Q6P073 (UB2J2_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 72.
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 J2 EC=6.3.2.19 Alternative name(s): Non-canonical ubiquitin-conjugating enzyme 2 Short name=NCUBE-2 | ||||
| Gene names |
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| Organism | Mus musculus (Mouse) | ||||
| 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 | 259 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the covalent attachment of ubiquitin to other proteins. Seems to function in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum (ERAD). Ref.1 Ref.2 Ref.5 In case of infection by the murid herpesvirus 4, its association with the viral E3 ligase K3 mediates ubiquitination of host surface class I (MHC-I) H-2D(b)/H2-D1 and H-2K(b)/H2-K1 molecules before they exit the endoplasmic reticulum, leading to their degradation by the ERAD system, thus blocking the immune detection of virus-infected cells. The complex formed with the murid herpesvirus 4 protein K3 mediates ubiquitination of lysine, as well as serine and threonine residues present in the cytoplasmic tail of surface class I molecules and promotes ubiquitination of hydroxylated serine or threonine residues via ester bonds instead of the classical isopeptide linkage. Ref.1 Ref.2 Ref.5 |
| Catalytic activity | ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine. |
| Pathway | |
| Subunit structure | Interacts with murid herpesvirus 4 protein K3 (mK3). Ref.5 |
| Subcellular location | Endoplasmic reticulum membrane; Single-pass type IV membrane protein Ref.1 Ref.2. |
| Sequence similarities | Belongs to the ubiquitin-conjugating enzyme family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Ubl conjugation pathway Unfolded protein response |
| Cellular component | Endoplasmic reticulum Membrane |
| Domain | Transmembrane Transmembrane helix |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Ligase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | response to unfolded protein Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membraneInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 259 | 259 | Ubiquitin-conjugating enzyme E2 J2 | PRO_0000082597 | |||||
Regions | |||||||||
| Topological domain | 1 – 226 | 226 | Cytoplasmic Potential | ||||||
| Transmembrane | 227 – 247 | 21 | Helical; Anchor for type IV membrane protein; Potential | ||||||
| Topological domain | 248 – 259 | 12 | Lumenal Potential | ||||||
Sites | |||||||||
| Active site | 94 | 1 | Glycyl thioester intermediate | ||||||
Experimental info | |||||||||
| Mutagenesis | 94 | 1 | C → S: Loss of catalytic activity. Slows down degradation of misfolded proteins from the ER. Ref.1 Ref.2 | ||||||
| Sequence conflict | 25 | 1 | K → T in BAC36280. Ref.3 | ||||||
| Sequence conflict | 32 | 1 | I → M in BAC36280. Ref.3 | ||||||
| Sequence conflict | 49 | 1 | R → G in BAC36280. Ref.3 | ||||||
| Sequence conflict | 80 | 1 | M → I in BAB26835. Ref.3 | ||||||
| Sequence conflict | 84 | 1 | N → H in BAB26835. Ref.3 | ||||||
| Sequence conflict | 87 | 1 | F → I in BAB26835. Ref.3 | ||||||
| Sequence conflict | 133 | 1 | E → K in BAB23421. Ref.3 | ||||||
| Sequence conflict | 150 | 1 | N → I in BAB26835. Ref.3 | ||||||
| Sequence conflict | 157 | 1 | C → G in BAC36280. Ref.3 | ||||||
| Sequence conflict | 162 | 1 | E → K in BAB23421. Ref.3 | ||||||
| Sequence conflict | 186 | 1 | L → W in BAC36280. Ref.3 | ||||||
| Sequence conflict | 217 – 218 | 2 | AG → GW in AAF21504. Ref.2 | ||||||
| Sequence conflict | 237 | 1 | F → L in BAC36280. Ref.3 | ||||||
| Sequence conflict | 246 | 1 | A → P in AAK52607. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Endoplasmic reticulum (ER)-associated degradation of T cell receptor subunits. Involvement of ER-associated ubiquitin-conjugating enzymes (E2s)." Tiwari S., Weissman A.M. J. Biol. Chem. 276:16193-16200(2001) [PubMed: 11278356] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF CYS-94, SUBCELLULAR LOCATION. Strain: C57BL/6J. Tissue: Fetus. |
| [2] | "A role for mammalian Ubc6 homologues in ER-associated protein degradation." Lenk U., Yu H., Walter J., Gelman M.S., Hartmann E., Kopito R.R., Sommer T. J. Cell Sci. 115:3007-3014(2002) [PubMed: 12082160] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF CYS-94, SUBCELLULAR LOCATION. |
| [3] | "The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Lung and Skin. |
| [4] | "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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Thymus. |
| [5] | "Ube2j2 ubiquitinates hydroxylated amino acids on ER-associated degradation substrates." Wang X., Herr R.A., Rabelink M., Hoeben R.C., Wiertz E.J., Hansen T.H. J. Cell Biol. 187:655-668(2009) [PubMed: 19951915] [Abstract] Cited for: FUNCTION IN CASE OF INFECTION BY THE MURID HERPESVIRUS 4, INTERACTION WITH MURID HERPESVIRUS 4 K3. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF296656 mRNA. Translation: AAK52607.1. U93242 mRNA. Translation: AAF21504.1. AK004626 mRNA. Translation: BAB23421.1. AK010302 mRNA. Translation: BAB26835.1. AK076265 mRNA. Translation: BAC36280.1. BC065779 mRNA. Translation: AAH65779.1. |
| IPI | IPI00420213. |
| RefSeq | NP_001034246.1. NM_001039157.1. NP_001034247.1. NM_001039158.1. NP_001034248.1. NM_001039159.1. NP_067377.4. NM_021402.5. |
| UniGene | Mm.371673. |
3D structure databases | |
| ProteinModelPortal | Q6P073. |
| SMR | Q6P073. Positions 11-171. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q6P073. |
Proteomic databases | |
| PRIDE | Q6P073. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000103175; ENSMUSP00000099464; ENSMUSG00000023286. ENSMUST00000105581; ENSMUSP00000101206; ENSMUSG00000023286. ENSMUST00000166489; ENSMUSP00000127712; ENSMUSG00000023286. |
| GeneID | 140499. |
| KEGG | mmu:140499. |
Organism-specific databases | |
| CTD | 118424. |
| MGI | MGI:2153608. Ube2j2. |
Phylogenomic databases | |
| eggNOG | roNOG14047. |
| GeneTree | ENSGT00530000063379. |
| HOVERGEN | HBG058434. |
| InParanoid | Q6P073. |
| OrthoDB | EOG4BP1CG. |
| PhylomeDB | Q6P073. |
Gene expression databases | |
| ArrayExpress | Q6P073. |
| Bgee | Q6P073. |
| Genevestigator | Q6P073. |
| GermOnline | ENSMUSG00000023286. Mus musculus. |
Family and domain databases | |
| InterPro | IPR000608. UBQ-conjugat_E2. IPR016135. UBQ-conjugating_enzyme/RWD. [Graphical view] |
| Gene3D | G3DSA:3.10.110.10. UBQ-conjugat_E2. 1 hit. |
| KO | K04554. |
| Pfam | PF00179. UQ_con. 1 hit. [Graphical view] |
| SUPFAM | SSF54495. UBQ-conjugat/RWD-like. 1 hit. |
| PROSITE | PS00183. UBIQUITIN_CONJUGAT_1. False negative. PS50127. UBIQUITIN_CONJUGAT_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 369836. |
| SOURCE | Search... |
Entry information
| Entry name | UB2J2_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q6P073 Secondary accession number(s): Q8C6A1 Q9QX58 | ||||||||
| 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