UB2J2_MOUSE
ID UB2J2_MOUSE Reviewed; 259 AA.
AC Q6P073; Q8C6A1; Q91Y64; Q9CWY5; Q9DC18; Q9QX58;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 J2;
DE EC=2.3.2.23;
DE AltName: Full=Non-canonical ubiquitin-conjugating enzyme 2;
DE Short=NCUBE-2;
GN Name=Ube2j2; Synonyms=Ncube2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF CYS-94, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=C57BL/6J; TISSUE=Fetus;
RX PubMed=11278356; DOI=10.1074/jbc.m007640200;
RA Tiwari S., Weissman A.M.;
RT "Endoplasmic reticulum (ER)-associated degradation of T cell receptor
RT subunits. Involvement of ER-associated ubiquitin-conjugating enzymes
RT (E2s).";
RL J. Biol. Chem. 276:16193-16200(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF CYS-94, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12082160; DOI=10.1242/jcs.115.14.3007;
RA Lenk U., Yu H., Walter J., Gelman M.S., Hartmann E., Kopito R.R.,
RA Sommer T.;
RT "A role for mammalian Ubc6 homologues in ER-associated protein
RT degradation.";
RL J. Cell Sci. 115:3007-3014(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION IN CASE OF INFECTION BY THE MURID HERPESVIRUS 4, AND INTERACTION
RP WITH MURID HERPESVIRUS 4 K3.
RX PubMed=19951915; DOI=10.1083/jcb.200908036;
RA Wang X., Herr R.A., Rabelink M., Hoeben R.C., Wiertz E.J., Hansen T.H.;
RT "Ube2j2 ubiquitinates hydroxylated amino acids on ER-associated degradation
RT substrates.";
RL J. Cell Biol. 187:655-668(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC proteins. Seems to function in the selective degradation of misfolded
CC membrane proteins from the endoplasmic reticulum (ERAD).
CC {ECO:0000269|PubMed:12082160}.
CC -!- FUNCTION: In case of infection by the murid herpesvirus 4, its
CC association with the viral E3 ligase K3 mediates ubiquitination of host
CC surface class I (MHC-I) H-2D(b)/H2-D1 and H-2K(b)/H2-K1 molecules
CC before they exit the endoplasmic reticulum, leading to their
CC degradation by the ERAD system, thus blocking the immune detection of
CC virus-infected cells. The complex formed with the murid herpesvirus 4
CC protein K3 mediates ubiquitination of lysine, as well as serine and
CC threonine residues present in the cytoplasmic tail of surface class I
CC molecules and promotes ubiquitination of hydroxylated serine or
CC threonine residues via ester bonds instead of the classical isopeptide
CC linkage. {ECO:0000269|PubMed:11278356, ECO:0000269|PubMed:19951915}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00388};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBUNIT: Interacts with murid herpesvirus 4 protein K3 (mK3).
CC {ECO:0000269|PubMed:19951915}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11278356, ECO:0000269|PubMed:12082160}; Single-pass
CC type IV membrane protein {ECO:0000269|PubMed:11278356,
CC ECO:0000269|PubMed:12082160}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; AF296656; AAK52607.1; -; mRNA.
DR EMBL; U93242; AAF21504.1; -; mRNA.
DR EMBL; AK004626; BAB23421.1; -; mRNA.
DR EMBL; AK010302; BAB26835.1; -; mRNA.
DR EMBL; AK076265; BAC36280.1; -; mRNA.
DR EMBL; BC065779; AAH65779.1; -; mRNA.
DR CCDS; CCDS19051.1; -.
DR RefSeq; NP_001034246.1; NM_001039157.2.
DR RefSeq; NP_001034247.1; NM_001039158.2.
DR RefSeq; NP_001034248.1; NM_001039159.2.
DR RefSeq; NP_001271241.1; NM_001284312.1.
DR RefSeq; NP_001271243.1; NM_001284314.1.
DR RefSeq; NP_067377.4; NM_021402.6.
DR AlphaFoldDB; Q6P073; -.
DR SMR; Q6P073; -.
DR BioGRID; 228272; 1.
DR STRING; 10090.ENSMUSP00000024056; -.
DR PhosphoSitePlus; Q6P073; -.
DR EPD; Q6P073; -.
DR MaxQB; Q6P073; -.
DR PaxDb; Q6P073; -.
DR PRIDE; Q6P073; -.
DR ProteomicsDB; 298166; -.
DR Antibodypedia; 26182; 144 antibodies from 25 providers.
DR DNASU; 140499; -.
DR Ensembl; ENSMUST00000103175; ENSMUSP00000099464; ENSMUSG00000023286.
DR Ensembl; ENSMUST00000105581; ENSMUSP00000101206; ENSMUSG00000023286.
DR Ensembl; ENSMUST00000166489; ENSMUSP00000127712; ENSMUSG00000023286.
DR GeneID; 140499; -.
DR KEGG; mmu:140499; -.
DR UCSC; uc007ubh.1; mouse.
DR CTD; 118424; -.
DR MGI; MGI:2153608; Ube2j2.
DR VEuPathDB; HostDB:ENSMUSG00000023286; -.
DR eggNOG; KOG0894; Eukaryota.
DR GeneTree; ENSGT00940000156173; -.
DR InParanoid; Q6P073; -.
DR OMA; DKMFCEL; -.
DR OrthoDB; 1230974at2759; -.
DR Reactome; R-MMU-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 140499; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Ube2j2; mouse.
DR PRO; PR:Q6P073; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q6P073; protein.
DR Bgee; ENSMUSG00000023286; Expressed in spermatocyte and 65 other tissues.
DR ExpressionAtlas; Q6P073; baseline and differential.
DR Genevisible; Q6P073; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:MGI.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Endoplasmic reticulum; Membrane; Nucleotide-binding;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Unfolded protein response.
FT CHAIN 1..259
FT /note="Ubiquitin-conjugating enzyme E2 J2"
FT /id="PRO_0000082597"
FT TOPO_DOM 1..226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..259
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 12..162
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 94
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT MUTAGEN 94
FT /note="C->S: Loss of catalytic activity. Slows down
FT degradation of misfolded proteins from the ER."
FT /evidence="ECO:0000269|PubMed:11278356,
FT ECO:0000269|PubMed:12082160"
FT CONFLICT 25
FT /note="K -> T (in Ref. 3; BAC36280)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="I -> M (in Ref. 3; BAC36280)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="R -> G (in Ref. 3; BAC36280)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="M -> I (in Ref. 3; BAB26835)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="N -> H (in Ref. 3; BAB26835)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="F -> I (in Ref. 3; BAB26835)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="E -> K (in Ref. 3; BAB23421)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="N -> I (in Ref. 3; BAB26835)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="C -> G (in Ref. 3; BAC36280)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="E -> K (in Ref. 3; BAB23421)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="L -> W (in Ref. 3; BAC36280)"
FT /evidence="ECO:0000305"
FT CONFLICT 217..218
FT /note="AG -> GW (in Ref. 2; AAF21504)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="F -> L (in Ref. 3; BAC36280)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="A -> P (in Ref. 1; AAK52607)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 259 AA; 28954 MW; 0C539BC0ACEAC7C7 CRC64;
MSNNSNKRAP TTATQRLKQD YLRIKKDPVP YICAEPLPSN ILEWHYVVRG PEMTPYEGGY
YHGKLIFPRE FPFKPPSIYM ITPNGRFKCN TRLCLSITDF HPDTWNPAWS VSTILTGLLS
FMVEKGPTLG SIETSDFTKK QLAAQSLVFN LKDKVFCELF PEVVEEIKQK QKAQDELSNR
PQNLPLPDVV PDGELHRGQH GIQLLNGHAP AAGPNLAGLP QANRHHGLLG GALANLFVIV
GFAAFAYTVK YVLRSIAQE
