CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010855
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ubiquitin carboxyl-terminal hydrolase 3 
Protein Synonyms/Alias
 Deubiquitinating enzyme 3; Ubiquitin thioesterase 3; Ubiquitin-specific-processing protease 3 
Gene Name
 UBP3 
Gene Synonyms/Alias
 YER151C 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
260TKSHSIPKHNEEVKTubiquitination[1]
756EYELLPFKSSSGNDVubiquitination[1]
Reference
 [1] Identification, analysis, and prediction of protein ubiquitination sites.
 Radivojac P, Vacic V, Haynes C, Cocklin RR, Mohan A, Heyen JW, Goebl MG, Iakoucheva LM.
 Proteins. 2010 Feb 1;78(2):365-80. [PMID: 19722269
Functional Description
 Has an ATP-independent isopeptidase activity, cleaving at the C-terminus of the ubiquitin moiety in natural or engineered linear fusion proteins, irrespective of their size or the presence of an N-terminal extension to ubiquitin. Plays a role in regulation of silencing by interacting with SIR4. Also, in conjunction with BRE5, cleaves ubiquitin, leading to the subsequent mono-ubiquitination of SEC23. 
Sequence Annotation
 ACT_SITE 469 469 Nucleophile (By similarity).
 ACT_SITE 861 861 Proton acceptor (By similarity).  
Keyword
 3D-structure; Complete proteome; Hydrolase; Protease; Reference proteome; Thiol protease; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 912 AA 
Protein Sequence
MNMQDANKEE SYSMYPKTSS PPPPTPTNMQ IPIYQAPLQM YGYTQAPYLY PTQIPAYSFN 60
MVNQNQPIYH QSGSPHHLPP QNNINGGSTT NNNNINKKKW HSNGITNNNG SSGNQGANSS 120
GSGMSYNKSH TYHHNYSNNH IPMMASPNSG SNAGMKKQTN SSNGNGSSAT SPSYSSYNSS 180
SQYDLYKFDV TKLKNLKENS SNLIQLPLFI NTTEAEFAAA SVQRYELNMK ALNLNSESLE 240
NSSVEKSSAH HHTKSHSIPK HNEEVKTETH GEEEDAHDKK PHASKDAHEL KKKTEVKKED 300
AKQDRNEKVI QEPQATVLPV VDKKEPEESV EENTSKTSSP SPSPPAAKSW SAIASDAIKS 360
RQASNKTVSG SMVTKTPISG TTAGVSSTNM AAATIGKSSS PLLSKQPQKK DKKYVPPSTK 420
GIEPLGSIAL RMCFDPDFIS YVLRNKDVEN KIPVHSIIPR GIINRANICF MSSVLQVLLY 480
CKPFIDVINV LSTRNTNSRV GTSSCKLLDA CLTMYKQFDK ETYEKKFLEN ADDAEKTTES 540
DAKKSSKSKS FQHCATADAV KPDEFYKTLS TIPKFKDLQW GHQEDAEEFL THLLDQLHEE 600
LISAIDGLTD NEIQNMLQSI NDEQLKVFFI RNLSRYGKAE FIKNASPRLK ELIEKYGVIN 660
DDSTEENGWH EVSGSSKRGK KTKTAAKRTV EIVPSPISKL FGGQFRSVLD IPNNKESQSI 720
TLDPFQTIQL DISDAGVNDL ETAFKKFSEY ELLPFKSSSG NDVEAKKQTF IDKLPQVLLI 780
QFKRFSFINN VNKDNAMTNY NAYNGRIEKI RKKIKYGHEL IIPEESMSSI TLKNNTSGID 840
DRRYKLTGVI YHHGVSSDGG HYTADVYHSE HNKWYRIDDV NITELEDDDV LKGGEEASDS 900
RTAYILMYQK RN 912 
Gene Ontology
 GO:0005737; C:cytoplasm; IC:SGD.
 GO:0003729; F:mRNA binding; IDA:SGD.
 GO:0004221; F:ubiquitin thiolesterase activity; IEA:InterPro.
 GO:0004843; F:ubiquitin-specific protease activity; IDA:SGD.
 GO:0016579; P:protein deubiquitination; IDA:SGD.
 GO:0060628; P:regulation of ER to Golgi vesicle-mediated transport; IMP:SGD.
 GO:0047484; P:regulation of response to osmotic stress; IMP:SGD.
 GO:0034517; P:ribophagy; IMP:SGD.
 GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. 
Interpro
 IPR018200; Pept_C19ubi-hydrolase_C_CS.
 IPR001394; Peptidase_C19. 
Pfam
 PF00443; UCH 
SMART
  
PROSITE
 PS00972; UCH_2_1
 PS00973; UCH_2_2
 PS50235; UCH_2_3 
PRINTS