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Ubiquitin-conjugating enzyme E2 D2 (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme D2) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme D2) (Ubiquitin carrier protein D2) (Ubiquitin-conjugating enzyme E2(17)KB 2) (Ubiquitin-conjugating enzyme E2-17 kDa 2) (Ubiquitin-protein ligase D2) (p53-regulated ubiquitin-conjugating enzyme 1)

 UB2D2_HUMAN             Reviewed;         147 AA.
P62837; D3DQC9; P51669; Q3MN78; Q96RP6;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 1.
05-DEC-2018, entry version 170.
RecName: Full=Ubiquitin-conjugating enzyme E2 D2;
EC=2.3.2.23 {ECO:0000269|PubMed:18042044, ECO:0000269|PubMed:18703417, ECO:0000269|PubMed:19854139, ECO:0000269|PubMed:20061386};
AltName: Full=(E3-independent) E2 ubiquitin-conjugating enzyme D2;
EC=2.3.2.24 {ECO:0000269|PubMed:17588522};
AltName: Full=E2 ubiquitin-conjugating enzyme D2;
AltName: Full=Ubiquitin carrier protein D2;
AltName: Full=Ubiquitin-conjugating enzyme E2(17)KB 2;
AltName: Full=Ubiquitin-conjugating enzyme E2-17 kDa 2;
AltName: Full=Ubiquitin-protein ligase D2;
AltName: Full=p53-regulated ubiquitin-conjugating enzyme 1;
Name=UBE2D2; Synonyms=PUBC1, UBC4, UBC5B, UBCH4, UBCH5B;
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).
TISSUE=Peripheral blood lymphocyte;
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].
PubMed=7724550; DOI=10.1073/pnas.92.8.3264;
Rolfe M., Beer-Romero P., Glass S., Eckstein J., Berdo I.,
Theodoras A., Pagano M., Draetta G.;
"Reconstitution of p53-ubiquitinylation reactions from purified
components: the role of human ubiquitin-conjugating enzyme UBC4 and
E6-associated protein (E6AP).";
Proc. Natl. Acad. Sci. U.S.A. 92:3264-3268(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=16112646; DOI=10.1016/j.bbrc.2005.08.024;
Guinn B.-A., Bland E.A., Lodi U., Liggins A.P., Tobal K., Petters S.,
Wells J.W., Banham A.H., Mufti G.J.;
"Humoral detection of leukaemia-associated antigens in presentation
acute myeloid leukaemia.";
Biochem. Biophys. Res. Commun. 335:1293-1304(2005).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Yin Y.;
"Cloning and identification of a p53-regulated ubiquitin-conjugating
enzyme, PUBC1.";
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Teratocarcinoma;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[7]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
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).
[9]
PROTEIN SEQUENCE OF 73-90, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Afjehi-Sadat L.;
Submitted (MAR-2007) to UniProtKB.
[10]
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).
[11]
INTERACTION WITH SCF COMPLEX.
PubMed=10918611; DOI=10.1038/sj.onc.1203647;
Strack P., Caligiuri M., Pelletier M., Boisclair M., Theodoras A.,
Beer-Romero P., Glass S., Parsons T., Copeland R.A., Auger K.R.,
Benfield P., Brizuela L., Rolfe M.;
"SCF(beta-TRCP) and phosphorylation dependent ubiquitination of I
kappa B alpha catalyzed by Ubc3 and Ubc4.";
Oncogene 19:3529-3536(2000).
[12]
INTERACTION WITH PJA1 AND PJA2.
PubMed=12036302; DOI=10.1006/geno.2002.6770;
Yu P., Chen Y., Tagle D.A., Cai T.;
"PJA1, encoding a RING-H2 finger ubiquitin ligase, is a novel human X
chromosome gene abundantly expressed in brain.";
Genomics 79:869-874(2002).
[13]
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).
[14]
INTERACTION WITH CNOT4, AND MUTAGENESIS OF LYS-63.
PubMed=15001359; DOI=10.1016/j.jmb.2004.01.031;
Winkler G.S., Albert T.K., Dominguez C., Legtenberg Y.I., Boelens R.,
Timmers H.T.;
"An altered-specificity ubiquitin-conjugating enzyme/ubiquitin-protein
ligase pair.";
J. Mol. Biol. 337:157-165(2004).
[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]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=18042044; DOI=10.1042/BJ20071338;
Windheim M., Peggie M., Cohen P.;
"Two different classes of E2 ubiquitin-conjugating enzymes are
required for the mono-ubiquitination of proteins and elongation by
polyubiquitin chains with a specific topology.";
Biochem. J. 409:723-729(2008).
[17]
FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-85.
PubMed=18703417; DOI=10.1095/biolreprod.108.071407;
Chiang M.H., Chen L.F., Chen H.;
"Ubiquitin-conjugating enzyme UBE2D2 is responsible for FBXW2 (F-box
and WD repeat domain containing 2)-mediated human GCM1 (glial cell
missing homolog 1) ubiquitination and degradation.";
Biol. Reprod. 79:914-920(2008).
[18]
FUNCTION.
PubMed=18359941; DOI=10.1074/jbc.M800402200;
Grou C.P., Carvalho A.F., Pinto M.P., Wiese S., Piechura H.,
Meyer H.E., Warscheid B., Sa-Miranda C., Azevedo J.E.;
"Members of the E2D (UbcH5) family mediate the ubiquitination of the
conserved cysteine of Pex5p, the peroxisomal import receptor.";
J. Biol. Chem. 283:14190-14197(2008).
[19]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=19854139; DOI=10.1016/j.molcel.2009.09.037;
Zeng W., Xu M., Liu S., Sun L., Chen Z.J.;
"Key role of Ubc5 and lysine-63 polyubiquitination in viral activation
of IRF3.";
Mol. Cell 36:315-325(2009).
[20]
FUNCTION.
PubMed=20403326; DOI=10.1016/j.cell.2010.03.029;
Zeng W., Sun L., Jiang X., Chen X., Hou F., Adhikari A., Xu M.,
Chen Z.J.;
"Reconstitution of the RIG-I pathway reveals a signaling role of
unanchored polyubiquitin chains in innate immunity.";
Cell 141:315-330(2010).
[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]
FUNCTION, INTERACTION WITH CBLC, AND MUTAGENESIS OF CYS-85.
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]
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).
[24]
STRUCTURE BY NMR.
PubMed=15522302; DOI=10.1016/j.jmb.2004.09.054;
Houben K., Dominguez C., van Schaik F.M., Timmers H.T., Bonvin A.M.,
Boelens R.;
"Solution structure of the ubiquitin-conjugating enzyme UbcH5B.";
J. Mol. Biol. 344:513-526(2004).
[25]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS).
PubMed=20152160; DOI=10.1016/j.str.2009.11.007;
Sakata E., Satoh T., Yamamoto S., Yamaguchi Y., Yagi-Utsumi M.,
Kurimoto E., Tanaka K., Wakatsuki S., Kato K.;
"Crystal structure of UbcH5b~ubiquitin intermediate: insight into the
formation of the self-assembled E2~Ub conjugates.";
Structure 18:138-147(2010).
[26] {ECO:0000244|PDB:5D0K, ECO:0000244|PDB:5D0M}
X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) IN COMPLEX WITH RNF165.
PubMed=26656854; DOI=10.1038/nsmb.3142;
Wright J.D., Mace P.D., Day C.L.;
"Secondary ubiquitin-RING docking enhances Arkadia and Ark2C E3 ligase
activity.";
Nat. Struct. Mol. Biol. 23:45-52(2016).
-!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
covalent attachment to other proteins. In vitro catalyzes 'Lys-
48'-linked polyubiquitination. Mediates the selective degradation
of short-lived and abnormal proteins. Functions in the E6/E6-AP-
induced ubiquitination of p53/TP53. Mediates ubiquitination of
PEX5 and autoubiquitination of STUB1 and TRAF6. Involved in the
signal-induced conjugation and subsequent degradation of NFKBIA,
FBXW2-mediated GCM1 ubiquitination and degradation, MDM2-dependent
degradation of p53/TP53 and the activation of MAVS in the
mitochondria by DDX58/RIG-I in response to viral infection.
Essential for viral activation of IRF3.
{ECO:0000269|PubMed:10329681, ECO:0000269|PubMed:15280377,
ECO:0000269|PubMed:18042044, ECO:0000269|PubMed:18359941,
ECO:0000269|PubMed:18703417, ECO:0000269|PubMed:19854139,
ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:20403326,
ECO:0000269|PubMed:20525694}.
-!- 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:0000255|PROSITE-ProRule:PRU00388,
ECO:0000255|PROSITE-ProRule:PRU10133,
ECO:0000269|PubMed:18042044, ECO:0000269|PubMed:18703417,
ECO:0000269|PubMed:19854139, ECO:0000269|PubMed:20061386};
-!- 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: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. Interacts with CNOT4 (via RING domain). Interacts
with E3 ubiquitin-protein ligases CBLC, PJA1 and PJA2. Interacts
with PDZRN3. Interacts with PPP1R11 (By similarity).
{ECO:0000250|UniProtKB:P62838, ECO:0000269|PubMed:10918611,
ECO:0000269|PubMed:12036302, ECO:0000269|PubMed:15001359,
ECO:0000269|PubMed:20525694}.
-!- INTERACTION:
Q13489:BIRC3; NbExp=2; IntAct=EBI-347677, EBI-517709;
P22681:CBL; NbExp=4; IntAct=EBI-347677, EBI-518228;
Q13191-1:CBLB; NbExp=2; IntAct=EBI-347677, EBI-15555129;
O15151:MDM4; NbExp=2; IntAct=EBI-347677, EBI-398437;
O15344:MID1; NbExp=3; IntAct=EBI-347677, EBI-2340316;
Q99PZ6:ospG (xeno); NbExp=3; IntAct=EBI-347677, EBI-9316527;
Q96FW1:OTUB1; NbExp=11; IntAct=EBI-347677, EBI-1058491;
Q06587:RING1; NbExp=3; IntAct=EBI-347677, EBI-752313;
Q9Y3C5:RNF11; NbExp=7; IntAct=EBI-347677, EBI-396669;
Q9Y4L5:RNF115; NbExp=5; IntAct=EBI-347677, EBI-2129242;
Q9BV68:RNF126; NbExp=4; IntAct=EBI-347677, EBI-357322;
Q96GF1:RNF185; NbExp=3; IntAct=EBI-347677, EBI-2340249;
Q99496:RNF2; NbExp=3; IntAct=EBI-347677, EBI-722416;
Q96EP0:RNF31; NbExp=3; IntAct=EBI-347677, EBI-948111;
Q68DV7:RNF43; NbExp=2; IntAct=EBI-347677, EBI-1647060;
Q99942:RNF5; NbExp=6; IntAct=EBI-347677, EBI-348482;
O76064:RNF8; NbExp=3; IntAct=EBI-347677, EBI-373337;
Q9Y4K3:TRAF6; NbExp=4; IntAct=EBI-347677, EBI-359276;
O95155-1:UBE4B; NbExp=2; IntAct=EBI-347677, EBI-15869194;
P98170:XIAP; NbExp=2; IntAct=EBI-347677, EBI-517127;
Q8ND25:ZNRF1; NbExp=6; IntAct=EBI-347677, EBI-2129250;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P62837-1; Sequence=Displayed;
Name=2;
IsoId=P62837-2; Sequence=VSP_045180;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
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EMBL; U39317; AAA91460.1; -; mRNA.
EMBL; L40146; AAC41750.1; -; Genomic_DNA.
EMBL; AY651263; AAX35690.1; -; mRNA.
EMBL; AF317220; AAK93958.1; -; mRNA.
EMBL; AK001311; BAG50891.1; -; mRNA.
EMBL; AK001428; BAG50911.1; -; mRNA.
EMBL; AC010378; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471062; EAW62095.1; -; Genomic_DNA.
EMBL; CH471062; EAW62096.1; -; Genomic_DNA.
EMBL; CH471062; EAW62097.1; -; Genomic_DNA.
EMBL; BC033349; AAH33349.1; -; mRNA.
CCDS; CCDS43369.1; -. [P62837-1]
CCDS; CCDS47275.1; -. [P62837-2]
PIR; I59365; I59365.
RefSeq; NP_003330.1; NM_003339.2. [P62837-1]
RefSeq; NP_862821.1; NM_181838.1. [P62837-2]
UniGene; Hs.108332; -.
PDB; 1UR6; NMR; -; A=1-147.
PDB; 1W4U; NMR; -; A=1-147.
PDB; 2CLW; X-ray; 1.94 A; A/B/C/D=1-147.
PDB; 2ESK; X-ray; 1.36 A; A=1-147.
PDB; 2ESO; X-ray; 1.50 A; A=1-147.
PDB; 2ESP; X-ray; 1.52 A; A=1-147.
PDB; 2ESQ; X-ray; 1.44 A; A=1-147.
PDB; 3A33; X-ray; 2.20 A; A=1-147.
PDB; 3JVZ; X-ray; 3.30 A; A/B=2-147.
PDB; 3JW0; X-ray; 3.10 A; A/B=2-147.
PDB; 3L1Y; X-ray; 1.60 A; A=1-147.
PDB; 3TGD; X-ray; 1.80 A; A=1-147.
PDB; 3ZNI; X-ray; 2.21 A; C/G/K/O=2-147.
PDB; 4A49; X-ray; 2.21 A; B=1-147.
PDB; 4A4B; X-ray; 2.79 A; C=1-147.
PDB; 4A4C; X-ray; 2.70 A; C=1-147.
PDB; 4AUQ; X-ray; 2.18 A; A/D=1-147.
PDB; 4DDG; X-ray; 3.30 A; A/B/C/J/K/L=1-147.
PDB; 4DDI; X-ray; 3.80 A; D/E/F/G/H/I=2-20.
PDB; 4LDT; X-ray; 1.90 A; C=1-147.
PDB; 4V3K; X-ray; 2.04 A; A/D=2-147.
PDB; 4V3L; X-ray; 1.53 A; A=2-147.
PDB; 4WZ3; X-ray; 2.70 A; A=1-147.
PDB; 5D0K; X-ray; 2.65 A; A/D/G/J=1-147.
PDB; 5D0M; X-ray; 1.91 A; A=1-147.
PDB; 5D1K; X-ray; 1.78 A; A=1-147.
PDB; 5D1L; X-ray; 1.62 A; A=1-147.
PDB; 5D1M; X-ray; 1.58 A; A=1-147.
PDB; 5EDV; X-ray; 3.48 A; C/D/I=2-147.
PDB; 5MNJ; X-ray; 2.16 A; A/E=1-147.
PDB; 5ULF; X-ray; 1.80 A; A/C=1-147.
PDB; 5ULH; X-ray; 1.95 A; A=1-147.
PDB; 5ULK; X-ray; 2.38 A; A=1-147.
PDB; 5VZW; X-ray; 2.28 A; A/B=1-147.
PDBsum; 1UR6; -.
PDBsum; 1W4U; -.
PDBsum; 2CLW; -.
PDBsum; 2ESK; -.
PDBsum; 2ESO; -.
PDBsum; 2ESP; -.
PDBsum; 2ESQ; -.
PDBsum; 3A33; -.
PDBsum; 3JVZ; -.
PDBsum; 3JW0; -.
PDBsum; 3L1Y; -.
PDBsum; 3TGD; -.
PDBsum; 3ZNI; -.
PDBsum; 4A49; -.
PDBsum; 4A4B; -.
PDBsum; 4A4C; -.
PDBsum; 4AUQ; -.
PDBsum; 4DDG; -.
PDBsum; 4DDI; -.
PDBsum; 4LDT; -.
PDBsum; 4V3K; -.
PDBsum; 4V3L; -.
PDBsum; 4WZ3; -.
PDBsum; 5D0K; -.
PDBsum; 5D0M; -.
PDBsum; 5D1K; -.
PDBsum; 5D1L; -.
PDBsum; 5D1M; -.
PDBsum; 5EDV; -.
PDBsum; 5MNJ; -.
PDBsum; 5ULF; -.
PDBsum; 5ULH; -.
PDBsum; 5ULK; -.
PDBsum; 5VZW; -.
ProteinModelPortal; P62837; -.
SMR; P62837; -.
BioGrid; 113170; 256.
CORUM; P62837; -.
DIP; DIP-29267N; -.
IntAct; P62837; 122.
MINT; P62837; -.
STRING; 9606.ENSP00000381717; -.
MoonDB; P62837; Predicted.
TCDB; 3.A.20.1.1; the peroxisomal protein importer (ppi) family.
iPTMnet; P62837; -.
PhosphoSitePlus; P62837; -.
BioMuta; UBE2D2; -.
DMDM; 51338685; -.
EPD; P62837; -.
MaxQB; P62837; -.
PaxDb; P62837; -.
PeptideAtlas; P62837; -.
PRIDE; P62837; -.
ProteomicsDB; 57432; -.
Ensembl; ENST00000398733; ENSP00000381717; ENSG00000131508. [P62837-1]
Ensembl; ENST00000398734; ENSP00000381718; ENSG00000131508. [P62837-1]
Ensembl; ENST00000505548; ENSP00000424941; ENSG00000131508. [P62837-2]
Ensembl; ENST00000511725; ENSP00000429613; ENSG00000131508. [P62837-2]
GeneID; 7322; -.
KEGG; hsa:7322; -.
UCSC; uc003ler.3; human. [P62837-1]
CTD; 7322; -.
DisGeNET; 7322; -.
EuPathDB; HostDB:ENSG00000131508.15; -.
GeneCards; UBE2D2; -.
H-InvDB; HIX0019025; -.
H-InvDB; HIX0028451; -.
HGNC; HGNC:12475; UBE2D2.
HPA; HPA003920; -.
MIM; 602962; gene.
neXtProt; NX_P62837; -.
OpenTargets; ENSG00000131508; -.
PharmGKB; PA37125; -.
eggNOG; KOG0417; Eukaryota.
eggNOG; COG5078; LUCA.
GeneTree; ENSGT00940000153169; -.
HOGENOM; HOG000233455; -.
HOVERGEN; HBG063308; -.
InParanoid; P62837; -.
KO; K06689; -.
OMA; QNDSPYQ; -.
PhylomeDB; P62837; -.
TreeFam; TF101108; -.
BioCyc; MetaCyc:HS05542-MONOMER; -.
BRENDA; 2.3.2.B5; 2681.
BRENDA; 2.3.2.B6; 2681.
BRENDA; 2.3.2.B8; 2681.
Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-HSA-168927; TICAM1, RIP1-mediated IKK complex recruitment.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-9033241; Peroxisomal protein import.
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; P62837; -.
SIGNOR; P62837; -.
UniPathway; UPA00143; -.
ChiTaRS; UBE2D2; human.
EvolutionaryTrace; P62837; -.
GeneWiki; UBE2D2; -.
GenomeRNAi; 7322; -.
PRO; PR:P62837; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000131508; Expressed in 236 organ(s), highest expression level in testis.
CleanEx; HS_UBE2D2; -.
ExpressionAtlas; P62837; baseline and differential.
Genevisible; P62837; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0032991; C:protein-containing complex; IDA:MGI.
GO; GO:0000151; C:ubiquitin ligase complex; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:ParkinsonsUK-UCL.
GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0006464; P:cellular protein modification process; TAS:ProtInc.
GO; GO:0051865; P:protein autoubiquitination; IDA:ParkinsonsUK-UCL.
GO; GO:0070979; P:protein K11-linked ubiquitination; IBA:GO_Central.
GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; IDA:BHF-UCL.
GO; GO:0006625; P:protein targeting to peroxisome; TAS:Reactome.
GO; GO:0016567; P:protein ubiquitination; IDA:ParkinsonsUK-UCL.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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; ATP-binding; Complete proteome;
Direct protein sequencing; Nucleotide-binding; Reference proteome;
Transferase; Ubl conjugation pathway.
CHAIN 1 147 Ubiquitin-conjugating enzyme E2 D2.
/FTId=PRO_0000082462.
ACT_SITE 85 85 Glycyl thioester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00388,
ECO:0000255|PROSITE-ProRule:PRU10133}.
VAR_SEQ 1 29 Missing (in isoform 2).
{ECO:0000303|Ref.4}.
/FTId=VSP_045180.
MUTAGEN 63 63 K->A,E: Strongly reduced interaction with
CNTO4. {ECO:0000269|PubMed:15001359}.
MUTAGEN 85 85 C->A: Catalytically inactive. Loss of
ability to promote FBXW2-mediated GCM1
ubiquitination. Inhibition of TNF-alpha-
induced degradation of NFKBIA.
{ECO:0000269|PubMed:10329681,
ECO:0000269|PubMed:18703417,
ECO:0000269|PubMed:20525694}.
CONFLICT 128 128 K -> Q (in Ref. 2; AAC41750).
{ECO:0000305}.
HELIX 1 15 {ECO:0000244|PDB:2ESK}.
STRAND 19 28 {ECO:0000244|PDB:2ESK}.
STRAND 32 38 {ECO:0000244|PDB:2ESK}.
STRAND 41 43 {ECO:0000244|PDB:4V3L}.
TURN 44 47 {ECO:0000244|PDB:2ESK}.
STRAND 49 55 {ECO:0000244|PDB:2ESK}.
TURN 58 61 {ECO:0000244|PDB:2ESK}.
STRAND 66 71 {ECO:0000244|PDB:2ESK}.
STRAND 76 78 {ECO:0000244|PDB:4A4B}.
STRAND 82 84 {ECO:0000244|PDB:1W4U}.
HELIX 87 89 {ECO:0000244|PDB:2ESK}.
TURN 90 92 {ECO:0000244|PDB:2ESK}.
HELIX 99 111 {ECO:0000244|PDB:2ESK}.
STRAND 115 117 {ECO:0000244|PDB:4V3L}.
HELIX 121 129 {ECO:0000244|PDB:2ESK}.
HELIX 131 145 {ECO:0000244|PDB:2ESK}.
SEQUENCE 147 AA; 16735 MW; C942BE7853CBC355 CRC64;
MALKRIHKEL NDLARDPPAQ CSAGPVGDDM FHWQATIMGP NDSPYQGGVF FLTIHFPTDY
PFKPPKVAFT TRIYHPNINS NGSICLDILR SQWSPALTIS KVLLSICSLL CDPNPDDPLV
PEIARIYKTD REKYNRIARE WTQKYAM


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