ID   UBE2W_BOVIN             Reviewed;         151 AA.
AC   A6H795;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 W;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme W;
DE   AltName: Full=N-terminal E2 ubiquitin-conjugating enzyme;
DE            EC=2.3.2.25;
DE   AltName: Full=N-terminus-conjugating E2;
DE   AltName: Full=Ubiquitin carrier protein W;
DE   AltName: Full=Ubiquitin-protein ligase W;
GN   Name=UBE2W;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Hypothalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
CC       covalent attachment to other proteins. Specifically monoubiquitinates
CC       the N-terminus of various substrates, including ATXN3, MAPT/TAU,
CC       POLR2H/RPB8 and STUB1/CHIP, by recognizing backbone atoms of disordered
CC       N-termini. Involved in degradation of misfolded chaperone substrates by
CC       mediating monoubiquitination of STUB1/CHIP, leading to recruitment of
CC       ATXN3 to monoubiquitinated STUB1/CHIP, and restriction of the length of
CC       ubiquitin chain attached to STUB1/CHIP substrates by ATXN3. After UV
CC       irradiation, but not after mitomycin-C (MMC) treatment, acts as a
CC       specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex
CC       by associating with E3 ubiquitin-protein ligase FANCL and catalyzing
CC       monoubiquitination of FANCD2, a key step in the DNA damage pathway. In
CC       vitro catalyzes 'Lys-11'-linked polyubiquitination. UBE2W-catalyzed
CC       ubiquitination occurs also in the presence of inactive RING/U-box type
CC       E3s, i.e. lacking the active site cysteine residues to form thioester
CC       bonds with ubiquitin, or even in the absence of E3, albeit at a slower
CC       rate. {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   -!- SUBUNIT: Homodimer. Interacts with FANCL. Interacts with STUB1/CHIP.
CC       {ECO:0000250|UniProtKB:Q8VDW4, ECO:0000250|UniProtKB:Q96B02}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96B02}. Note=In
CC       the nucleus, colocalizes with FANCL. {ECO:0000250|UniProtKB:Q96B02}.
CC   -!- PTM: Ubiquitinated in vitro in the presence of FANCL. Autoubiquitinated
CC       at Met-1. {ECO:0000250|UniProtKB:Q8VDW4, 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; BC146162; AAI46163.1; -; mRNA.
DR   RefSeq; NP_001092592.1; NM_001099122.1.
DR   AlphaFoldDB; A6H795; -.
DR   SMR; A6H795; -.
DR   STRING; 9913.ENSBTAP00000010872; -.
DR   PaxDb; 9913-ENSBTAP00000010872; -.
DR   Ensembl; ENSBTAT00000083257.1; ENSBTAP00000064722.1; ENSBTAG00000048843.1.
DR   GeneID; 613423; -.
DR   KEGG; bta:613423; -.
DR   CTD; 55284; -.
DR   VEuPathDB; HostDB:ENSBTAG00000048843; -.
DR   eggNOG; KOG0427; Eukaryota.
DR   GeneTree; ENSGT00940000156908; -.
DR   HOGENOM; CLU_030988_15_1_1; -.
DR   InParanoid; A6H795; -.
DR   TreeFam; TF314582; -.
DR   Reactome; R-BTA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR   Reactome; R-BTA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000009136; Chromosome 14.
DR   Bgee; ENSBTAG00000048843; Expressed in neutrophil and 109 other cell types or tissues.
DR   ExpressionAtlas; A6H795; baseline and differential.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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; Ubl conjugation pathway.
FT   CHAIN           1..151
FT                   /note="Ubiquitin-conjugating enzyme E2 W"
FT                   /id="PRO_0000414630"
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   CROSSLNK        1
FT                   /note="Peptide (Met-Gly) (interchain with G-Cter in
FT                   ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q96B02"
SQ   SEQUENCE   151 AA;  17331 MW;  276B585BBC4CEB71 CRC64;
     MASMQKRLQK ELLALQNDPP PGMTLNEKSV QNSITQWIVD MEGAPGTLYE GEKFQLLFKF
     SSRYPFDSPQ VMFTGENIPV HPHVYSNGHI CLSILTEDWS PALSVQSVCL SIISMLSSCK
     EKRRPPDNSF YVRTCNKNPK KTKWWYHDDT C
//