDPDFN QSNGGTKRQK ISHQNYIAYQ KQVIRRSMRH RKVRGEKALL 960
VSANQTLKEL KIQIMHAFSV APFDQNLSID GKILSDDCAT LGTLGVIPES VILLKADEPI 1020
ADYAAMDDVM QVCMPEEGFK GTGLLGH 1047 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:HPA.
 GO:0005634; C:nucleus; IDA:HPA.
 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.
 IPR019955; Ubiquitin_supergroup. 
Pfam
 PF00443; UCH 
SMART
  
PROSITE
 PS51283; DUSP
 PS50053; UBIQUITIN_2
 PS00973; UCH_2_2
 PS50235; UCH_2_3 
PRINTS