Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q8CFI2

- UB2R1_MOUSE

UniProt

Q8CFI2 - UB2R1_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Ubiquitin-conjugating enzyme E2 R1

Gene

Cdc34

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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 ICERIIgamma and 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).By similarity

Catalytic activityi

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

Enzyme regulationi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei93 – 931Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. acid-amino acid ligase activity Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. ubiquitin-protein transferase activity Source: UniProtKB

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
  3. protein K48-linked ubiquitination Source: UniProtKB
  4. protein monoubiquitination Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Cell cycle, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Cdc34
Synonyms:Ubch3, Ube2r1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 10

Organism-specific databases

MGIiMGI:102657. Cdc34.

Subcellular locationi

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).By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 235235Ubiquitin-conjugating enzyme E2 R1PRO_0000082452Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei203 – 2031Phosphoserine; by CK2By similarity
Modified residuei221 – 2211Phosphoserine; by CK2By similarity
Modified residuei230 – 2301Phosphoserine; by CK2By similarity
Modified residuei232 – 2321Phosphothreonine; by CK2By similarity
Modified residuei235 – 2351Phosphoserine; by CK2By similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8CFI2.
PaxDbiQ8CFI2.
PRIDEiQ8CFI2.

PTM databases

PhosphoSiteiQ8CFI2.

Expressioni

Gene expression databases

BgeeiQ8CFI2.
CleanExiMM_CDC34.
GenevestigatoriQ8CFI2.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi229706. 2 interactions.
IntActiQ8CFI2. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ8CFI2.
SMRiQ8CFI2. Positions 4-212.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni190 – 23546SCF-bindingBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi200 – 23536Asp/Glu-rich (acidic)Add
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00730000110436.
HOGENOMiHOG000233454.
HOVERGENiHBG063308.
InParanoidiQ8CFI2.
KOiK02207.
OMAiRVNLVDE.
OrthoDBiEOG7VB2HT.
PhylomeDBiQ8CFI2.
TreeFamiTF101107.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8CFI2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MARPLVPSSQ KALLLELKGL QEEPVEGFRV TLVDEGDLYN WEVAIFGPPN
60 70 80 90 100
TYYEGGYFKA RLKFPIDYPY SPPAFRFLTK MWHPNIYETG DVCISILHPP
110 120 130 140 150
VDDPQSGELP SERWNPTQNV RTILLSVISL LNEPNTFSPA NVDASVMYRK
160 170 180 190 200
WKESKGKDRE YTDIIRKQVL GTKVDAERDG VKVPTTLAEY CVKTKAPAPD
210 220 230
EGSDLFYDDY YEDGEVEEAD SCFGDEEDDS GTEES
Length:235
Mass (Da):26,622
Last modified:March 1, 2003 - v1
Checksum:i3259FA0CD407E1E3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC039160 mRNA. Translation: AAH39160.1.
BC094502 mRNA. Translation: AAH94502.1.
CCDSiCCDS23983.1.
RefSeqiNP_808281.1. NM_177613.2.
XP_006513543.1. XM_006513480.1.
XP_006513544.1. XM_006513481.1.
UniGeneiMm.21981.

Genome annotation databases

EnsembliENSMUST00000020550; ENSMUSP00000020550; ENSMUSG00000020307.
ENSMUST00000166603; ENSMUSP00000128806; ENSMUSG00000020307.
GeneIDi216150.
KEGGimmu:216150.
UCSCiuc007fzi.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC039160 mRNA. Translation: AAH39160.1 .
BC094502 mRNA. Translation: AAH94502.1 .
CCDSi CCDS23983.1.
RefSeqi NP_808281.1. NM_177613.2.
XP_006513543.1. XM_006513480.1.
XP_006513544.1. XM_006513481.1.
UniGenei Mm.21981.

3D structure databases

ProteinModelPortali Q8CFI2.
SMRi Q8CFI2. Positions 4-212.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 229706. 2 interactions.
IntActi Q8CFI2. 3 interactions.

PTM databases

PhosphoSitei Q8CFI2.

Proteomic databases

MaxQBi Q8CFI2.
PaxDbi Q8CFI2.
PRIDEi Q8CFI2.

Protocols and materials databases

DNASUi 216150.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000020550 ; ENSMUSP00000020550 ; ENSMUSG00000020307 .
ENSMUST00000166603 ; ENSMUSP00000128806 ; ENSMUSG00000020307 .
GeneIDi 216150.
KEGGi mmu:216150.
UCSCi uc007fzi.1. mouse.

Organism-specific databases

CTDi 997.
MGIi MGI:102657. Cdc34.

Phylogenomic databases

eggNOGi COG5078.
GeneTreei ENSGT00730000110436.
HOGENOMi HOG000233454.
HOVERGENi HBG063308.
InParanoidi Q8CFI2.
KOi K02207.
OMAi RVNLVDE.
OrthoDBi EOG7VB2HT.
PhylomeDBi Q8CFI2.
TreeFami TF101107.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

ChiTaRSi CDC34. mouse.
NextBioi 375008.
PROi Q8CFI2.
SOURCEi Search...

Gene expression databases

Bgeei Q8CFI2.
CleanExi MM_CDC34.
Genevestigatori Q8CFI2.

Family and domain databases

Gene3Di 3.10.110.10. 1 hit.
InterProi IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view ]
Pfami PF00179. UQ_con. 1 hit.
[Graphical view ]
SUPFAMi SSF54495. SSF54495. 1 hit.
PROSITEi PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiUB2R1_MOUSE
AccessioniPrimary (citable) accession number: Q8CFI2
Secondary accession number(s): Q505K8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: March 1, 2003
Last modified: October 29, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3