CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013555
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ubiquitin carboxyl-terminal hydrolase 13 
Protein Synonyms/Alias
 Deubiquitinating enzyme 13; Ubiquitin thioesterase 13; Ubiquitin-specific-processing protease 13 
Gene Name
 Usp13 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
324VIQESGTKLKPMYGPubiquitination[1]
326QESGTKLKPMYGPGYubiquitination[1]
638IVIPDDSKDRLMNQLubiquitination[1, 2]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113
Functional Description
 Deubiquitinase that mediates deubiquitination of target proteins such as BECN1, MITF, SKP2 and USP10 and is involved in various processes such as autophagy and endoplasmic reticulum- associated degradation (ERAD). Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. Also deubiquitinates USP10, an essential regulator of p53/TP53 stability. In turn, PIK3C3/VPS34- containing complexes regulate USP13 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Recruited by nuclear UFD1 and mediates deubiquitination of SKP2, thereby regulating endoplasmic reticulum-associated degradation (ERAD). Mediates stabilization of SIAH2 independently of deubiquitinase activity: binds ubiquitinated SIAH2 and acts by impairing SIAH2 autoubiquitination. Has a weak deubiquitinase activity in vitro and preferentially cleaves 'Lys-63'-linked polyubiquitin chains. In contrast to USP5, it is not able to mediate unanchored polyubiquitin disassembly. Able to cleave ISG15 in vitro; however, additional experiments are required to confirm such data (By similarity). 
Sequence Annotation
 DOMAIN 650 691 UBA 1.
 DOMAIN 722 762 UBA 2.
 ZN_FING 207 279 UBP-type.
 ACT_SITE 343 343 Nucleophile (By similarity).
 ACT_SITE 818 818 Proton acceptor (By similarity).
 MOD_RES 112 112 Phosphoserine (By similarity).  
Keyword
 Autophagy; Complete proteome; Hydrolase; Metal-binding; Phosphoprotein; Protease; Reference proteome; Repeat; Thiol protease; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 858 AA 
Protein Sequence
MQRRGALFSV PGGGGKMAAG DLGELLVPHM PTIRVPRSGD RVYKNECAFS YDSPNSEGGL 60
YVCMNTFLAF GREHVERHFR KTGQSVYMHL KRHMREKVRG ASGGALPKRR NSKIFLDLDM 120
DDDLNSDDYE YEDEAKLVIF PDHYEIALPN IEELPALVTI ACDAVLSSKS PYRKQDPDTW 180
ENEVPVSKYA NNLVQLDNGV RIPPSGWKCA RCDLRENLWL NLTDGSVLCG KWFFDSSGGN 240
GHALEHYRDM GYPLAVKLGT ITPDGADVYS FQEEGPVSDP HLAKHLAHFG IDMLHTQGTE 300
NGLRDNDIKP RVSEWEVIQE SGTKLKPMYG PGYTGLKNLG NSCYLSSVMQ AIFSIPEFQR 360
AYVGNLPRIF DYSPLDPTQD FNTQMTKLGH GLLSGQYSKP PVKSELIEQV MKEEHKPQQN 420
GISPRMFKAF VSKSHPEFSS NRQQDAQEFF LHLVNLVERN RIGSENPSDV FRFLVEERIQ 480
CCQTRKVRYT ERVDYLMQLP VAMEAATNKD ELITYELMRR EAEANRRPLP ELVRAKIPFS 540
ACLQAFAEPD NVDDFWSSAL QAKSAGVKTS RFASFPEYLV VQIKKFTFGL DWVPRKFDVS 600
IDMPDLLDIS HLRARGLQPG EEELPDISPP IVIPDDSKDR LMNQLIDPSD IDESSVMQLA 660
EMGFPLEACR KAVYFTGNTG AEVAFNWIIV HMEEPDFAEP LAIPGYGGAG ASVFGATGLD 720
NQPPEEIVAI ITSMGFQRNQ AVQALQATNH NLERALDWIF SHPEFEEDSD FVIEMENNAN 780
ANIVSEAKPE GPRVKDGSGM YELFAFISHM GTSTMSGHYV CHIKKEGRWV IYNDHKVCAS 840
ERPPKDLGYM YFYRRIPS 858 
Gene Ontology
 GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
 GO:0008242; F:omega peptidase activity; IEA:InterPro.
 GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
 GO:0004221; F:ubiquitin thiolesterase activity; ISS:UniProtKB.
 GO:0004843; F:ubiquitin-specific protease activity; ISS:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006914; P:autophagy; IEA:UniProtKB-KW.
 GO:0008283; P:cell proliferation; ISS:UniProtKB.
 GO:0070536; P:protein K63-linked deubiquitination; ISS:UniProtKB.
 GO:0050821; P:protein stabilization; ISS:UniProtKB.
 GO:0010506; P:regulation of autophagy; ISS:UniProtKB.
 GO:0006355; P:regulation of transcription, DNA-dependent; ISS:UniProtKB.
 GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. 
Interpro
 IPR018200; Pept_C19ubi-hydrolase_C_CS.
 IPR001394; Peptidase_C19.
 IPR009060; UBA-like.
 IPR000449; UBA/transl_elong_EF1B_N.
 IPR015940; UBA/transl_elong_EF1B_N_euk.
 IPR016652; Ubiquitinyl_hydrolase.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR001607; Znf_UBP. 
Pfam
 PF00627; UBA
 PF00443; UCH
 PF02148; zf-UBP 
SMART
 SM00165; UBA
 SM00290; ZnF_UBP 
PROSITE
 PS50030; UBA
 PS00972; UCH_2_1
 PS00973; UCH_2_2
 PS50235; UCH_2_3
 PS50271; ZF_UBP 
PRINTS