CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015616
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ubiquitin carboxyl-terminal hydrolase 45 
Protein Synonyms/Alias
 Deubiquitinating enzyme 45; Ubiquitin thioesterase 45; Ubiquitin-specific-processing protease 45 
Gene Name
 USP45 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
141LSTHCNKKVLAQIVDubiquitination[1]
391IIEERVSKPLLWGRMubiquitination[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] 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] 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
 ZN_FING 60 136 UBP-type.
 ACT_SITE 199 199 Nucleophile (By similarity).
 ACT_SITE 746 746 Proton acceptor (By similarity).  
Keyword
 Alternative splicing; Complete proteome; Hydrolase; Metal-binding; Polymorphism; Protease; Reference proteome; Thiol protease; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 814 AA 
Protein Sequence
MRVKDPTKAL PEKAKRSKRP TVPHDEDSSD DIAVGLTCQH VSHAISVNHV KRAIAENLWS 60
VCSECLKERR FYDGQLVLTS DIWLCLKCGF QGCGKNSESQ HSLKHFKSSR TEPHCIIINL 120
STWIIWCYEC DEKLSTHCNK KVLAQIVDFL QKHASKTQTS AFSRIMKLCE EKCETDEIQK 180
GGKCRNLSVR GITNLGNTCF FNAVMQNLAQ TYTLTDLMNE IKESSTKLKI FPSSDSQLDP 240
LVVELSRPGP LTSALFLFLH SMKETEKGPL SPKVLFNQLC QKAPRFKDFQ QQDSQELLHY 300
LLDAVRTEET KRIQASILKA FNNPTTKTAD DETRKKVKAY GKEGVKMNFI DRIFIGELTS 360
TVMCEECANI STVKDPFIDI SLPIIEERVS KPLLWGRMNK YRSLRETDHD RYSGNVTIEN 420
IHQPRAAKKH SSSKDKSQLI HDRKCIRKLS SGETVTYQKN ENLEMNGDSL MFASLMNSES 480
RLNESPTDDS EKEASHSESN VDADSEPSES ESASKQTGLF RSSSGSGVQP DGPLYPLSAG 540
KLLYTKETDS GDKEMAEAIS ELRLSSTVTG DQDFDRENQP LNISNNLCFL EGKHLRSYSP 600
QNAFQTLSQS YITTSKECSI QSCLYQFTSM ELLMGNNKLL CENCTKNKQK YQEETSFAEK 660
KVEGVYTNAR KQLLISAVPA VLILHLKRFH QAGLSLRKVN RHVDFPLMLD LAPFCSATCK 720
NASVGDKVLY GLYGIVEHSG SMREGHYTAY VKVRTPSRKL SEHNTKKKNV PGLKAADNES 780
AGQWVHVSDT YLQVVPESRA LSAQAYLLFY ERVL 814 
Gene Ontology
 GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
 GO:0004221; F:ubiquitin thiolesterase activity; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. 
Interpro
 IPR018200; Pept_C19ubi-hydrolase_C_CS.
 IPR001394; Peptidase_C19.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR001607; Znf_UBP. 
Pfam
 PF00443; UCH
 PF02148; zf-UBP 
SMART
  
PROSITE
 PS00972; UCH_2_1
 PS00973; UCH_2_2
 PS50235; UCH_2_3
 PS50271; ZF_UBP 
PRINTS