ID   UB2J2_DICDI             Reviewed;         241 AA.
AC   Q54LP7;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   02-SEP-2026, entry version 127.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 J2;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme J2;
GN   Name=ube2j2; ORFNames=DDB_G0286511;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16512674; DOI=10.1021/pr050350q;
RA   Reinders Y., Schulz I., Graef R., Sickmann A.;
RT   "Identification of novel centrosomal proteins in Dictyostelium discoideum
RT   by comparative proteomic approaches.";
RL   J. Proteome Res. 5:589-598(2006).
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. {ECO:0000255|PROSITE-
CC       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   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9Y385}; Single-pass type IV membrane protein
CC       {ECO:0000250|UniProtKB:Q9Y385}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; AAFI02000087; EAL64182.1; -; Genomic_DNA.
DR   RefSeq; XP_637685.1; XM_632593.1.
DR   AlphaFoldDB; Q54LP7; -.
DR   SMR; Q54LP7; -.
DR   FunCoup; Q54LP7; 679.
DR   IntAct; Q54LP7; 2.
DR   STRING; 44689.Q54LP7; -.
DR   GlyGen; Q54LP7; 2 sites.
DR   PaxDb; 44689-Q54LP7; -.
DR   GeneID; 8625651; -.
DR   KEGG; ddi:DDB_G0286511; -.
DR   dictyBase; DDB_G0286511; -.
DR   VEuPathDB; AmoebaDB:DDB_G0286511; -.
DR   eggNOG; KOG0894; Eukaryota.
DR   HOGENOM; CLU_041481_1_0_1; -.
DR   InParanoid; Q54LP7; -.
DR   OMA; MNEDTPT; -.
DR   PhylomeDB; Q54LP7; -.
DR   Reactome; R-DDI-9609523; Insertion of tail-anchored proteins into the endoplasmic reticulum membrane.
DR   Reactome; R-DDI-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q54LP7; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR   GO; GO:0036503; P:ERAD pathway; IBA:GO_Central.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   CDD; cd23799; UBCc_UBE2J; 1.
DR   FunFam; 3.10.110.10:FF:000058; Ubiquitin-conjugating enzyme E2 6; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR050113; Ub_conjugating_enzyme-E2-like.
DR   InterPro; IPR000608; UBC.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
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   Endoplasmic reticulum; Membrane; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix; Ubl conjugation pathway.
FT   CHAIN           1..241
FT                   /note="Ubiquitin-conjugating enzyme E2 J2"
FT                   /id="PRO_0000329284"
FT   TOPO_DOM        1..219
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        220..240
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        241
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          5..164
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   REGION          170..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        193..210
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        89
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
SQ   SEQUENCE   241 AA;  27154 MW;  F047CE7C91D620AC CRC64;
     MSTQVCVTRL KKELLALSKN EDIKDIFIAK PSISNILEWH YVIYGPPDTP YHGGYYHGQI
     IFPVEYPYKP PSILMTTPSG RFVCNSRICT SMSDFHPDTW SPFWSNCTII LGLISFMTED
     ENGFGSIVKS KETRKQLASQ SMAFNLKNPV FVKLFPELIS DYKKKGTFYS SSSTPSSTPP
     PSSTPSSSSS SSNISKRNVP IPTTKTTPQD TNKKKEQKNN NIPYIILFIA LIIILLYLFL
     K
//