UBC1_CAEEL
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 03-AUG-2022, entry version 170.
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_500480.1; NM_068079.5.
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 PDBsum; 1Q34; -.
DR PDBsum; 1Z3D; -.
DR AlphaFoldDB; P52478; -.
DR SMR; P52478; -.
DR BioGRID; 42306; 17.
DR DIP; DIP-24573N; -.
DR IntAct; P52478; 8.
DR MINT; P52478; -.
DR STRING; 6239.C35B1.1; -.
DR EPD; P52478; -.
DR PaxDb; P52478; -.
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 CTD; 177170; -.
DR WormBase; C35B1.1; CE27822; WBGene00006701; ubc-1.
DR eggNOG; KOG0419; Eukaryota.
DR GeneTree; ENSGT00940000174704; -.
DR HOGENOM; CLU_030988_10_2_1; -.
DR InParanoid; P52478; -.
DR OMA; DHKSQYI; -.
DR OrthoDB; 1292821at2759; -.
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 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0016574; P:histone ubiquitination; IBA:GO_Central.
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; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Nucleotide-binding; Reference proteome;
KW 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 COMPBIAS 171..186
FT /note="Basic and acidic residues"
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
