UCHL3_MOUSE - dbPTM
UCHL3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UCHL3_MOUSE
UniProt AC Q9JKB1
Protein Name Ubiquitin carboxyl-terminal hydrolase isozyme L3
Gene Name Uchl3
Organism Mus musculus (Mouse).
Sequence Length 230
Subcellular Localization Cytoplasm .
Protein Description 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", and exhibits a preference towards 'Lys-48'-linked ubiquitin chains. 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..
Protein Sequence MEGQRWLPLEANPEVTNQFLKQLGLHPNWQFVDVYGMEPELLSMVPRPVCAVLLLFPITEKYEVFRTEEEEKIKSQGQDVTSSVYFMKQTISNACGTIGLIHAIANNKDKMHFESGSTLKKFLEESVSMSPEERAKFLENYDAIRVTHETSAHEGQTEAPSIDEKVDLHFIALVHVDGHLYELDGRKPFPINHGKTSDETLLEDAIEVCKKFMERDPDELRFNAIALSAA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
61UbiquitinationLLFPITEKYEVFRTE
HHEECCCCEEECCCH
37.75-
74UbiquitinationTEEEEKIKSQGQDVT
CHHHHHHHHCCCCHH
48.0422790023
95GlutathionylationKQTISNACGTIGLIH
HHHHHHHHHHHHHHH
6.0524333276
95S-palmitoylationKQTISNACGTIGLIH
HHHHHHHHHHHHHHH
6.0528680068
115PhosphorylationKDKMHFESGSTLKKF
CCCCCCCCCHHHHHH
36.7828464351
121UbiquitinationESGSTLKKFLEESVS
CCCHHHHHHHHHHHC
59.2922790023
126PhosphorylationLKKFLEESVSMSPEE
HHHHHHHHHCCCHHH
15.3226239621
128PhosphorylationKFLEESVSMSPEERA
HHHHHHHCCCHHHHH
23.8726239621
130PhosphorylationLEESVSMSPEERAKF
HHHHHCCCHHHHHHH
22.9627742792
136UbiquitinationMSPEERAKFLENYDA
CCHHHHHHHHHHCCE
57.6222790023
161PhosphorylationEGQTEAPSIDEKVDL
CCCCCCCCCCCCCCE
50.1226824392
165UbiquitinationEAPSIDEKVDLHFIA
CCCCCCCCCCEEEEE
36.98-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of UCHL3_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UCHL3_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of UCHL3_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of UCHL3_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UCHL3_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND MASSSPECTROMETRY.

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