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Q6P073 (UB2J2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 89. 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 J2

EC=6.3.2.19
Alternative name(s):
Non-canonical ubiquitin-conjugating enzyme 2
Short name=NCUBE-2
Gene names
Name:Ube2j2
Synonyms:Ncube2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length259 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Protein modification; protein ubiquitination.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 259259Ubiquitin-conjugating enzyme E2 J2
PRO_0000082597

Regions

Topological domain1 – 226226Cytoplasmic Potential
Transmembrane227 – 24721Helical; Anchor for type IV membrane protein; Potential
Topological domain248 – 25912Lumenal Potential

Sites

Active site941Glycyl thioester intermediate

Experimental info

Mutagenesis941C → S: Loss of catalytic activity. Slows down degradation of misfolded proteins from the ER. Ref.1 Ref.2
Sequence conflict251K → T in BAC36280. Ref.3
Sequence conflict321I → M in BAC36280. Ref.3
Sequence conflict491R → G in BAC36280. Ref.3
Sequence conflict801M → I in BAB26835. Ref.3
Sequence conflict841N → H in BAB26835. Ref.3
Sequence conflict871F → I in BAB26835. Ref.3
Sequence conflict1331E → K in BAB23421. Ref.3
Sequence conflict1501N → I in BAB26835. Ref.3
Sequence conflict1571C → G in BAC36280. Ref.3
Sequence conflict1621E → K in BAB23421. Ref.3
Sequence conflict1861L → W in BAC36280. Ref.3
Sequence conflict217 – 2182AG → GW in AAF21504. Ref.2
Sequence conflict2371F → L in BAC36280. Ref.3
Sequence conflict2461A → P in AAK52607. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q6P073 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 0C539BC0ACEAC7C7

FASTA25928,954
        10         20         30         40         50         60 
MSNNSNKRAP TTATQRLKQD YLRIKKDPVP YICAEPLPSN ILEWHYVVRG PEMTPYEGGY 

        70         80         90        100        110        120 
YHGKLIFPRE FPFKPPSIYM ITPNGRFKCN TRLCLSITDF HPDTWNPAWS VSTILTGLLS 

       130        140        150        160        170        180 
FMVEKGPTLG SIETSDFTKK QLAAQSLVFN LKDKVFCELF PEVVEEIKQK QKAQDELSNR 

       190        200        210        220        230        240 
PQNLPLPDVV PDGELHRGQH GIQLLNGHAP AAGPNLAGLP QANRHHGLLG GALANLFVIV 

       250 
GFAAFAYTVK YVLRSIAQE 

« Hide

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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.
RefSeqNP_001034246.1. NM_001039157.2.
NP_001034247.1. NM_001039158.2.
NP_001034248.1. NM_001039159.2.
NP_001271241.1. NM_001284312.1.
NP_001271243.1. NM_001284314.1.
NP_067377.4. NM_021402.6.
UniGeneMm.371673.

3D structure databases

ProteinModelPortalQ6P073.
SMRQ6P073. Positions 11-171.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ6P073.

Proteomic databases

PaxDbQ6P073.
PRIDEQ6P073.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000103175; ENSMUSP00000099464; ENSMUSG00000023286.
ENSMUST00000105581; ENSMUSP00000101206; ENSMUSG00000023286.
ENSMUST00000166489; ENSMUSP00000127712; ENSMUSG00000023286.
GeneID140499.
KEGGmmu:140499.
UCSCuc007ubh.1. mouse.

Organism-specific databases

CTD118424.
MGIMGI:2153608. Ube2j2.

Phylogenomic databases

eggNOGCOG5078.
GeneTreeENSGT00530000063379.
HOGENOMHOG000170330.
HOVERGENHBG058434.
InParanoidQ6P073.
KOK04554.
OrthoDBEOG780RNH.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

BgeeQ6P073.
GenevestigatorQ6P073.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio369836.
PROQ6P073.
SOURCESearch...

Entry information

Entry nameUB2J2_MOUSE
AccessionPrimary (citable) accession number: Q6P073
Secondary accession number(s): Q8C6A1 expand/collapse secondary AC list , Q91Y64, Q9CWY5, Q9DC18, Q9QX58
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 89 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