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 R2  

UniProtKB / Swiss-Prot ID :  UB2R2_HUMAN

Gene Name (Synonyms) : 
UBE2R2, CDC34B, UBC3B  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :  Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes monoubiquitination and 'Lys-48'-linked polyubiquitination. May be involved in degradation of katenin. 

Protein Sequence MAQQQMTSSQKALMLELKSLQEEPVEGFRITLVDESDLYNWEVAIFGPPNTLYEGGYFKAHIKFPIDYPY...
Predicted Secondary Structure CCCCCCCHHHHHHHHHHHHHHHCCCCEEEEECCCCCCCEEEEEEEECCCCCCCCCCEEEEEEECCCCCCC...
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.---MAQQQM
---CCCCCC
18.85UniProtKB
Link-
11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TSSQKALML
CHHHHHHHH
45.49Phosphositeplus
Link-
18Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)MLELKSLQE
HHHHHHHHH
39.48Phosphositeplus
Link-
63Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KAHIKFPID
EEEEECCCC
34.91Phosphositeplus
Link-
167Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EIIRKQVSA
HHHHHHCCH
44.64Phosphositeplus
Link-
173Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VSATKAEAE
CCHHHHHHH
43.90Phosphositeplus
Link-
233PhosphoserineDDDDSGNEE
CCCCCCCCC
50.98Phosphositeplus
Link-
233Phosphoserine (CK2_alpha)DDDDSGNEE
CCCCCCCCC
50.98PhosphoELM
Link-
233Phosphoserine (CSNK2A1)DDDDSGNEE
CCCCCCCCC
50.98HPRD
Link-
233Phosphoserine (CSNK2A2)DDDDSGNEE
CCCCCCCCC
50.98HPRD
Link-
233Phosphoserine; by CK2.DDDDSGNEE
CCCCCCCCC
50.98UniProtKB
Link-
238PhosphoserineGNEES
CCCCC
39.07HPRD
Link-
238PhosphoserineGNEES
CCCCC
39.07PhosphoELM
Link-
238PhosphoserineGNEES
CCCCC
39.07Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
FBW1A_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:15602HPRD12037680
UBA1_HUMANENSP00000263228STRING
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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
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"CK2-dependent phosphorylation of the E2 ubiquitin conjugating enzymeUBC3B induces its interaction with beta-TrCP and enhances beta-catenindegradation.";
Semplici F., Meggio F., Pinna L.A., Oliviero S.;
Oncogene 21:3978-3987(2002).
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, FUNCTION, INTERACTIONWITH BTRC, PHOSPHORYLATION AT SER-233, AND MUTAGENESIS OF CYS-93;LEU-97 AND SER-233.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures