ID   UBC1_CAEEL              Reviewed;         192 AA.
AC   P52478; O45062;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   04-NOV-2026, entry version 186.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 1;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme 1;
DE   AltName: Full=Ubiquitin carrier protein 1;
DE   AltName: Full=Ubiquitin-protein ligase 1;
GN   Name=ubc-1; ORFNames=C35B1.1;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=7546294; DOI=10.1089/dna.1995.14.883;
RA   Leggett D.S., Jones D., Candido E.P.M.;
RT   "Caenorhabditis elegans UBC-1, a ubiquitin-conjugating enzyme homologous to
RT   yeast RAD6/UBC2, contains a novel carboxy-terminal extension that is
RT   conserved in nematodes.";
RL   DNA Cell Biol. 14:883-891(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3]
RP   INTERACTION WITH UBC-13.
RX   PubMed=15530417; DOI=10.1016/j.bbrc.2004.10.047;
RA   Gudgen M., Chandrasekaran A., Frazier T., Boyd L.;
RT   "Interactions within the ubiquitin pathway of Caenorhabditis elegans.";
RL   Biochem. Biophys. Res. Commun. 325:479-486(2004).
RN   [4]
RP   INTERACTION WITH UBR-1 AND RFP-1, AND DISRUPTION PHENOTYPE.
RX   PubMed=14732404; DOI=10.1016/j.ydbio.2003.09.037;
RA   Crowe E., Candido E.P.M.;
RT   "Characterization of C. elegans RING finger protein 1, a binding partner of
RT   ubiquitin-conjugating enzyme 1.";
RL   Dev. Biol. 265:446-459(2004).
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins.
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, ECO:0000305};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SUBUNIT: Interacts with ubr-1 and rfp-1 (PubMed:14732404). Interacts
CC       with ubc-13 (PubMed:15530417). {ECO:0000269|PubMed:14732404,
CC       ECO:0000269|PubMed:15530417}.
CC   -!- INTERACTION:
CC       P52478; P34537: rfp-1; NbExp=7; IntAct=EBI-316677, EBI-316712;
CC   -!- DISRUPTION PHENOTYPE: Worms are viable, fertile, and do not show any
CC       obvious anomaly. {ECO:0000269|PubMed:14732404}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; U08139; AAA83388.1; -; Genomic_DNA.
DR   EMBL; FO080784; CCD66736.1; -; Genomic_DNA.
DR   PIR; T32959; T32959.
DR   RefSeq; NP_001379774.1; NM_001392291.1.
DR   PDB; 1Q34; X-ray; 2.90 A; A/B/C=1-163.
DR   PDB; 1Z3D; X-ray; 2.50 A; A=1-154.
DR   AlphaFoldDB; P52478; -.
DR   SMR; P52478; -.
DR   BioGRID; 42306; 18.
DR   DIP; DIP-24573N; -.
DR   FunCoup; P52478; 2891.
DR   IntAct; P52478; 8.
DR   STRING; 6239.C35B1.1.1; -.
DR   PaxDb; 6239-C35B1.1.1; -.
DR   PeptideAtlas; P52478; -.
DR   EnsemblMetazoa; C35B1.1.1; C35B1.1.1; WBGene00006701.
DR   GeneID; 177170; -.
DR   KEGG; cel:CELE_C35B1.1; -.
DR   UCSC; C35B1.1; c. elegans.
DR   AGR; WB:WBGene00006701; -.
DR   CTD; 177170; -.
DR   WormBase; C35B1.1; CE27822; WBGene00006701; ubc-1.
DR   eggNOG; KOG0419; Eukaryota.
DR   HOGENOM; CLU_030988_10_2_1; -.
DR   InParanoid; P52478; -.
DR   OMA; AAPCENN; -.
DR   OrthoDB; 9984419at2759; -.
DR   PhylomeDB; P52478; -.
DR   Reactome; R-CEL-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR   Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   EvolutionaryTrace; P52478; -.
DR   PRO; PR:P52478; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00006701; Expressed in pharyngeal muscle cell (C elegans) and 4 other cell types or tissues.
DR   GO; GO:0033503; C:HULC complex; IBA:GO_Central.
DR   GO; GO:0031371; C:ubiquitin conjugating enzyme complex; IDA:WormBase.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:WormBase.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:WormBase.
DR   GO; GO:0006281; P:DNA repair; IDA:WormBase.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:WormBase.
DR   CDD; cd23790; UBCc_UBE2A_2B; 1.
DR   FunFam; 3.10.110.10:FF:000004; Ubiquitin-conjugating enzyme E2 A; 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; IPR023313; UBQ-conjugating_AS.
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; PS00183; UBC_1; 1.
DR   PROSITE; PS50127; UBC_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome; Transferase; Ubl conjugation pathway.
FT   CHAIN           1..192
FT                   /note="Ubiquitin-conjugating enzyme E2 1"
FT                   /id="PRO_0000082514"
FT   DOMAIN          4..150
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   REGION          171..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        88
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
FT   HELIX           4..18
FT                   /evidence="ECO:0007829|PDB:1Z3D"
FT   STRAND          24..29
FT                   /evidence="ECO:0007829|PDB:1Z3D"
FT   STRAND          32..41
FT                   /evidence="ECO:0007829|PDB:1Z3D"
FT   STRAND          44..46
FT                   /evidence="ECO:0007829|PDB:1Q34"
FT   TURN            47..50
FT                   /evidence="ECO:0007829|PDB:1Z3D"
FT   STRAND          52..58
FT                   /evidence="ECO:0007829|PDB:1Z3D"
FT   TURN            61..65
FT                   /evidence="ECO:0007829|PDB:1Z3D"
FT   STRAND          69..74
FT                   /evidence="ECO:0007829|PDB:1Z3D"
FT   STRAND          85..87
FT                   /evidence="ECO:0007829|PDB:1Q34"
FT   HELIX           90..92
FT                   /evidence="ECO:0007829|PDB:1Z3D"
FT   TURN            93..95
FT                   /evidence="ECO:0007829|PDB:1Q34"
FT   HELIX           102..111
FT                   /evidence="ECO:0007829|PDB:1Z3D"
FT   HELIX           124..132
FT                   /evidence="ECO:0007829|PDB:1Z3D"
FT   HELIX           134..148
FT                   /evidence="ECO:0007829|PDB:1Z3D"
FT   TURN            149..151
FT                   /evidence="ECO:0007829|PDB:1Z3D"
SQ   SEQUENCE   192 AA;  21513 MW;  7CF26B8FB96EF33D CRC64;
     MTTPSRRRLM RDFKKLQEDP PAGVSGAPTE DNILTWEAII FGPQETPFED GTFKLSLEFT
     EEYPNKPPTV KFISKMFHPN VYADGSICLD ILQNRWSPTY DVAAILTSIQ SLLDEPNPNS
     PANSLAAQLY QENRREYEKR VQQIVEQSWL NFGENEGDAV LKDDVEIEEI AAPGANDADD
     DRMDEGASGS NA
//