UBC12_MOUSE - dbPTM
UBC12_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBC12_MOUSE
UniProt AC P61082
Protein Name NEDD8-conjugating enzyme Ubc12
Gene Name Ube2m
Organism Mus musculus (Mouse).
Sequence Length 183
Subcellular Localization
Protein Description Accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX1, but not RBX2, suggests that the RBX1-UBE2M complex neddylates specific target proteins, such as CUL1, CUL2, CUL3 and CUL4. Involved in cell proliferation (By similarity)..
Protein Sequence MIKLFSLKQQKKEEESAGGTKGSSKKASAAQLRIQKDINELNLPKTCDISFSDPDDLLNFKLVICPDEGFYKSGKFVFSFKVGQGYPHDPPKVKCETMVYHPNIDLEGNVCLNILREDWKPVLTINSIIYGLQYLFLEPNPEDPLNKEAAEVLQNNRRLFEQNVQRSMRGGYIGSTYFERCLK
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
1Acetylation-------MIKLFSLK
-------CCCCCCCC
5.71-
3Acetylation-----MIKLFSLKQQ
-----CCCCCCCCHH
42.0322826441
3Ubiquitination-----MIKLFSLKQQ
-----CCCCCCCCHH
42.0322790023
6Phosphorylation--MIKLFSLKQQKKE
--CCCCCCCCHHHHH
45.1322942356
8UbiquitinationMIKLFSLKQQKKEEE
CCCCCCCCHHHHHHH
49.8622790023
8AcetylationMIKLFSLKQQKKEEE
CCCCCCCCHHHHHHH
49.8622826441
28PhosphorylationKGSSKKASAAQLRIQ
CCCCHHHHHHHHHHH
32.7730352176
36UbiquitinationAAQLRIQKDINELNL
HHHHHHHHCHHHCCC
59.2022790023
36AcetylationAAQLRIQKDINELNL
HHHHHHHHCHHHCCC
59.2022826441
45UbiquitinationINELNLPKTCDISFS
HHHCCCCCCCCCCCC
66.02-
50PhosphorylationLPKTCDISFSDPDDL
CCCCCCCCCCCHHHH
12.8726745281
52PhosphorylationKTCDISFSDPDDLLN
CCCCCCCCCHHHHCC
41.2526745281
72UbiquitinationCPDEGFYKSGKFVFS
CCCCCCCCCCEEEEE
50.9322790023
75UbiquitinationEGFYKSGKFVFSFKV
CCCCCCCEEEEEEEE
45.5022790023
92UbiquitinationGYPHDPPKVKCETMV
CCCCCCCCCEEEEEE
60.77-
97PhosphorylationPPKVKCETMVYHPNI
CCCCEEEEEEECCCC
22.7730635358
100PhosphorylationVKCETMVYHPNIDLE
CEEEEEEECCCCCCC
10.7530635358
169MethylationQNVQRSMRGGYIGST
HHHHHHHCCCCCCHH
36.3124129315
169Asymmetric dimethylarginineQNVQRSMRGGYIGST
HHHHHHHCCCCCCHH
36.31-
172PhosphorylationQRSMRGGYIGSTYFE
HHHHCCCCCCHHHHH
12.6325367039
175PhosphorylationMRGGYIGSTYFERCL
HCCCCCCHHHHHHHC
15.4625367039
177PhosphorylationGGYIGSTYFERCLK-
CCCCCHHHHHHHCC-
12.7329514104
181GlutathionylationGSTYFERCLK-----
CHHHHHHHCC-----
4.4724333276

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 UBC12_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
1MAcetylation

-

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 UBC12_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CPNE1_HUMANCPNE1physical
12522145
CPNE4_HUMANCPNE4physical
12522145

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBC12_MOUSE

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Related Literatures of Post-Translational Modification

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