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Ubiquitin-conjugating enzyme E2 D3 (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme D3) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme D3) (Phosphoarginine phosphatase) (PAPase) (Ubiquitin carrier protein D3) (Ubiquitin-conjugating enzyme E2(17)KB 3) (Ubiquitin-conjugating enzyme E2-17 kDa 3) (Ubiquitin-protein ligase D3)

 UB2D3_RAT               Reviewed;         147 AA.
P61078; P47986;
26-APR-2004, integrated into UniProtKB/Swiss-Prot.
26-APR-2004, sequence version 1.
05-DEC-2018, entry version 117.
RecName: Full=Ubiquitin-conjugating enzyme E2 D3;
EC=2.3.2.23;
AltName: Full=(E3-independent) E2 ubiquitin-conjugating enzyme D3;
EC=2.3.2.24;
AltName: Full=E2 ubiquitin-conjugating enzyme D3;
AltName: Full=Phosphoarginine phosphatase;
Short=PAPase;
AltName: Full=Ubiquitin carrier protein D3;
AltName: Full=Ubiquitin-conjugating enzyme E2(17)KB 3;
AltName: Full=Ubiquitin-conjugating enzyme E2-17 kDa 3;
AltName: Full=Ubiquitin-protein ligase D3;
Name=Ube2d3;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
PubMed=7826319; DOI=10.1042/bj3050125;
Wing S.S., Jain P.;
"Molecular cloning, expression and characterization of a ubiquitin
conjugation enzyme (E2(17)kB) highly expressed in rat testis.";
Biochem. J. 305:125-132(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Liver;
Yokoi F., Hamato N., Kamei K., Hara S., Miyagi M., Tsunasawa S.,
Hiraishi H., Kumon A.;
"Nomega-phosphoarginine phosphatase activity of ubiquitin-conjugating
enzymes type UBC4A/10A and UBC2E.";
Res. Commun. Biochem. Cell Mol. Biol. 2:331-346(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Heart;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
covalent attachment to other proteins. In vitro catalyzes 'Lys-
11'-, as well as 'Lys-48'-linked polyubiquitination. Cooperates
with the E2 CDC34 and the SCF(FBXW11) E3 ligase complex for the
polyubiquitination of NFKBIA leading to its subsequent proteasomal
degradation. Acts as an initiator E2, priming the phosphorylated
NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a
monoubiquitin. Ubiquitin chain elongation is then performed by
CDC34, building ubiquitin chains from the UBE2D3-primed NFKBIA-
linked ubiquitin. Acts also as an initiator E2, in conjunction
with RNF8, for the priming of PCNA. Monoubiquitination of PCNA,
and its subsequent polyubiquitination, are essential events in the
operation of the DNA damage tolerance (DDT) pathway that is
activated after DNA damage caused by UV or chemical agents during
S-phase. Associates with the BRCA1/BARD1 E3 ligase complex to
perform ubiquitination at DNA damage sites following ionizing
radiation leading to DNA repair. Targets DAPK3 for ubiquitination
which influences promyelocytic leukemia protein nuclear body (PML-
NB) formation in the nucleus. In conjunction with the MDM2 and
TOPORS E3 ligases, functions ubiquitination of p53/TP53. Supports
NRDP1-mediated ubiquitination and degradation of ERBB3 and of
BRUCE which triggers apoptosis. In conjunction with the CBL E3
ligase, targets EGFR for polyubiquitination at the plasma membrane
as well as during its internalization and transport on endosomes.
In conjunction with the STUB1 E3 quality control E3 ligase,
ubiquitinates unfolded proteins to catalyze their immediate
destruction. {ECO:0000250|UniProtKB:P61077}.
-!- CATALYTIC ACTIVITY:
Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
+ [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
Evidence={ECO:0000250|UniProtKB:P61077, ECO:0000255|PROSITE-
ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133};
-!- CATALYTIC ACTIVITY:
Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
+ [acceptor protein]-L-lysine = [E1 ubiquitin-activating
enzyme]-L-cysteine + N(6)-monoubiquitinyl-[acceptor protein]-L-
lysine.; EC=2.3.2.24; Evidence={ECO:0000250|UniProtKB:P61077};
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-!- SUBUNIT: Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin
ligase complex; when Cullin is neddylated, the interaction between
the E2 and the SCF complex is strengthened. Interacts with DAPK3.
Interacts with BRCA1; the DNA damage checkpoint promotes the
association with BRCA1 after ionizing radiation. Interacts non-
covalently with ubiquitin. Interacts with E3 ubiquitin-protein
ligase CBLC. Interacts with UBTD1 (By similarity).
{ECO:0000250|UniProtKB:P61077}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P61077}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P61077}. Endosome membrane
{ECO:0000250|UniProtKB:P61077}; Peripheral membrane protein
{ECO:0000250|UniProtKB:P61077}.
-!- PTM: Phosphorylated by AURKB. {ECO:0000250|UniProtKB:P61079}.
-!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U13177; AAA85102.1; -; mRNA.
EMBL; U13175; AAA85100.1; -; mRNA.
EMBL; AB006852; BAA87330.1; -; mRNA.
EMBL; BC072696; AAH72696.1; -; mRNA.
PIR; S53358; S53358.
RefSeq; NP_112516.1; NM_031237.1.
RefSeq; XP_006233398.1; XM_006233336.3.
RefSeq; XP_006233399.1; XM_006233337.2.
RefSeq; XP_006233400.1; XM_006233338.2.
UniGene; Rn.2778; -.
ProteinModelPortal; P61078; -.
SMR; P61078; -.
STRING; 10116.ENSRNOP00000060962; -.
iPTMnet; P61078; -.
PhosphoSitePlus; P61078; -.
SwissPalm; P61078; -.
PaxDb; P61078; -.
PeptideAtlas; P61078; -.
PRIDE; P61078; -.
Ensembl; ENSRNOT00000066204; ENSRNOP00000060962; ENSRNOG00000013741.
GeneID; 81920; -.
KEGG; rno:81920; -.
CTD; 7323; -.
RGD; 619912; Ube2d3.
eggNOG; KOG0417; Eukaryota.
eggNOG; COG5078; LUCA.
GeneTree; ENSGT00940000153169; -.
HOGENOM; HOG000233455; -.
HOVERGEN; HBG063308; -.
InParanoid; P61078; -.
KO; K06689; -.
OMA; MIHFPPD; -.
OrthoDB; EOG091G0GF8; -.
PhylomeDB; P61078; -.
Reactome; R-RNO-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-RNO-201451; Signaling by BMP.
Reactome; R-RNO-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
Reactome; R-RNO-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
Reactome; R-RNO-8951664; Neddylation.
Reactome; R-RNO-9033241; Peroxisomal protein import.
Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
PRO; PR:P61078; -.
Proteomes; UP000002494; Chromosome 2.
Bgee; ENSRNOG00000013741; Expressed in 10 organ(s), highest expression level in spleen.
ExpressionAtlas; P61078; baseline and differential.
Genevisible; P61078; RN.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:RGD.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0051865; P:protein autoubiquitination; IEA:Ensembl.
GO; GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB.
GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
GO; GO:0006513; P:protein monoubiquitination; IEA:Ensembl.
GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:RGD.
CDD; cd00195; UBCc; 1.
Gene3D; 3.10.110.10; -; 1.
InterPro; IPR000608; UBQ-conjugat_E2.
InterPro; IPR023313; UBQ-conjugating_AS.
InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
Pfam; PF00179; UQ_con; 1.
SUPFAM; SSF54495; SSF54495; 1.
PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
2: Evidence at transcript level;
Apoptosis; ATP-binding; Cell membrane; Complete proteome;
Disulfide bond; DNA damage; DNA repair; Endosome; Membrane;
Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
Ubl conjugation pathway.
CHAIN 1 147 Ubiquitin-conjugating enzyme E2 D3.
/FTId=PRO_0000082468.
ACT_SITE 85 85 Glycyl thioester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00388,
ECO:0000255|PROSITE-ProRule:PRU10133}.
DISULFID 21 107 {ECO:0000250|UniProtKB:P61077}.
SEQUENCE 147 AA; 16687 MW; ADD74A8A708EFEE3 CRC64;
MALKRINKEL SDLARDPPAQ CSAGPVGDDM FHWQATIMGP NDSPYQGGVF FLTIHFPTDY
PFKPPKVAFT TRIYHPNINS NGSICLDILR SQWSPALTIS KVLLSICSLL CDPNPDDPLV
PEIARIYKTD RDKYNRISRE WTQKYAM


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