UB2Q2_RABIT
ID UB2Q2_RABIT Reviewed; 369 AA.
AC Q7YQJ9;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
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-conjugating enzyme UBCi;
DE AltName: Full=Ubiquitin-protein ligase Q2;
GN Name=UBE2Q2;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Endometrium;
RX PubMed=14561654; DOI=10.1095/biolreprod.103.020719;
RA Melner M.H., Ducharme N.A., Brash A.R., Winfrey V.P., Olson G.E.;
RT "Differential expression of genes in the endometrium at implantation:
RT upregulation of a novel member of the E2 class of ubiquitin-conjugating
RT enzymes.";
RL Biol. Reprod. 70:406-414(2004).
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 -!- TISSUE SPECIFICITY: Detected at embryo implantation sites in the
CC luminal epithelium of pregnant endometrium. Detected at low levels in
CC ovary and liver. {ECO:0000269|PubMed:14561654}.
CC -!- INDUCTION: Up-regulated in pregnant endometrium during implantation.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY330351; AAP93920.1; -; mRNA.
DR RefSeq; NP_001076163.1; NM_001082694.1.
DR AlphaFoldDB; Q7YQJ9; -.
DR SMR; Q7YQJ9; -.
DR STRING; 9986.ENSOCUP00000021489; -.
DR Ensembl; ENSOCUT00000029964; ENSOCUP00000021489; ENSOCUG00000022720.
DR GeneID; 100009425; -.
DR KEGG; ocu:100009425; -.
DR CTD; 92912; -.
DR eggNOG; KOG0897; Eukaryota.
DR GeneTree; ENSGT00940000155357; -.
DR HOGENOM; CLU_053863_0_0_1; -.
DR InParanoid; Q7YQJ9; -.
DR OMA; LHCNITX; -.
DR OrthoDB; 1214134at2759; -.
DR TreeFam; TF313338; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000022720; Expressed in left lung and 15 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:UniProtKB-EC.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; 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; 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..369
FT /note="Ubiquitin-conjugating enzyme E2 Q2"
FT /id="PRO_0000223881"
FT DOMAIN 198..362
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 117..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 298
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
SQ SEQUENCE 369 AA; 42192 MW; 3B88532499960CF3 CRC64;
MSVSGLKAEL KFLASIFDKN HERFRIVSWK LDELHCQFLV PPPAPPLLTL HCNITESYPS
SSPIWFVDSD DPNLTSVLER LEDSKNNNSL RQQLKWLICE LCRLYNLPKH LDVEMLDQPL
PTGQNGTTEE VTSEEEEEEE MAEDIEDLDH YEMKEEEPIN GRKSEDEGIE KENLAILEKI
RKSQRQDHLN GAVSGSVQAS DRLMKELRDI YRSQSYKTGI YSVELINDSL YDWHVKLQKV
DPDSPLHSDL QILKEKEGIE YILLNFSFKD NFPFDPPFVR VVLPVLSGGY VLGGGALCME
LLTKQGWSSA YSIESVIMQI NATLVKGKAR VQFGANKNQY NLARAQQSYN SIVQIHEKNG
WYTPPKEDG
