UCHL1_MOUSE - dbPTM
UCHL1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UCHL1_MOUSE
UniProt AC Q9R0P9
Protein Name Ubiquitin carboxyl-terminal hydrolase isozyme L1
Gene Name Uchl1
Organism Mus musculus (Mouse).
Sequence Length 223
Subcellular Localization Cytoplasm . Endoplasmic reticulum membrane
Lipid-anchor.
Protein Description Ubiquitin-protein hydrolase involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. Also binds to free monoubiquitin and may prevent its degradation in lysosomes. The homodimer may have ATP-independent ubiquitin ligase activity..
Protein Sequence MQLKPMEINPEMLNKVLAKLGVAGQWRFADVLGLEEETLGSVPSPACALLLLFPLTAQHENFRKKQIEELKGQEVSPKVYFMKQTIGNSCGTIGLIHAVANNQDKLEFEDGSVLKQFLSETEKLSPEDRAKCFEKNEAIQAAHDSVAQEGQCRVDDKVNFHFILFNNVDGHLYELDGRMPFPVNHGASSEDSLLQDAAKVCREFTEREQGEVRFSAVALCKAA
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
4Ubiquitination----MQLKPMEINPE
----CCCCCCCCCHH
25.9822790023
15UbiquitinationINPEMLNKVLAKLGV
CCHHHHHHHHHHHCC
34.3622790023
19UbiquitinationMLNKVLAKLGVAGQW
HHHHHHHHHCCCCCC
41.4322790023
19AcetylationMLNKVLAKLGVAGQW
HHHHHHHHHCCCCCC
41.4322826441
65UbiquitinationQHENFRKKQIEELKG
CCCCHHHHHHHHHCC
52.8627667366
71UbiquitinationKKQIEELKGQEVSPK
HHHHHHHCCCCCCHH
62.9222790023
76PhosphorylationELKGQEVSPKVYFMK
HHCCCCCCHHHEEEE
20.4628066266
78UbiquitinationKGQEVSPKVYFMKQT
CCCCCCHHHEEEECC
41.9022790023
90S-palmitoylationKQTIGNSCGTIGLIH
ECCCCCCHHHHHHHH
6.9028680068
90S-nitrosylationKQTIGNSCGTIGLIH
ECCCCCCHHHHHHHH
6.9024895380
119PhosphorylationSVLKQFLSETEKLSP
HHHHHHHHHHHCCCH
43.7028066266
121PhosphorylationLKQFLSETEKLSPED
HHHHHHHHHCCCHHH
34.7428066266
123UbiquitinationQFLSETEKLSPEDRA
HHHHHHHCCCHHHHH
62.7822790023
123AcetylationQFLSETEKLSPEDRA
HHHHHHHCCCHHHHH
62.7822826441
125PhosphorylationLSETEKLSPEDRAKC
HHHHHCCCHHHHHHH
36.9922324799
135UbiquitinationDRAKCFEKNEAIQAA
HHHHHHHHHHHHHHH
39.5722790023
135AcetylationDRAKCFEKNEAIQAA
HHHHHHHHHHHHHHH
39.5722826441
145PhosphorylationAIQAAHDSVAQEGQC
HHHHHCHHHHHCCCC
14.9729899451
152S-nitrosocysteineSVAQEGQCRVDDKVN
HHHHCCCCCCCCCEE
7.23-
152S-nitrosylationSVAQEGQCRVDDKVN
HHHHCCCCCCCCCEE
7.2324895380
157UbiquitinationGQCRVDDKVNFHFIL
CCCCCCCCEEEEEEE
34.32-
188PhosphorylationFPVNHGASSEDSLLQ
CCCCCCCCCHHHHHH
38.5625293948
189PhosphorylationPVNHGASSEDSLLQD
CCCCCCCCHHHHHHH
44.9125293948
192PhosphorylationHGASSEDSLLQDAAK
CCCCCHHHHHHHHHH
27.2525293948
199AcetylationSLLQDAAKVCREFTE
HHHHHHHHHHHHHHH
43.5222826441
220FarnesylationRFSAVALCKAA----
EEEEEHHHHCC----
1.71-
220S-nitrosylationRFSAVALCKAA----
EEEEEHHHHCC----
1.7124895380

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 UCHL1_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UCHL1_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 UCHL1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBC_MOUSEUbcphysical
12913066
PTOV1_MOUSEPtov1physical
21678139
CDK1_MOUSECdk1physical
21678139
TBA1A_MOUSETuba1aphysical
18250096
CSN5_MOUSECops5physical
19377830

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UCHL1_MOUSE

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Related Literatures of Post-Translational Modification

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