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Ubiquitin-conjugating enzyme E2 D1 (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme D1) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme D1) (Stimulator of Fe transport) (SFT) (UBC4/5 homolog) (UbcH5) (Ubiquitin carrier protein D1) (Ubiquitin-conjugating enzyme E2(17)KB 1) (Ubiquitin-conjugating enzyme E2-17 kDa 1) (Ubiquitin-protein ligase D1)

 UB2D1_HUMAN             Reviewed;         147 AA.
P51668; A6NLF6; A8K786;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
22-NOV-2017, entry version 174.
RecName: Full=Ubiquitin-conjugating enzyme E2 D1;
EC=2.3.2.23 {ECO:0000269|PubMed:18042044, ECO:0000269|PubMed:19854139, ECO:0000269|PubMed:20061386};
AltName: Full=(E3-independent) E2 ubiquitin-conjugating enzyme D1;
EC=2.3.2.24 {ECO:0000269|PubMed:17588522};
AltName: Full=E2 ubiquitin-conjugating enzyme D1;
AltName: Full=Stimulator of Fe transport;
Short=SFT;
AltName: Full=UBC4/5 homolog;
AltName: Full=UbcH5;
AltName: Full=Ubiquitin carrier protein D1;
AltName: Full=Ubiquitin-conjugating enzyme E2(17)KB 1;
AltName: Full=Ubiquitin-conjugating enzyme E2-17 kDa 1;
AltName: Full=Ubiquitin-protein ligase D1;
Name=UBE2D1; Synonyms=SFT, UBC5A, UBCH5, UBCH5A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8090726; DOI=10.1073/pnas.91.19.8797;
Scheffner M., Huibregtse J.M., Howley P.M.;
"Identification of a human ubiquitin-conjugating enzyme that mediates
the E6-AP-dependent ubiquitination of p53.";
Proc. Natl. Acad. Sci. U.S.A. 91:8797-8801(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
PubMed=12480712; DOI=10.1182/blood-2002-07-2192;
Gehrke S.G., Riedel H.-D., Herrmann T., Hadaschik B., Bents K.,
Veltkamp C., Stremmel W.;
"UbcH5A, a member of human E2 ubiquitin-conjugating enzymes, is
closely related to SFT, a stimulator of iron transport, and is up-
regulated in hereditary hemochromatosis.";
Blood 101:3288-3293(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skeletal muscle;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[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].
TISSUE=Bone marrow, and Skin;
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]
NUCLEOTIDE SEQUENCE [MRNA] OF 134-147, AND TISSUE SPECIFICITY.
PubMed=9362508; DOI=10.1083/jcb.139.4.895;
Gutierrez J.A., Yu J., Rivera S., Wessling-Resnick M.;
"Functional expression cloning and characterization of SFT, a
stimulator of Fe transport.";
J. Cell Biol. 139:895-905(1997).
[9]
ERRATUM.
Gutierrez J.A., Yu J., Rivera S., Wessling-Resnick M.;
J. Cell Biol. 147:205-205(1999).
[10]
SUBUNIT OF A COMPLEX WITH SIAH1; CACYBP; SKP1; APC AND TBL1X.
PubMed=11389839; DOI=10.1016/S1097-2765(01)00242-8;
Matsuzawa S., Reed J.C.;
"Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin
degradation linked to p53 responses.";
Mol. Cell 7:915-926(2001).
[11]
INTERACTION WITH RNF11.
PubMed=14562029; DOI=10.1038/sj.bjc.6601301;
Subramaniam V., Li H., Wong M.J., Kitching R., Attisano L., Wrana J.,
Zubovits J., Burger A.M., Seth A.K.;
"The RING-H2 protein RNF11 is overexpressed in breast cancer and is a
target of Smurf2 E3 ligase.";
Br. J. Cancer 89:1538-1544(2003).
[12]
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).
[13]
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).
[14]
SUBCELLULAR LOCATION.
PubMed=18845142; DOI=10.1016/j.yexcr.2008.09.011;
Espinosa A., Oke V., Elfving A., Nyberg F., Covacu R.,
Wahren-Herlenius M.;
"The autoantigen Ro52 is an E3 ligase resident in the cytoplasm but
enters the nucleus upon cellular exposure to nitric oxide.";
Exp. Cell Res. 314:3605-3613(2008).
[15]
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).
[16]
FUNCTION.
PubMed=19103148; DOI=10.1016/j.abb.2008.12.001;
Pabarcus M.K., Hoe N., Sadeghi S., Patterson C., Wiertz E.,
Correia M.A.;
"CYP3A4 ubiquitination by gp78 (the tumor autocrine motility factor
receptor, AMFR) and CHIP E3 ligases.";
Arch. Biochem. Biophys. 483:66-74(2009).
[17]
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).
[18]
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).
[19]
FUNCTION, AUTOUBIQUITINATION, AND MUTAGENESIS OF LYS-4; ASP-42;
PHE-62; ASP-87; SER-94; THR-98; ASP-112; ASP-116 AND ASP-117.
PubMed=22496338; DOI=10.1074/mcp.O111.013706;
Sheng Y., Hong J.H., Doherty R., Srikumar T., Shloush J.,
Avvakumov G.V., Walker J.R., Xue S., Neculai D., Wan J.W., Kim S.K.,
Arrowsmith C.H., Raught B., Dhe-Paganon S.;
"A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure-
function screen.";
Mol. Cell. Proteomics 11:329-341(2012).
[20]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH MYLIP.
PubMed=21685362; DOI=10.1101/gad.2056211;
Zhang L., Fairall L., Goult B.T., Calkin A.C., Hong C., Millard C.J.,
Tontonoz P., Schwabe J.W.;
"The IDOL-UBE2D complex mediates sterol-dependent degradation of the
LDL receptor.";
Genes Dev. 25:1262-1274(2011).
-!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
covalent attachment to other proteins (PubMed:22496338). In vitro
catalyzes 'Lys-48'-linked polyubiquitination (PubMed:20061386).
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 auto-ubiquitination
of STUB1, TRAF6 and TRIM63/MURF1 (PubMed:18042044,
PubMed:18359941). Ubiquitinates STUB1-associated HSP90AB1 in vitro
(PubMed:18042044). Lacks inherent specificity for any particular
lysine residue of ubiquitin (PubMed:18042044). Essential for viral
activation of IRF3 (PubMed:19854139). Mediates polyubiquitination
of CYP3A4 (PubMed:19103148). {ECO:0000269|PubMed:18042044,
ECO:0000269|PubMed:18359941, ECO:0000269|PubMed:19103148,
ECO:0000269|PubMed:19854139, ECO:0000269|PubMed:20061386,
ECO:0000269|PubMed:22496338}.
-!- 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:18042044, ECO:0000269|PubMed:19854139,
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: Component of a E3 ubiquitin ligase complex containing
UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X. Interacts with
RNF11. {ECO:0000269|PubMed:11389839, ECO:0000269|PubMed:14562029,
ECO:0000269|PubMed:21685362}.
-!- INTERACTION:
Q86UW9:DTX2; NbExp=8; IntAct=EBI-743540, EBI-740376;
Q8N9I9:DTX3; NbExp=3; IntAct=EBI-743540, EBI-2340258;
O15344:MID1; NbExp=6; IntAct=EBI-743540, EBI-2340316;
Q9UJV3-2:MID2; NbExp=5; IntAct=EBI-743540, EBI-10172526;
Q9H000:MKRN2; NbExp=5; IntAct=EBI-743540, EBI-2341005;
Q13064:MKRN3; NbExp=4; IntAct=EBI-743540, EBI-2340269;
Q96FW1:OTUB1; NbExp=10; IntAct=EBI-743540, EBI-1058491;
Q06587:RING1; NbExp=3; IntAct=EBI-743540, EBI-752313;
Q9Y3C5:RNF11; NbExp=6; IntAct=EBI-743540, EBI-396669;
Q6ZNA4:RNF111; NbExp=5; IntAct=EBI-743540, EBI-2129175;
Q9Y4L5:RNF115; NbExp=8; IntAct=EBI-743540, EBI-2129242;
Q9BV68:RNF126; NbExp=8; IntAct=EBI-743540, EBI-357322;
Q9UBS8:RNF14; NbExp=4; IntAct=EBI-743540, EBI-2130308;
Q9CZW6:Rnf146 (xeno); NbExp=2; IntAct=EBI-743540, EBI-16124494;
Q96GF1:RNF185; NbExp=3; IntAct=EBI-743540, EBI-2340249;
Q99496:RNF2; NbExp=3; IntAct=EBI-743540, EBI-722416;
O88846:Rnf4 (xeno); NbExp=4; IntAct=EBI-743540, EBI-7258907;
Q99942:RNF5; NbExp=7; IntAct=EBI-743540, EBI-348482;
Q9Y4K3:TRAF6; NbExp=2; IntAct=EBI-743540, EBI-359276;
Q9HCM9:TRIM39; NbExp=6; IntAct=EBI-743540, EBI-739510;
Q9BZR9:TRIM8; NbExp=3; IntAct=EBI-743540, EBI-2340370;
P62990:UBC (xeno); NbExp=2; IntAct=EBI-743540, EBI-413053;
P98170:XIAP; NbExp=7; IntAct=EBI-743540, EBI-517127;
Q8ND25:ZNRF1; NbExp=6; IntAct=EBI-743540, EBI-2129250;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18845142}.
-!- TISSUE SPECIFICITY: Ubiquitous. Up-regulated in livers of iron-
overloaded patients with hereditary hemochromatosis.
{ECO:0000269|PubMed:12480712, ECO:0000269|PubMed:9362508}.
-!- PTM: Autoubiquitinated in vitro. {ECO:0000269|PubMed:22496338}.
-!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-!- CAUTION: PubMed:9362508 cloned and sequenced SFT which consisted
of UBE2D1 last coding exon along with intronic sequences on the
5'-end of this exon. A function in iron transport has been
described. {ECO:0000305}.
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EMBL; X78140; CAA55019.1; -; mRNA.
EMBL; AF257220; AAM81086.1; -; mRNA.
EMBL; AJ272367; CAC82177.1; -; mRNA.
EMBL; AK291901; BAF84590.1; -; mRNA.
EMBL; AJ293565; CAC82097.1; -; Genomic_DNA.
EMBL; BT007041; AAP35690.1; -; mRNA.
EMBL; AC016396; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC023170; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471083; EAW54169.1; -; Genomic_DNA.
EMBL; BC005980; AAH05980.1; -; mRNA.
EMBL; BC015997; AAH15997.1; -; mRNA.
EMBL; AF020761; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS7252.1; -.
PIR; I39202; I39202.
RefSeq; NP_003329.1; NM_003338.4.
UniGene; Hs.129683; -.
PDB; 2C4P; X-ray; 2.35 A; A/B=1-147.
PDB; 2YHO; X-ray; 2.10 A; B/D/F/H=1-147.
PDB; 3OJ4; X-ray; 3.40 A; A/D=1-147.
PDB; 3PTF; X-ray; 2.70 A; A/B=1-147.
PDB; 4AP4; X-ray; 2.21 A; B/E=1-147.
PDB; 4QPL; X-ray; 1.90 A; B/D=1-147.
PDB; 5FER; X-ray; 2.34 A; B/E=1-147.
PDBsum; 2C4P; -.
PDBsum; 2YHO; -.
PDBsum; 3OJ4; -.
PDBsum; 3PTF; -.
PDBsum; 4AP4; -.
PDBsum; 4QPL; -.
PDBsum; 5FER; -.
ProteinModelPortal; P51668; -.
SMR; P51668; -.
BioGrid; 113169; 272.
DIP; DIP-44088N; -.
IntAct; P51668; 115.
MINT; MINT-1433717; -.
STRING; 9606.ENSP00000363019; -.
iPTMnet; P51668; -.
PhosphoSitePlus; P51668; -.
BioMuta; UBE2D1; -.
DMDM; 1717848; -.
EPD; P51668; -.
MaxQB; P51668; -.
PaxDb; P51668; -.
PeptideAtlas; P51668; -.
PRIDE; P51668; -.
DNASU; 7321; -.
Ensembl; ENST00000373910; ENSP00000363019; ENSG00000072401.
GeneID; 7321; -.
KEGG; hsa:7321; -.
UCSC; uc001jke.3; human.
CTD; 7321; -.
DisGeNET; 7321; -.
EuPathDB; HostDB:ENSG00000072401.14; -.
GeneCards; UBE2D1; -.
HGNC; HGNC:12474; UBE2D1.
HPA; HPA003920; -.
MIM; 602961; gene.
neXtProt; NX_P51668; -.
OpenTargets; ENSG00000072401; -.
PharmGKB; PA37124; -.
eggNOG; KOG0417; Eukaryota.
eggNOG; COG5078; LUCA.
GeneTree; ENSGT00760000119012; -.
HOGENOM; HOG000233455; -.
HOVERGEN; HBG063308; -.
InParanoid; P51668; -.
KO; K06689; -.
OMA; YWQATIM; -.
OrthoDB; EOG091G0GF8; -.
PhylomeDB; P51668; -.
TreeFam; TF101108; -.
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-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
Reactome; R-HSA-168927; TICAM1, RIP1-mediated IKK complex recruitment.
Reactome; R-HSA-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-HSA-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
Reactome; R-HSA-176408; Regulation of APC/C activators between G1/S and early anaphase.
Reactome; R-HSA-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
Reactome; R-HSA-176412; Phosphorylation of the APC/C.
Reactome; R-HSA-179409; APC-Cdc20 mediated degradation of Nek2A.
Reactome; R-HSA-201451; Signaling by BMP.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
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-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; P51668; -.
SIGNOR; P51668; -.
UniPathway; UPA00143; -.
ChiTaRS; UBE2D1; human.
EvolutionaryTrace; P51668; -.
GeneWiki; UBE2D1; -.
GenomeRNAi; 7321; -.
PRO; PR:P51668; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000072401; -.
CleanEx; HS_UBE2D1; -.
ExpressionAtlas; P51668; baseline and differential.
Genevisible; P51668; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0043234; C:protein 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:BHF-UCL.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
GO; GO:0030509; P:BMP signaling pathway; TAS:Reactome.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
GO; GO:1902916; P:positive regulation of protein polyubiquitination; IEA:Ensembl.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB.
GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition; TAS:Reactome.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
GO; GO:0051439; P:regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
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; ATP-binding; Complete proteome; Cytoplasm;
Nucleotide-binding; Reference proteome; Transferase; Ubl conjugation;
Ubl conjugation pathway.
CHAIN 1 147 Ubiquitin-conjugating enzyme E2 D1.
/FTId=PRO_0000082460.
ACT_SITE 85 85 Glycyl thioester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00388,
ECO:0000255|PROSITE-ProRule:PRU10133}.
MUTAGEN 4 4 K->E: Decrease in autoubiquitination.
{ECO:0000269|PubMed:22496338}.
MUTAGEN 42 42 D->R: Decrease in autoubiquitination.
{ECO:0000269|PubMed:22496338}.
MUTAGEN 62 62 F->A: Decrease in autoubiquitination.
{ECO:0000269|PubMed:22496338}.
MUTAGEN 87 87 D->R: Decrease in autoubiquitination.
{ECO:0000269|PubMed:22496338}.
MUTAGEN 94 94 S->E: Decrease in autoubiquitination.
{ECO:0000269|PubMed:22496338}.
MUTAGEN 98 98 T->E: Decrease in autoubiquitination.
{ECO:0000269|PubMed:22496338}.
MUTAGEN 112 112 D->R: Decrease in autoubiquitination.
{ECO:0000269|PubMed:22496338}.
MUTAGEN 116 116 D->R: Decrease in autoubiquitination.
{ECO:0000269|PubMed:22496338}.
MUTAGEN 117 117 D->R: Decrease in autoubiquitination.
{ECO:0000269|PubMed:22496338}.
HELIX 1 15 {ECO:0000244|PDB:4QPL}.
STRAND 21 26 {ECO:0000244|PDB:4QPL}.
STRAND 29 38 {ECO:0000244|PDB:4QPL}.
STRAND 41 43 {ECO:0000244|PDB:4AP4}.
TURN 44 47 {ECO:0000244|PDB:4QPL}.
STRAND 49 55 {ECO:0000244|PDB:4QPL}.
TURN 58 61 {ECO:0000244|PDB:4QPL}.
STRAND 66 69 {ECO:0000244|PDB:4QPL}.
HELIX 87 89 {ECO:0000244|PDB:4QPL}.
TURN 90 92 {ECO:0000244|PDB:4QPL}.
HELIX 99 111 {ECO:0000244|PDB:4QPL}.
STRAND 115 117 {ECO:0000244|PDB:5FER}.
HELIX 121 129 {ECO:0000244|PDB:4QPL}.
HELIX 131 146 {ECO:0000244|PDB:4QPL}.
SEQUENCE 147 AA; 16602 MW; 2E96FD0179EE119D CRC64;
MALKRIQKEL SDLQRDPPAH CSAGPVGDDL FHWQATIMGP PDSAYQGGVF FLTVHFPTDY
PFKPPKIAFT TKIYHPNINS NGSICLDILR SQWSPALTVS KVLLSICSLL CDPNPDDPLV
PDIAQIYKSD KEKYNRHARE WTQKYAM


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