UBC12_BOVIN
ID UBC12_BOVIN Reviewed; 183 AA.
AC A3KN22;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 100.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) 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 -!- SUBUNIT: Interacts with UBA3 and RBX1. Interacts (N-terminally
CC acetylated form) with (via DCUN1 domain) DCUN1D1, DCUN1D2, DCUN1D3,
CC DCUN1D4 and DCUN1D5. {ECO:0000250|UniProtKB:P61081}.
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|UniProtKB:P61081}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. UBC12
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; BC133501; AAI33502.1; -; mRNA.
DR RefSeq; NP_001076972.1; NM_001083503.1.
DR AlphaFoldDB; A3KN22; -.
DR SMR; A3KN22; -.
DR STRING; 9913.ENSBTAP00000016937; -.
DR PaxDb; A3KN22; -.
DR PeptideAtlas; A3KN22; -.
DR PRIDE; A3KN22; -.
DR Ensembl; ENSBTAT00000016937; ENSBTAP00000016937; ENSBTAG00000012744.
DR GeneID; 613343; -.
DR KEGG; bta:613343; -.
DR CTD; 9040; -.
DR VEuPathDB; HostDB:ENSBTAG00000012744; -.
DR VGNC; VGNC:36589; UBE2M.
DR eggNOG; KOG0420; Eukaryota.
DR GeneTree; ENSGT00940000162814; -.
DR HOGENOM; CLU_030988_6_0_1; -.
DR InParanoid; A3KN22; -.
DR OMA; GYPHDAP; -.
DR OrthoDB; 1302735at2759; -.
DR TreeFam; TF101125; -.
DR UniPathway; UPA00885; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000012744; Expressed in temporal cortex and 104 other tissues.
DR ExpressionAtlas; A3KN22; baseline.
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: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; Methylation; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation pathway.
FT CHAIN 1..183
FT /note="NEDD8-conjugating enzyme Ubc12"
FT /id="PRO_0000328397"
FT DOMAIN 29..173
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 1..57
FT /note="Interaction with UBA3"
FT /evidence="ECO:0000250"
FT REGION 1..29
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|UniProtKB:P61081"
FT MOD_RES 3
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P61081"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61081"
FT MOD_RES 169
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P61082"
FT MOD_RES 169
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P61081"
SQ SEQUENCE 183 AA; 20900 MW; E3C288CA6A98BC5C CRC64;
MIKLFSLKQQ KKEEESAGGT KGSSKKASAA QLRIQKDINE LNLPKTCDIS FSDPDDLLNF
KLVICPDEGF YKSGKFVFSF KVGQGYPHDP PKVKCETMVY HPNIDLEGNV CLNILREDWK
PVLTINSIIY GLQYLFLEPN PEDPLNKEAA EVLQNNRRLF EQNVQRSMRG GYIGSTYFER
CLK
