Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Ubiquitin-conjugating enzyme E2 variant 1  

UniProtKB / Swiss-Prot ID :  UB2V1_HUMAN

Gene Name (Synonyms) : 
UBE2V1, CROC1, UBE2V, UEV1 P/OKcl.19  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. Note=Excluded from the nucleolus. 

Protein Function :  Has no ubiquitin ligase activity on its own. The UBE2V1- UBE2N heterodimer catalyzes the synthesis of non-canonical poly- ubiquitin chains that are linked through Lys-63. This type of poly-ubiquitination activates IKK and does not seem to involve protein degradation by the proteasome. Plays a role in the activation of NF-kappa-B mediated by IL1B, TNF, TRAF6 and TRAF2. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. 

Protein Sequence MAATTGSGVKVPRNFRLLEELEEGQKGVGDGTVSWGLEDDEDMTLTRWTGMIIGPPRTIYENRIYSLKIE...
Predicted Secondary Structure CCCCCCCCCHHHHHHHCCHHHHHHHHHHHHHHHHHHHHHHHHHCCHHHHHHHHHCCCEECCCCCCEEEEC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAATTG
---CCCCCC
17.32UniProtKB
Link-
86PhosphothreonineVRFVTKINM
CCCCHHHHH
24.40HPRD
Link
86PhosphothreonineVRFVTKINM
CCCCHHHHH
24.40SysPTM
Link
146Phosphoserine.GQCYSN
EEECCCCCC
43.63UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
UBE2N_HUMANENSP00000344166STRING
TRAF6_HUMANENSP00000344166STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures