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Q8CFI2 (UB2R1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-conjugating enzyme E2 R1

EC=6.3.2.19
Alternative name(s):
Ubiquitin-conjugating enzyme E2-32 kDa complementing
Ubiquitin-conjugating enzyme E2-CDC34
Ubiquitin-protein ligase R1
Gene names
Name:Cdc34
Synonyms:Ubch3, Ube2r1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length235 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Cooperates with the E2 UBCH5C and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Performs ubiquitin chain elongation building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. UBE2D3 acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin. Cooperates with the SCF(SKP2) E3 ligase complex to regulate cell proliferation through ubiquitination and degradation of MYBL2 and KIP1. Involved in ubiquitin conjugation and degradation of CREM isoform ICERIIgammaand ATF15 resulting in abrogation of ICERIIgamma- and ATF5-mediated repression of cAMP-induced transcription during both meiotic and mitotic cell cycles. Involved in the regulation of the cell cycle G2/M phase through its targeting of the WEE1 kinase for ubiquitination and degradation. Also involved in the degradation of beta-catenin By similarity. Ref.2

Catalytic activity

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.

Enzyme regulation

CDC34-catalyzed polyubiquitin chain assembly activity is stimulated by the conjugation of NEDD8 to the CUL1 SCF E3 ligase complex subunit By similarity.

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex. Identified in a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex together with HINT1 and RBX1. When cullin is neddylated, the interaction between the E2 and the SCF complex is strengthened By similarity. When phosphorylated, interacts with beta-TrCP (BTRC) By similarity. Interacts with casein kinase subunit CSNK2B By similarity. Ref.2

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Note: The phosphorylation of the C-terminal tail plays an important role in mediating nuclear localization. Colocalizes with beta-tubulin on mitotic spindles in anaphase By similarity.

Domain

The C-terminal acidic tail is required for nuclear localization and is involved in the binding to SCF E3 ligase complexes, and more specifically with the CUL1 subunit By similarity.

Post-translational modification

Phosphorylated by CK2. Phosphorylation of the C-terminal tail by CK2 controles the nuclear localization By similarity.

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 235235Ubiquitin-conjugating enzyme E2 R1
PRO_0000082452

Regions

Region190 – 23546SCF-binding By similarity
Compositional bias200 – 23536Asp/Glu-rich (acidic)

Sites

Active site931Glycyl thioester intermediate By similarity

Amino acid modifications

Modified residue2031Phosphoserine; by CK2 By similarity
Modified residue2211Phosphoserine; by CK2 By similarity
Modified residue2301Phosphoserine; by CK2 By similarity
Modified residue2321Phosphothreonine; by CK2 By similarity
Modified residue2351Phosphoserine; by CK2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8CFI2 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 3259FA0CD407E1E3

FASTA23526,622
        10         20         30         40         50         60 
MARPLVPSSQ KALLLELKGL QEEPVEGFRV TLVDEGDLYN WEVAIFGPPN TYYEGGYFKA 

        70         80         90        100        110        120 
RLKFPIDYPY SPPAFRFLTK MWHPNIYETG DVCISILHPP VDDPQSGELP SERWNPTQNV 

       130        140        150        160        170        180 
RTILLSVISL LNEPNTFSPA NVDASVMYRK WKESKGKDRE YTDIIRKQVL GTKVDAERDG 

       190        200        210        220        230 
VKVPTTLAEY CVKTKAPAPD EGSDLFYDDY YEDGEVEEAD SCFGDEEDDS GTEES 

« Hide

References

« Hide 'large scale' references
[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: 129 and C57BL/6J.
Tissue: Mammary tumor.
[2]"Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of I kappa B alpha."
Tan P., Fuchs S.Y., Chen A., Wu K., Gomez C., Ronai Z., Pan Z.-Q.
Mol. Cell 3:527-533(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SCF COMPLEX, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC039160 mRNA. Translation: AAH39160.1.
BC094502 mRNA. Translation: AAH94502.1.
RefSeqNP_808281.1. NM_177613.2.
XP_006513543.1. XM_006513480.1.
XP_006513544.1. XM_006513481.1.
UniGeneMm.21981.

3D structure databases

ProteinModelPortalQ8CFI2.
SMRQ8CFI2. Positions 4-212.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid229706. 2 interactions.
IntActQ8CFI2. 3 interactions.

PTM databases

PhosphoSiteQ8CFI2.

Proteomic databases

PaxDbQ8CFI2.
PRIDEQ8CFI2.

Protocols and materials databases

DNASU216150.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020550; ENSMUSP00000020550; ENSMUSG00000020307.
ENSMUST00000166603; ENSMUSP00000128806; ENSMUSG00000020307.
GeneID216150.
KEGGmmu:216150.
UCSCuc007fzi.1. mouse.

Organism-specific databases

CTD997.
MGIMGI:102657. Cdc34.

Phylogenomic databases

eggNOGCOG5078.
GeneTreeENSGT00730000110436.
HOGENOMHOG000233454.
HOVERGENHBG063308.
InParanoidQ8CFI2.
KOK02207.
OMARVNLVDE.
OrthoDBEOG7VB2HT.
PhylomeDBQ8CFI2.
TreeFamTF101107.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

BgeeQ8CFI2.
CleanExMM_CDC34.
GenevestigatorQ8CFI2.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCDC34. mouse.
NextBio375008.
PROQ8CFI2.
SOURCESearch...

Entry information

Entry nameUB2R1_MOUSE
AccessionPrimary (citable) accession number: Q8CFI2
Secondary accession number(s): Q505K8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot