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Protein

Ubiquitin-conjugating enzyme E2 J2

Gene

Ube2j2

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

Functioni

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).
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.

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei94 – 941Glycyl thioester intermediate

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ligase activity Source: UniProtKB-KW
  3. ubiquitin conjugating enzyme activity Source: MGI
  4. ubiquitin-like protein transferase activity Source: GO_Central
  5. ubiquitin protein ligase activity Source: GO_Central
  6. ubiquitin protein ligase binding Source: GO_Central

GO - Biological processi

  1. ER-associated ubiquitin-dependent protein catabolic process Source: GO_Central
  2. protein polyubiquitination Source: GO_Central
  3. response to unfolded protein Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway, Unfolded protein response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
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 namesi
Name:Ube2j2
Synonyms:Ncube2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:2153608. Ube2j2.

Subcellular locationi

  1. Endoplasmic reticulum membrane 2 Publications; Single-pass type IV membrane protein 2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 226226CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei227 – 24721Helical; Anchor for type IV membrane proteinSequence AnalysisAdd
BLAST
Topological domaini248 – 25912LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum Source: MGI
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi94 – 941C → S: Loss of catalytic activity. Slows down degradation of misfolded proteins from the ER. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 259259Ubiquitin-conjugating enzyme E2 J2PRO_0000082597Add
BLAST

Proteomic databases

MaxQBiQ6P073.
PaxDbiQ6P073.
PRIDEiQ6P073.

PTM databases

PhosphoSiteiQ6P073.

Expressioni

Gene expression databases

BgeeiQ6P073.
ExpressionAtlasiQ6P073. baseline.
GenevestigatoriQ6P073.

Interactioni

Subunit structurei

Interacts with murid herpesvirus 4 protein K3 (mK3).1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ6P073.
SMRiQ6P073. Positions 11-171.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00530000063379.
HOGENOMiHOG000170330.
HOVERGENiHBG058434.
InParanoidiQ6P073.
KOiK04554.
OrthoDBiEOG780RNH.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q6P073-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNNSNKRAP TTATQRLKQD YLRIKKDPVP YICAEPLPSN ILEWHYVVRG
60 70 80 90 100
PEMTPYEGGY YHGKLIFPRE FPFKPPSIYM ITPNGRFKCN TRLCLSITDF
110 120 130 140 150
HPDTWNPAWS VSTILTGLLS FMVEKGPTLG SIETSDFTKK QLAAQSLVFN
160 170 180 190 200
LKDKVFCELF PEVVEEIKQK QKAQDELSNR PQNLPLPDVV PDGELHRGQH
210 220 230 240 250
GIQLLNGHAP AAGPNLAGLP QANRHHGLLG GALANLFVIV GFAAFAYTVK

YVLRSIAQE
Length:259
Mass (Da):28,954
Last modified:July 5, 2004 - v1
Checksum:i0C539BC0ACEAC7C7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251K → T in BAC36280 (PubMed:16141072).Curated
Sequence conflicti32 – 321I → M in BAC36280 (PubMed:16141072).Curated
Sequence conflicti49 – 491R → G in BAC36280 (PubMed:16141072).Curated
Sequence conflicti80 – 801M → I in BAB26835 (PubMed:16141072).Curated
Sequence conflicti84 – 841N → H in BAB26835 (PubMed:16141072).Curated
Sequence conflicti87 – 871F → I in BAB26835 (PubMed:16141072).Curated
Sequence conflicti133 – 1331E → K in BAB23421 (PubMed:16141072).Curated
Sequence conflicti150 – 1501N → I in BAB26835 (PubMed:16141072).Curated
Sequence conflicti157 – 1571C → G in BAC36280 (PubMed:16141072).Curated
Sequence conflicti162 – 1621E → K in BAB23421 (PubMed:16141072).Curated
Sequence conflicti186 – 1861L → W in BAC36280 (PubMed:16141072).Curated
Sequence conflicti217 – 2182AG → GW in AAF21504 (PubMed:12082160).Curated
Sequence conflicti237 – 2371F → L in BAC36280 (PubMed:16141072).Curated
Sequence conflicti246 – 2461A → P in AAK52607 (PubMed:11278356).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19051.1.
RefSeqiNP_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.
UniGeneiMm.371673.

Genome annotation databases

EnsembliENSMUST00000103175; ENSMUSP00000099464; ENSMUSG00000023286.
ENSMUST00000105581; ENSMUSP00000101206; ENSMUSG00000023286.
ENSMUST00000166489; ENSMUSP00000127712; ENSMUSG00000023286.
GeneIDi140499.
KEGGimmu:140499.
UCSCiuc007ubh.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19051.1.
RefSeqiNP_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.
UniGeneiMm.371673.

3D structure databases

ProteinModelPortaliQ6P073.
SMRiQ6P073. Positions 11-171.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ6P073.

Proteomic databases

MaxQBiQ6P073.
PaxDbiQ6P073.
PRIDEiQ6P073.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000103175; ENSMUSP00000099464; ENSMUSG00000023286.
ENSMUST00000105581; ENSMUSP00000101206; ENSMUSG00000023286.
ENSMUST00000166489; ENSMUSP00000127712; ENSMUSG00000023286.
GeneIDi140499.
KEGGimmu:140499.
UCSCiuc007ubh.1. mouse.

Organism-specific databases

CTDi118424.
MGIiMGI:2153608. Ube2j2.

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00530000063379.
HOGENOMiHOG000170330.
HOVERGENiHBG058434.
InParanoidiQ6P073.
KOiK04554.
OrthoDBiEOG780RNH.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

NextBioi369836.
PROiQ6P073.
SOURCEiSearch...

Gene expression databases

BgeeiQ6P073.
ExpressionAtlasiQ6P073. baseline.
GenevestigatoriQ6P073.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiUB2J2_MOUSE
AccessioniPrimary (citable) accession number: Q6P073
Secondary accession number(s): Q8C6A1
, Q91Y64, Q9CWY5, Q9DC18, Q9QX58
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: July 5, 2004
Last modified: April 1, 2015
This is version 97 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.