Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteprivacy & cookiesCuration ProcessContact
logos LINCs Logo Mt Sinai Logo NIH Logo NCI Logo
Protein Page:
USP13 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
USP13 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. Belongs to the peptidase C19 family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: EC 3.4.19.12; Ubiquitin-specific protease; Protease; Ubiquitin conjugating system
Chromosomal Location of Human Ortholog: 3q26.2-q26.3
Molecular Function: chaperone binding; cysteine-type endopeptidase activity; protein binding; ubiquitin binding; ubiquitin protein ligase binding; ubiquitin-specific protease activity
Biological Process: cell proliferation; melanocyte differentiation; protein stabilization; regulation of autophagy; regulation of transcription, DNA-dependent
Reference #:  Q92995 (UniProtKB)
Alt. Names/Synonyms: Deubiquitinating enzyme 13; Isopeptidase T-3; ISOT-3; ISOT3; Ubiquitin carboxyl-terminal hydrolase 13; ubiquitin specific peptidase 13 (isopeptidase T-3); ubiquitin specific protease 13 (isopeptidase T-3); Ubiquitin thioesterase 13; ubiquitin thiolesterase 13; Ubiquitin-specific-processing protease 13; UBP13; USP13
Gene Symbols: USP13
Molecular weight: 97,327 Da
Basal Isoelectric point: 5.33  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

USP13

Protein Structure Not Found.
Download PyMol Script
Download ChimeraX Script


STRING  |  cBioPortal  |  Wikipedia  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Scansite  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment



 LTP 

LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 1 R4‑m1 ____MQRrGALFGMP
0 3 S14‑p LFGMPGGsGGRkMAA
0 4 K18‑ub PGGsGGRkMAAGDIG
0 1 T34‑p LLVPHMPtIRVPRSG
0 3 S104‑p REKVRGAsGGALPKR
0 11 S114‑p ALPKRRNsKIFLDLD
0 21 T122‑p KIFLDLDtDDDLNsD
0 2 S128‑p DtDDDLNsDDYEYED
0 4 K176‑ub SSKSPYRkQDPDtWE
0 2 T181‑p YRkQDPDtWENELPV
0 8 K190‑ub ENELPVSkYANNLTQ
0 6 K259‑ub MGYPLAVkLGTITPD
0 1 T264 AVkLGTITPDGADVY
0 4 K326‑ub VIQESGTkLkPMYGP
0 10 K328‑ub QESGTkLkPMYGPGY
0 1 K339‑ub GPGYTGLkNLGNSCY
0 1 T380‑p DYSPLDPtQDFNtQM
0 1 T385‑p DPtQDFNtQMtKLGH
0 1 T388‑p QDFNtQMtKLGHGLL
0 1 S396‑p KLGHGLLsGQySkPP
0 1 Y399‑p HGLLsGQySkPPVkS
0 3 K401‑ub LLsGQySkPPVkSEL
0 3 K405‑ub QySkPPVkSELIEQV
0 1 K405‑sm QySkPPVkSELIEQV
0 1 S425‑p KPQQNGIsPRMFkAF
0 2 K430‑ub GIsPRMFkAFVSkSH
0 2 K435‑ub MFkAFVSkSHPEFSS
0 1 K511‑ub AMEAATNkDELIAYE
0 1 K565 WSSALQAKSAGVKTS
0 1 K570 QAKSAGVKTSRFASF
0 4 K586‑ub EYLVVQIkkFTFGLD
0 18 K587‑ub YLVVQIkkFTFGLDW
0 1 S630‑p EEELPDIsPPIVIPD
0 65 K640‑ub IVIPDDSkDRLMNQL
  USP13 iso2  
- gap
- gap
- gap
- gap
S39 REKVRGASGGALPKR
S49 ALPKRRNSKIFLDLD
T57 KIFLDLDTDDDLNSD
S63 DTDDDLNSDDYEYED
K111 SSKSPYRKQDPDTWE
T116 YRKQDPDTWENELPV
K125 ENELPVSKYANNLTQ
K194 MGYPLAVKLGTITPD
T199 AVKLGTITPDGADVY
K261 VIQESGTKLKPMYGP
K263 QESGTKLKPMYGPGY
K274 GPGYTGLKNLGNSCY
T315 DYSPLDPTQDFNTQM
T320 DPTQDFNTQMTKLGH
T323 QDFNTQMTKLGHGLL
S331 KLGHGLLSGQYSKPP
Y334 HGLLSGQYSKPPVKS
K336 LLSGQYSKPPVKSEL
K340 QYSKPPVKSELIEQV
K340 QYSKPPVKSELIEQV
S360 KPQQNGISPRMFKAF
K365 GISPRMFKAFVSKSH
K370 MFKAFVSKSHPEFSS
K446 AMEAATNKDELIAYE
K500 WSSALQAKSAGVKTS
K505 QAKSAGVKTSRFASF
K521 EYLVVQIKKFTFGLD
K522 YLVVQIKKFTFGLDW
S565 EEELPDISPPIVIPD
K575 IVIPDDSKDRLMNQL
  mouse

 
R4 ____MQRRGALFSVP
- gap
K16 SVPGGGGKMAAGDLG
T32 LLVPHMPTIRVPRSG
S102 REKVRGASGGALPKR
S112 ALPKRRNSKIFLDLD
M120 KIFLDLDMDDDLNSD
S126 DMDDDLNSDDYEYED
K174 SSKSPYRKQDPDTWE
T179 YRKQDPDTWENEVPV
K188 ENEVPVSKYANNLVQ
K257 MGYPLAVKLGTItPD
T262‑p AVKLGTItPDGADVY
K324‑ub VIQESGTkLKPMYGP
K326 QESGTkLKPMYGPGY
K337 GPGYTGLKNLGNSCY
T378 DYSPLDPTQDFNTQM
T383 DPTQDFNTQMTKLGH
T386 QDFNTQMTKLGHGLL
S394 KLGHGLLSGQYSKPP
Y397 HGLLSGQYSKPPVKS
K399 LLSGQYSKPPVKSEL
K403 QYSKPPVKSELIEQV
K403 QYSKPPVKSELIEQV
S423 KPQQNGISPRMFKAF
K428 GISPRMFKAFVSKSH
K433 MFKAFVSKSHPEFSS
K509 AMEAATNKDELITYE
K563‑ac WSSALQAkSAGVkTS
K568‑ac QAkSAGVkTSRFASF
K584 EYLVVQIKKFTFGLD
K585 YLVVQIKKFTFGLDW
S628 EEELPDISPPIVIPD
K638‑ub IVIPDDSkDRLMNQL
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.