CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013453
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 U4/U6.U5 tri-snRNP-associated protein 2 
Protein Synonyms/Alias
 Inactive ubiquitin-specific peptidase 39; SAD1 homolog; U4/U6.U5 tri-snRNP-associated 65 kDa protein; 65K 
Gene Name
 USP39 
Gene Synonyms/Alias
 CGI-21; HSPC332; PRO2855 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
210ANLDKQAKLSRAYDGubiquitination[1]
428KFNGITEKEYKTYKEacetylation[2]
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] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
Functional Description
 Plays a role in pre-mRNA splicing as a component of the U4/U6-U5 tri-snRNP, one of the building blocks of the spliceosome. Regulates AURKB mRNA levels, and thereby plays a role in cytokinesis and in the spindle checkpoint. Does not have ubiquitin-specific peptidase activity, but could be a competitor of ubiquitin C-terminal hydrolases (UCHs). 
Sequence Annotation
 ZN_FING 122 183 UBP-type.
 MOD_RES 82 82 Phosphoserine.  
Keyword
 Alternative splicing; Cell cycle; Cell division; Complete proteome; Metal-binding; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Spliceosome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 565 AA 
Protein Sequence
MSGRSKRESR GSTRGKRESE SRGSSGRVKR ERDREREPEA ASSRGSPVRV KREFEPASAR 60
EAPASVVPFV RVKREREVDE DSEPEREVRA KNGRVDSEDR RSRHCPYLDT INRSVLDFDF 120
EKLCSISLSH INAYACLVCG KYFQGRGLKS HAYIHSVQFS HHVFLNLHTL KFYCLPDNYE 180
IIDSSLEDIT YVLKPTFTKQ QIANLDKQAK LSRAYDGTTY LPGIVGLNNI KANDYANAVL 240
QALSNVPPLR NYFLEEDNYK NIKRPPGDIM FLLVQRFGEL MRKLWNPRNF KAHVSPHEML 300
QAVVLCSKKT FQITKQGDGV DFLSWFLNAL HSALGGTKKK KKTIVTDVFQ GSMRIFTKKL 360
PHPDLPAEEK EQLLHNDEYQ ETMVESTFMY LTLDLPTAPL YKDEKEQLII PQVPLFNILA 420
KFNGITEKEY KTYKENFLKR FQLTKLPPYL IFCIKRFTKN NFFVEKNPTI VNFPITNVDL 480
REYLSEEVQA VHKNTTYDLI ANIVHDGKPS EGSYRIHVLH HGTGKWYELQ DLQVTDILPQ 540
MITLSEAYIQ IWKRRDNDET NQQGA 565 
Gene Ontology
 GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
 GO:0004221; F:ubiquitin thiolesterase activity; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0000245; P:spliceosomal complex assembly; TAS:ProtInc.
 GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. 
Interpro
 IPR001394; Peptidase_C19.
 IPR015880; Znf_C2H2-like.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR001607; Znf_UBP. 
Pfam
 PF00443; UCH
 PF02148; zf-UBP 
SMART
 SM00355; ZnF_C2H2 
PROSITE
 PS00972; UCH_2_1
 PS00973; UCH_2_2
 PS50235; UCH_2_3
 PS50271; ZF_UBP 
PRINTS