ID   UBC12_XENLA             Reviewed;         183 AA.
AC   Q6DCZ9;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=NEDD8-conjugating enzyme Ubc12;
DE            EC=2.3.2.34 {ECO:0000250|UniProtKB:P61081};
DE   AltName: Full=NEDD8 carrier protein;
DE   AltName: Full=Ubiquitin-conjugating enzyme E2 M;
GN   Name=ube2m; Synonyms=ubc12;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1
CC       E1 complex and catalyzes its covalent attachment to other proteins. The
CC       specific interaction with the E3 ubiquitin ligase rbx1, but not rbx2,
CC       suggests that the rbx1-ube2m complex neddylates specific target
CC       proteins, such as cul1, cul2, cul3 and cul4. Involved in cell
CC       proliferation. {ECO:0000250|UniProtKB:P61081}.
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; Evidence={ECO:0000250|UniProtKB:P61081};
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   -!- PTM: The acetylation of Met-1 increases affinity for DCUN1D1 by about 2
CC       orders of magnitude and is crucial for NEDD8 transfer to cullins.
CC       {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; BC077833; AAH77833.1; -; mRNA.
DR   RefSeq; NP_001086965.1; NM_001093496.1.
DR   AlphaFoldDB; Q6DCZ9; -.
DR   SMR; Q6DCZ9; -.
DR   DNASU; 446800; -.
DR   GeneID; 446800; -.
DR   KEGG; xla:446800; -.
DR   CTD; 446800; -.
DR   Xenbase; XB-GENE-1005530; ube2m.L.
DR   OrthoDB; 1302735at2759; -.
DR   UniPathway; UPA00885; -.
DR   Proteomes; UP000186698; Chromosome 7L.
DR   Bgee; 446800; Expressed in oocyte and 19 other tissues.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019788; F:NEDD8 transferase activity; ISS:UniProtKB.
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:UniProtKB.
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   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Nucleotide-binding; Reference proteome;
KW   Transferase; Ubl conjugation pathway.
FT   CHAIN           1..183
FT                   /note="NEDD8-conjugating enzyme Ubc12"
FT                   /id="PRO_0000082490"
FT   DOMAIN          29..173
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        111
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   183 AA;  20953 MW;  07762478E92257CF CRC64;
     MIKLFSLKQQ KKEEESAGGT KGSSKKASAA QLRIQKDITE LNLPKTCEIE FSDHDDLLNF
     KLVICPDEGF YKGGKFVFSF KVGQGYPHDP PKVKCETMVY HPNIDLEGNV CLNILREDWK
     PVLTINSIIY GLQYLFLEPN PEDPLNKEAA EVLQNNRRLF EQNVQRSMRG GYIGSTYFER
     CLK