UBE2D1: Difference between revisions

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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Ubiquitin-conjugating enzyme E2 D1''' is a [[protein]] that in humans is encoded by the ''UBE2D1'' [[gene]].<ref name="pmid10072594">{{cite journal | vauthors = Robinson PA, Leek JP, Ardley HC, Thompson J, Rose SA, Markham AF | title = Assignment of UBE2D1 to human chromosome bands 10q11.2→q21 by in situ hybridization | journal = Cytogenet Cell Genet | volume = 83 | issue = 3–4 | pages = 247–8 | date = March 1999 | pmid = 10072594 | pmc =  | doi = 10.1159/000015195 }}</ref><ref name="pmid8530467">{{cite journal | vauthors = Jensen JP, Bates PW, Yang M, Vierstra RD, Weissman AM | title = Identification of a family of closely related human ubiquitin conjugating enzymes | journal = J Biol Chem | volume = 270 | issue = 51 | pages = 30408–14 | date = January 1996 | pmid = 8530467 | pmc = | doi = 10.1074/jbc.270.51.30408 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: UBE2D1 ubiquitin-conjugating enzyme E2D 1 (UBC4/5 homolog, yeast)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7321| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_UBE2D1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2c4p.
| PDB = {{PDB2|2c4p}}
| Name = Ubiquitin-conjugating enzyme E2D 1 (UBC4/5 homolog, yeast)
| HGNCid = 12474
| Symbol = UBE2D1
| AltSymbols =; E2(17)KB1; SFT; UBC4/5; UBCH5; UBCH5A
| OMIM = 602961
| ECnumber = 
| Homologene = 20714
| MGIid = 2384911
| GeneAtlas_image1 = PBB_GE_UBE2D1_214590_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_UBE2D1_211764_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004842 |text = ubiquitin-protein ligase activity}} {{GNF_GO|id=GO:0016874 |text = ligase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0000209 |text = protein polyubiquitination}} {{GNF_GO|id=GO:0006511 |text = ubiquitin-dependent protein catabolic process}} {{GNF_GO|id=GO:0006512 |text = ubiquitin cycle}} {{GNF_GO|id=GO:0031398 |text = positive regulation of protein ubiquitination}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7321
    | Hs_Ensembl = ENSG00000072401
    | Hs_RefseqProtein = NP_003329
    | Hs_RefseqmRNA = NM_003338
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 10
    | Hs_GenLoc_start = 59764745
    | Hs_GenLoc_end = 59800515
    | Hs_Uniprot = P51668
    | Mm_EntrezGene = 216080
    | Mm_Ensembl = ENSMUSG00000019927
    | Mm_RefseqmRNA = NM_145420
    | Mm_RefseqProtein = NP_663395
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 10
    | Mm_GenLoc_start = 70650280
    | Mm_GenLoc_end = 70657583
    | Mm_Uniprot = Q3UFQ4
  }}
}}
'''Ubiquitin-conjugating enzyme E2D 1 (UBC4/5 homolog, yeast)''', also known as '''UBE2D1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: UBE2D1 ubiquitin-conjugating enzyme E2D 1 (UBC4/5 homolog, yeast)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7321| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is closely related to a stimulator of iron transport (SFT), and is up-regulated in hereditary hemochromatosis. It also functions in the ubiquitination of the tumor-suppressor protein p53 and the hypoxia-inducible transcription factor HIF1alpha by interacting with the E1 ubiquitin-activating enzyme and the E3 ubiquitin-protein ligases.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is closely related to a stimulator of iron transport (SFT), and is up-regulated in hereditary hemochromatosis. It also functions in the ubiquitination of the tumor-suppressor protein p53 and the hypoxia-inducible transcription factor HIF1alpha by interacting with the E1 ubiquitin-activating enzyme and the E3 ubiquitin-protein ligases.<ref name="entrez">{{cite web | title = Entrez Gene: UBE2D1 ubiquitin-conjugating enzyme E2D 1 (UBC4/5 homolog, yeast)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7321| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  | author=Scheffner M, Huibregtse JM, Howley PM |title=Identification of a human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 19 |pages= 8797-801 |year= 1994 |pmid= 8090726 |doi=  }}
*{{cite journal  | author=Jensen JP, Bates PW, Yang M, ''et al.'' |title=Identification of a family of closely related human ubiquitin conjugating enzymes. |journal=J. Biol. Chem. |volume=270 |issue= 51 |pages= 30408-14 |year= 1996 |pmid= 8530467 |doi=  }}
*{{cite journal  | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi=  }}
*{{cite journal  | author=Hatakeyama S, Jensen JP, Weissman AM |title=Subcellular localization and ubiquitin-conjugating enzyme (E2) interactions of mammalian HECT family ubiquitin protein ligases. |journal=J. Biol. Chem. |volume=272 |issue= 24 |pages= 15085-92 |year= 1997 |pmid= 9182527 |doi=  }}
*{{cite journal  | author=Gutierrez JA, Yu J, Rivera S, Wessling-Resnick M |title=Functional expression cloning and characterization of SFT, a stimulator of Fe transport. |journal=J. Cell Biol. |volume=139 |issue= 4 |pages= 895-905 |year= 1997 |pmid= 9362508 |doi=  }}
*{{cite journal  | author=Gutierrez JA, Yu J, Wessling-Resnick M |title=Characterization and chromosomal mapping of the human gene for SFT, a stimulator of Fe transport. |journal=Biochem. Biophys. Res. Commun. |volume=253 |issue= 3 |pages= 739-42 |year= 1999 |pmid= 9918797 |doi= 10.1006/bbrc.1998.9836 }}
*{{cite journal  | author=Nuber U, Scheffner M |title=Identification of determinants in E2 ubiquitin-conjugating enzymes required for hect E3 ubiquitin-protein ligase interaction. |journal=J. Biol. Chem. |volume=274 |issue= 11 |pages= 7576-82 |year= 1999 |pmid= 10066826 |doi=  }}
*{{cite journal  | author=Robinson PA, Leek JP, Ardley HC, ''et al.'' |title=Assignment of UBE2D1 to human chromosome bands 10q11.2-->q21 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=83 |issue= 3-4 |pages= 247-8 |year= 1999 |pmid= 10072594 |doi=  }}
*{{cite journal  | author=Kamura T, Sato S, Iwai K, ''et al.'' |title=Activation of HIF1alpha ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complex. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 19 |pages= 10430-5 |year= 2000 |pmid= 10973499 |doi= 10.1073/pnas.190332597 }}
*{{cite journal  | author=Pringa E, Martinez-Noel G, Muller U, Harbers K |title=Interaction of the ring finger-related U-box motif of a nuclear dot protein with ubiquitin-conjugating enzymes. |journal=J. Biol. Chem. |volume=276 |issue= 22 |pages= 19617-23 |year= 2001 |pmid= 11274149 |doi= 10.1074/jbc.M100192200 }}
*{{cite journal  | author=Hashizume R, Fukuda M, Maeda I, ''et al.'' |title=The RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutation. |journal=J. Biol. Chem. |volume=276 |issue= 18 |pages= 14537-40 |year= 2001 |pmid= 11278247 |doi= 10.1074/jbc.C000881200 }}
*{{cite journal  | author=Matsuzawa SI, Reed JC |title=Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses. |journal=Mol. Cell |volume=7 |issue= 5 |pages= 915-26 |year= 2001 |pmid= 11389839 |doi=  }}
*{{cite journal  | author=Jiang J, Ballinger CA, Wu Y, ''et al.'' |title=CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation. |journal=J. Biol. Chem. |volume=276 |issue= 46 |pages= 42938-44 |year= 2001 |pmid= 11557750 |doi= 10.1074/jbc.M101968200 }}
*{{cite journal  | author=Chen A, Kleiman FE, Manley JL, ''et al.'' |title=Autoubiquitination of the BRCA1*BARD1 RING ubiquitin ligase. |journal=J. Biol. Chem. |volume=277 |issue= 24 |pages= 22085-92 |year= 2002 |pmid= 11927591 |doi= 10.1074/jbc.M201252200 }}
*{{cite journal  | author=Badciong JC, Haas AL |title=MdmX is a RING finger ubiquitin ligase capable of synergistically enhancing Mdm2 ubiquitination. |journal=J. Biol. Chem. |volume=277 |issue= 51 |pages= 49668-75 |year= 2003 |pmid= 12393902 |doi= 10.1074/jbc.M208593200 }}
*{{cite journal  | author=Kentsis A, Gordon RE, Borden KL |title=Control of biochemical reactions through supramolecular RING domain self-assembly. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 24 |pages= 15404-9 |year= 2003 |pmid= 12438698 |doi= 10.1073/pnas.202608799 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Gehrke SG, Riedel HD, Herrmann T, ''et al.'' |title=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. |journal=Blood |volume=101 |issue= 8 |pages= 3288-93 |year= 2003 |pmid= 12480712 |doi= 10.1182/blood-2002-07-2192 }}
*{{cite journal  | author=Mallery DL, Vandenberg CJ, Hiom K |title=Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains. |journal=EMBO J. |volume=21 |issue= 24 |pages= 6755-62 |year= 2004 |pmid= 12485996 |doi=  }}
*{{cite journal  | author=Takeyama K, Aguiar RC, Gu L, ''et al.'' |title=The BAL-binding protein BBAP and related Deltex family members exhibit ubiquitin-protein isopeptide ligase activity. |journal=J. Biol. Chem. |volume=278 |issue= 24 |pages= 21930-7 |year= 2003 |pmid= 12670957 |doi= 10.1074/jbc.M301157200 }}
}}
{{refend}}


{{protein-stub}}
UBE2D1 has been shown to [[Protein-protein interaction|interact]] with:
{{WikiDoc Sources}}
* [[BARD1]],<ref name = pmid12485996>{{cite journal | vauthors = Mallery DL, Vandenberg CJ, Hiom K | title = Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains | journal = EMBO J. | volume = 21 | issue = 24 | pages = 6755–62 | date = Dec 2002 | pmid = 12485996 | pmc = 139111 | doi =  10.1093/emboj/cdf691}}</ref><ref name = pmid12438698>{{cite journal | vauthors = Kentsis A, Gordon RE, Borden KL | title = Control of biochemical reactions through supramolecular RING domain self-assembly | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 99 | issue = 24 | pages = 15404–9 | date = November 2002 | pmid = 12438698 | pmc = 137729 | doi = 10.1073/pnas.202608799 }}</ref><ref name = pmid11927591>{{cite journal | vauthors = Chen A, Kleiman FE, Manley JL, Ouchi T, Pan ZQ | title = Autoubiquitination of the BRCA1*BARD1 RING ubiquitin ligase | journal = J. Biol. Chem. | volume = 277 | issue = 24 | pages = 22085–92 | date = June 2002 | pmid = 11927591 | doi = 10.1074/jbc.M201252200 }}</ref><ref name = pmid14636569>{{cite journal | vauthors = Dong Y, Hakimi MA, Chen X, Kumaraswamy E, Cooch NS, Godwin AK, Shiekhattar R | title = Regulation of BRCC, a holoenzyme complex containing BRCA1 and BRCA2, by a signalosome-like subunit and its role in DNA repair | journal = Mol. Cell | volume = 12 | issue = 5 | pages = 1087–99 | date = November 2003 | pmid = 14636569 | doi =  10.1016/s1097-2765(03)00424-6}}</ref><ref name = pmid15184379>{{cite journal | vauthors = Sato K, Hayami R, Wu W, Nishikawa T, Nishikawa H, Okuda Y, Ogata H, Fukuda M, Ohta T | title = Nucleophosmin/B23 is a candidate substrate for the BRCA1-BARD1 ubiquitin ligase | journal = J. Biol. Chem. | volume = 279 | issue = 30 | pages = 30919–22 | date = July 2004 | pmid = 15184379 | doi = 10.1074/jbc.C400169200 }}</ref><ref name = pmid12890688>{{cite journal | vauthors = Wu-Baer F, Lagrazon K, Yuan W, Baer R | title = The BRCA1/BARD1 heterodimer assembles polyubiquitin chains through an unconventional linkage involving lysine residue K6 of ubiquitin | journal = J. Biol. Chem. | volume = 278 | issue = 37 | pages = 34743–6 | date = September 2003 | pmid = 12890688 | doi = 10.1074/jbc.C300249200 }}</ref><ref name = pmid12887909>{{cite journal | vauthors = Vandenberg CJ, Gergely F, Ong CY, Pace P, Mallery DL, Hiom K, Patel KJ | title = BRCA1-independent ubiquitination of FANCD2 | journal = Mol. Cell | volume = 12 | issue = 1 | pages = 247–54 | date = July 2003 | pmid = 12887909 | doi =  10.1016/s1097-2765(03)00281-8}}</ref><ref name = pmid11278247>{{cite journal | vauthors = Hashizume R, Fukuda M, Maeda I, Nishikawa H, Oyake D, Yabuki Y, Ogata H, Ohta T | title = The RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutation | journal = J. Biol. Chem. | volume = 276 | issue = 18 | pages = 14537–40 | date = May 2001 | pmid = 11278247 | doi = 10.1074/jbc.C000881200 }}</ref>
* [[BRCA1]],<ref name = pmid12485996/><ref name = pmid12438698/><ref name = pmid11927591/><ref name = pmid14636569/><ref name = pmid15184379/><ref name = pmid12890688/><ref name = pmid12887909/><ref name = pmid11278247/><ref name = pmid12732733>{{cite journal | vauthors = Brzovic PS, Keeffe JR, Nishikawa H, Miyamoto K, Fox D, Fukuda M, Ohta T, Klevit R | title = Binding and recognition in the assembly of an active BRCA1/BARD1 ubiquitin-ligase complex | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 100 | issue = 10 | pages = 5646–51 | date = May 2003 | pmid = 12732733 | pmc = 156255 | doi = 10.1073/pnas.0836054100 }}</ref><ref name = pmid14638690>{{cite journal | vauthors = Nishikawa H, Ooka S, Sato K, Arima K, Okamoto J, Klevit RE, Fukuda M, Ohta T | title = Mass spectrometric and mutational analyses reveal Lys-6-linked polyubiquitin chains catalyzed by BRCA1-BARD1 ubiquitin ligase | journal = J. Biol. Chem. | volume = 279 | issue = 6 | pages = 3916–24 | date = February 2004 | pmid = 14638690 | doi = 10.1074/jbc.M308540200 }}</ref> and
* [[UBE3A]].<ref name = pmid8576257>{{cite journal | vauthors = Nuber U, Schwarz S, Kaiser P, Schneider R, Scheffner M | title = Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 (E2-F1) and characterization of their interaction with E6-AP and RSP5 | journal = J. Biol. Chem. | volume = 271 | issue = 5 | pages = 2795–800 | date = February 1996 | pmid = 8576257 | doi =  10.1074/jbc.271.5.2795}}</ref><ref name = pmid10066826>{{cite journal | vauthors = Nuber U, Scheffner M | title = Identification of determinants in E2 ubiquitin-conjugating enzymes required for hect E3 ubiquitin-protein ligase interaction | journal = J. Biol. Chem. | volume = 274 | issue = 11 | pages = 7576–82 | date = March 1999 | pmid = 10066826 | doi =  10.1074/jbc.274.11.7576}}</ref>
 
== References ==
{{Reflist}}
 
== Further reading ==
{{Refbegin | 2}}
* {{cite journal | vauthors = Scheffner M, Huibregtse JM, Howley PM | title = Identification of a human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53 | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 91 | issue = 19 | pages = 8797–801 | year = 1994 | pmid = 8090726 | pmc = 44693 | doi = 10.1073/pnas.91.19.8797 }}
* {{cite journal | vauthors = Bonaldo MF, Lennon G, Soares MB | title = Normalization and subtraction: two approaches to facilitate gene discovery | journal = Genome Res. | volume = 6 | issue = 9 | pages = 791–806 | year = 1997 | pmid = 8889548 | doi = 10.1101/gr.6.9.791 }}
* {{cite journal | vauthors = Hatakeyama S, Jensen JP, Weissman AM | title = Subcellular localization and ubiquitin-conjugating enzyme (E2) interactions of mammalian HECT family ubiquitin protein ligases | journal = J. Biol. Chem. | volume = 272 | issue = 24 | pages = 15085–92 | year = 1997 | pmid = 9182527 | doi = 10.1074/jbc.272.24.15085 }}
* {{cite journal | vauthors = Gutierrez JA, Yu J, Rivera S, Wessling-Resnick M | title = Functional Expression Cloning and Characterization of SFT, a Stimulator of Fe Transport | journal = J. Cell Biol. | volume = 139 | issue = 4 | pages = 895–905 | year = 1997 | pmid = 9362508 | pmc = 2139974 | doi = 10.1083/jcb.139.4.895 }}
* {{cite journal | vauthors = Gutierrez JA, Yu J, Wessling-Resnick M | title = Characterization and chromosomal mapping of the human gene for SFT, a stimulator of Fe transport | journal = Biochem. Biophys. Res. Commun. | volume = 253 | issue = 3 | pages = 739–42 | year = 1999 | pmid = 9918797 | doi = 10.1006/bbrc.1998.9836 }}
* {{cite journal | vauthors = Nuber U, Scheffner M | title = Identification of determinants in E2 ubiquitin-conjugating enzymes required for hect E3 ubiquitin-protein ligase interaction | journal = J. Biol. Chem. | volume = 274 | issue = 11 | pages = 7576–82 | year = 1999 | pmid = 10066826 | doi = 10.1074/jbc.274.11.7576 }}
* {{cite journal | vauthors = Kamura T, Sato S, Iwai K, Czyzyk-Krzeska M, Conaway RC, Conaway JW | title = Activation of HIF1α ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complex | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 97 | issue = 19 | pages = 10430–5 | year = 2000 | pmid = 10973499 | pmc = 27041 | doi = 10.1073/pnas.190332597 }}
* {{cite journal | vauthors = Pringa E, Martinez-Noel G, Muller U, Harbers K | title = Interaction of the ring finger-related U-box motif of a nuclear dot protein with ubiquitin-conjugating enzymes | journal = J. Biol. Chem. | volume = 276 | issue = 22 | pages = 19617–23 | year = 2001 | pmid = 11274149 | doi = 10.1074/jbc.M100192200 }}
* {{cite journal | vauthors = Hashizume R, Fukuda M, Maeda I, Nishikawa H, Oyake D, Yabuki Y, Ogata H, Ohta T | title = The RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutation | journal = J. Biol. Chem. | volume = 276 | issue = 18 | pages = 14537–40 | year = 2001 | pmid = 11278247 | doi = 10.1074/jbc.C000881200 }}
* {{cite journal | vauthors = Matsuzawa SI, Reed JC | title = Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses | journal = Mol. Cell | volume = 7 | issue = 5 | pages = 915–26 | year = 2001 | pmid = 11389839 | doi = 10.1016/S1097-2765(01)00242-8 }}
* {{cite journal | vauthors = Jiang J, Ballinger CA, Wu Y, Dai Q, Cyr DM, Höhfeld J, Patterson C | title = CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation | journal = J. Biol. Chem. | volume = 276 | issue = 46 | pages = 42938–44 | year = 2001 | pmid = 11557750 | doi = 10.1074/jbc.M101968200 }}
* {{cite journal | vauthors = Chen A, Kleiman FE, Manley JL, Ouchi T, Pan ZQ | title = Autoubiquitination of the BRCA1*BARD1 RING ubiquitin ligase | journal = J. Biol. Chem. | volume = 277 | issue = 24 | pages = 22085–92 | year = 2002 | pmid = 11927591 | doi = 10.1074/jbc.M201252200 }}
* {{cite journal | vauthors = Badciong JC, Haas AL | title = MdmX is a RING finger ubiquitin ligase capable of synergistically enhancing Mdm2 ubiquitination | journal = J. Biol. Chem. | volume = 277 | issue = 51 | pages = 49668–75 | year = 2003 | pmid = 12393902 | doi = 10.1074/jbc.M208593200 }}
* {{cite journal | vauthors = Kentsis A, Gordon RE, Borden KL | title = Control of biochemical reactions through supramolecular RING domain self-assembly | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 99 | issue = 24 | pages = 15404–9 | year = 2003 | pmid = 12438698 | pmc = 137729 | doi = 10.1073/pnas.202608799 }}
* {{cite journal | vauthors = Gehrke SG, Riedel HD, Herrmann T, Hadaschik B, Bents K, Veltkamp C, Stremmel W | title = 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 | journal = Blood | volume = 101 | issue = 8 | pages = 3288–93 | year = 2003 | pmid = 12480712 | doi = 10.1182/blood-2002-07-2192 }}
* {{cite journal | vauthors = Mallery DL, Vandenberg CJ, Hiom K | title = Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains | journal = EMBO J. | volume = 21 | issue = 24 | pages = 6755–62 | year = 2004 | pmid = 12485996 | pmc = 139111 | doi = 10.1093/emboj/cdf691 }}
* {{cite journal | vauthors = Takeyama K, Aguiar RC, Gu L, He C, Freeman GJ, Kutok JL, Aster JC, Shipp MA | title = The BAL-binding protein BBAP and related Deltex family members exhibit ubiquitin-protein isopeptide ligase activity | journal = J. Biol. Chem. | volume = 278 | issue = 24 | pages = 21930–7 | year = 2003 | pmid = 12670957 | doi = 10.1074/jbc.M301157200 }}
{{Refend}}
 
{{PDB Gallery|geneid=7321}}
{{Ubiquitin-conjugating enzymes}}

Latest revision as of 09:31, 17 September 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Ubiquitin-conjugating enzyme E2 D1 is a protein that in humans is encoded by the UBE2D1 gene.[1][2][3]

Function

The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. This enzyme is closely related to a stimulator of iron transport (SFT), and is up-regulated in hereditary hemochromatosis. It also functions in the ubiquitination of the tumor-suppressor protein p53 and the hypoxia-inducible transcription factor HIF1alpha by interacting with the E1 ubiquitin-activating enzyme and the E3 ubiquitin-protein ligases.[3]

Interactions

UBE2D1 has been shown to interact with:

References

  1. ↑ Robinson PA, Leek JP, Ardley HC, Thompson J, Rose SA, Markham AF (March 1999). "Assignment of UBE2D1 to human chromosome bands 10q11.2→q21 by in situ hybridization". Cytogenet Cell Genet. 83 (3–4): 247–8. doi:10.1159/000015195. PMID 10072594.
  2. ↑ Jensen JP, Bates PW, Yang M, Vierstra RD, Weissman AM (January 1996). "Identification of a family of closely related human ubiquitin conjugating enzymes". J Biol Chem. 270 (51): 30408–14. doi:10.1074/jbc.270.51.30408. PMID 8530467.
  3. ↑ 3.0 3.1 "Entrez Gene: UBE2D1 ubiquitin-conjugating enzyme E2D 1 (UBC4/5 homolog, yeast)".
  4. ↑ 4.0 4.1 Mallery DL, Vandenberg CJ, Hiom K (Dec 2002). "Activation of the E3 ligase function of the BRCA1/BARD1 complex by polyubiquitin chains". EMBO J. 21 (24): 6755–62. doi:10.1093/emboj/cdf691. PMC 139111. PMID 12485996.
  5. ↑ 5.0 5.1 Kentsis A, Gordon RE, Borden KL (November 2002). "Control of biochemical reactions through supramolecular RING domain self-assembly". Proc. Natl. Acad. Sci. U.S.A. 99 (24): 15404–9. doi:10.1073/pnas.202608799. PMC 137729. PMID 12438698.
  6. ↑ 6.0 6.1 Chen A, Kleiman FE, Manley JL, Ouchi T, Pan ZQ (June 2002). "Autoubiquitination of the BRCA1*BARD1 RING ubiquitin ligase". J. Biol. Chem. 277 (24): 22085–92. doi:10.1074/jbc.M201252200. PMID 11927591.
  7. ↑ 7.0 7.1 Dong Y, Hakimi MA, Chen X, Kumaraswamy E, Cooch NS, Godwin AK, Shiekhattar R (November 2003). "Regulation of BRCC, a holoenzyme complex containing BRCA1 and BRCA2, by a signalosome-like subunit and its role in DNA repair". Mol. Cell. 12 (5): 1087–99. doi:10.1016/s1097-2765(03)00424-6. PMID 14636569.
  8. ↑ 8.0 8.1 Sato K, Hayami R, Wu W, Nishikawa T, Nishikawa H, Okuda Y, Ogata H, Fukuda M, Ohta T (July 2004). "Nucleophosmin/B23 is a candidate substrate for the BRCA1-BARD1 ubiquitin ligase". J. Biol. Chem. 279 (30): 30919–22. doi:10.1074/jbc.C400169200. PMID 15184379.
  9. ↑ 9.0 9.1 Wu-Baer F, Lagrazon K, Yuan W, Baer R (September 2003). "The BRCA1/BARD1 heterodimer assembles polyubiquitin chains through an unconventional linkage involving lysine residue K6 of ubiquitin". J. Biol. Chem. 278 (37): 34743–6. doi:10.1074/jbc.C300249200. PMID 12890688.
  10. ↑ 10.0 10.1 Vandenberg CJ, Gergely F, Ong CY, Pace P, Mallery DL, Hiom K, Patel KJ (July 2003). "BRCA1-independent ubiquitination of FANCD2". Mol. Cell. 12 (1): 247–54. doi:10.1016/s1097-2765(03)00281-8. PMID 12887909.
  11. ↑ 11.0 11.1 Hashizume R, Fukuda M, Maeda I, Nishikawa H, Oyake D, Yabuki Y, Ogata H, Ohta T (May 2001). "The RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutation". J. Biol. Chem. 276 (18): 14537–40. doi:10.1074/jbc.C000881200. PMID 11278247.
  12. ↑ Brzovic PS, Keeffe JR, Nishikawa H, Miyamoto K, Fox D, Fukuda M, Ohta T, Klevit R (May 2003). "Binding and recognition in the assembly of an active BRCA1/BARD1 ubiquitin-ligase complex". Proc. Natl. Acad. Sci. U.S.A. 100 (10): 5646–51. doi:10.1073/pnas.0836054100. PMC 156255. PMID 12732733.
  13. ↑ Nishikawa H, Ooka S, Sato K, Arima K, Okamoto J, Klevit RE, Fukuda M, Ohta T (February 2004). "Mass spectrometric and mutational analyses reveal Lys-6-linked polyubiquitin chains catalyzed by BRCA1-BARD1 ubiquitin ligase". J. Biol. Chem. 279 (6): 3916–24. doi:10.1074/jbc.M308540200. PMID 14638690.
  14. ↑ Nuber U, Schwarz S, Kaiser P, Schneider R, Scheffner M (February 1996). "Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 (E2-F1) and characterization of their interaction with E6-AP and RSP5". J. Biol. Chem. 271 (5): 2795–800. doi:10.1074/jbc.271.5.2795. PMID 8576257.
  15. ↑ Nuber U, Scheffner M (March 1999). "Identification of determinants in E2 ubiquitin-conjugating enzymes required for hect E3 ubiquitin-protein ligase interaction". J. Biol. Chem. 274 (11): 7576–82. doi:10.1074/jbc.274.11.7576. PMID 10066826.

Further reading

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