ID UB2D2_HUMAN Reviewed; 147 AA. AC P62837; D3DQC9; P51669; Q3MN78; Q96RP6; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 1. DT 20-DEC-2017, entry version 160. DE RecName: Full=Ubiquitin-conjugating enzyme E2 D2; DE EC=2.3.2.23 {ECO:0000269|PubMed:18042044, ECO:0000269|PubMed:18703417, ECO:0000269|PubMed:19854139, ECO:0000269|PubMed:20061386}; DE AltName: Full=(E3-independent) E2 ubiquitin-conjugating enzyme D2; DE EC=2.3.2.24 {ECO:0000269|PubMed:17588522}; DE AltName: Full=E2 ubiquitin-conjugating enzyme D2; DE AltName: Full=Ubiquitin carrier protein D2; DE AltName: Full=Ubiquitin-conjugating enzyme E2(17)KB 2; DE AltName: Full=Ubiquitin-conjugating enzyme E2-17 kDa 2; DE AltName: Full=Ubiquitin-protein ligase D2; DE AltName: Full=p53-regulated ubiquitin-conjugating enzyme 1; GN Name=UBE2D2; Synonyms=PUBC1, UBC4, UBC5B, UBCH4, UBCH5B; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Peripheral blood lymphocyte; RX PubMed=8530467; DOI=10.1074/jbc.270.51.30408; RA Jensen J.P., Bates P.W., Yang M., Vierstra R.D., Weissman A.M.; RT "Identification of a family of closely related human ubiquitin RT conjugating enzymes."; RL J. Biol. Chem. 270:30408-30414(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7724550; DOI=10.1073/pnas.92.8.3264; RA Rolfe M., Beer-Romero P., Glass S., Eckstein J., Berdo I., RA Theodoras A., Pagano M., Draetta G.; RT "Reconstitution of p53-ubiquitinylation reactions from purified RT components: the role of human ubiquitin-conjugating enzyme UBC4 and RT E6-associated protein (E6AP)."; RL Proc. Natl. Acad. Sci. U.S.A. 92:3264-3268(1995). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Testis; RX PubMed=16112646; DOI=10.1016/j.bbrc.2005.08.024; RA Guinn B.-A., Bland E.A., Lodi U., Liggins A.P., Tobal K., Petters S., RA Wells J.W., Banham A.H., Mufti G.J.; RT "Humoral detection of leukaemia-associated antigens in presentation RT acute myeloid leukaemia."; RL Biochem. Biophys. Res. Commun. 335:1293-1304(2005). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA Yin Y.; RT "Cloning and identification of a p53-regulated ubiquitin-conjugating RT enzyme, PUBC1."; RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Teratocarcinoma; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP PROTEIN SEQUENCE OF 73-90, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, and Cajal-Retzius cell; RA Lubec G., Afjehi-Sadat L.; RL Submitted (MAR-2007) to UniProtKB. RN [10] RP FUNCTION, AND MUTAGENESIS OF CYS-85. RX PubMed=10329681; DOI=10.1074/jbc.274.21.14823; RA Gonen H., Bercovich B., Orian A., Carrano A., Takizawa C., RA Yamanaka K., Pagano M., Iwai K., Ciechanover A.; RT "Identification of the ubiquitin carrier proteins, E2s, involved in RT signal-induced conjugation and subsequent degradation of RT IkappaBalpha."; RL J. Biol. Chem. 274:14823-14830(1999). RN [11] RP INTERACTION WITH SCF COMPLEX. RX PubMed=10918611; DOI=10.1038/sj.onc.1203647; RA Strack P., Caligiuri M., Pelletier M., Boisclair M., Theodoras A., RA Beer-Romero P., Glass S., Parsons T., Copeland R.A., Auger K.R., RA Benfield P., Brizuela L., Rolfe M.; RT "SCF(beta-TRCP) and phosphorylation dependent ubiquitination of I RT kappa B alpha catalyzed by Ubc3 and Ubc4."; RL Oncogene 19:3529-3536(2000). RN [12] RP INTERACTION WITH PJA1 AND PJA2. RX PubMed=12036302; DOI=10.1006/geno.2002.6770; RA Yu P., Chen Y., Tagle D.A., Cai T.; RT "PJA1, encoding a RING-H2 finger ubiquitin ligase, is a novel human X RT chromosome gene abundantly expressed in brain."; RL Genomics 79:869-874(2002). RN [13] RP FUNCTION. RX PubMed=15280377; DOI=10.1074/jbc.M403362200; RA Saville M.K., Sparks A., Xirodimas D.P., Wardrop J., Stevenson L.F., RA Bourdon J.C., Woods Y.L., Lane D.P.; RT "Regulation of p53 by the ubiquitin-conjugating enzymes UbcH5B/C in RT vivo."; RL J. Biol. Chem. 279:42169-42181(2004). RN [14] RP INTERACTION WITH CNOT4, AND MUTAGENESIS OF LYS-63. RX PubMed=15001359; DOI=10.1016/j.jmb.2004.01.031; RA Winkler G.S., Albert T.K., Dominguez C., Legtenberg Y.I., Boelens R., RA Timmers H.T.; RT "An altered-specificity ubiquitin-conjugating enzyme/ubiquitin-protein RT ligase pair."; RL J. Mol. Biol. 337:157-165(2004). RN [15] RP CATALYTIC ACTIVITY AS E3-INDEPENDENT E2 UBIQUITIN-CONJUGATING ENZYME. RX PubMed=17588522; DOI=10.1016/j.molcel.2007.05.014; RA Hoeller D., Hecker C.M., Wagner S., Rogov V., Doetsch V., Dikic I.; RT "E3-independent monoubiquitination of ubiquitin-binding proteins."; RL Mol. Cell 26:891-898(2007). RN [16] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=18042044; DOI=10.1042/BJ20071338; RA Windheim M., Peggie M., Cohen P.; RT "Two different classes of E2 ubiquitin-conjugating enzymes are RT required for the mono-ubiquitination of proteins and elongation by RT polyubiquitin chains with a specific topology."; RL Biochem. J. 409:723-729(2008). RN [17] RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-85. RX PubMed=18703417; DOI=10.1095/biolreprod.108.071407; RA Chiang M.H., Chen L.F., Chen H.; RT "Ubiquitin-conjugating enzyme UBE2D2 is responsible for FBXW2 (F-box RT and WD repeat domain containing 2)-mediated human GCM1 (glial cell RT missing homolog 1) ubiquitination and degradation."; RL Biol. Reprod. 79:914-920(2008). RN [18] RP FUNCTION. RX PubMed=18359941; DOI=10.1074/jbc.M800402200; RA Grou C.P., Carvalho A.F., Pinto M.P., Wiese S., Piechura H., RA Meyer H.E., Warscheid B., Sa-Miranda C., Azevedo J.E.; RT "Members of the E2D (UbcH5) family mediate the ubiquitination of the RT conserved cysteine of Pex5p, the peroxisomal import receptor."; RL J. Biol. Chem. 283:14190-14197(2008). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=19854139; DOI=10.1016/j.molcel.2009.09.037; RA Zeng W., Xu M., Liu S., Sun L., Chen Z.J.; RT "Key role of Ubc5 and lysine-63 polyubiquitination in viral activation RT of IRF3."; RL Mol. Cell 36:315-325(2009). RN [20] RP FUNCTION. RX PubMed=20403326; DOI=10.1016/j.cell.2010.03.029; RA Zeng W., Sun L., Jiang X., Chen X., Hou F., Adhikari A., Xu M., RA Chen Z.J.; RT "Reconstitution of the RIG-I pathway reveals a signaling role of RT unanchored polyubiquitin chains in innate immunity."; RL Cell 141:315-330(2010). RN [21] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=20061386; DOI=10.1074/jbc.M109.089003; RA David Y., Ziv T., Admon A., Navon A.; RT "The E2 ubiquitin-conjugating enzymes direct polyubiquitination to RT preferred lysines."; RL J. Biol. Chem. 285:8595-8604(2010). RN [22] RP FUNCTION, INTERACTION WITH CBLC, AND MUTAGENESIS OF CYS-85. RX PubMed=20525694; DOI=10.1074/jbc.M109.091157; RA Ryan P.E., Sivadasan-Nair N., Nau M.M., Nicholas S., Lipkowitz S.; RT "The N terminus of Cbl-c regulates ubiquitin ligase activity by RT modulating affinity for the ubiquitin-conjugating enzyme."; RL J. Biol. Chem. 285:23687-23698(2010). RN [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [24] RP STRUCTURE BY NMR. RX PubMed=15522302; DOI=10.1016/j.jmb.2004.09.054; RA Houben K., Dominguez C., van Schaik F.M., Timmers H.T., Bonvin A.M., RA Boelens R.; RT "Solution structure of the ubiquitin-conjugating enzyme UbcH5B."; RL J. Mol. Biol. 344:513-526(2004). RN [25] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS). RX PubMed=20152160; DOI=10.1016/j.str.2009.11.007; RA Sakata E., Satoh T., Yamamoto S., Yamaguchi Y., Yagi-Utsumi M., RA Kurimoto E., Tanaka K., Wakatsuki S., Kato K.; RT "Crystal structure of UbcH5b~ubiquitin intermediate: insight into the RT formation of the self-assembled E2~Ub conjugates."; RL Structure 18:138-147(2010). RN [26] {ECO:0000244|PDB:5D0K, ECO:0000244|PDB:5D0M} RP X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) IN COMPLEX WITH RNF165. RX PubMed=26656854; DOI=10.1038/nsmb.3142; RA Wright J.D., Mace P.D., Day C.L.; RT "Secondary ubiquitin-RING docking enhances Arkadia and Ark2C E3 ligase RT activity."; RL Nat. Struct. Mol. Biol. 23:45-52(2016). CC -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its CC covalent attachment to other proteins. In vitro catalyzes 'Lys- CC 48'-linked polyubiquitination. Mediates the selective degradation CC of short-lived and abnormal proteins. Functions in the E6/E6-AP- CC induced ubiquitination of p53/TP53. Mediates ubiquitination of CC PEX5 and autoubiquitination of STUB1 and TRAF6. Involved in the CC signal-induced conjugation and subsequent degradation of NFKBIA, CC FBXW2-mediated GCM1 ubiquitination and degradation, MDM2-dependent CC degradation of p53/TP53 and the activation of MAVS in the CC mitochondria by DDX58/RIG-I in response to viral infection. CC Essential for viral activation of IRF3. CC {ECO:0000269|PubMed:10329681, ECO:0000269|PubMed:15280377, CC ECO:0000269|PubMed:18042044, ECO:0000269|PubMed:18359941, CC ECO:0000269|PubMed:18703417, ECO:0000269|PubMed:19854139, CC ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:20403326, CC ECO:0000269|PubMed:20525694}. CC -!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating CC enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine CC = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 CC ubiquitin-conjugating enzyme]-L-cysteine. {ECO:0000255|PROSITE- CC ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133, CC ECO:0000269|PubMed:18042044, ECO:0000269|PubMed:18703417, CC ECO:0000269|PubMed:19854139, ECO:0000269|PubMed:20061386}. CC -!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating CC enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin- CC activating enzyme]-L-cysteine + N(6)-monoubiquitinyl-[acceptor CC protein]-L-lysine. {ECO:0000269|PubMed:17588522}. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000255|PROSITE-ProRule:PRU00388}. CC -!- SUBUNIT: Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin CC ligase complex. Interacts with CNOT4 (via RING domain). Interacts CC with E3 ubiquitin-protein ligases CBLC, PJA1 and PJA2. Interacts CC with PDZRN3. {ECO:0000269|PubMed:10918611, CC ECO:0000269|PubMed:12036302, ECO:0000269|PubMed:15001359, CC ECO:0000269|PubMed:20525694}. CC -!- INTERACTION: CC Q13489:BIRC3; NbExp=2; IntAct=EBI-347677, EBI-517709; CC P22681:CBL; NbExp=4; IntAct=EBI-347677, EBI-518228; CC Q13191-1:CBLB; NbExp=2; IntAct=EBI-347677, EBI-15555129; CC O15151:MDM4; NbExp=2; IntAct=EBI-347677, EBI-398437; CC O15344:MID1; NbExp=3; IntAct=EBI-347677, EBI-2340316; CC Q99PZ6:ospG (xeno); NbExp=3; IntAct=EBI-347677, EBI-9316527; CC Q96FW1:OTUB1; NbExp=11; IntAct=EBI-347677, EBI-1058491; CC Q9Y3C5:RNF11; NbExp=7; IntAct=EBI-347677, EBI-396669; CC Q9Y4L5:RNF115; NbExp=5; IntAct=EBI-347677, EBI-2129242; CC Q9BV68:RNF126; NbExp=4; IntAct=EBI-347677, EBI-357322; CC Q96GF1:RNF185; NbExp=3; IntAct=EBI-347677, EBI-2340249; CC Q99496:RNF2; NbExp=3; IntAct=EBI-347677, EBI-722416; CC Q96EP0:RNF31; NbExp=3; IntAct=EBI-347677, EBI-948111; CC Q68DV7:RNF43; NbExp=2; IntAct=EBI-347677, EBI-1647060; CC Q99942:RNF5; NbExp=6; IntAct=EBI-347677, EBI-348482; CC Q9Y4K3:TRAF6; NbExp=4; IntAct=EBI-347677, EBI-359276; CC Q9BYV2:TRIM54; NbExp=4; IntAct=EBI-347677, EBI-2130429; CC O95155-1:UBE4B; NbExp=2; IntAct=EBI-347677, EBI-15869194; CC P98170:XIAP; NbExp=2; IntAct=EBI-347677, EBI-517127; CC Q8ND25:ZNRF1; NbExp=4; IntAct=EBI-347677, EBI-2129250; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P62837-1; Sequence=Displayed; CC Name=2; CC IsoId=P62837-2; Sequence=VSP_045180; CC Note=No experimental confirmation available.; 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; U39317; AAA91460.1; -; mRNA. DR EMBL; L40146; AAC41750.1; -; Genomic_DNA. DR EMBL; AY651263; AAX35690.1; -; mRNA. DR EMBL; AF317220; AAK93958.1; -; mRNA. DR EMBL; AK001311; BAG50891.1; -; mRNA. DR EMBL; AK001428; BAG50911.1; -; mRNA. DR EMBL; AC010378; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471062; EAW62095.1; -; Genomic_DNA. DR EMBL; CH471062; EAW62096.1; -; Genomic_DNA. DR EMBL; CH471062; EAW62097.1; -; Genomic_DNA. DR EMBL; BC033349; AAH33349.1; -; mRNA. DR CCDS; CCDS43369.1; -. [P62837-1] DR CCDS; CCDS47275.1; -. [P62837-2] DR PIR; I59365; I59365. DR RefSeq; NP_003330.1; NM_003339.2. [P62837-1] DR RefSeq; NP_862821.1; NM_181838.1. [P62837-2] DR UniGene; Hs.108332; -. DR PDB; 1UR6; NMR; -; A=1-147. DR PDB; 1W4U; NMR; -; A=1-147. DR PDB; 2CLW; X-ray; 1.94 A; A/B/C/D=1-147. DR PDB; 2ESK; X-ray; 1.36 A; A=1-147. DR PDB; 2ESO; X-ray; 1.50 A; A=1-147. DR PDB; 2ESP; X-ray; 1.52 A; A=1-147. DR PDB; 2ESQ; X-ray; 1.44 A; A=1-147. DR PDB; 3A33; X-ray; 2.20 A; A=1-147. DR PDB; 3JVZ; X-ray; 3.30 A; A/B=2-147. DR PDB; 3JW0; X-ray; 3.10 A; A/B=2-147. DR PDB; 3L1Y; X-ray; 1.60 A; A=1-147. DR PDB; 3TGD; X-ray; 1.80 A; A=1-147. DR PDB; 3ZNI; X-ray; 2.21 A; C/G/K/O=2-147. DR PDB; 4A49; X-ray; 2.21 A; B=1-147. DR PDB; 4A4B; X-ray; 2.79 A; C=1-147. DR PDB; 4A4C; X-ray; 2.70 A; C=1-147. DR PDB; 4AUQ; X-ray; 2.18 A; A/D=1-147. DR PDB; 4DDG; X-ray; 3.30 A; A/B/C/J/K/L=1-147. DR PDB; 4DDI; X-ray; 3.80 A; D/E/F/G/H/I=2-20. DR PDB; 4LDT; X-ray; 1.90 A; C=1-147. DR PDB; 4V3K; X-ray; 2.04 A; A/D=2-147. DR PDB; 4V3L; X-ray; 1.53 A; A=2-147. DR PDB; 4WZ3; X-ray; 2.70 A; A=1-147. DR PDB; 5D0K; X-ray; 2.65 A; A/D/G/J=1-147. DR PDB; 5D0M; X-ray; 1.91 A; A=1-147. DR PDB; 5D1K; X-ray; 1.78 A; A=1-147. DR PDB; 5D1L; X-ray; 1.62 A; A=1-147. DR PDB; 5D1M; X-ray; 1.58 A; A=1-147. DR PDB; 5EDV; X-ray; 3.48 A; C/D/I=2-147. DR PDB; 5MNJ; X-ray; 2.16 A; A/E=1-147. DR PDB; 5ULF; X-ray; 1.80 A; A/C=1-147. DR PDB; 5ULH; X-ray; 1.95 A; A=1-147. DR PDB; 5ULK; X-ray; 2.38 A; A=1-147. DR PDB; 5VZW; X-ray; 2.28 A; A/B=1-147. DR PDBsum; 1UR6; -. DR PDBsum; 1W4U; -. DR PDBsum; 2CLW; -. DR PDBsum; 2ESK; -. DR PDBsum; 2ESO; -. DR PDBsum; 2ESP; -. DR PDBsum; 2ESQ; -. DR PDBsum; 3A33; -. DR PDBsum; 3JVZ; -. DR PDBsum; 3JW0; -. DR PDBsum; 3L1Y; -. DR PDBsum; 3TGD; -. DR PDBsum; 3ZNI; -. DR PDBsum; 4A49; -. DR PDBsum; 4A4B; -. DR PDBsum; 4A4C; -. DR PDBsum; 4AUQ; -. DR PDBsum; 4DDG; -. DR PDBsum; 4DDI; -. DR PDBsum; 4LDT; -. DR PDBsum; 4V3K; -. DR PDBsum; 4V3L; -. DR PDBsum; 4WZ3; -. DR PDBsum; 5D0K; -. DR PDBsum; 5D0M; -. DR PDBsum; 5D1K; -. DR PDBsum; 5D1L; -. DR PDBsum; 5D1M; -. DR PDBsum; 5EDV; -. DR PDBsum; 5MNJ; -. DR PDBsum; 5ULF; -. DR PDBsum; 5ULH; -. DR PDBsum; 5ULK; -. DR PDBsum; 5VZW; -. DR ProteinModelPortal; P62837; -. DR SMR; P62837; -. DR BioGrid; 113170; 248. DR DIP; DIP-29267N; -. DR IntAct; P62837; 121. DR MINT; MINT-1035011; -. DR STRING; 9606.ENSP00000381717; -. DR TCDB; 3.A.20.1.1; the peroxisomal protein importer (ppi) family. DR iPTMnet; P62837; -. DR PhosphoSitePlus; P62837; -. DR BioMuta; UBE2D2; -. DR DMDM; 51338685; -. DR EPD; P62837; -. DR MaxQB; P62837; -. DR PaxDb; P62837; -. DR PeptideAtlas; P62837; -. DR PRIDE; P62837; -. DR Ensembl; ENST00000398733; ENSP00000381717; ENSG00000131508. [P62837-1] DR Ensembl; ENST00000398734; ENSP00000381718; ENSG00000131508. [P62837-1] DR Ensembl; ENST00000505548; ENSP00000424941; ENSG00000131508. [P62837-2] DR Ensembl; ENST00000511725; ENSP00000429613; ENSG00000131508. [P62837-2] DR GeneID; 7322; -. DR KEGG; hsa:7322; -. DR UCSC; uc003ler.3; human. [P62837-1] DR CTD; 7322; -. DR DisGeNET; 7322; -. DR EuPathDB; HostDB:ENSG00000131508.15; -. DR GeneCards; UBE2D2; -. DR H-InvDB; HIX0019025; -. DR H-InvDB; HIX0028451; -. DR HGNC; HGNC:12475; UBE2D2. DR HPA; HPA003920; -. DR MIM; 602962; gene. DR neXtProt; NX_P62837; -. DR OpenTargets; ENSG00000131508; -. DR PharmGKB; PA37125; -. DR eggNOG; KOG0417; Eukaryota. DR eggNOG; COG5078; LUCA. DR GeneTree; ENSGT00760000119012; -. DR HOGENOM; HOG000233455; -. DR HOVERGEN; HBG063308; -. DR InParanoid; P62837; -. DR KO; K06689; -. DR OMA; IAHIYKQ; -. DR PhylomeDB; P62837; -. DR TreeFam; TF101108; -. DR BioCyc; MetaCyc:HS05542-MONOMER; -. DR BRENDA; 2.3.2.B5; 2681. DR BRENDA; 2.3.2.B6; 2681. DR BRENDA; 2.3.2.B8; 2681. DR Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha. DR Reactome; R-HSA-168927; TICAM1, RIP1-mediated IKK complex recruitment. DR Reactome; R-HSA-202424; Downstream TCR signaling. DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation. DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling. DR Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes. DR Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins. DR Reactome; R-HSA-8951664; Neddylation. DR Reactome; R-HSA-936440; Negative regulators of DDX58/IFIH1 signaling. DR Reactome; R-HSA-937041; IKK complex recruitment mediated by RIP1. DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR SignaLink; P62837; -. DR SIGNOR; P62837; -. DR UniPathway; UPA00143; -. DR ChiTaRS; UBE2D2; human. DR EvolutionaryTrace; P62837; -. DR GeneWiki; UBE2D2; -. DR GenomeRNAi; 7322; -. DR PRO; PR:P62837; -. DR Proteomes; UP000005640; Chromosome 5. DR Bgee; ENSG00000131508; -. DR CleanEx; HS_UBE2D2; -. DR ExpressionAtlas; P62837; baseline and differential. DR Genevisible; P62837; HS. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0043234; C:protein complex; IDA:MGI. DR GO; GO:0000151; C:ubiquitin ligase complex; IDA:BHF-UCL. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:ParkinsonsUK-UCL. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB. DR GO; GO:0006464; P:cellular protein modification process; TAS:ProtInc. DR GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome. DR GO; GO:0002756; P:MyD88-independent toll-like receptor signaling pathway; TAS:Reactome. DR GO; GO:0051865; P:protein autoubiquitination; IDA:ParkinsonsUK-UCL. DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB. DR GO; GO:0000209; P:protein polyubiquitination; IDA:BHF-UCL. DR GO; GO:0016567; P:protein ubiquitination; IDA:ParkinsonsUK-UCL. DR GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome. DR GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome. DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome. DR GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; TAS:Reactome. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:ProtInc. 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; UBIQUITIN_CONJUGAT_1; 1. DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Complete proteome; KW Direct protein sequencing; Nucleotide-binding; Reference proteome; KW Transferase; Ubl conjugation pathway. FT CHAIN 1 147 Ubiquitin-conjugating enzyme E2 D2. FT /FTId=PRO_0000082462. FT ACT_SITE 85 85 Glycyl thioester intermediate. FT {ECO:0000255|PROSITE-ProRule:PRU00388, FT ECO:0000255|PROSITE-ProRule:PRU10133}. FT VAR_SEQ 1 29 Missing (in isoform 2). FT {ECO:0000303|Ref.4}. FT /FTId=VSP_045180. FT MUTAGEN 63 63 K->A,E: Strongly reduced interaction with FT CNTO4. {ECO:0000269|PubMed:15001359}. FT MUTAGEN 85 85 C->A: Catalytically inactive. Loss of FT ability to promote FBXW2-mediated GCM1 FT ubiquitination. Inhibition of TNF-alpha- FT induced degradation of NFKBIA. FT {ECO:0000269|PubMed:10329681, FT ECO:0000269|PubMed:18703417, FT ECO:0000269|PubMed:20525694}. FT CONFLICT 128 128 K -> Q (in Ref. 2; AAC41750). FT {ECO:0000305}. FT HELIX 1 15 {ECO:0000244|PDB:2ESK}. FT STRAND 19 28 {ECO:0000244|PDB:2ESK}. FT STRAND 32 38 {ECO:0000244|PDB:2ESK}. FT STRAND 41 43 {ECO:0000244|PDB:4V3L}. FT TURN 44 47 {ECO:0000244|PDB:2ESK}. FT STRAND 49 55 {ECO:0000244|PDB:2ESK}. FT TURN 58 61 {ECO:0000244|PDB:2ESK}. FT STRAND 66 71 {ECO:0000244|PDB:2ESK}. FT STRAND 76 78 {ECO:0000244|PDB:4A4B}. FT STRAND 82 84 {ECO:0000244|PDB:1W4U}. FT HELIX 87 89 {ECO:0000244|PDB:2ESK}. FT TURN 90 92 {ECO:0000244|PDB:2ESK}. FT HELIX 99 111 {ECO:0000244|PDB:2ESK}. FT STRAND 115 117 {ECO:0000244|PDB:4V3L}. FT HELIX 121 129 {ECO:0000244|PDB:2ESK}. FT HELIX 131 145 {ECO:0000244|PDB:2ESK}. SQ SEQUENCE 147 AA; 16735 MW; C942BE7853CBC355 CRC64; MALKRIHKEL NDLARDPPAQ CSAGPVGDDM FHWQATIMGP NDSPYQGGVF FLTIHFPTDY PFKPPKVAFT TRIYHPNINS NGSICLDILR SQWSPALTIS KVLLSICSLL CDPNPDDPLV PEIARIYKTD REKYNRIARE WTQKYAM //