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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) (Ubiquitin carrier protein D3) (Ubiquitin-conjugating enzyme E2(17)KB 3) (Ubiquitin-conjugating enzyme E2-17 kDa 3) (Ubiquitin-protein ligase D3)

 UB2D3_HUMAN             Reviewed;         147 AA.
P61077; A6NJ93; A6NJB1; A6NM99; P47986; Q6IB88; Q6NXS4; Q8N924;
26-APR-2004, integrated into UniProtKB/Swiss-Prot.
26-APR-2004, sequence version 1.
25-OCT-2017, entry version 150.
RecName: Full=Ubiquitin-conjugating enzyme E2 D3;
EC=2.3.2.23 {ECO:0000269|PubMed:20061386};
AltName: Full=(E3-independent) E2 ubiquitin-conjugating enzyme D3;
EC=2.3.2.24 {ECO:0000269|PubMed:17588522};
AltName: Full=E2 ubiquitin-conjugating enzyme D3;
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; Synonyms=UBC5C, UBCH5C;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8530467; DOI=10.1074/jbc.270.51.30408;
Jensen J.P., Bates P.W., Yang M., Vierstra R.D., Weissman A.M.;
"Identification of a family of closely related human ubiquitin
conjugating enzymes.";
J. Biol. Chem. 270:30408-30414(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Chang H.-M., Tsai S.-F.;
"Genome sequencing of the chromosome 4q region implicated in human
hepatocellular carcinoma pathogenesis.";
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Chondrocyte, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Placenta;
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).
[8]
FUNCTION, AND MUTAGENESIS OF CYS-85.
PubMed=10329681; DOI=10.1074/jbc.274.21.14823;
Gonen H., Bercovich B., Orian A., Carrano A., Takizawa C.,
Yamanaka K., Pagano M., Iwai K., Ciechanover A.;
"Identification of the ubiquitin carrier proteins, E2s, involved in
signal-induced conjugation and subsequent degradation of
IkappaBalpha.";
J. Biol. Chem. 274:14823-14830(1999).
[9]
FUNCTION.
PubMed=11743028; DOI=10.1093/embo-reports/kve246;
Murata S., Minami Y., Minami M., Chiba T., Tanaka K.;
"CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded
protein.";
EMBO Rep. 2:1133-1138(2001).
[10]
FUNCTION.
PubMed=12646252; DOI=10.1016/S0006-291X(03)00282-1;
Yogosawa S., Miyauchi Y., Honda R., Tanaka H., Yasuda H.;
"Mammalian Numb is a target protein of Mdm2, ubiquitin ligase.";
Biochem. Biophys. Res. Commun. 302:869-872(2003).
[11]
FUNCTION.
PubMed=15247280; DOI=10.1074/jbc.C400300200;
Rajendra R., Malegaonkar D., Pungaliya P., Marshall H., Rasheed Z.,
Brownell J., Liu L.F., Lutzker S., Saleem A., Rubin E.H.;
"Topors functions as an E3 ubiquitin ligase with specific E2 enzymes
and ubiquitinates p53.";
J. Biol. Chem. 279:36440-36444(2004).
[12]
FUNCTION.
PubMed=15280377; DOI=10.1074/jbc.M403362200;
Saville M.K., Sparks A., Xirodimas D.P., Wardrop J., Stevenson L.F.,
Bourdon J.C., Woods Y.L., Lane D.P.;
"Regulation of p53 by the ubiquitin-conjugating enzymes UbcH5B/C in
vivo.";
J. Biol. Chem. 279:42169-42181(2004).
[13]
FUNCTION.
PubMed=15496420; DOI=10.1074/jbc.M410583200;
Huang J., Huang Q., Zhou X., Shen M.M., Yen A., Yu S.X., Dong G.,
Qu K., Huang P., Anderson E.M., Daniel-Issakani S., Buller R.M.,
Payan D.G., Lu H.H.;
"The poxvirus p28 virulence factor is an E3 ubiquitin ligase.";
J. Biol. Chem. 279:54110-54116(2004).
[14]
INTERACTION WITH BRCA1, AND FUNCTION.
PubMed=16628214; DOI=10.1038/sj.emboj.7601102;
Polanowska J., Martin J.S., Garcia-Muse T., Petalcorin M.I.R.,
Boulton S.J.;
"A conserved pathway to activate BRCA1-dependent ubiquitylation at DNA
damage sites.";
EMBO J. 25:2178-2188(2006).
[15]
CATALYTIC ACTIVITY AS E3-INDEPENDENT E2 UBIQUITIN-CONJUGATING ENZYME.
PubMed=17588522; DOI=10.1016/j.molcel.2007.05.014;
Hoeller D., Hecker C.M., Wagner S., Rogov V., Doetsch V., Dikic I.;
"E3-independent monoubiquitination of ubiquitin-binding proteins.";
Mol. Cell 26:891-898(2007).
[16]
INTERACTION WITH DAPK3, AND FUNCTION.
PubMed=18515077; DOI=10.1016/j.bbrc.2008.05.113;
Ohbayashi N., Okada K., Kawakami S., Togi S., Sato N., Ikeda O.,
Kamitani S., Muromoto R., Sekine Y., Kawai T., Akira S., Matsuda T.;
"Physical and functional interactions between ZIP kinase and UbcH5.";
Biochem. Biophys. Res. Commun. 372:708-712(2008).
[17]
FUNCTION.
PubMed=18948756; DOI=10.4161/cc.7.21.6949;
Zhang S., Chea J., Meng X., Zhou Y., Lee E.Y.C., Lee M.Y.W.T.;
"PCNA is ubiquitinated by RNF8.";
Cell Cycle 7:3399-3404(2008).
[18]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18508924; DOI=10.1091/mbc.E07-10-0988;
Umebayashi K., Stenmark H., Yoshimori T.;
"Ubc4/5 and c-Cbl continue to ubiquitinate EGF receptor after
internalization to facilitate polyubiquitination and degradation.";
Mol. Biol. Cell 19:3454-3462(2008).
[19]
INTERACTION WITH SCF COMPLEX.
PubMed=18851830; DOI=10.1016/j.molcel.2008.08.021;
Saha A., Deshaies R.J.;
"Multimodal activation of the ubiquitin ligase SCF by Nedd8
conjugation.";
Mol. Cell 32:21-31(2008).
[20]
FUNCTION.
PubMed=18284575; DOI=10.1111/j.1365-2958.2008.06124.x;
Kubori T., Hyakutake A., Nagai H.;
"Legionella translocates an E3 ubiquitin ligase that has multiple U-
boxes with distinct functions.";
Mol. Microbiol. 67:1307-1319(2008).
[21]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=20061386; DOI=10.1074/jbc.M109.089003;
David Y., Ziv T., Admon A., Navon A.;
"The E2 ubiquitin-conjugating enzymes direct polyubiquitination to
preferred lysines.";
J. Biol. Chem. 285:8595-8604(2010).
[22]
INTERACTION WITH CBLC.
PubMed=20525694; DOI=10.1074/jbc.M109.091157;
Ryan P.E., Sivadasan-Nair N., Nau M.M., Nicholas S., Lipkowitz S.;
"The N terminus of Cbl-c regulates ubiquitin ligase activity by
modulating affinity for the ubiquitin-conjugating enzyme.";
J. Biol. Chem. 285:23687-23698(2010).
[23]
FUNCTION.
PubMed=20347421; DOI=10.1016/j.molcel.2010.02.025;
Wu K., Kovacev J., Pan Z.Q.;
"Priming and extending: a UbcH5/Cdc34 E2 handoff mechanism for
polyubiquitination on a SCF substrate.";
Mol. Cell 37:784-796(2010).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[25]
FUNCTION, AND MUTAGENESIS OF ASN-77; ASP-87 AND ASP-117.
PubMed=21532592; DOI=10.1038/nature09966;
Wenzel D.M., Lissounov A., Brzovic P.S., Klevit R.E.;
"UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT
hybrids.";
Nature 474:105-108(2011).
[26]
INTERACTION WITH UBTD1.
PubMed=24211586; DOI=10.1016/j.bbrc.2013.10.137;
Uhler J.P., Spaahr H., Farge G., Clavel S., Larsson N.G.,
Falkenberg M., Samuelsson T., Gustafsson C.M.;
"The UbL protein UBTD1 stably interacts with the UBE2D family of E2
ubiquitin conjugating enzymes.";
Biochem. Biophys. Res. Commun. 443:7-12(2014).
[27]
STRUCTURE BY NMR OF 2-147 IN COMPLEX WITH THE BRCA1/BARD1 RING-DOMAIN
HETERODIMER, AND INTERACTION WITH BRCA1.
PubMed=16543155; DOI=10.1016/j.molcel.2006.02.008;
Brzovic P.S., Lissounov A., Christensen D.E., Hoyt D.W., Klevit R.E.;
"A UbcH5/ubiquitin noncovalent complex is required for processive
BRCA1-directed ubiquitination.";
Mol. Cell 21:873-880(2006).
[28]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-147, AND DISULFIDE BOND.
Nakanishi M., Teshima N., Mizushima T., Murata S., Tanaka K.,
Yamane T.;
"Crystal structure of UBCH5C.";
Submitted (FEB-2009) to the PDB data bank.
[29]
X-RAY CRYSTALLOGRAPHY (3.17 ANGSTROMS) OF 1-147 IN COMPLEX WITH U-BOX
DOMAIN OF UBE4B.
Benirschke R., Thompson J.R., Mer G.;
"Crystal structure of the U-Box domain of human e4b ubiquitin ligase
in complex with UBCH5C E2 ubiquitin conjugating enzyme.";
Submitted (MAY-2010) to the PDB data bank.
-!- 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:0000269|PubMed:10329681,
ECO:0000269|PubMed:11743028, ECO:0000269|PubMed:12646252,
ECO:0000269|PubMed:15247280, ECO:0000269|PubMed:15280377,
ECO:0000269|PubMed:15496420, ECO:0000269|PubMed:16628214,
ECO:0000269|PubMed:18284575, ECO:0000269|PubMed:18508924,
ECO:0000269|PubMed:18515077, ECO:0000269|PubMed:18948756,
ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:20347421,
ECO:0000269|PubMed:21532592}.
-!- CATALYTIC ACTIVITY: 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. {ECO:0000255|PROSITE-
ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133,
ECO:0000269|PubMed:20061386}.
-!- CATALYTIC ACTIVITY: 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. {ECO:0000269|PubMed:17588522}.
-!- 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 (PubMed:24211586).
{ECO:0000269|PubMed:16543155, ECO:0000269|PubMed:16628214,
ECO:0000269|PubMed:18515077, ECO:0000269|PubMed:18851830,
ECO:0000269|PubMed:20525694, ECO:0000269|PubMed:24211586,
ECO:0000269|Ref.29}.
-!- INTERACTION:
O54784:Dapk3 (xeno); NbExp=2; IntAct=EBI-348268, EBI-77359;
Q86UW9:DTX2; NbExp=8; IntAct=EBI-348268, EBI-740376;
O15344:MID1; NbExp=8; IntAct=EBI-348268, EBI-2340316;
Q99PZ6:ospG (xeno); NbExp=6; IntAct=EBI-348268, EBI-9316527;
Q96FW1:OTUB1; NbExp=13; IntAct=EBI-348268, EBI-1058491;
Q9Y3C5:RNF11; NbExp=3; IntAct=EBI-348268, EBI-396669;
Q6ZNA4:RNF111; NbExp=5; IntAct=EBI-348268, EBI-2129175;
Q9Y4L5:RNF115; NbExp=6; IntAct=EBI-348268, EBI-2129242;
Q9BV68:RNF126; NbExp=5; IntAct=EBI-348268, EBI-357322;
Q99496:RNF2; NbExp=3; IntAct=EBI-348268, EBI-722416;
Q68DV7:RNF43; NbExp=2; IntAct=EBI-348268, EBI-1647060;
Q99942:RNF5; NbExp=8; IntAct=EBI-348268, EBI-348482;
P0CE12:sspH2 (xeno); NbExp=7; IntAct=EBI-348268, EBI-10761075;
Q9Y4K3:TRAF6; NbExp=2; IntAct=EBI-348268, EBI-359276;
Q9HCM9:TRIM39; NbExp=5; IntAct=EBI-348268, EBI-739510;
O95155-1:UBE4B; NbExp=3; IntAct=EBI-15567256, EBI-15869194;
P98170:XIAP; NbExp=2; IntAct=EBI-348268, EBI-517127;
Q8ND25:ZNRF1; NbExp=3; IntAct=EBI-348268, EBI-2129250;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18508924};
Peripheral membrane protein {ECO:0000269|PubMed:18508924}.
Endosome membrane {ECO:0000269|PubMed:18508924}; Peripheral
membrane protein {ECO:0000269|PubMed:18508924}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P61077-1; Sequence=Displayed;
Name=2;
IsoId=P61077-2; Sequence=VSP_038097;
Name=3;
IsoId=P61077-3; Sequence=VSP_038096;
-!- PTM: Phosphorylated by AURKB. {ECO:0000250|UniProtKB:P61079}.
-!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
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EMBL; U39318; AAA91461.1; -; mRNA.
EMBL; AF213884; AAF35234.1; -; Genomic_DNA.
EMBL; AK095822; BAC04632.1; -; mRNA.
EMBL; DB045280; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; CR456916; CAG33197.1; -; mRNA.
EMBL; AC018797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471057; EAX06138.1; -; Genomic_DNA.
EMBL; CH471057; EAX06143.1; -; Genomic_DNA.
EMBL; BC003395; AAH03395.1; -; mRNA.
EMBL; BC037894; AAH37894.1; -; mRNA.
EMBL; BC066917; AAH66917.1; -; mRNA.
CCDS; CCDS3659.1; -. [P61077-3]
CCDS; CCDS3660.1; -. [P61077-1]
CCDS; CCDS3661.1; -. [P61077-2]
RefSeq; NP_003331.1; NM_003340.6. [P61077-1]
RefSeq; NP_871615.1; NM_181886.3. [P61077-1]
RefSeq; NP_871616.1; NM_181887.2. [P61077-1]
RefSeq; NP_871617.1; NM_181888.3. [P61077-1]
RefSeq; NP_871618.1; NM_181889.2. [P61077-1]
RefSeq; NP_871619.1; NM_181890.2. [P61077-1]
RefSeq; NP_871620.1; NM_181891.2. [P61077-1]
RefSeq; NP_871621.1; NM_181892.3. [P61077-2]
RefSeq; NP_871622.1; NM_181893.2. [P61077-3]
UniGene; Hs.518773; -.
UniGene; Hs.595430; -.
UniGene; Hs.621366; -.
PDB; 1X23; X-ray; 1.85 A; A/B/C/D=1-147.
PDB; 2FUH; NMR; -; A=2-147.
PDB; 3L1Z; X-ray; 3.17 A; A=1-147.
PDB; 3RPG; X-ray; 2.65 A; A=2-147.
PDB; 3UGB; X-ray; 2.35 A; A=1-147.
PDB; 4BVU; X-ray; 2.70 A; B=1-147.
PDB; 4R8P; X-ray; 3.28 A; L/N=2-147.
PDB; 4S3O; X-ray; 2.00 A; A/D=2-147.
PDB; 5EGG; X-ray; 1.76 A; A=1-147.
PDB; 5IFR; X-ray; 2.20 A; A=2-147.
PDBsum; 1X23; -.
PDBsum; 2FUH; -.
PDBsum; 3L1Z; -.
PDBsum; 3RPG; -.
PDBsum; 3UGB; -.
PDBsum; 4BVU; -.
PDBsum; 4R8P; -.
PDBsum; 4S3O; -.
PDBsum; 5EGG; -.
PDBsum; 5IFR; -.
ProteinModelPortal; P61077; -.
SMR; P61077; -.
BioGrid; 113171; 222.
CORUM; P61077; -.
DIP; DIP-29062N; -.
IntAct; P61077; 109.
MINT; MINT-1032046; -.
iPTMnet; P61077; -.
PhosphoSitePlus; P61077; -.
DMDM; 46577654; -.
EPD; P61077; -.
MaxQB; P61077; -.
PaxDb; P61077; -.
PeptideAtlas; P61077; -.
PRIDE; P61077; -.
TopDownProteomics; P61077-1; -. [P61077-1]
TopDownProteomics; P61077-2; -. [P61077-2]
Ensembl; ENST00000321805; ENSP00000318494; ENSG00000109332. [P61077-1]
Ensembl; ENST00000338145; ENSP00000337208; ENSG00000109332. [P61077-1]
Ensembl; ENST00000343106; ENSP00000345285; ENSG00000109332. [P61077-2]
Ensembl; ENST00000349311; ENSP00000344069; ENSG00000109332. [P61077-1]
Ensembl; ENST00000357194; ENSP00000349722; ENSG00000109332. [P61077-3]
Ensembl; ENST00000394801; ENSP00000378280; ENSG00000109332. [P61077-1]
Ensembl; ENST00000394803; ENSP00000378282; ENSG00000109332. [P61077-1]
Ensembl; ENST00000394804; ENSP00000378283; ENSG00000109332. [P61077-1]
Ensembl; ENST00000453744; ENSP00000396901; ENSG00000109332. [P61077-1]
GeneID; 7323; -.
KEGG; hsa:7323; -.
UCSC; uc003hwi.5; human. [P61077-1]
CTD; 7323; -.
DisGeNET; 7323; -.
EuPathDB; HostDB:ENSG00000109332.19; -.
GeneCards; UBE2D3; -.
HGNC; HGNC:12476; UBE2D3.
HPA; HPA003920; -.
MIM; 602963; gene.
neXtProt; NX_P61077; -.
OpenTargets; ENSG00000109332; -.
PharmGKB; PA37126; -.
eggNOG; KOG0417; Eukaryota.
eggNOG; COG5078; LUCA.
GeneTree; ENSGT00900000141035; -.
HOVERGEN; HBG063308; -.
InParanoid; P61077; -.
KO; K06689; -.
OMA; LAQEWTT; -.
OrthoDB; EOG091G0GF8; -.
PhylomeDB; P61077; -.
TreeFam; TF101108; -.
BRENDA; 2.3.2.B6; 2681.
Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-HSA-201451; Signaling by BMP.
Reactome; R-HSA-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-936440; Negative regulators of DDX58/IFIH1 signaling.
Reactome; R-HSA-937041; IKK complex recruitment mediated by RIP1.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SignaLink; P61077; -.
UniPathway; UPA00143; -.
ChiTaRS; UBE2D3; human.
EvolutionaryTrace; P61077; -.
GeneWiki; UBE2D3; -.
GenomeRNAi; 7323; -.
PRO; PR:P61077; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000109332; -.
CleanEx; HS_UBE2D3; -.
ExpressionAtlas; P61077; baseline and differential.
Genevisible; P61077; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:ParkinsonsUK-UCL.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0030509; P:BMP signaling pathway; TAS:Reactome.
GO; GO:0006464; P:cellular protein modification process; TAS:ProtInc.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; IMP:ParkinsonsUK-UCL.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0051865; P:protein autoubiquitination; IDA:ParkinsonsUK-UCL.
GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB.
GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
GO; GO:0006513; P:protein monoubiquitination; IDA:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:ProtInc.
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.
1: Evidence at protein level;
3D-structure; Alternative splicing; 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_0000082466.
ACT_SITE 85 85 Glycyl thioester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00388,
ECO:0000255|PROSITE-ProRule:PRU10133}.
DISULFID 21 107 {ECO:0000269|Ref.28}.
VAR_SEQ 1 8 MALKRINK -> MLSNRKCLSK (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038096.
VAR_SEQ 134 147 YNRISREWTQKYAM -> YNRLAREWTEKYAML (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038097.
MUTAGEN 77 77 N->S: Activity is restricted HECT-type
and not RING-containing E3 ubiquitin-
protein ligases. Exhibits ubiquitin
transfer with ARIH1 and PRKN.
{ECO:0000269|PubMed:21532592}.
MUTAGEN 85 85 C->A: Loss of function.
{ECO:0000269|PubMed:10329681}.
MUTAGEN 87 87 D->E,P: Has intermediate lysine
reactivity.
{ECO:0000269|PubMed:21532592}.
MUTAGEN 87 87 D->K: Abolishes affect lysine reactivity.
{ECO:0000269|PubMed:21532592}.
MUTAGEN 87 87 D->N: Does not affect lysine reactivity.
{ECO:0000269|PubMed:21532592}.
MUTAGEN 117 117 D->H: Strongly impairs lysine reactivity
but retains some ability to transfer
ubiquitin to BRCA1.
{ECO:0000269|PubMed:21532592}.
CONFLICT 50 50 Missing (in Ref. 3; DB045280).
{ECO:0000305}.
CONFLICT 123 123 I -> L (in Ref. 7; AAH66917).
{ECO:0000305}.
CONFLICT 137 137 I -> V (in Ref. 3; CAG33197).
{ECO:0000305}.
CONFLICT 147 147 M -> I (in Ref. 3; CAG33197).
{ECO:0000305}.
HELIX 1 15 {ECO:0000244|PDB:5EGG}.
STRAND 19 21 {ECO:0000244|PDB:2FUH}.
STRAND 22 28 {ECO:0000244|PDB:5EGG}.
STRAND 32 38 {ECO:0000244|PDB:5EGG}.
STRAND 41 43 {ECO:0000244|PDB:4S3O}.
TURN 44 47 {ECO:0000244|PDB:5EGG}.
STRAND 49 55 {ECO:0000244|PDB:5EGG}.
TURN 58 61 {ECO:0000244|PDB:5EGG}.
STRAND 66 71 {ECO:0000244|PDB:5EGG}.
STRAND 76 78 {ECO:0000244|PDB:4R8P}.
STRAND 80 84 {ECO:0000244|PDB:4R8P}.
HELIX 87 89 {ECO:0000244|PDB:5EGG}.
TURN 90 92 {ECO:0000244|PDB:5EGG}.
HELIX 99 111 {ECO:0000244|PDB:5EGG}.
HELIX 121 129 {ECO:0000244|PDB:5EGG}.
HELIX 131 145 {ECO:0000244|PDB:5EGG}.
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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