Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
UCHL3 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
UCHL3 Deubiquitinating enzyme (DUB) that controls levels of cellular ubiquitin through processing of ubiquitin precursors and ubiquitinated proteins. Thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8. Has a 10-fold preference for Arg and Lys at position P3. Deubiquitinates ENAC in apical compartments, thereby regulating apical membrane recycling. Indirectly increases the phosphorylation of IGFIR, AKT and FOXO1 and promotes insulin- signaling and insulin-induced adipogenesis. Required for stress- response retinal, skeletal muscle and germ cell maintenance. May be involved in working memory. Can hydrolyze UBB(+1), a mutated form of ubiquitin which is not effectively degraded by the proteasome and is associated with neurogenerative disorders. Preferentially binds diubiquitin; the interaction does not hydrolyze diubiquitin but, in vitro, inhibits the hydrolyzing activity on other substrates. Highly expressed in heart, skeletal muscle, and testis. Inhibited by monoubiquitin and diubiquitin. Belongs to the peptidase C12 family. Note: This description may include information from UniProtKB.
Protein type: EC 3.4.19.12; Ubiquitin conjugating system; Protease
Cellular Component: cytoplasm; nucleus
Molecular Function: ubiquitin thiolesterase activity; peptidase activity; ubiquitin binding; protein binding; ubiquitin-specific protease activity
Biological Process: ubiquitin-dependent protein catabolic process; protein catabolic process
Reference #:  P15374 (UniProtKB)
Alt. Names/Synonyms: ubiquitin carboxyl-terminal esterase L3 (ubiquitin thiolesterase); Ubiquitin carboxyl-terminal hydrolase isozyme L3; Ubiquitin thioesterase L3; ubiquitin thiolesterase; UCH-L3; UCHL3
Gene Symbols: UCHL3
Molecular weight: 26,183 Da
Basal Isoelectric point: 4.84  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

UCHL3

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho3D  |  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


 SS 

SS: 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.


 MS 

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


       human

 
0 5 K61-u LLFPITEkYEVFRTE
0 2 S75-p EEEEKIKsQGQDVTS
0 2 K121-u ESGSTLKkFLEESVS
0 11 S130-p LEESVSMsPEERARY
0 1 R136 MsPEERARYLENyDA
0 4 Y141-p RARYLENyDAIRVTH
0 1 S151-p IRVTHETsAHEGQTE
0 15 K165-u EAPSIDEkVDLHFIA
0 1 K210-u EDAIEVCkKFMERDP
  mouse

 
K61-u LLFPITEkYEVFRTE
S75 EEEEKIKSQGQDVTS
K121-u ESGSTLKkFLEESVS
S130-p LEESVSMsPEERAkF
K136-u MsPEERAkFLENYDA
Y141 RAkFLENYDAIRVTH
S151 IRVTHETSAHEGQTE
K165-u EAPSIDEkVDLHFIA
K210 EDAIEVCKKFMERDP
  rat

 
K61 LLFPITEKYEVFRTE
S75 EEEEKIKSQGQDVTS
K121 ESGSALKKFLEESVA
S130 LEESVAMSPEERARH
R136 MSPEERARHLENYDA
Y141 RARHLENYDAIRVTH
S151 IRVTHETSAHEGQTE
K165 EAPSIDEKVDLHFIA
K210 EDAIEVCKKFMERDP
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.