UBE2W_RAT
ID UBE2W_RAT Reviewed; 151 AA.
AC B5DEI4;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 W;
DE EC=2.3.2.25;
DE AltName: Full=E2 ubiquitin-conjugating enzyme W;
DE AltName: Full=N-terminal E2 ubiquitin-conjugating enzyme;
DE EC=2.3.2.23;
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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: Autoubiquitinated at Met-1. {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; BC168682; AAI68682.1; -; mRNA.
DR RefSeq; XP_006237984.2; XM_006237922.2.
DR RefSeq; XP_008756764.1; XM_008758542.2.
DR RefSeq; XP_008771705.1; XM_008773483.2.
DR AlphaFoldDB; B5DEI4; -.
DR SMR; B5DEI4; -.
DR STRING; 10116.ENSRNOP00000063975; -.
DR PaxDb; B5DEI4; -.
DR PeptideAtlas; B5DEI4; -.
DR GeneID; 100909445; -.
DR CTD; 55284; -.
DR RGD; 1595332; LOC682704.
DR eggNOG; KOG0427; Eukaryota.
DR InParanoid; B5DEI4; -.
DR OrthoDB; 1522577at2759; -.
DR PhylomeDB; B5DEI4; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:B5DEI4; -.
DR Proteomes; UP000002494; Unplaced.
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; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 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_0000414631"
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
