UBC13_CAEEL
ID UBC13_CAEEL Reviewed; 151 AA.
AC Q95XX0;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 13 {ECO:0000312|WormBase:Y54G2A.31};
DE EC=2.3.2.23 {ECO:0000269|PubMed:15530417};
GN Name=ubc-13 {ECO:0000312|WormBase:Y54G2A.31};
GN ORFNames=Y54G2A.31 {ECO:0000312|WormBase:Y54G2A.31};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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 [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND INTERACTION WITH NHL-1; UEV-1
RP AND UBC-1.
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 [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17663792; DOI=10.1186/1471-2121-8-32;
RA Howard R.A., Sharma P., Hajjar C., Caldwell K.A., Caldwell G.A.,
RA du Breuil R., Moore R., Boyd L.;
RT "Ubiquitin conjugating enzymes participate in polyglutamine protein
RT aggregation.";
RL BMC Cell Biol. 8:32-32(2007).
RN [4] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH UEV-1.
RX PubMed=21179194; DOI=10.1371/journal.pone.0014291;
RA Kramer L.B., Shim J., Previtera M.L., Isack N.R., Lee M.C., Firestein B.L.,
RA Rongo C.;
RT "UEV-1 is an ubiquitin-conjugating enzyme variant that regulates glutamate
RT receptor trafficking in C. elegans neurons.";
RL PLoS ONE 5:E14291-E14291(2010).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22494772; DOI=10.1186/1471-2121-13-10;
RA Skibinski G.A., Boyd L.;
RT "Ubiquitination is involved in secondary growth, not initial formation of
RT polyglutamine protein aggregates in C. elegans.";
RL BMC Cell Biol. 13:10-10(2012).
RN [6] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24595290; DOI=10.1242/dev.103044;
RA Sato M., Konuma R., Sato K., Tomura K., Sato K.;
RT "Fertilization-induced K63-linked ubiquitylation mediates clearance of
RT maternal membrane proteins.";
RL Development 141:1324-1331(2014).
CC -!- FUNCTION: Involved in protein ubiquitination, but has no ubiquitin
CC ligase activity on its own (PubMed:15530417). The uev-1-ubc-13
CC heterodimers catalyze the synthesis of non-canonical 'Lys-63'-linked
CC polyubiquitin chains (PubMed:15530417, PubMed:24595290). Involved in
CC sorting Lys-63-linked polyubiquitinated maternal membrane proteins for
CC degradation by targeting to multivesicular bodies (PubMed:24595290).
CC May be involved in the ubiquitination and growth of intracellular
CC polyglutamine protein aggregates (PubMed:17663792, PubMed:22494772).
CC May have a role in AMPA-type glutamate receptor trafficking in neurons
CC (PubMed:21179194). {ECO:0000255|PROSITE-ProRule:PRU00388,
CC ECO:0000269|PubMed:15530417, ECO:0000269|PubMed:17663792,
CC ECO:0000269|PubMed:21179194, ECO:0000269|PubMed:22494772,
CC ECO:0000269|PubMed:24595290}.
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:0000269|PubMed:15530417};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000269|PubMed:15530417}.
CC -!- SUBUNIT: Interacts with the E3 ubiquitin ligase nhl-1 and the E2
CC ubiquitin ligase ubc-1 (PubMed:15530417). Heterodimer with uev-1
CC (PubMed:15530417, PubMed:21179194). {ECO:0000269|PubMed:15530417,
CC ECO:0000269|PubMed:21179194}.
CC -!- DISRUPTION PHENOTYPE: Temperature sensitive with partial embryonic
CC lethality at 25 degrees Celsius (PubMed:24595290). Inhibited
CC degradation of maternal membrane proteins, cav-1, chs-1 and rme-2, and
CC ubiquitination of cav-1 with accumulation of these proteins on the
CC maternal plasma membrane and endosome-like vesicles in later-stage
CC embryos (PubMed:24595290). RNAi-mediated knockdown prevents
CC localization of ubiquitin and proteasomes to polyglutamine protein
CC aggregates (PubMed:17663792). Reduced growth of polyglutamine protein
CC aggregates (PubMed:17663792, PubMed:22494772). Inhibited degradation of
CC maternal membrane protein, cav-1 in embryos (PubMed:24595290).
CC {ECO:0000269|PubMed:17663792, ECO:0000269|PubMed:22494772,
CC ECO:0000269|PubMed:24595290}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|RuleBase:RU004027}.
CC -!- CAUTION: Has no ubiquitin ligase activity on its own; may require
CC ubiquitin-conjugating enzyme, ubc-13. {ECO:0000269|PubMed:15530417}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX284604; CCD83521.1; -; Genomic_DNA.
DR RefSeq; NP_500272.2; NM_067871.6.
DR AlphaFoldDB; Q95XX0; -.
DR SMR; Q95XX0; -.
DR ComplexPortal; CPX-4625; ubc-13-uev-1 ubiquitin-conjugating enzyme E2 complex.
DR IntAct; Q95XX0; 3.
DR MINT; Q95XX0; -.
DR STRING; 6239.Y54G2A.31; -.
DR EPD; Q95XX0; -.
DR PaxDb; Q95XX0; -.
DR PeptideAtlas; Q95XX0; -.
DR EnsemblMetazoa; Y54G2A.31.1; Y54G2A.31.1; WBGene00006708.
DR GeneID; 177073; -.
DR KEGG; cel:CELE_Y54G2A.31; -.
DR UCSC; Y54G2A.31; c. elegans.
DR CTD; 177073; -.
DR WormBase; Y54G2A.31; CE31652; WBGene00006708; ubc-13.
DR eggNOG; KOG0417; Eukaryota.
DR GeneTree; ENSGT00540000070023; -.
DR HOGENOM; CLU_030988_13_2_1; -.
DR InParanoid; Q95XX0; -.
DR OMA; QWKVNES; -.
DR OrthoDB; 1345547at2759; -.
DR PhylomeDB; Q95XX0; -.
DR Reactome; R-CEL-1169408; ISG15 antiviral mechanism.
DR Reactome; R-CEL-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-CEL-9020702; Interleukin-1 signaling.
DR Reactome; R-CEL-9646399; Aggrephagy.
DR Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q95XX0; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00006708; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0035370; C:UBC13-UEV1A complex; IPI:ComplexPortal.
DR GO; GO:0031371; C:ubiquitin conjugating enzyme complex; IDA:WormBase.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:1902533; P:positive regulation of intracellular signal transduction; IC:ComplexPortal.
DR GO; GO:1902523; P:positive regulation of protein K63-linked ubiquitination; IC:ComplexPortal.
DR GO; GO:0006301; P:postreplication repair; IBA:GO_Central.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IDA:WormBase.
DR GO; GO:2000008; P:regulation of protein localization to cell surface; IMP: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 Ligase; Reference proteome; Transferase; Ubl conjugation pathway.
FT CHAIN 1..151
FT /note="Ubiquitin-conjugating enzyme E2 13"
FT /evidence="ECO:0000305"
FT /id="PRO_0000434947"
FT DOMAIN 4..150
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 88
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
SQ SEQUENCE 151 AA; 16902 MW; BEE42F2D2D82C69E CRC64;
MAGQLPRRII KETQRLLADP VPGISANPDE SNARYFHVMI AGPDDSPFAG GVFKLELFLP
EEYPMAAPKV RFMTKIYHPN IDKLGRICLD ILKDKWSPAL QIRTVLLSIQ ALLSAPNPED
PLATDVAEQW KTNEAEAIKT AKQWTMNYAQ A
