UB2J1_MOUSE
ID UB2J1_MOUSE Reviewed; 318 AA.
AC Q9JJZ4; Q9DC92;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 J1;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme J1;
DE AltName: Full=Non-canonical ubiquitin-conjugating enzyme 1;
DE Short=NCUBE-1;
GN Name=Ube2j1; Synonyms=Ncube1;
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].
RX PubMed=10708578; DOI=10.1006/bbrc.2000.2302;
RA Lester D.H., Farquharson C., Russell G.C., Houston B.;
RT "Identification of a family of non-canonical ubiquitin-conjugating enzymes
RT structurally related to yeast UBC6.";
RL Biochem. Biophys. Res. Commun. 269:474-480(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17208939; DOI=10.1074/mcp.m600218-mcp200;
RA Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT MS/MS/MS.";
RL Mol. Cell. Proteomics 6:669-676(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25320092; DOI=10.1074/jbc.m114.604132;
RA Koenig P.A., Nicholls P.K., Schmidt F.I., Hagiwara M., Maruyama T.,
RA Frydman G.H., Watson N., Page D.C., Ploegh H.L.;
RT "The E2 ubiquitin-conjugating enzyme UBE2J1 is required for spermiogenesis
RT in mice.";
RL J. Biol. Chem. 289:34490-34502(2014).
CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC proteins. Functions in the selective degradation of misfolded membrane
CC proteins from the endoplasmic reticulum (ERAD) and is essential for
CC cells to recover from ER stress. Plays a role in MAPKAPK2-dependent
CC translational control of TNF-alpha synthesis. Acts also as a platform
CC for perinuclear positioning of the endosomal system by mediating
CC ubiquitination of SQSTM1 through interaction with the E3 ubiquitin-
CC protein ligase RNF26. {ECO:0000250|UniProtKB:Q9Y385}.
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: Component of the HRD1 complex, which comprises at least
CC SYNV1/HRD1, DERL1/2, FAM8A1, HERPUD1/HERP, OS9, SEL1L and UBE2J1.
CC Interacts with E3 ligase RNF26. {ECO:0000250|UniProtKB:Q9Y385}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9Y385}; Single-pass type IV membrane protein
CC {ECO:0000250|UniProtKB:Q9Y385}.
CC -!- PTM: Phosphorylated at Ser-184 in a cytosolic stress-dependent manner
CC by MAP kinase p38 MAPKAPK2. {ECO:0000250|UniProtKB:Q9Y385}.
CC -!- PTM: Phosphorylated UBE2J1 is rapidly ubiquitinated and subsequently
CC degraded by the proteasome. {ECO:0000250|UniProtKB:Q9Y385}.
CC -!- DISRUPTION PHENOTYPE: Deletion mice have reduced viability and fail to
CC thrive early after birth. Specific components of the ER dislocation
CC machinery are up-regulated. In addition, males are sterile due to a
CC defect in late spermatogenesis. {ECO:0000269|PubMed:25320092}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; AJ245899; CAB83217.1; -; mRNA.
DR EMBL; AK003050; BAB22532.1; -; mRNA.
DR EMBL; AK031669; BAC27502.1; -; mRNA.
DR EMBL; BC024623; AAH24623.1; -; mRNA.
DR CCDS; CCDS18019.1; -.
DR RefSeq; NP_062532.2; NM_019586.3.
DR AlphaFoldDB; Q9JJZ4; -.
DR SMR; Q9JJZ4; -.
DR BioGRID; 207860; 3.
DR STRING; 10090.ENSMUSP00000118333; -.
DR iPTMnet; Q9JJZ4; -.
DR PhosphoSitePlus; Q9JJZ4; -.
DR EPD; Q9JJZ4; -.
DR jPOST; Q9JJZ4; -.
DR MaxQB; Q9JJZ4; -.
DR PaxDb; Q9JJZ4; -.
DR PeptideAtlas; Q9JJZ4; -.
DR PRIDE; Q9JJZ4; -.
DR ProteomicsDB; 298165; -.
DR ABCD; Q9JJZ4; 1 sequenced antibody.
DR Antibodypedia; 1140; 356 antibodies from 25 providers.
DR DNASU; 56228; -.
DR Ensembl; ENSMUST00000124992; ENSMUSP00000118333; ENSMUSG00000028277.
DR GeneID; 56228; -.
DR KEGG; mmu:56228; -.
DR UCSC; uc008sfp.1; mouse.
DR CTD; 51465; -.
DR MGI; MGI:1926245; Ube2j1.
DR VEuPathDB; HostDB:ENSMUSG00000028277; -.
DR eggNOG; KOG0428; Eukaryota.
DR GeneTree; ENSGT00940000156652; -.
DR InParanoid; Q9JJZ4; -.
DR OMA; CGSTMKD; -.
DR OrthoDB; 1230974at2759; -.
DR PhylomeDB; Q9JJZ4; -.
DR TreeFam; TF101124; -.
DR BRENDA; 2.3.2.23; 3474.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 56228; 9 hits in 73 CRISPR screens.
DR ChiTaRS; Ube2j1; mouse.
DR PRO; PR:Q9JJZ4; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9JJZ4; protein.
DR Bgee; ENSMUSG00000028277; Expressed in seminiferous tubule of testis and 265 other tissues.
DR ExpressionAtlas; Q9JJZ4; baseline and differential.
DR Genevisible; Q9JJZ4; MM.
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: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:1904153; P:negative regulation of retrograde protein transport, ER to cytosol; ISO:MGI.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0010935; P:regulation of macrophage cytokine production; IGI:MGI.
DR GO; GO:0032680; P:regulation of tumor necrosis factor production; IGI:MGI.
DR GO; GO:0007286; P:spermatid development; IMP:MGI.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IDA: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 Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..318
FT /note="Ubiquitin-conjugating enzyme E2 J1"
FT /id="PRO_0000082595"
FT TOPO_DOM 1..282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..318
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 10..168
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 215..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 246..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 91
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y385"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17208939,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y385"
FT CONFLICT 286
FT /note="G -> V (in Ref. 1; CAB83217)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="M -> V (in Ref. 1; CAB83217)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 318 AA; 34990 MW; 61A409ADF397EA36 CRC64;
METRYNLKSP AVKRLMKEAA ELKDPTDHYH AQPLEDNLFE WHFTVRGPPD SDFDGGVYHG
RIVLPPEYPM KPPSIILLTA NGRFEVGKKI CLSISGHHPE TWQPSWSIRT ALLAIIGFMP
TKGEGAIGSL DYTPEERRAL AKKSQDFCCE GCGSAMKDVL LPLKSGSGSS QADQEAKELA
RQISFKAEVN SSGKTIAESD LNQCFSLNDS QDDLPTTFQG ATASTSYGAQ NPSGAPLPQP
TQPAPKNTSM SPRQRRAQQQ SQRRPSTSPD VLQGQPPRAH HTEHGGSAML IIILTLALAA
LIFRRIYLAN EYIFDFEL
