ID UB2J1_HUMAN Reviewed; 318 AA. AC Q9Y385; A8K3F9; Q53F25; Q5W0N4; Q9BZ32; Q9NQL3; Q9NY66; Q9P011; Q9P0S0; AC Q9UF10; DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2004, sequence version 2. DT 27-NOV-2024, entry version 196. DE RecName: Full=Ubiquitin-conjugating enzyme E2 J1; DE EC=2.3.2.23 {ECO:0000269|PubMed:33472082}; DE AltName: Full=E2 ubiquitin-conjugating enzyme J1; DE AltName: Full=Non-canonical ubiquitin-conjugating enzyme 1; DE Short=NCUBE-1; DE AltName: Full=Yeast ubiquitin-conjugating enzyme UBC6 homolog E; DE Short=HsUBC6e; GN Name=UBE2J1 {ECO:0000312|HGNC:HGNC:17598}; Synonyms=NCUBE1; GN ORFNames=CGI-76, HSPC153, HSPC205; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; 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 [MRNA], VARIANT VAL-55, FUNCTION, MUTAGENESIS OF RP CYS-91, AND 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]. RX PubMed=10810093; DOI=10.1101/gr.10.5.703; RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.; RT "Identification of novel human genes evolutionarily conserved in RT Caenorhabditis elegans by comparative proteomics."; RL Genome Res. 10:703-713(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-229. RC TISSUE=Umbilical cord blood; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for 300 RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor RT cells."; RL Genome Res. 10:1546-1560(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-229. RC TISSUE=Spleen; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-229. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-229. RC TISSUE=Muscle; 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 [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [15] RP FUNCTION IN ERAD PATHWAY. RX PubMed=22607976; DOI=10.1016/j.molcel.2012.04.015; RA Sato T., Sako Y., Sho M., Momohara M., Suico M.A., Shuto T., Nishitoh H., RA Okiyoneda T., Kokame K., Kaneko M., Taura M., Miyata M., Chosa K., Koga T., RA Morino-Koga S., Wada I., Kai H.; RT "STT3B-dependent posttranslational N-glycosylation as a surveillance system RT for secretory protein."; RL Mol. Cell 47:99-110(2012). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184; SER-266 AND SER-268, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [17] RP FUNCTION, PHOSPHORYLATION AT SER-184, MUTAGENESIS OF SER-184, AND RP SUBCELLULAR LOCATION. RX PubMed=24020373; DOI=10.1042/bj20130755; RA Menon M.B., Tiedje C., Lafera J., Ronkina N., Konen T., Kotlyarov A., RA Gaestel M.; RT "Endoplasmic reticulum-associated ubiquitin-conjugating enzyme Ube2j1 is a RT novel substrate of MK2 (MAPKAP kinase-2) involved in MK2-mediated TNFalpha RT production."; RL Biochem. J. 456:163-172(2013). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [19] RP IDENTIFICATION IN THE HRD1 COMPLEX. RX PubMed=28827405; DOI=10.1242/jcs.206847; RA Schulz J., Avci D., Queisser M.A., Gutschmidt A., Dreher L.S., Fenech E.J., RA Volkmar N., Hayashi Y., Hoppe T., Christianson J.C.; RT "Conserved cytoplasmic domains promote Hrd1 ubiquitin ligase complex RT formation for ER-associated degradation (ERAD)."; RL J. Cell Sci. 130:3322-3335(2017). RN [20] RP FUNCTION, MUTAGENESIS OF SER-184, AND UBIQUITINATION. RX PubMed=28321712; DOI=10.1007/s12079-017-0386-6; RA Elangovan M., Chong H.K., Park J.H., Yeo E.J., Yoo Y.J.; RT "The role of ubiquitin-conjugating enzyme Ube2j1 phosphorylation and its RT degradation by proteasome during endoplasmic stress recovery."; RL J. Cell Commun. Signal. 11:265-273(2017). RN [21] RP FUNCTION (MICROBIAL INFECTION), AND INDUCTION BY DENGUE VIRUS INFECTION. RX PubMed=30157886; DOI=10.1186/s12985-018-1040-5; RA Feng T., Deng L., Lu X., Pan W., Wu Q., Dai J.; RT "Ubiquitin-conjugating enzyme UBE2J1 negatively modulates interferon RT pathway and promotes RNA virus infection."; RL Virol. J. 15:132-132(2018). RN [22] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RNF26, AND CATALYTIC RP ACTIVITY. RX PubMed=33472082; DOI=10.1016/j.celrep.2020.108659; RA Cremer T., Jongsma M.L.M., Trulsson F., Vertegaal A.C.O., Neefjes J., RA Berlin I.; RT "The ER-embedded UBE2J1/RNF26 ubiquitylation complex exerts spatiotemporal RT control over the endolysosomal pathway."; RL Cell Rep. 34:108659-108659(2021). RN [23] RP TISSUE SPECIFICITY, FUNCTION, INTERACTION WITH RNF133, AND SUBCELLULAR RP LOCATION. RX PubMed=35831855; DOI=10.1186/s12915-022-01368-2; RA Nozawa K., Fujihara Y., Devlin D.J., Deras R.E., Kent K., Larina I.V., RA Umezu K., Yu Z., Sutton C.M., Ye Q., Dean L.K., Emori C., Ikawa M., RA Garcia T.X., Matzuk M.M.; RT "The testis-specific E3 ubiquitin ligase RNF133 is required for fecundity RT in mice."; RL BMC Biol. 20:161-161(2022). 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 (PubMed:28321712). Plays a role in CC MAPKAPK2-dependent translational control of TNF-alpha synthesis CC (PubMed:24020373). Acts also as a platform for perinuclear positioning CC of the endosomal system by mediating ubiquitination of SQSTM1 through CC interaction with the E3 ubiquitin-protein ligase RNF26 CC (PubMed:33472082). Plays a role in male fecundity through the CC interaction with the E3 ubiquitin-protein ligase RNF133 CC (PubMed:35831855). {ECO:0000255|PROSITE-ProRule:PRU00388, CC ECO:0000269|PubMed:12082160, ECO:0000269|PubMed:22607976, CC ECO:0000269|PubMed:24020373, ECO:0000269|PubMed:28321712, CC ECO:0000269|PubMed:33472082, ECO:0000269|PubMed:35831855}. CC -!- FUNCTION: (Microbial infection) Promotes Dengue virus RNA replication CC by negatively regulating IFN-beta signaling and mediating 'Lys-48'- CC linked ubiquitination on IRF3 (PubMed:30157886). CC {ECO:0000269|PubMed:30157886}. 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 (PubMed:28827405). Interacts with E3 ligase RNF26 (PubMed:33472082). CC Interacts with E3 ligase RNF133 (PubMed:35831855). CC {ECO:0000269|PubMed:28827405, ECO:0000269|PubMed:33472082, CC ECO:0000269|PubMed:35831855}. CC -!- INTERACTION: CC Q9Y385; P11912: CD79A; NbExp=3; IntAct=EBI-988826, EBI-7797864; CC Q9Y385; Q92903: CDS1; NbExp=3; IntAct=EBI-988826, EBI-13295305; CC Q9Y385; Q9HBJ8: CLTRN; NbExp=3; IntAct=EBI-988826, EBI-3924906; CC Q9Y385; P49447: CYB561; NbExp=3; IntAct=EBI-988826, EBI-8646596; CC Q9Y385; Q9BUN8: DERL1; NbExp=3; IntAct=EBI-988826, EBI-398977; CC Q9Y385; Q15125: EBP; NbExp=3; IntAct=EBI-988826, EBI-3915253; CC Q9Y385; Q9GZR5: ELOVL4; NbExp=3; IntAct=EBI-988826, EBI-18535450; CC Q9Y385; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-988826, EBI-781551; CC Q9Y385; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-988826, EBI-18304435; CC Q9Y385; Q96KR6: FAM210B; NbExp=3; IntAct=EBI-988826, EBI-18938272; CC Q9Y385; Q9NS71: GKN1; NbExp=3; IntAct=EBI-988826, EBI-3933251; CC Q9Y385; Q6ZVE7: GOLT1A; NbExp=3; IntAct=EBI-988826, EBI-17231387; CC Q9Y385; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-988826, EBI-10266796; CC Q9Y385; Q13571: LAPTM5; NbExp=3; IntAct=EBI-988826, EBI-2865663; CC Q9Y385; O95867: LY6G6C; NbExp=3; IntAct=EBI-988826, EBI-9088345; CC Q9Y385; Q9Y5Y7: LYVE1; NbExp=3; IntAct=EBI-988826, EBI-10329546; CC Q9Y385; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-988826, EBI-373355; CC Q9Y385; Q96ES6: MFSD3; NbExp=3; IntAct=EBI-988826, EBI-745345; CC Q9Y385; Q96DS6: MS4A6E; NbExp=3; IntAct=EBI-988826, EBI-17931225; CC Q9Y385; O60361: NME2P1; NbExp=2; IntAct=EBI-988826, EBI-2558379; CC Q9Y385; Q96GM1: PLPPR2; NbExp=3; IntAct=EBI-988826, EBI-12955265; CC Q9Y385; O60260-5: PRKN; NbExp=3; IntAct=EBI-988826, EBI-21251460; CC Q9Y385; Q8NFJ6: PROKR2; NbExp=3; IntAct=EBI-988826, EBI-12902928; CC Q9Y385; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-988826, EBI-7545592; CC Q9Y385; Q9BY50: SEC11C; NbExp=3; IntAct=EBI-988826, EBI-2855401; CC Q9Y385; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-988826, EBI-18159983; CC Q9Y385; P58743-6: SLC26A5; NbExp=3; IntAct=EBI-988826, EBI-18029942; CC Q9Y385; Q9NP94: SLC39A2; NbExp=3; IntAct=EBI-988826, EBI-12898013; CC Q9Y385; Q86TM6: SYVN1; NbExp=15; IntAct=EBI-988826, EBI-947849; CC Q9Y385; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-988826, EBI-12947623; CC Q9Y385; Q96CE8: TM4SF18; NbExp=3; IntAct=EBI-988826, EBI-13351685; CC Q9Y385; Q96DZ7: TM4SF19; NbExp=3; IntAct=EBI-988826, EBI-6448756; CC Q9Y385; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-988826, EBI-8638294; CC Q9Y385; Q9NW97: TMEM51; NbExp=3; IntAct=EBI-988826, EBI-726044; CC Q9Y385; Q9Y320: TMX2; NbExp=3; IntAct=EBI-988826, EBI-6447886; CC Q9Y385; P34981: TRHR; NbExp=3; IntAct=EBI-988826, EBI-18055230; CC Q9Y385; Q96MV8: ZDHHC15; NbExp=3; IntAct=EBI-988826, EBI-12837904; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:12082160, ECO:0000269|PubMed:24020373, CC ECO:0000269|PubMed:33472082, ECO:0000269|PubMed:35831855}; Single-pass CC type IV membrane protein {ECO:0000269|PubMed:12082160}. CC -!- TISSUE SPECIFICITY: Expressed in testes. {ECO:0000269|PubMed:35831855}. CC -!- INDUCTION: By Dengue virus infection. {ECO:0000269|PubMed:30157886}. CC -!- PTM: Phosphorylated at Ser-184 in a cytosolic stress-dependent manner CC by MAP kinase p38 MAPKAPK2. {ECO:0000269|PubMed:24020373}. CC -!- PTM: Phosphorylated UBE2J1 is rapidly ubiquitinated and subsequently CC degraded by the proteasome. {ECO:0000269|PubMed:28321712}. CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. CC {ECO:0000255|PROSITE-ProRule:PRU00388}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD34071.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAF36125.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ245898; CAB83212.1; -; mRNA. DR EMBL; U93243; AAF21505.1; -; mRNA. DR EMBL; AF151834; AAD34071.1; ALT_INIT; mRNA. DR EMBL; AF151039; AAF36125.1; ALT_FRAME; mRNA. DR EMBL; AF161502; AAF29117.1; -; mRNA. DR EMBL; AK290574; BAF83263.1; -; mRNA. DR EMBL; AK223464; BAD97184.1; -; mRNA. DR EMBL; AL138717; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL139804; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471051; EAW48555.1; -; Genomic_DNA. DR EMBL; CH471051; EAW48556.1; -; Genomic_DNA. DR EMBL; BC013973; AAH13973.1; -; mRNA. DR CCDS; CCDS5021.1; -. DR RefSeq; NP_057105.2; NM_016021.2. DR AlphaFoldDB; Q9Y385; -. DR SMR; Q9Y385; -. DR BioGRID; 119555; 220. DR CORUM; Q9Y385; -. DR DIP; DIP-45598N; -. DR IntAct; Q9Y385; 81. DR MINT; Q9Y385; -. DR STRING; 9606.ENSP00000451261; -. DR GlyGen; Q9Y385; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9Y385; -. DR MetOSite; Q9Y385; -. DR PhosphoSitePlus; Q9Y385; -. DR SwissPalm; Q9Y385; -. DR BioMuta; UBE2J1; -. DR DMDM; 52000881; -. DR OGP; Q9Y385; -. DR CPTAC; CPTAC-1370; -. DR jPOST; Q9Y385; -. DR MassIVE; Q9Y385; -. DR PaxDb; 9606-ENSP00000451261; -. DR PeptideAtlas; Q9Y385; -. DR ProteomicsDB; 85984; -. DR Pumba; Q9Y385; -. DR ABCD; Q9Y385; 1 sequenced antibody. DR Antibodypedia; 1140; 362 antibodies from 25 providers. DR CPTC; Q9Y385; 3 antibodies. DR DNASU; 51465; -. DR Ensembl; ENST00000435041.3; ENSP00000451261.1; ENSG00000198833.7. DR GeneID; 51465; -. DR KEGG; hsa:51465; -. DR MANE-Select; ENST00000435041.3; ENSP00000451261.1; NM_016021.3; NP_057105.2. DR UCSC; uc003pnc.4; human. DR AGR; HGNC:17598; -. DR CTD; 51465; -. DR DisGeNET; 51465; -. DR GeneCards; UBE2J1; -. DR HGNC; HGNC:17598; UBE2J1. DR HPA; ENSG00000198833; Low tissue specificity. DR MIM; 616175; gene. DR neXtProt; NX_Q9Y385; -. DR OpenTargets; ENSG00000198833; -. DR PharmGKB; PA134906541; -. DR VEuPathDB; HostDB:ENSG00000198833; -. DR eggNOG; KOG0428; Eukaryota. DR GeneTree; ENSGT00940000156652; -. DR HOGENOM; CLU_041481_0_0_1; -. DR InParanoid; Q9Y385; -. DR OMA; CGSTMKD; -. DR OrthoDB; 180749at2759; -. DR PhylomeDB; Q9Y385; -. DR TreeFam; TF101124; -. DR BRENDA; 2.3.2.23; 2681. DR PathwayCommons; Q9Y385; -. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; Q9Y385; -. DR SIGNOR; Q9Y385; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 51465; 46 hits in 1174 CRISPR screens. DR ChiTaRS; UBE2J1; human. DR GeneWiki; UBE2J1; -. DR GenomeRNAi; 51465; -. DR Pharos; Q9Y385; Tbio. DR PRO; PR:Q9Y385; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q9Y385; protein. DR Bgee; ENSG00000198833; Expressed in sperm and 204 other cell types or tissues. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProt. 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; IMP:MGI. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0036503; P:ERAD pathway; IMP:UniProtKB. DR GO; GO:1904153; P:negative regulation of retrograde protein transport, ER to cytosol; IMP:ParkinsonsUK-UCL. DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; IMP:UniProtKB. DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central. DR GO; GO:0010935; P:regulation of macrophage cytokine production; IEA:Ensembl. DR GO; GO:0032680; P:regulation of tumor necrosis factor production; IEA:Ensembl. DR GO; GO:0007286; P:spermatid development; IEA:Ensembl. DR CDD; cd00195; UBCc; 1. DR FunFam; 3.10.110.10:FF:000043; ubiquitin-conjugating enzyme E2 J1; 1. DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1. DR InterPro; IPR050113; Ub_conjugating_enzyme. DR InterPro; IPR000608; UBQ-conjugat_E2. DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD. DR PANTHER; PTHR24067:SF257; UBC CORE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1. DR Pfam; PF00179; UQ_con; 1. DR SMART; SM00212; UBCc; 1. DR SUPFAM; SSF54495; UBC-like; 1. DR PROSITE; PS50127; UBC_2; 1. PE 1: Evidence at protein level; KW ATP-binding; Endoplasmic reticulum; Membrane; Nucleotide-binding; KW Phosphoprotein; Proteomics identification; Reference proteome; Transferase; KW Transmembrane; Transmembrane helix; Ubl conjugation; KW Ubl conjugation pathway. FT CHAIN 1..318 FT /note="Ubiquitin-conjugating enzyme E2 J1" FT /id="PRO_0000082594" 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..160 FT /note="UBC core" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388" FT REGION 229..283 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 229..275 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; by MAPKAPK2" FT /evidence="ECO:0000269|PubMed:24020373, FT ECO:0007744|PubMed:23186163" FT MOD_RES 266 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 268 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT VARIANT 55 FT /note="G -> V (in dbSNP:rs8099)" FT /evidence="ECO:0000269|PubMed:12082160" FT /id="VAR_019689" FT VARIANT 229 FT /note="L -> V (in dbSNP:rs10502)" FT /evidence="ECO:0000269|PubMed:11042152, FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.6, FT ECO:0000269|Ref.8" FT /id="VAR_019690" FT MUTAGEN 91 FT /note="C->S: Loss of catalytic activity. Slows down FT degradation of misfolded proteins from the ER." FT /evidence="ECO:0000269|PubMed:12082160" FT MUTAGEN 184 FT /note="S->A: Complete loss of stress-dependent FT phosphorylation. Loss of cell recovery for ER stress." FT /evidence="ECO:0000269|PubMed:24020373, FT ECO:0000269|PubMed:28321712" FT CONFLICT 32..33 FT /note="QP -> HA (in Ref. 3; AAD34071)" FT /evidence="ECO:0000305" FT CONFLICT 276 FT /note="Q -> H (in Ref. 2; AAF21505)" FT /evidence="ECO:0000305" SQ SEQUENCE 318 AA; 35199 MW; CFF5FE00C2BBD39E CRC64; METRYNLKSP AVKRLMKEAA ELKDPTDHYH AQPLEDNLFE WHFTVRGPPD SDFDGGVYHG RIVLPPEYPM KPPSIILLTA NGRFEVGKKI CLSISGHHPE TWQPSWSIRT ALLAIIGFMP TKGEGAIGSL DYTPEERRAL AKKSQDFCCE GCGSAMKDVL LPLKSGSDSS QADQEAKELA RQISFKAEVN SSGKTISESD LNHSFSLTDL QDDIPTTFQG ATASTSYGLQ NSSAASFHQP TQPVAKNTSM SPRQRRAQQQ SQRRLSTSPD VIQGHQPRDN HTDHGGSAVL IVILTLALAA LIFRRIYLAN EYIFDFEL //