Q8CFI2 (UB2R1_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 89.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | 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 names |
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| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 235 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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 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. 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 | |
| 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. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 235 | 235 | Ubiquitin-conjugating enzyme E2 R1 | PRO_0000082452 | |||||
Regions | |||||||||
| Region | 190 – 235 | 46 | SCF-binding By similarity | ||||||
| Compositional bias | 200 – 235 | 36 | Asp/Glu-rich (acidic) | ||||||
Sites | |||||||||
| Active site | 93 | 1 | Glycyl thioester intermediate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 203 | 1 | Phosphoserine; by CK2 By similarity | ||||||
| Modified residue | 221 | 1 | Phosphoserine; by CK2 By similarity | ||||||
| Modified residue | 230 | 1 | Phosphoserine; by CK2 By similarity | ||||||
| Modified residue | 232 | 1 | Phosphothreonine; by CK2 By similarity | ||||||
| Modified residue | 235 | 1 | Phosphoserine; by CK2 By similarity | ||||||
Sequences
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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. |
| IPI | IPI00229310. |
| RefSeq | NP_808281.1. NM_177613.2. |
| UniGene | Mm.21981. |
3D structure databases | |
| ProteinModelPortal | Q8CFI2. |
| SMR | Q8CFI2. Positions 7-183. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q8CFI2. 3 interactions. |
PTM databases | |
| PhosphoSite | Q8CFI2. |
Proteomic databases | |
| PaxDb | Q8CFI2. |
| PRIDE | Q8CFI2. |
Protocols and materials databases | |
| DNASU | 216150. |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000020550; ENSMUSP00000020550; ENSMUSG00000020307. ENSMUST00000166603; ENSMUSP00000128806; ENSMUSG00000020307. |
| GeneID | 216150. |
| KEGG | mmu:216150. |
Organism-specific databases | |
| CTD | 997. |
| MGI | MGI:102657. Cdc34. |
Phylogenomic databases | |
| eggNOG | COG5078. |
| GeneTree | ENSGT00530000063512. |
| HOGENOM | HOG000233454. |
| HOVERGEN | HBG063308. |
| InParanoid | Q8CFI2. |
| KO | K02207. |
| OMA | EYCIKSK. |
| OrthoDB | EOG4DBTFM. |
Enzyme and pathway databases | |
| UniPathway | UPA00143. |
Gene expression databases | |
| Bgee | Q8CFI2. |
| CleanEx | MM_CDC34. |
| Genevestigator | Q8CFI2. |
| GermOnline | ENSMUSG00000020307. Mus musculus. |
Family and domain databases | |
| Gene3D | 3.10.110.10. 1 hit. |
| InterPro | IPR000608. UBQ-conjugat_E2. IPR023313. UBQ-conjugating_AS. IPR016135. UBQ-conjugating_enzyme/RWD. [Graphical view] |
| Pfam | PF00179. UQ_con. 1 hit. [Graphical view] |
| SUPFAM | SSF54495. UBQ-conjugat/RWD-like. 1 hit. |
| PROSITE | PS00183. UBIQUITIN_CONJUGAT_1. 1 hit. PS50127. UBIQUITIN_CONJUGAT_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChiTaRS | CDC34. mouse. |
| NextBio | 375008. |
| SOURCE | Search... |
Entry information
| Entry name | UB2R1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q8CFI2 Secondary accession number(s): Q505K8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
