Skip Header

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

Q6P073

- UB2J2_MOUSE

UniProt

Q6P073 - UB2J2_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 J2

Gene

Ube2j2

Organism
Mus musculus (Mouse)
Status
Reviewed - 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. acid-amino acid ligase activity Source: InterPro
  2. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. protein ubiquitination Source: UniProtKB-UniPathway
  2. 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: Chromosome 4

Organism-specific databases

MGIiMGI:2153608. Ube2j2.

Subcellular locationi

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

GO - Cellular componenti

  1. endoplasmic reticulum Source: MGI
  2. 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...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 226226CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini248 – 25912LumenalSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei227 – 24721Helical; Anchor for type IV membrane proteinSequence AnalysisAdd
BLAST

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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS19051.1.
RefSeqi NP_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.
UniGenei Mm.371673.

3D structure databases

ProteinModelPortali Q6P073.
SMRi Q6P073. Positions 11-171.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q6P073.

Proteomic databases

MaxQBi Q6P073.
PaxDbi Q6P073.
PRIDEi Q6P073.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000103175 ; ENSMUSP00000099464 ; ENSMUSG00000023286 .
ENSMUST00000105581 ; ENSMUSP00000101206 ; ENSMUSG00000023286 .
ENSMUST00000166489 ; ENSMUSP00000127712 ; ENSMUSG00000023286 .
GeneIDi 140499.
KEGGi mmu:140499.
UCSCi uc007ubh.1. mouse.

Organism-specific databases

CTDi 118424.
MGIi MGI:2153608. Ube2j2.

Phylogenomic databases

eggNOGi COG5078.
GeneTreei ENSGT00530000063379.
HOGENOMi HOG000170330.
HOVERGENi HBG058434.
InParanoidi Q6P073.
KOi K04554.
OrthoDBi EOG780RNH.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

NextBioi 369836.
PROi Q6P073.
SOURCEi Search...

Gene expression databases

Bgeei Q6P073.
ExpressionAtlasi Q6P073. baseline.
Genevestigatori Q6P073.

Family and domain databases

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

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: October 29, 2014
This is version 93 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