UB2D1_HUMAN
ID UB2D1_HUMAN Reviewed; 147 AA.
AC P51668; A6NLF6; A8K786;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 D1;
DE EC=2.3.2.23 {ECO:0000269|PubMed:18042044, ECO:0000269|PubMed:19854139, ECO:0000269|PubMed:20061386};
DE AltName: Full=(E3-independent) E2 ubiquitin-conjugating enzyme D1;
DE EC=2.3.2.24 {ECO:0000269|PubMed:17588522};
DE AltName: Full=E2 ubiquitin-conjugating enzyme D1;
DE AltName: Full=Stimulator of Fe transport;
DE Short=SFT;
DE AltName: Full=UBC4/5 homolog;
DE AltName: Full=UbcH5;
DE AltName: Full=Ubiquitin carrier protein D1;
DE AltName: Full=Ubiquitin-conjugating enzyme E2(17)KB 1;
DE AltName: Full=Ubiquitin-conjugating enzyme E2-17 kDa 1;
DE AltName: Full=Ubiquitin-protein ligase D1;
GN Name=UBE2D1; Synonyms=SFT, UBC5A, UBCH5, UBCH5A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8090726; DOI=10.1073/pnas.91.19.8797;
RA Scheffner M., Huibregtse J.M., Howley P.M.;
RT "Identification of a human ubiquitin-conjugating enzyme that mediates the
RT E6-AP-dependent ubiquitination of p53.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:8797-8801(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RX PubMed=12480712; DOI=10.1182/blood-2002-07-2192;
RA Gehrke S.G., Riedel H.-D., Herrmann T., Hadaschik B., Bents K.,
RA Veltkamp C., Stremmel W.;
RT "UbcH5A, a member of human E2 ubiquitin-conjugating enzymes, is closely
RT related to SFT, a stimulator of iron transport, and is up-regulated in
RT hereditary hemochromatosis.";
RL Blood 101:3288-3293(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, and Skin;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 134-147, AND TISSUE SPECIFICITY.
RX PubMed=9362508; DOI=10.1083/jcb.139.4.895;
RA Gutierrez J.A., Yu J., Rivera S., Wessling-Resnick M.;
RT "Functional expression cloning and characterization of SFT, a stimulator of
RT Fe transport.";
RL J. Cell Biol. 139:895-905(1997).
RN [9]
RP ERRATUM OF PUBMED:9362508.
RA Gutierrez J.A., Yu J., Rivera S., Wessling-Resnick M.;
RL J. Cell Biol. 147:205-205(1999).
RN [10]
RP SUBUNIT OF A COMPLEX WITH SIAH1; CACYBP; SKP1; APC AND TBL1X.
RX PubMed=11389839; DOI=10.1016/s1097-2765(01)00242-8;
RA Matsuzawa S., Reed J.C.;
RT "Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin
RT degradation linked to p53 responses.";
RL Mol. Cell 7:915-926(2001).
RN [11]
RP INTERACTION WITH RNF11.
RX PubMed=14562029; DOI=10.1038/sj.bjc.6601301;
RA Subramaniam V., Li H., Wong M.J., Kitching R., Attisano L., Wrana J.,
RA Zubovits J., Burger A.M., Seth A.K.;
RT "The RING-H2 protein RNF11 is overexpressed in breast cancer and is a
RT target of Smurf2 E3 ligase.";
RL Br. J. Cancer 89:1538-1544(2003).
RN [12]
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 [13]
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 required for
RT the mono-ubiquitination of proteins and elongation by polyubiquitin chains
RT with a specific topology.";
RL Biochem. J. 409:723-729(2008).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=18845142; DOI=10.1016/j.yexcr.2008.09.011;
RA Espinosa A., Oke V., Elfving A., Nyberg F., Covacu R., Wahren-Herlenius M.;
RT "The autoantigen Ro52 is an E3 ligase resident in the cytoplasm but enters
RT the nucleus upon cellular exposure to nitric oxide.";
RL Exp. Cell Res. 314:3605-3613(2008).
RN [15]
RP FUNCTION.
RX PubMed=18359941; DOI=10.1074/jbc.m800402200;
RA Grou C.P., Carvalho A.F., Pinto M.P., Wiese S., Piechura H., Meyer H.E.,
RA 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 [16]
RP FUNCTION.
RX PubMed=19103148; DOI=10.1016/j.abb.2008.12.001;
RA Pabarcus M.K., Hoe N., Sadeghi S., Patterson C., Wiertz E., Correia M.A.;
RT "CYP3A4 ubiquitination by gp78 (the tumor autocrine motility factor
RT receptor, AMFR) and CHIP E3 ligases.";
RL Arch. Biochem. Biophys. 483:66-74(2009).
RN [17]
RP 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 of
RT IRF3.";
RL Mol. Cell 36:315-325(2009).
RN [18]
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 [19]
RP FUNCTION, AUTOUBIQUITINATION, AND MUTAGENESIS OF LYS-4; ASP-42; PHE-62;
RP ASP-87; SER-94; THR-98; ASP-112; ASP-116 AND ASP-117.
RX PubMed=22496338; DOI=10.1074/mcp.o111.013706;
RA Sheng Y., Hong J.H., Doherty R., Srikumar T., Shloush J., Avvakumov G.V.,
RA Walker J.R., Xue S., Neculai D., Wan J.W., Kim S.K., Arrowsmith C.H.,
RA Raught B., Dhe-Paganon S.;
RT "A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure-
RT function screen.";
RL Mol. Cell. Proteomics 11:329-341(2012).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH MYLIP.
RX PubMed=21685362; DOI=10.1101/gad.2056211;
RA Zhang L., Fairall L., Goult B.T., Calkin A.C., Hong C., Millard C.J.,
RA Tontonoz P., Schwabe J.W.;
RT "The IDOL-UBE2D complex mediates sterol-dependent degradation of the LDL
RT receptor.";
RL Genes Dev. 25:1262-1274(2011).
CC -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins (PubMed:22496338). In vitro
CC catalyzes 'Lys-48'-linked polyubiquitination (PubMed:20061386).
CC Mediates the selective degradation of short-lived and abnormal
CC proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53.
CC Mediates ubiquitination of PEX5 and auto-ubiquitination of STUB1, TRAF6
CC and TRIM63/MURF1 (PubMed:18042044, PubMed:18359941). Ubiquitinates
CC STUB1-associated HSP90AB1 in vitro (PubMed:18042044). Lacks inherent
CC specificity for any particular lysine residue of ubiquitin
CC (PubMed:18042044). Essential for viral activation of IRF3
CC (PubMed:19854139). Mediates polyubiquitination of CYP3A4
CC (PubMed:19103148). {ECO:0000269|PubMed:18042044,
CC ECO:0000269|PubMed:18359941, ECO:0000269|PubMed:19103148,
CC ECO:0000269|PubMed:19854139, ECO:0000269|PubMed:20061386,
CC ECO:0000269|PubMed:22496338}.
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, ECO:0000269|PubMed:18042044,
CC ECO:0000269|PubMed:19854139, ECO:0000269|PubMed:20061386};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-
CC cysteine + N(6)-monoubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.24; Evidence={ECO:0000269|PubMed:17588522};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBUNIT: Component of a E3 ubiquitin ligase complex containing UBE2D1,
CC SIAH1, CACYBP/SIP, SKP1, APC and TBL1X. Interacts with RNF11.
CC {ECO:0000269|PubMed:11389839, ECO:0000269|PubMed:14562029,
CC ECO:0000269|PubMed:21685362}.
CC -!- INTERACTION:
CC P51668; Q96B67: ARRDC3; NbExp=5; IntAct=EBI-743540, EBI-2875665;
CC P51668; Q96EP1-2: CHFR; NbExp=3; IntAct=EBI-743540, EBI-12344389;
CC P51668; Q86UW9: DTX2; NbExp=7; IntAct=EBI-743540, EBI-740376;
CC P51668; Q8N9I9: DTX3; NbExp=6; IntAct=EBI-743540, EBI-2340258;
CC P51668; P62879: GNB2; NbExp=3; IntAct=EBI-743540, EBI-356942;
CC P51668; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-743540, EBI-16439278;
CC P51668; O15344: MID1; NbExp=7; IntAct=EBI-743540, EBI-2340316;
CC P51668; Q9UJV3-2: MID2; NbExp=6; IntAct=EBI-743540, EBI-10172526;
CC P51668; Q9UHC7: MKRN1; NbExp=3; IntAct=EBI-743540, EBI-373524;
CC P51668; Q9H000: MKRN2; NbExp=6; IntAct=EBI-743540, EBI-2341005;
CC P51668; Q13064: MKRN3; NbExp=4; IntAct=EBI-743540, EBI-2340269;
CC P51668; Q96FW1: OTUB1; NbExp=14; IntAct=EBI-743540, EBI-1058491;
CC P51668; Q06587: RING1; NbExp=6; IntAct=EBI-743540, EBI-752313;
CC P51668; Q9Y3C5: RNF11; NbExp=9; IntAct=EBI-743540, EBI-396669;
CC P51668; Q6ZNA4: RNF111; NbExp=5; IntAct=EBI-743540, EBI-2129175;
CC P51668; Q9Y4L5: RNF115; NbExp=12; IntAct=EBI-743540, EBI-2129242;
CC P51668; Q9BV68: RNF126; NbExp=7; IntAct=EBI-743540, EBI-357322;
CC P51668; Q9UBS8: RNF14; NbExp=4; IntAct=EBI-743540, EBI-2130308;
CC P51668; Q9P0P0: RNF181; NbExp=4; IntAct=EBI-743540, EBI-2129136;
CC P51668; Q8N6D2: RNF182; NbExp=3; IntAct=EBI-743540, EBI-2130099;
CC P51668; Q96GF1: RNF185; NbExp=4; IntAct=EBI-743540, EBI-2340249;
CC P51668; Q99496: RNF2; NbExp=4; IntAct=EBI-743540, EBI-722416;
CC P51668; Q96BH1: RNF25; NbExp=5; IntAct=EBI-743540, EBI-2129220;
CC P51668; Q99942: RNF5; NbExp=10; IntAct=EBI-743540, EBI-348482;
CC P51668; Q9Y4K3: TRAF6; NbExp=2; IntAct=EBI-743540, EBI-359276;
CC P51668; O75382: TRIM3; NbExp=3; IntAct=EBI-743540, EBI-2129889;
CC P51668; Q9HCM9: TRIM39; NbExp=6; IntAct=EBI-743540, EBI-739510;
CC P51668; Q9HCM9-2: TRIM39; NbExp=5; IntAct=EBI-743540, EBI-11523450;
CC P51668; Q86XT4: TRIM50; NbExp=5; IntAct=EBI-743540, EBI-9867283;
CC P51668; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-743540, EBI-2130429;
CC P51668; Q9BVG3: TRIM62; NbExp=3; IntAct=EBI-743540, EBI-6929619;
CC P51668; Q9BZR9: TRIM8; NbExp=4; IntAct=EBI-743540, EBI-2340370;
CC P51668; Q9HAC8: UBTD1; NbExp=3; IntAct=EBI-743540, EBI-745871;
CC P51668; P55072: VCP; NbExp=3; IntAct=EBI-743540, EBI-355164;
CC P51668; P98170: XIAP; NbExp=6; IntAct=EBI-743540, EBI-517127;
CC P51668; Q8ND25: ZNRF1; NbExp=9; IntAct=EBI-743540, EBI-2129250;
CC P51668; Q9CZW6: Rnf146; Xeno; NbExp=2; IntAct=EBI-743540, EBI-16124494;
CC P51668; O88846: Rnf4; Xeno; NbExp=4; IntAct=EBI-743540, EBI-7258907;
CC P51668; P62990: UBC; Xeno; NbExp=2; IntAct=EBI-743540, EBI-413053;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18845142}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Up-regulated in livers of iron-
CC overloaded patients with hereditary hemochromatosis.
CC {ECO:0000269|PubMed:12480712, ECO:0000269|PubMed:9362508}.
CC -!- PTM: Autoubiquitinated in vitro. {ECO:0000269|PubMed:22496338}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- CAUTION: PubMed:9362508 cloned and sequenced SFT which consisted of
CC UBE2D1 last coding exon along with intronic sequences on the 5'-end of
CC this exon. A function in iron transport has been described.
CC {ECO:0000305}.
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DR EMBL; X78140; CAA55019.1; -; mRNA.
DR EMBL; AF257220; AAM81086.1; -; mRNA.
DR EMBL; AJ272367; CAC82177.1; -; mRNA.
DR EMBL; AK291901; BAF84590.1; -; mRNA.
DR EMBL; AJ293565; CAC82097.1; -; Genomic_DNA.
DR EMBL; BT007041; AAP35690.1; -; mRNA.
DR EMBL; AC016396; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC023170; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471083; EAW54169.1; -; Genomic_DNA.
DR EMBL; BC005980; AAH05980.1; -; mRNA.
DR EMBL; BC015997; AAH15997.1; -; mRNA.
DR EMBL; AF020761; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS7252.1; -.
DR PIR; I39202; I39202.
DR RefSeq; NP_003329.1; NM_003338.4.
DR PDB; 2C4P; X-ray; 2.35 A; A/B=1-147.
DR PDB; 2YHO; X-ray; 2.10 A; B/D/F/H=1-147.
DR PDB; 3OJ4; X-ray; 3.40 A; A/D=1-147.
DR PDB; 3PTF; X-ray; 2.70 A; A/B=1-147.
DR PDB; 4AP4; X-ray; 2.21 A; B/E=1-147.
DR PDB; 4QPL; X-ray; 1.90 A; B/D=1-147.
DR PDB; 5FER; X-ray; 2.34 A; B/E=1-147.
DR PDB; 5TUT; X-ray; 2.60 A; A=1-147.
DR PDB; 6D4P; X-ray; 2.11 A; A=1-147.
DR PDBsum; 2C4P; -.
DR PDBsum; 2YHO; -.
DR PDBsum; 3OJ4; -.
DR PDBsum; 3PTF; -.
DR PDBsum; 4AP4; -.
DR PDBsum; 4QPL; -.
DR PDBsum; 5FER; -.
DR PDBsum; 5TUT; -.
DR PDBsum; 6D4P; -.
DR AlphaFoldDB; P51668; -.
DR BMRB; P51668; -.
DR SMR; P51668; -.
DR BioGRID; 113169; 311.
DR DIP; DIP-44088N; -.
DR IntAct; P51668; 118.
DR MINT; P51668; -.
DR STRING; 9606.ENSP00000363019; -.
DR ChEMBL; CHEMBL4105766; -.
DR MoonDB; P51668; Predicted.
DR iPTMnet; P51668; -.
DR PhosphoSitePlus; P51668; -.
DR BioMuta; UBE2D1; -.
DR DMDM; 1717848; -.
DR EPD; P51668; -.
DR jPOST; P51668; -.
DR MassIVE; P51668; -.
DR MaxQB; P51668; -.
DR PaxDb; P51668; -.
DR PeptideAtlas; P51668; -.
DR PRIDE; P51668; -.
DR ProteomicsDB; 56362; -.
DR Antibodypedia; 14190; 299 antibodies from 33 providers.
DR DNASU; 7321; -.
DR Ensembl; ENST00000373910.9; ENSP00000363019.3; ENSG00000072401.15.
DR GeneID; 7321; -.
DR KEGG; hsa:7321; -.
DR MANE-Select; ENST00000373910.9; ENSP00000363019.3; NM_003338.5; NP_003329.1.
DR UCSC; uc001jke.3; human.
DR CTD; 7321; -.
DR DisGeNET; 7321; -.
DR GeneCards; UBE2D1; -.
DR HGNC; HGNC:12474; UBE2D1.
DR HPA; ENSG00000072401; Tissue enhanced (skeletal muscle, tongue).
DR MIM; 602961; gene.
DR neXtProt; NX_P51668; -.
DR OpenTargets; ENSG00000072401; -.
DR PharmGKB; PA37124; -.
DR VEuPathDB; HostDB:ENSG00000072401; -.
DR eggNOG; KOG0417; Eukaryota.
DR GeneTree; ENSGT00940000155109; -.
DR HOGENOM; CLU_030988_13_3_1; -.
DR InParanoid; P51668; -.
DR OMA; FCELNRE; -.
DR OrthoDB; 1337945at2759; -.
DR PhylomeDB; P51668; -.
DR TreeFam; TF101108; -.
DR BRENDA; 2.3.2.23; 2681.
DR BRENDA; 2.3.2.24; 2681.
DR BRENDA; 2.3.2.27; 2681.
DR BRENDA; 2.3.2.B8; 2681.
DR PathwayCommons; P51668; -.
DR Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-HSA-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR Reactome; R-HSA-168927; TICAM1, RIP1-mediated IKK complex recruitment.
DR Reactome; R-HSA-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-HSA-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR Reactome; R-HSA-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-HSA-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
DR Reactome; R-HSA-176412; Phosphorylation of the APC/C.
DR Reactome; R-HSA-179409; APC-Cdc20 mediated degradation of Nek2A.
DR Reactome; R-HSA-201451; Signaling by BMP.
DR Reactome; R-HSA-202424; Downstream TCR signaling.
DR Reactome; R-HSA-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex.
DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-HSA-8853884; Transcriptional Regulation by VENTX.
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-9033241; Peroxisomal protein import.
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-9687136; Aberrant regulation of mitotic exit in cancer due to RB1 defects.
DR Reactome; R-HSA-9705462; Inactivation of CSF3 (G-CSF) signaling.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; P51668; -.
DR SIGNOR; P51668; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 7321; 12 hits in 1091 CRISPR screens.
DR ChiTaRS; UBE2D1; human.
DR EvolutionaryTrace; P51668; -.
DR GeneWiki; UBE2D1; -.
DR GenomeRNAi; 7321; -.
DR Pharos; P51668; Tbio.
DR PRO; PR:P51668; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P51668; protein.
DR Bgee; ENSG00000072401; Expressed in biceps brachii and 202 other tissues.
DR ExpressionAtlas; P51668; baseline and differential.
DR Genevisible; P51668; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing 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:BHF-UCL.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; TAS:Reactome.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:Reactome.
DR GO; GO:1902916; P:positive regulation of protein polyubiquitination; IEA:Ensembl.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA: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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Nucleotide-binding;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..147
FT /note="Ubiquitin-conjugating enzyme E2 D1"
FT /id="PRO_0000082460"
FT DOMAIN 1..147
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 85
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT MUTAGEN 4
FT /note="K->E: Decrease in autoubiquitination."
FT /evidence="ECO:0000269|PubMed:22496338"
FT MUTAGEN 42
FT /note="D->R: Decrease in autoubiquitination."
FT /evidence="ECO:0000269|PubMed:22496338"
FT MUTAGEN 62
FT /note="F->A: Decrease in autoubiquitination."
FT /evidence="ECO:0000269|PubMed:22496338"
FT MUTAGEN 87
FT /note="D->R: Decrease in autoubiquitination."
FT /evidence="ECO:0000269|PubMed:22496338"
FT MUTAGEN 94
FT /note="S->E: Decrease in autoubiquitination."
FT /evidence="ECO:0000269|PubMed:22496338"
FT MUTAGEN 98
FT /note="T->E: Decrease in autoubiquitination."
FT /evidence="ECO:0000269|PubMed:22496338"
FT MUTAGEN 112
FT /note="D->R: Decrease in autoubiquitination."
FT /evidence="ECO:0000269|PubMed:22496338"
FT MUTAGEN 116
FT /note="D->R: Decrease in autoubiquitination."
FT /evidence="ECO:0000269|PubMed:22496338"
FT MUTAGEN 117
FT /note="D->R: Decrease in autoubiquitination."
FT /evidence="ECO:0000269|PubMed:22496338"
FT HELIX 1..15
FT /evidence="ECO:0007829|PDB:4QPL"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:4QPL"
FT STRAND 29..38
FT /evidence="ECO:0007829|PDB:4QPL"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:4AP4"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:4QPL"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:4QPL"
FT TURN 58..61
FT /evidence="ECO:0007829|PDB:4QPL"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:4QPL"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:4QPL"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:4QPL"
FT HELIX 99..111
FT /evidence="ECO:0007829|PDB:4QPL"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:5FER"
FT HELIX 121..129
FT /evidence="ECO:0007829|PDB:4QPL"
FT HELIX 131..146
FT /evidence="ECO:0007829|PDB:4QPL"
SQ SEQUENCE 147 AA; 16602 MW; 2E96FD0179EE119D CRC64;
MALKRIQKEL SDLQRDPPAH CSAGPVGDDL FHWQATIMGP PDSAYQGGVF FLTVHFPTDY
PFKPPKIAFT TKIYHPNINS NGSICLDILR SQWSPALTVS KVLLSICSLL CDPNPDDPLV
PDIAQIYKSD KEKYNRHARE WTQKYAM
