UB2G1_HUMAN - dbPTM
UB2G1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UB2G1_HUMAN
UniProt AC P62253
Protein Name Ubiquitin-conjugating enzyme E2 G1
Gene Name UBE2G1
Organism Homo sapiens (Human).
Sequence Length 170
Subcellular Localization
Protein Description Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. May be involved in degradation of muscle-specific proteins. Mediates polyubiquitination of CYP3A4..
Protein Sequence MTELQSALLLRRQLAELNKNPVEGFSAGLIDDNDLYRWEVLIIGPPDTLYEGGVFKAHLTFPKDYPLRPPKMKFITEIWHPNVDKNGDVCISILHEPGEDKYGYEKPEERWLPIHTVETIMISVISMLADPNGDSPANVDAAKEWREDRNGEFKRKVARCVRKSQETAFE
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-------MTELQSAL
-------CCHHHHHH
6.2422814378
2Acetylation------MTELQSALL
------CCHHHHHHH
45.4622223895
2Phosphorylation------MTELQSALL
------CCHHHHHHH
45.4620068231
6Phosphorylation--MTELQSALLLRRQ
--CCHHHHHHHHHHH
33.2420068231
19UbiquitinationRQLAELNKNPVEGFS
HHHHHHCCCCCCCCC
75.22-
56UbiquitinationLYEGGVFKAHLTFPK
EEECCEEEEEEECCC
32.2733845483
63UbiquitinationKAHLTFPKDYPLRPP
EEEEECCCCCCCCCC
66.7523000965
65PhosphorylationHLTFPKDYPLRPPKM
EEECCCCCCCCCCCC
15.4217384208
71UbiquitinationDYPLRPPKMKFITEI
CCCCCCCCCCEEEEE
58.3623000965
73UbiquitinationPLRPPKMKFITEIWH
CCCCCCCCEEEEECC
39.4823000965
76PhosphorylationPPKMKFITEIWHPNV
CCCCCEEEEECCCCC
25.26-
85UbiquitinationIWHPNVDKNGDVCIS
ECCCCCCCCCCEEEE
59.5521963094
101UbiquitinationLHEPGEDKYGYEKPE
EECCCCCCCCCCCCH
35.9521963094
102PhosphorylationHEPGEDKYGYEKPEE
ECCCCCCCCCCCCHH
36.9428796482
104PhosphorylationPGEDKYGYEKPEERW
CCCCCCCCCCCHHHC
20.0728796482
106UbiquitinationEDKYGYEKPEERWLP
CCCCCCCCCHHHCCC
49.6027667366
163UbiquitinationKVARCVRKSQETAFE
HHHHHHHHHHHHHCC
35.7724816145

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
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:20804422

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UB2G1_HUMAN !!

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 UB2G1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HOIL1_HUMANRBCK1physical
19549727
AMFR_HUMANAMFRphysical
19560420
A4_HUMANAPPphysical
21832049
UBP8_HUMANUSP8physical
22939629
WWP2_HUMANWWP2physical
22939629
UB2G1_HUMANUBE2G1physical
20061386

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UB2G1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides.";
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.;
Nat. Biotechnol. 21:566-569(2003).
Cited for: PROTEIN SEQUENCE OF 2-11, AND ACETYLATION AT THR-2.

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