UB2Q2_BOVIN
ID UB2Q2_BOVIN Reviewed; 342 AA.
AC Q32L27;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 Q2;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme Q2;
DE AltName: Full=Ubiquitin carrier protein Q2;
DE AltName: Full=Ubiquitin-protein ligase Q2;
GN Name=UBE2Q2;
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=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. In vitro catalyzes 'Lys-48'-
CC linked polyubiquitination. {ECO:0000250|UniProtKB:Q8WVN8}.
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};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8WVN8}.
CC -!- PTM: Auto-ubiquitinated in vitro. {ECO:0000250|UniProtKB:Q8WVN8}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; BC109798; AAI09799.1; -; mRNA.
DR RefSeq; NP_001068998.1; NM_001075530.2.
DR AlphaFoldDB; Q32L27; -.
DR SMR; Q32L27; -.
DR STRING; 9913.ENSBTAP00000005257; -.
DR PaxDb; Q32L27; -.
DR PRIDE; Q32L27; -.
DR Ensembl; ENSBTAT00000005257; ENSBTAP00000005257; ENSBTAG00000004024.
DR GeneID; 511631; -.
DR KEGG; bta:511631; -.
DR CTD; 92912; -.
DR VEuPathDB; HostDB:ENSBTAG00000004024; -.
DR VGNC; VGNC:36593; UBE2Q2.
DR eggNOG; KOG0897; Eukaryota.
DR GeneTree; ENSGT00940000155357; -.
DR HOGENOM; CLU_053863_0_0_1; -.
DR InParanoid; Q32L27; -.
DR OrthoDB; 1214134at2759; -.
DR TreeFam; TF313338; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 21.
DR Bgee; ENSBTAG00000004024; Expressed in spermatocyte and 105 other tissues.
DR ExpressionAtlas; Q32L27; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 2.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 2.
DR PROSITE; PS50127; UBC_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Reference proteome;
KW Transferase; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..342
FT /note="Ubiquitin-conjugating enzyme E2 Q2"
FT /id="PRO_0000223878"
FT DOMAIN 171..335
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 88..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 271
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
SQ SEQUENCE 342 AA; 38717 MW; 5BB0CFBD4222BA51 CRC64;
MSVSGLKAEL KFLASIFDKN HERFRIVSWK LDELHCQFLV PPPAPPGSPH SPPPPLTLHC
NITESYPSSS PIWFVDSDDP NLTSVLERLE DTKNNNSNGT TEEVTSEEEE EEEMAEDIED
LDHYEMKEEE PISGKKSEDE GIEKENLAIL EKIRKTQRQD HLNGAVSGSV QASDRLMKEL
RDIYRSQSYK TGIYSVELIN DSLYDWHVKL QKVDPDSPLH SDLQILKEKE GIEYILLNFS
FKDNFPFDPP FVRVVLPVLS GGYVLGGGAL CMELLTKQGW SSAYSIESVI MQINATLVKG
KARVQFGANK NQYNLARAQQ SYNSIVQIHE KNGWYTPPKE DG
