UB2J1_HUMAN
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 03-AUG-2022, entry version 183.
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; Synonyms=NCUBE1; 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).
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). {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}.
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 {ECO:0000269|PubMed:28827405, ECO:0000269|PubMed:33472082}.
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; 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}; Single-pass type IV membrane protein
CC {ECO:0000269|PubMed:12082160}.
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; 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; 205.
DR CORUM; Q9Y385; -.
DR DIP; DIP-45598N; -.
DR IntAct; Q9Y385; 65.
DR MINT; Q9Y385; -.
DR STRING; 9606.ENSP00000451261; -.
DR iPTMnet; Q9Y385; -.
DR MetOSite; Q9Y385; -.
DR PhosphoSitePlus; Q9Y385; -.
DR BioMuta; UBE2J1; -.
DR DMDM; 52000881; -.
DR OGP; Q9Y385; -.
DR CPTAC; CPTAC-1370; -.
DR EPD; Q9Y385; -.
DR jPOST; Q9Y385; -.
DR MassIVE; Q9Y385; -.
DR MaxQB; Q9Y385; -.
DR PaxDb; Q9Y385; -.
DR PeptideAtlas; Q9Y385; -.
DR PRIDE; Q9Y385; -.
DR ProteomicsDB; 85984; -.
DR ABCD; Q9Y385; 1 sequenced antibody.
DR Antibodypedia; 1140; 356 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 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; 1230974at2759; -.
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; 45 hits in 1097 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 202 other tissues.
DR Genevisible; Q9Y385; HS.
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; IMP:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
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 GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:UniProtKB.
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_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
