UBC2_CAEEL
ID UBC2_CAEEL Reviewed; 147 AA.
AC P35129;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 2;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 2;
DE AltName: Full=Lethal protein 70;
DE AltName: Full=Ubiquitin carrier protein 2;
DE AltName: Full=Ubiquitin-protein ligase 2;
GN Name=let-70 {ECO:0000303|PubMed:8670823, ECO:0000312|WormBase:M7.1};
GN Synonyms=ubc-2 {ECO:0000303|PubMed:8441382, ECO:0000312|WormBase:M7.1};
GN ORFNames=M7.1 {ECO:0000312|WormBase:M7.1};
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], AND DEVELOPMENTAL STAGE.
RX PubMed=8441382; DOI=10.1128/mcb.13.3.1371-1377.1993;
RA Zhen M., Heinlein R., Jones D., Jentsch S., Candido E.P.M.;
RT "The ubc-2 gene of Caenorhabditis elegans encodes a ubiquitin-conjugating
RT enzyme involved in selective protein degradation.";
RL Mol. Cell. Biol. 13:1371-1377(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND MUTAGENESIS OF HIS-75.
RX PubMed=8670823; DOI=10.1002/j.1460-2075.1996.tb00687.x;
RA Zhen M., Scheni J.E., Baillie D.L., Candido E.P.M.;
RT "An essential ubiquitin-conjugating enzyme with tissue and developmental
RT specificity in the nematode Caenorhabditis elegans.";
RL EMBO J. 15:3229-3237(1996).
RN [3]
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 [4]
RP FUNCTION, INTERACTION WITH BRC-1-BRD-1 HETERODIMER, SUBCELLULAR LOCATION,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=16628214; DOI=10.1038/sj.emboj.7601102;
RA Polanowska J., Martin J.S., Garcia-Muse T., Petalcorin M.I.R.,
RA Boulton S.J.;
RT "A conserved pathway to activate BRCA1-dependent ubiquitylation at DNA
RT damage sites.";
RL EMBO J. 25:2178-2188(2006).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF PRO-61.
RX PubMed=26952214; DOI=10.7554/elife.12821;
RA Kinet M.J., Malin J.A., Abraham M.C., Blum E.S., Silverman M.R., Lu Y.,
RA Shaham S.;
RT "HSF-1 activates the ubiquitin proteasome system to promote non-apoptotic
RT developmental cell death in C. elegans.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC proteins (By similarity). Mediates the selective degradation of short-
CC lived and abnormal proteins (PubMed:16628214). Plays a role in the DNA
CC damage response (PubMed:16628214). In particular, in response to
CC ionizing radiation, associates with the E3 ubiquitin-protein ligase
CC brc-1-brd-1 heterodimer on chromatin to activate E3-ubiquitin ligase
CC activity of the heterodimer, and thus its DNA damage repair mechanisms
CC (PubMed:16628214). Required, cell autonomously, for death of the linker
CC cell, a male-specific cell which guides the elongation of the gonad;
CC perhaps acting as part of the ubiquitin proteasome system (UPS) and
CC modulated by heat shock transcription factor hsf-1 (PubMed:26952214).
CC {ECO:0000250|UniProtKB:P06104, ECO:0000269|PubMed:16628214,
CC ECO:0000269|PubMed:26952214}.
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:0000255|PROSITE-
CC ProRule:PRU10133};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBUNIT: Interacts with the brc-1-brd-1 heterodimer following ionizing
CC irradiation. {ECO:0000269|PubMed:16628214}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16628214,
CC ECO:0000269|PubMed:26952214}. Chromosome {ECO:0000269|PubMed:16628214}.
CC Cytoplasm {ECO:0000269|PubMed:26952214}.
CC -!- TISSUE SPECIFICITY: Expressed in the nervous system.
CC {ECO:0000269|PubMed:8670823}.
CC -!- DEVELOPMENTAL STAGE: Expressed at all stages of development
CC (PubMed:8441382, PubMed:8670823). Expressed in most embryonic tissues
CC and larval tissues at the early stages (PubMed:8670823). Highly
CC expressed in neurons, pharynx, the hyperdermis and body muscles in L1,
CC L2, L3 and dauer larvae (PubMed:8670823). From the L4 stage of larval
CC development and in adults, expression is mainly restricted to the
CC nervous system, but is also expressed in the pharynx and hyperdermis
CC (PubMed:8670823). Expressed in the linker cell, a male-specific cell
CC which guides the elongation of the gonad, about 1-2 hours before
CC induction of linker cell death (PubMed:26952214).
CC {ECO:0000269|PubMed:26952214, ECO:0000269|PubMed:8441382,
CC ECO:0000269|PubMed:8670823}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in reduced
CC ubiquitination at DNA damage sites (PubMed:16628214). Inappropriate
CC survival of male gonadal linker cell (PubMed:26952214).
CC {ECO:0000269|PubMed:16628214, ECO:0000269|PubMed:26952214}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; S56051; AAB25489.2; -; Genomic_DNA.
DR EMBL; Z68337; CAA92745.1; -; Genomic_DNA.
DR PIR; A48145; A48145.
DR PIR; T23820; T23820.
DR RefSeq; NP_502065.1; NM_069664.4.
DR PDB; 1Z2U; X-ray; 1.10 A; A=1-147.
DR PDBsum; 1Z2U; -.
DR AlphaFoldDB; P35129; -.
DR SMR; P35129; -.
DR BioGRID; 43106; 23.
DR DIP; DIP-24306N; -.
DR IntAct; P35129; 2.
DR STRING; 6239.M7.1; -.
DR EPD; P35129; -.
DR PaxDb; P35129; -.
DR PeptideAtlas; P35129; -.
DR EnsemblMetazoa; M7.1.1; M7.1.1; WBGene00002344.
DR GeneID; 178006; -.
DR KEGG; cel:CELE_M7.1; -.
DR UCSC; M7.1; c. elegans.
DR CTD; 178006; -.
DR WormBase; M7.1; CE03482; WBGene00002344; let-70.
DR eggNOG; KOG0417; Eukaryota.
DR GeneTree; ENSGT00940000155109; -.
DR HOGENOM; CLU_030988_13_3_1; -.
DR InParanoid; P35129; -.
DR OMA; QMDICLL; -.
DR OrthoDB; 1337945at2759; -.
DR PhylomeDB; P35129; -.
DR Reactome; R-CEL-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-CEL-201451; Signaling by BMP.
DR Reactome; R-CEL-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR Reactome; R-CEL-5689896; Ovarian tumor domain proteases.
DR Reactome; R-CEL-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-CEL-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-CEL-8951664; Neddylation.
DR Reactome; R-CEL-9033241; Peroxisomal protein import.
DR Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; P35129; -.
DR PRO; PR:P35129; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00002344; Expressed in embryo and 4 other tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IMP:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:WormBase.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:WormBase.
DR GO; GO:0010623; P:programmed cell death involved in cell development; IMP:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IDA:WormBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; 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; Chromosome; Cytoplasm; Nucleotide-binding;
KW Nucleus; Reference proteome; Transferase; Ubl conjugation pathway.
FT CHAIN 1..147
FT /note="Ubiquitin-conjugating enzyme E2 2"
FT /id="PRO_0000082515"
FT DOMAIN 1..147
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 85
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT MUTAGEN 61
FT /note="P->S: In ns770; Viable. Inappropriate survival of
FT male gonadal linker cell; exacerbated on a heat shock
FT transcription factor hsf-1 mutant background. Simultaneous
FT RNAi-mediated knockdown of cul-3 causes a synergistic
FT increase in linker cell survival."
FT /evidence="ECO:0000269|PubMed:26952214"
FT MUTAGEN 75
FT /note="H->Y: In s1132; hermaphrodites arrest during the
FT early stages of larval stages."
FT /evidence="ECO:0000269|PubMed:8670823"
FT HELIX 1..15
FT /evidence="ECO:0007829|PDB:1Z2U"
FT STRAND 19..26
FT /evidence="ECO:0007829|PDB:1Z2U"
FT STRAND 29..38
FT /evidence="ECO:0007829|PDB:1Z2U"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:1Z2U"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:1Z2U"
FT TURN 58..61
FT /evidence="ECO:0007829|PDB:1Z2U"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:1Z2U"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:1Z2U"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:1Z2U"
FT HELIX 99..111
FT /evidence="ECO:0007829|PDB:1Z2U"
FT HELIX 121..129
FT /evidence="ECO:0007829|PDB:1Z2U"
FT HELIX 131..145
FT /evidence="ECO:0007829|PDB:1Z2U"
SQ SEQUENCE 147 AA; 16705 MW; 9E91884D307F2120 CRC64;
MALKRIQKEL QDLGRDPPAQ CSAGPVGDDL FHWQATIMGP PESPYQGGVF FLTIHFPTDY
PFKPPKVAFT TRIYHPNINS NGSICLDILR SQWSPALTIS KVLLSICSLL CDPNPDDPLV
PEIARIYKTD RERYNQLARE WTQKYAM
