UBE2T_BOVIN
ID UBE2T_BOVIN Reviewed; 195 AA.
AC Q32LD2; G3X6G9;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 T;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme T;
DE AltName: Full=Ubiquitin carrier protein T;
DE AltName: Full=Ubiquitin-protein ligase T;
GN Name=UBE2T;
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 GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) 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 mitomycin-C (MMC)-induced DNA repair: acts as a specific E2
CC ubiquitin-conjugating enzyme for the Fanconi anemia complex by
CC associating with E3 ubiquitin-protein ligase FANCL and catalyzing
CC monoubiquitination of FANCD2, a key step in the DNA damage pathway.
CC Also mediates monoubiquitination of FANCL and FANCI. May contribute to
CC ubiquitination and degradation of BRCA1. In vitro able to promote
CC polyubiquitination using all 7 ubiquitin Lys residues, but may prefer
CC 'Lys-11'-, 'Lys-27'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination.
CC {ECO:0000250|UniProtKB:Q9NPD8}.
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 FANCL and BRCA1.
CC {ECO:0000250|UniProtKB:Q9NPD8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NPD8}.
CC Note=Accumulates to chromatin. {ECO:0000250|UniProtKB:Q9NPD8}.
CC -!- PTM: Auto-ubiquitinated. Effects of auto-monoubiquitination at Lys-91
CC and Lys-180 are unclear. {ECO:0000250|UniProtKB:Q9NPD8}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; DAAA02043707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC109637; AAI09638.1; -; mRNA.
DR RefSeq; NP_001033123.1; NM_001038034.2.
DR AlphaFoldDB; Q32LD2; -.
DR SMR; Q32LD2; -.
DR STRING; 9913.ENSBTAP00000006290; -.
DR PaxDb; Q32LD2; -.
DR PRIDE; Q32LD2; -.
DR GeneID; 505314; -.
DR KEGG; bta:505314; -.
DR CTD; 29089; -.
DR eggNOG; KOG0417; Eukaryota.
DR HOGENOM; CLU_030988_13_2_1; -.
DR InParanoid; Q32LD2; -.
DR OrthoDB; 1431031at2759; -.
DR TreeFam; TF354203; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
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:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0044314; P:protein K27-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0035519; P:protein K29-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0085020; P:protein K6-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
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 2: Evidence at transcript level;
KW ATP-binding; DNA damage; DNA repair; Isopeptide bond; Nucleotide-binding;
KW Nucleus; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..195
FT /note="Ubiquitin-conjugating enzyme E2 T"
FT /id="PRO_0000281863"
FT DOMAIN 2..152
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 146..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 86
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT CROSSLNK 91
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9NPD8"
FT CROSSLNK 180
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9NPD8"
FT CROSSLNK 189
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NPD8"
FT CONFLICT 110
FT /note="S -> C (in Ref. 2; AAI09638)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 195 AA; 21765 MW; 191CF2C9F50CE22B CRC64;
MQRTSRLKRE LSLLAAEPPP GITCWQDGDR MEDLRAQILG GANTPYEKGV FKLEVHIPER
YPFEPPQIRF LTPIYHPNID SAGRICLDVL KLPPKGAWRP SLNIATLLTS IQQLMAEPNP
DDPLMADISS EFKYNKPVFF KNARQWTEKH ARQKTDEEGM PGSLPEVGGS EGPSAAQKRK
AGQLSSGGKR FCPDV
