ID   UB2WB_DANRE             Reviewed;         151 AA.
AC   Q1JPX4; A4VCG8; F1QRU3;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=Probable ubiquitin-conjugating enzyme E2 W-B;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme W-B;
DE   AltName: Full=N-terminal E2 ubiquitin-conjugating enzyme;
DE            EC=2.3.2.25;
DE   AltName: Full=Ubiquitin carrier protein W-B;
DE   AltName: Full=Ubiquitin-protein ligase W-B;
GN   Name=ube2wb; ORFNames=zgc:136503;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye, and Ovary;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
CC       covalent attachment to other proteins. Catalyzes monoubiquitination.
CC       Involved in degradation of misfolded chaperone substrate and DNA
CC       repair. {ECO:0000250|UniProtKB:Q96B02}.
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:0000250|UniProtKB:Q96B02, ECO:0000255|PROSITE-
CC         ProRule:PRU00388};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC         [acceptor protein]-N-terminal-amino acid = [E1 ubiquitin-activating
CC         enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein].;
CC         EC=2.3.2.25; Evidence={ECO:0000250|UniProtKB:Q96B02};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96B02}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; CR405710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC116563; AAI16564.1; -; mRNA.
DR   EMBL; BC139652; AAI39653.1; -; mRNA.
DR   EMBL; BC162614; AAI62614.1; -; mRNA.
DR   RefSeq; NP_001038758.2; NM_001045293.2.
DR   AlphaFoldDB; Q1JPX4; -.
DR   SMR; Q1JPX4; -.
DR   STRING; 7955.ENSDARP00000108136; -.
DR   PaxDb; 7955-ENSDARP00000108136; -.
DR   GeneID; 692325; -.
DR   KEGG; dre:692325; -.
DR   AGR; ZFIN:ZDB-GENE-050113-1; -.
DR   CTD; 692325; -.
DR   ZFIN; ZDB-GENE-050113-1; ube2wb.
DR   eggNOG; KOG0427; Eukaryota.
DR   InParanoid; Q1JPX4; -.
DR   OrthoDB; 452at2759; -.
DR   PhylomeDB; Q1JPX4; -.
DR   Reactome; R-DRE-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR   Reactome; R-DRE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q1JPX4; -.
DR   Proteomes; UP000000437; Alternate scaffold 24.
DR   Proteomes; UP000000437; Chromosome 24.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR   GO; GO:0071218; P:cellular response to misfolded protein; ISS:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0006513; P:protein monoubiquitination; ISS:UniProtKB.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; ISS:UniProtKB.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   PANTHER; PTHR24067:SF373; UBIQUITIN-CONJUGATING ENZYME E2 W; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 1.
DR   PROSITE; PS50127; UBC_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; DNA damage; DNA repair; Nucleotide-binding; Nucleus;
KW   Reference proteome; Transferase; Ubl conjugation pathway.
FT   CHAIN           1..151
FT                   /note="Probable ubiquitin-conjugating enzyme E2 W-B"
FT                   /id="PRO_0000416881"
FT   DOMAIN          3..151
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   ACT_SITE        91
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   CONFLICT        66
FT                   /note="F -> S (in Ref. 2; AAI39653)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   151 AA;  17307 MW;  43F0F7590CDBF548 CRC64;
     MASMQKRLQK ELLALQNDPP PGMTLNEKSV QNTITQWIVD MEGASGTVYE GEKFQLLFKF
     SSRYPFDSPQ VMFTGDNIPV HPHVYSNGHI CLSILTEDWS PALSVQSVCL SIISMLSSCK
     EKRRPPDNSF YVRTCNKNPK KTKWWYHDDT C
//