UB2R2_RABIT
ID UB2R2_RABIT Reviewed; 238 AA.
AC Q29503;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 R2;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme R2;
DE AltName: Full=Ubiquitin carrier protein R2;
DE AltName: Full=Ubiquitin-conjugating enzyme E2-CDC34B;
DE AltName: Full=Ubiquitin-protein ligase R2;
GN Name=UBE2R2; Synonyms=CDC34B;
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].
RC TISSUE=Heart;
RX PubMed=9116038; DOI=10.1016/s0167-4781(96)00209-6;
RA Sun B.G., Jeyaseelan K., Chung M.C.M., Tan T.-W., Chock P.B., Teo T.-S.;
RT "Cloning, characterization and expression of a cDNA clone encoding rabbit
RT ubiquitin-conjugating enzyme, E2(32k).";
RL Biochim. Biophys. Acta 1351:231-238(1997).
CC -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. In vitro catalyzes
CC monoubiquitination and 'Lys-48'-linked polyubiquitination. May be
CC involved in degradation of katenin. {ECO:0000250|UniProtKB:Q712K3}.
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: When phosphorylated, interacts with beta-TrCP (BTRC).
CC {ECO:0000250|UniProtKB:Q712K3}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- CAUTION: Was originally thought to be UBE2R1/CDC34.
CC {ECO:0000305|PubMed:9116038}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB02656.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U58652; AAB02656.1; ALT_INIT; mRNA.
DR RefSeq; XP_008273222.1; XM_008275000.2.
DR AlphaFoldDB; Q29503; -.
DR SMR; Q29503; -.
DR BioGRID; 1172455; 5.
DR STRING; 9986.ENSOCUP00000024929; -.
DR Ensembl; ENSOCUT00000027595; ENSOCUP00000024929; ENSOCUG00000023588.
DR GeneID; 100009436; -.
DR KEGG; ocu:100009436; -.
DR CTD; 54926; -.
DR eggNOG; KOG0425; Eukaryota.
DR GeneTree; ENSGT00940000158828; -.
DR InParanoid; Q29503; -.
DR OrthoDB; 1116856at2759; -.
DR TreeFam; TF101107; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001811; Chromosome 1.
DR Bgee; ENSOCUG00000023588; Expressed in blood and 16 other tissues.
DR ExpressionAtlas; Q29503; baseline.
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 GO; GO:0006513; P:protein monoubiquitination; ISS:UniProtKB.
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; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transferase; Ubl conjugation pathway.
FT CHAIN 1..238
FT /note="Ubiquitin-conjugating enzyme E2 R2"
FT /id="PRO_0000082453"
FT DOMAIN 8..174
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 194..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..238
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 93
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT MOD_RES 233
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q712K3"
SQ SEQUENCE 238 AA; 27166 MW; E896CF0116A56308 CRC64;
MAQQQMTSSQ KALMLELKSL QEEPVEGFRI TLVDESDLYN WEVAIFGPPN TLYEGGYFKA
HIKFPIDYPY SPPTFRFLTK MWHPNIYENG DVCISILHPP VDDPQSGELP SERWNPTQNV
RTILLSVISL LNEPNTFSPA NVDASVMFRK WRDSKGKDKE YAEIIRKQVS ATKAEAEKDG
VKVPTTLAEY CIKTKVPSND NSSDLLYDDL YDDDIDDEDE EEEDADCYDD DDSGNEES
