UBC12_DICDI
ID UBC12_DICDI Reviewed; 230 AA.
AC Q54TI6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=NEDD8-conjugating enzyme Ubc12;
DE EC=2.3.2.34;
DE AltName: Full=NEDD8 carrier protein;
DE AltName: Full=Ubiquitin-conjugating enzyme E2M;
GN Name=ube2m; ORFNames=DDB_G0281725;
OS Dictyostelium discoideum (Slime mold).
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).
CC -!- FUNCTION: Accepts the ubiquitin-like protein nedd8 from the uba3-nae1
CC E1 complex and catalyzes its covalent attachment to other proteins.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[E1 NEDD8-activating enzyme]-S-[NEDD8 protein]-yl-L-cysteine +
CC [E2 NEDD8-conjugating enzyme]-L-cysteine = [E1 NEDD8-activating
CC enzyme]-L-cysteine + [E2 NEDD8-conjugating enzyme]-S-[NEDD8-protein]-
CC yl-L-cysteine.; EC=2.3.2.34;
CC -!- PATHWAY: Protein modification; protein neddylation.
CC -!- DOMAIN: Both the N-terminal docking peptide and the catalytic core
CC domain must bind the uba3-nae1 complex simultaneously for optimal
CC transfer of nedd8. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. UBC12
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; AAFI02000042; EAL66624.1; -; Genomic_DNA.
DR RefSeq; XP_640605.1; XM_635513.1.
DR AlphaFoldDB; Q54TI6; -.
DR SMR; Q54TI6; -.
DR STRING; 44689.DDB0238042; -.
DR PaxDb; Q54TI6; -.
DR PRIDE; Q54TI6; -.
DR EnsemblProtists; EAL66624; EAL66624; DDB_G0281725.
DR GeneID; 8623215; -.
DR KEGG; ddi:DDB_G0281725; -.
DR dictyBase; DDB_G0281725; ube2m.
DR eggNOG; KOG0420; Eukaryota.
DR HOGENOM; CLU_030988_6_0_1; -.
DR InParanoid; Q54TI6; -.
DR OMA; GYPHDAP; -.
DR PhylomeDB; Q54TI6; -.
DR Reactome; R-DDI-8951664; Neddylation.
DR Reactome; R-DDI-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00885; -.
DR PRO; PR:Q54TI6; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019788; F:NEDD8 transferase activity; ISS:dictyBase.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0036211; P:protein modification process; ISS:UniProtKB.
DR GO; GO:0045116; P:protein neddylation; ISS:dictyBase.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Nucleotide-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..230
FT /note="NEDD8-conjugating enzyme Ubc12"
FT /id="PRO_0000328398"
FT DOMAIN 77..221
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 159
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
SQ SEQUENCE 230 AA; 26066 MW; 439C54512D5DF5F6 CRC64;
MFRLKELQKK QQQQQQQQQQ AAAPATNGTD AVTTEPTDVK RQNSNDLKEI RKQKSKDSYF
SLKTKQSSES GSKRANPAEL RAQKDIDEME VPTGCAVSFK DTNDILNFNL SITPTDGLYQ
SATFQFTINI PSTYPYDPPK VHCDTLVYHP NIDLEGHVCL NILRQDWMPV LNIGTVIFGL
MTLFLEPNPD DPLNKDAAQL MIDNKKTFEA NVRQSLRGGY ISNRQFPKLL
