UB2J2_HUMAN
ID UB2J2_HUMAN Reviewed; 259 AA.
AC Q8N2K1; A8MYC7; Q504T9; Q96N26; Q96T84;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 J2;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme J2;
DE AltName: Full=Non-canonical ubiquitin-conjugating enzyme 2;
DE Short=NCUBE-2;
GN Name=UBE2J2; Synonyms=NCUBE2;
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] (ISOFORM 1).
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Ovary;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-205 (ISOFORM 3).
RC TISSUE=Brain, Hippocampus, and Placenta;
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 [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-185.
RG Structural genomics consortium (SGC);
RT "Structure of the endoplasmic reticulum (ER)-associated human ubiquitin-
RT conjugating enzyme E2 J2.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [7] {ECO:0007744|PDB:2F4W}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-185, AND AUTOUBIQUITINATION.
RX PubMed=22496338; DOI=10.1074/mcp.o111.013706;
RA Sheng Y., Hong J.H., Doherty R., Srikumar T., Shloush J., Avvakumov G.V.,
RA Walker J.R., Xue S., Neculai D., Wan J.W., Kim S.K., Arrowsmith C.H.,
RA Raught B., Dhe-Paganon S.;
RT "A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure-
RT function screen.";
RL Mol. Cell. Proteomics 11:329-341(2012).
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:0000255|PROSITE-ProRule:PRU00388}.
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 -!- INTERACTION:
CC Q8N2K1; Q13520: AQP6; NbExp=3; IntAct=EBI-2340110, EBI-13059134;
CC Q8N2K1; A1L3X0: ELOVL7; NbExp=3; IntAct=EBI-2340110, EBI-10285373;
CC Q8N2K1; P62879: GNB2; NbExp=3; IntAct=EBI-2340110, EBI-356942;
CC Q8N2K1; P09455: RBP1; NbExp=3; IntAct=EBI-2340110, EBI-2623483;
CC Q8N2K1; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-2340110, EBI-8638294;
CC Q8N2K1; Q8IWR1: TRIM59; NbExp=3; IntAct=EBI-2340110, EBI-10262539;
CC Q8N2K1; O76024: WFS1; NbExp=3; IntAct=EBI-2340110, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9Y385}; Single-pass type IV membrane protein
CC {ECO:0000250|UniProtKB:Q9Y385}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8N2K1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N2K1-2; Sequence=VSP_011572;
CC Name=3;
CC IsoId=Q8N2K1-3; Sequence=VSP_045219;
CC -!- PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:22496338}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BM544827; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BM544827; Type=Miscellaneous discrepancy; Evidence={ECO:0000305};
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DR EMBL; AF296658; AAK52609.1; -; mRNA.
DR EMBL; AK056065; BAB71086.1; -; mRNA.
DR EMBL; AK075017; BAC11355.1; -; mRNA.
DR EMBL; AK291935; BAF84624.1; -; mRNA.
DR EMBL; AL162741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471183; EAW56256.1; -; Genomic_DNA.
DR EMBL; CH471183; EAW56259.1; -; Genomic_DNA.
DR EMBL; BC094777; AAH94777.1; -; mRNA.
DR EMBL; BC104890; AAI04891.1; -; mRNA.
DR EMBL; BC113430; AAI13431.1; -; mRNA.
DR EMBL; BC143657; AAI43658.1; -; mRNA.
DR EMBL; BM544827; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS14.1; -. [Q8N2K1-1]
DR CCDS; CCDS15.1; -. [Q8N2K1-3]
DR RefSeq; NP_477515.2; NM_058167.2. [Q8N2K1-1]
DR RefSeq; NP_919296.1; NM_194315.1. [Q8N2K1-3]
DR RefSeq; NP_919440.1; NM_194458.1.
DR RefSeq; XP_005244775.1; XM_005244718.3. [Q8N2K1-1]
DR RefSeq; XP_005244776.1; XM_005244719.4. [Q8N2K1-1]
DR RefSeq; XP_006710396.1; XM_006710333.3. [Q8N2K1-1]
DR RefSeq; XP_011538915.1; XM_011540613.2. [Q8N2K1-2]
DR RefSeq; XP_011538916.1; XM_011540614.2. [Q8N2K1-1]
DR PDB; 2F4W; X-ray; 2.00 A; A/B=1-185.
DR PDBsum; 2F4W; -.
DR AlphaFoldDB; Q8N2K1; -.
DR SMR; Q8N2K1; -.
DR BioGRID; 125598; 38.
DR IntAct; Q8N2K1; 11.
DR STRING; 9606.ENSP00000383719; -.
DR iPTMnet; Q8N2K1; -.
DR PhosphoSitePlus; Q8N2K1; -.
DR BioMuta; UBE2J2; -.
DR DMDM; 251757431; -.
DR EPD; Q8N2K1; -.
DR jPOST; Q8N2K1; -.
DR MassIVE; Q8N2K1; -.
DR MaxQB; Q8N2K1; -.
DR PeptideAtlas; Q8N2K1; -.
DR PRIDE; Q8N2K1; -.
DR ProteomicsDB; 2392; -.
DR ProteomicsDB; 71714; -. [Q8N2K1-1]
DR ProteomicsDB; 71715; -. [Q8N2K1-2]
DR Antibodypedia; 26182; 144 antibodies from 25 providers.
DR DNASU; 118424; -.
DR Ensembl; ENST00000349431.11; ENSP00000305826.7; ENSG00000160087.21. [Q8N2K1-1]
DR Ensembl; ENST00000360466.6; ENSP00000353653.2; ENSG00000160087.21. [Q8N2K1-1]
DR Ensembl; ENST00000400930.8; ENSP00000383719.4; ENSG00000160087.21. [Q8N2K1-3]
DR GeneID; 118424; -.
DR KEGG; hsa:118424; -.
DR MANE-Select; ENST00000349431.11; ENSP00000305826.7; NM_058167.3; NP_477515.2.
DR UCSC; uc001ado.4; human. [Q8N2K1-1]
DR CTD; 118424; -.
DR DisGeNET; 118424; -.
DR GeneCards; UBE2J2; -.
DR HGNC; HGNC:19268; UBE2J2.
DR HPA; ENSG00000160087; Low tissue specificity.
DR MIM; 619756; gene.
DR neXtProt; NX_Q8N2K1; -.
DR PharmGKB; PA134882268; -.
DR VEuPathDB; HostDB:ENSG00000160087; -.
DR eggNOG; KOG0894; Eukaryota.
DR GeneTree; ENSGT00940000156173; -.
DR HOGENOM; CLU_041481_1_2_1; -.
DR InParanoid; Q8N2K1; -.
DR OMA; DKMFCEL; -.
DR OrthoDB; 1230974at2759; -.
DR PhylomeDB; Q8N2K1; -.
DR TreeFam; TF101123; -.
DR BRENDA; 2.3.2.23; 2681.
DR PathwayCommons; Q8N2K1; -.
DR Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins. [Q8N2K1-1]
DR Reactome; R-HSA-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane. [Q8N2K1-1]
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q8N2K1; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 118424; 106 hits in 1086 CRISPR screens.
DR ChiTaRS; UBE2J2; human.
DR EvolutionaryTrace; Q8N2K1; -.
DR GenomeRNAi; 118424; -.
DR Pharos; Q8N2K1; Tbio.
DR PRO; PR:Q8N2K1; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8N2K1; protein.
DR Bgee; ENSG00000160087; Expressed in left testis and 181 other tissues.
DR ExpressionAtlas; Q8N2K1; baseline and differential.
DR Genevisible; Q8N2K1; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
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; IPI:ParkinsonsUK-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; HMP:ParkinsonsUK-UCL.
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; IMP:ParkinsonsUK-UCL.
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 3D-structure; Alternative splicing; ATP-binding; Endoplasmic reticulum;
KW Membrane; Nucleotide-binding; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation;
KW Ubl conjugation pathway; Unfolded protein response.
FT CHAIN 1..259
FT /note="Ubiquitin-conjugating enzyme E2 J2"
FT /id="PRO_0000082596"
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 VAR_SEQ 1..44
FT /note="MSSTSSKRAPTTATQRLKQDYLRIKKDPVPYICAEPLPSNILEW -> MWPQ
FT DIAGR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_011572"
FT VAR_SEQ 44
FT /note="W -> WFKRFSWLSLLSSWDYR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045219"
FT CONFLICT 2
FT /note="S -> N (in Ref. 2; BAC11355)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="F -> S (in Ref. 2; BAC11355)"
FT /evidence="ECO:0000305"
FT CONFLICT 214..238
FT /note="PNLAGLQQANRHHGLLGGALANLFV -> QTSQGSSRPTGTTDSGWRPGELV
FT C (in Ref. 1; AAK52609)"
FT /evidence="ECO:0000305"
FT HELIX 13..26
FT /evidence="ECO:0007829|PDB:2F4W"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:2F4W"
FT STRAND 40..49
FT /evidence="ECO:0007829|PDB:2F4W"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:2F4W"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:2F4W"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:2F4W"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:2F4W"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:2F4W"
FT HELIX 111..123
FT /evidence="ECO:0007829|PDB:2F4W"
FT HELIX 136..151
FT /evidence="ECO:0007829|PDB:2F4W"
FT HELIX 154..159
FT /evidence="ECO:0007829|PDB:2F4W"
FT HELIX 161..167
FT /evidence="ECO:0007829|PDB:2F4W"
SQ SEQUENCE 259 AA; 28898 MW; 7DB5280D2947CE7E CRC64;
MSSTSSKRAP TTATQRLKQD YLRIKKDPVP YICAEPLPSN ILEWHYVVRG PEMTPYEGGY
YHGKLIFPRE FPFKPPSIYM ITPNGRFKCN TRLCLSITDF HPDTWNPAWS VSTILTGLLS
FMVEKGPTLG SIETSDFTKR QLAVQSLAFN LKDKVFCELF PEVVEEIKQK QKAQDELSSR
PQTLPLPDVV PDGETHLVQN GIQLLNGHAP GAVPNLAGLQ QANRHHGLLG GALANLFVIV
GFAAFAYTVK YVLRSIAQE
