UBE2D2: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Ubiquitin-conjugating enzyme E2 D2''' is a [[protein]] that in humans is encoded by the ''UBE2D2'' [[gene]].<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 = The Journal of Biological Chemistry | volume = 270 | issue = 51 | pages = 30408–14 | date = Dec 1995 | pmid = 8530467 | pmc = | doi = 10.1074/jbc.270.51.30408 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: UBE2D2 ubiquitin-conjugating enzyme E2D 2 (UBC4/5 homolog, yeast)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7322| 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_UBE2D2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ur6.
| PDB = {{PDB2|1ur6}}, {{PDB2|1w4u}}, {{PDB2|1x23}}, {{PDB2|1z2u}}, {{PDB2|2c4o}}, {{PDB2|2esk}}, {{PDB2|2eso}}, {{PDB2|2esp}}, {{PDB2|2esq}}, {{PDB2|2fuh}}
| Name = Ubiquitin-conjugating enzyme E2D 2 (UBC4/5 homolog, yeast)
| HGNCid = 12475
| Symbol = UBE2D2
| AltSymbols =; UBC4/5; E2(17)KB2; PUBC1; UBC4; UBCH5B
| OMIM = 602962
| ECnumber = 
| Homologene = 86060
| MGIid = 1930715
| GeneAtlas_image1 = PBB_GE_UBE2D2_201343_at_tn.png
| GeneAtlas_image2 = PBB_GE_UBE2D2_201344_at_tn.png
| GeneAtlas_image3 = PBB_GE_UBE2D2_201345_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004842 |text = ubiquitin-protein ligase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016874 |text = ligase activity}}
| Component =
| Process = {{GNF_GO|id=GO:0006511 |text = ubiquitin-dependent protein catabolic process}} {{GNF_GO|id=GO:0006512 |text = ubiquitin cycle}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7322
    | Hs_Ensembl = ENSG00000131508
    | Hs_RefseqProtein = NP_003330
    | Hs_RefseqmRNA = NM_003339
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 5
    | Hs_GenLoc_start = 138920935
    | Hs_GenLoc_end = 138988200
    | Hs_Uniprot = 
    | Mm_EntrezGene = 56550
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = NM_019912
    | Mm_RefseqProtein = NP_064296
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Ubiquitin-conjugating enzyme E2D 2 (UBC4/5 homolog, yeast)''', also known as '''UBE2D2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: UBE2D2 ubiquitin-conjugating enzyme E2D 2 (UBC4/5 homolog, yeast)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7322| 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 functions in the ubiquitination of the tumor-suppressor protein p53, which is induced by an E3 ubiquitin-protein ligase. Two alternatively spliced transcript variants have been found for this gene and they encode distinct isoforms.<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 functions in the ubiquitination of the tumor-suppressor protein p53, which is induced by an E3 ubiquitin-protein ligase. Two alternatively spliced transcript variants have been found for this gene and they encode distinct isoforms.<ref name="entrez">{{cite web | title = Entrez Gene: UBE2D2 ubiquitin-conjugating enzyme E2D 2 (UBC4/5 homolog, yeast)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7322| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
UBE2D2 has been shown to [[Protein-protein interaction|interact]] with:
{{div col|colwidth=20em}}
* [[Baculoviral IAP repeat-containing protein 3]],<ref name = pmid18784070>{{cite journal | vauthors = Mace PD, Linke K, Feltham R, Schumacher FR, Smith CA, Vaux DL, Silke J, Day CL | title = Structures of the cIAP2 RING domain reveal conformational changes associated with ubiquitin-conjugating enzyme (E2) recruitment | journal = The Journal of Biological Chemistry | volume = 283 | issue = 46 | pages = 31633–40 | date = Nov 2008 | pmid = 18784070 | doi = 10.1074/jbc.M804753200 }}</ref>
* [[NEDD4]],<ref name = pmid9990509/><ref name = pmid9182527/>
* [[PJA1]],<ref name = pmid12036302>{{cite journal | vauthors = Yu P, Chen Y, Tagle DA, Cai T | title = PJA1, encoding a RING-H2 finger ubiquitin ligase, is a novel human X chromosome gene abundantly expressed in brain | journal = Genomics | volume = 79 | issue = 6 | pages = 869–74 | date = Jun 2002 | pmid = 12036302 | doi = 10.1006/geno.2002.6770 }}</ref>
* [[PJA2]],<ref name = pmid12036302/>  and
* [[UBE3A]].<ref name = pmid9990509>{{cite journal | vauthors = Anan T, Nagata Y, Koga H, Honda Y, Yabuki N, Miyamoto C, Kuwano A, Matsuda I, Endo F, Saya H, Nakao M | title = Human ubiquitin-protein ligase Nedd4: expression, subcellular localization and selective interaction with ubiquitin-conjugating enzymes | journal = Genes to Cells | volume = 3 | issue = 11 | pages = 751–63 | date = Nov 1998 | pmid = 9990509 | doi =  10.1046/j.1365-2443.1998.00227.x}}</ref><ref name = pmid9182527>{{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 = The Journal of Biological Chemistry | volume = 272 | issue = 24 | pages = 15085–92 | date = Jun 1997 | pmid = 9182527 | doi =  10.1074/jbc.272.24.15085}}</ref>
{{Div col end}}
 
== References ==
{{Reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Rolfe M, Beer-Romero P, Glass S, Eckstein J, Berdo I, Theodoras A, Pagano M, Draetta G | title = Reconstitution of p53-ubiquitinylation reactions from purified components: the role of human ubiquitin-conjugating enzyme UBC4 and E6-associated protein (E6AP) | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 92 | issue = 8 | pages = 3264–8 | date = Apr 1995 | pmid = 7724550 | pmc = 42146 | doi = 10.1073/pnas.92.8.3264 }}
| citations =
* {{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 = Proceedings of the National Academy of Sciences of the United States of America | volume = 91 | issue = 19 | pages = 8797–801 | date = Sep 1994 | pmid = 8090726 | pmc = 44693 | doi = 10.1073/pnas.91.19.8797 }}
*{{cite journal | author=Rolfe M, Beer-Romero P, Glass S, ''et al.'' |title=Reconstitution of p53-ubiquitinylation reactions from purified components: the role of human ubiquitin-conjugating enzyme UBC4 and E6-associated protein (E6AP). |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 8 |pages= 3264-8 |year= 1995 |pmid= 7724550 |doi= }}
* {{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 = The Journal of Biological Chemistry | volume = 272 | issue = 24 | pages = 15085–92 | date = Jun 1997 | pmid = 9182527 | doi = 10.1074/jbc.272.24.15085 }}
*{{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 | vauthors = Anan T, Nagata Y, Koga H, Honda Y, Yabuki N, Miyamoto C, Kuwano A, Matsuda I, Endo F, Saya H, Nakao M | title = Human ubiquitin-protein ligase Nedd4: expression, subcellular localization and selective interaction with ubiquitin-conjugating enzymes | journal = Genes to Cells | volume = 3 | issue = 11 | pages = 751–63 | date = Nov 1998 | pmid = 9990509 | doi = 10.1046/j.1365-2443.1998.00227.x }}
*{{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 | vauthors = Gonen H, Bercovich B, Orian A, Carrano A, Takizawa C, Yamanaka K, Pagano M, Iwai K, Ciechanover A | title = Identification of the ubiquitin carrier proteins, E2s, involved in signal-induced conjugation and subsequent degradation of IkappaBalpha | journal = The Journal of Biological Chemistry | volume = 274 | issue = 21 | pages = 14823–30 | date = May 1999 | pmid = 10329681 | doi = 10.1074/jbc.274.21.14823 }}
*{{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 | vauthors = Joazeiro CA, Wing SS, Huang H, Leverson JD, Hunter T, Liu YC | title = The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase | journal = Science | volume = 286 | issue = 5438 | pages = 309–12 | date = Oct 1999 | pmid = 10514377 | doi = 10.1126/science.286.5438.309 }}
*{{cite journal | author=Anan T, Nagata Y, Koga H, ''et al.'' |title=Human ubiquitin-protein ligase Nedd4: expression, subcellular localization and selective interaction with ubiquitin-conjugating enzymes. |journal=Genes Cells |volume=3 |issue= 11 |pages= 751-63 |year= 1999 |pmid= 9990509 |doi= }}
* {{cite journal | vauthors = Tongaonkar P, Chen L, Lambertson D, Ko B, Madura K | title = Evidence for an interaction between ubiquitin-conjugating enzymes and the 26S proteasome | journal = Molecular and Cellular Biology | volume = 20 | issue = 13 | pages = 4691–8 | date = Jul 2000 | pmid = 10848595 | pmc = 85887 | doi = 10.1128/MCB.20.13.4691-4698.2000 }}
*{{cite journal | author=Gonen H, Bercovich B, Orian A, ''et al.'' |title=Identification of the ubiquitin carrier proteins, E2s, involved in signal-induced conjugation and subsequent degradation of IkappaBalpha. |journal=J. Biol. Chem. |volume=274 |issue= 21 |pages= 14823-30 |year= 1999 |pmid= 10329681 |doi= }}
* {{cite journal | vauthors = Strack P, Caligiuri M, Pelletier M, Boisclair M, Theodoras A, Beer-Romero P, Glass S, Parsons T, Copeland RA, Auger KR, Benfield P, Brizuela L, Rolfe M | title = SCF(beta-TRCP) and phosphorylation dependent ubiquitinationof I kappa B alpha catalyzed by Ubc3 and Ubc4 | journal = Oncogene | volume = 19 | issue = 31 | pages = 3529–36 | date = Jul 2000 | pmid = 10918611 | doi = 10.1038/sj.onc.1203647 }}
*{{cite journal | author=Joazeiro CA, Wing SS, Huang H, ''et al.'' |title=The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase. |journal=Science |volume=286 |issue= 5438 |pages= 309-12 |year= 1999 |pmid= 10514377 |doi= }}
* {{cite journal | vauthors = Fang S, Ferrone M, Yang C, Jensen JP, Tiwari S, Weissman AM | title = The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 98 | issue = 25 | pages = 14422–7 | date = Dec 2001 | pmid = 11724934 | pmc = 64697 | doi = 10.1073/pnas.251401598 }}
*{{cite journal | author=Tongaonkar P, Chen L, Lambertson D, ''et al.'' |title=Evidence for an interaction between ubiquitin-conjugating enzymes and the 26S proteasome. |journal=Mol. Cell. Biol. |volume=20 |issue= 13 |pages= 4691-8 |year= 2000 |pmid= 10848595 |doi= }}
* {{cite journal | vauthors = Yu P, Chen Y, Tagle DA, Cai T | title = PJA1, encoding a RING-H2 finger ubiquitin ligase, is a novel human X chromosome gene abundantly expressed in brain | journal = Genomics | volume = 79 | issue = 6 | pages = 869–74 | date = Jun 2002 | pmid = 12036302 | doi = 10.1006/geno.2002.6770 }}
*{{cite journal | author=Strack P, Caligiuri M, Pelletier M, ''et al.'' |title=SCF(beta-TRCP) and phosphorylation dependent ubiquitinationof I kappa B alpha catalyzed by Ubc3 and Ubc4. |journal=Oncogene |volume=19 |issue= 31 |pages= 3529-36 |year= 2000 |pmid= 10918611 |doi= 10.1038/sj.onc.1203647 }}
* {{cite journal | vauthors = Xia Y, Pao GM, Chen HW, Verma IM, Hunter T | title = Enhancement of BRCA1 E3 ubiquitin ligase activity through direct interaction with the BARD1 protein | journal = The Journal of Biological Chemistry | volume = 278 | issue = 7 | pages = 5255–63 | date = Feb 2003 | pmid = 12431996 | doi = 10.1074/jbc.M204591200 }}
*{{cite journal | author=Fang S, Ferrone M, Yang C, ''et al.'' |title=The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 25 |pages= 14422-7 |year= 2002 |pmid= 11724934 |doi= 10.1073/pnas.251401598 }}
* {{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 = The Journal of Biological Chemistry | volume = 278 | issue = 24 | pages = 21930–7 | date = Jun 2003 | pmid = 12670957 | doi = 10.1074/jbc.M301157200 }}
*{{cite journal | author=Yu P, Chen Y, Tagle DA, Cai T |title=PJA1, encoding a RING-H2 finger ubiquitin ligase, is a novel human X chromosome gene abundantly expressed in brain. |journal=Genomics |volume=79 |issue= 6 |pages= 869-74 |year= 2002 |pmid= 12036302 |doi= 10.1006/geno.2002.6770 }}
* {{cite journal | vauthors = Xu L, Yang L, Moitra PK, Hashimoto K, Rallabhandi P, Kaul S, Meroni G, Jensen JP, Weissman AM, D'Arpa P | title = BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite motif protein, TRIM5delta | journal = Experimental Cell Research | volume = 288 | issue = 1 | pages = 84–93 | date = Aug 2003 | pmid = 12878161 | doi = 10.1016/S0014-4827(03)00187-3 }}
*{{cite journal | author=Xia Y, Pao GM, Chen HW, ''et al.'' |title=Enhancement of BRCA1 E3 ubiquitin ligase activity through direct interaction with the BARD1 protein. |journal=J. Biol. Chem. |volume=278 |issue= 7 |pages= 5255-63 |year= 2003 |pmid= 12431996 |doi= 10.1074/jbc.M204591200 }}
* {{cite journal | vauthors = Subramaniam V, Li H, Wong M, Kitching R, Attisano L, Wrana J, Zubovits J, Burger AM, Seth A | title = The RING-H2 protein RNF11 is overexpressed in breast cancer and is a target of Smurf2 E3 ligase | journal = British Journal of Cancer | volume = 89 | issue = 8 | pages = 1538–44 | date = Oct 2003 | pmid = 14562029 | pmc = 2394340 | doi = 10.1038/sj.bjc.6601301 }}
*{{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 | vauthors = Shimura H, Schwartz D, Gygi SP, Kosik KS | title = CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival | journal = The Journal of Biological Chemistry | volume = 279 | issue = 6 | pages = 4869–76 | date = Feb 2004 | pmid = 14612456 | doi = 10.1074/jbc.M305838200 }}
*{{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 }}
* {{cite journal | vauthors = Lehner B, Semple JI, Brown SE, Counsell D, Campbell RD, Sanderson CM | title = Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region | journal = Genomics | volume = 83 | issue = 1 | pages = 153–67 | date = Jan 2004 | pmid = 14667819 | doi = 10.1016/S0888-7543(03)00235-0 }}
*{{cite journal | author=Xu L, Yang L, Moitra PK, ''et al.'' |title=BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite motif protein, TRIM5delta. |journal=Exp. Cell Res. |volume=288 |issue= 1 |pages= 84-93 |year= 2003 |pmid= 12878161 |doi= }}
* {{cite journal | vauthors = Winkler GS, Albert TK, Dominguez C, Legtenberg YI, Boelens R, Timmers HT | title = An altered-specificity ubiquitin-conjugating enzyme/ubiquitin-protein ligase pair | journal = Journal of Molecular Biology | volume = 337 | issue = 1 | pages = 157–65 | date = Mar 2004 | pmid = 15001359 | doi = 10.1016/j.jmb.2004.01.031 }}
*{{cite journal | author=Subramaniam V, Li H, Wong M, ''et al.'' |title=The RING-H2 protein RNF11 is overexpressed in breast cancer and is a target of Smurf2 E3 ligase. |journal=Br. J. Cancer |volume=89 |issue= 8 |pages= 1538-44 |year= 2003 |pmid= 14562029 |doi= 10.1038/sj.bjc.6601301 }}
*{{cite journal | author=Shimura H, Schwartz D, Gygi SP, Kosik KS |title=CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival. |journal=J. Biol. Chem. |volume=279 |issue= 6 |pages= 4869-76 |year= 2004 |pmid= 14612456 |doi= 10.1074/jbc.M305838200 }}
*{{cite journal  | author=Lehner B, Semple JI, Brown SE, ''et al.'' |title=Analysis of a high-throughput yeast two-hybrid system and its use to predict the function of intracellular proteins encoded within the human MHC class III region. |journal=Genomics |volume=83 |issue= 1 |pages= 153-67 |year= 2004 |pmid= 14667819 |doi=  }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | author=Winkler GS, Albert TK, Dominguez C, ''et al.'' |title=An altered-specificity ubiquitin-conjugating enzyme/ubiquitin-protein ligase pair. |journal=J. Mol. Biol. |volume=337 |issue= 1 |pages= 157-65 |year= 2004 |pmid= 15001359 |doi= 10.1016/j.jmb.2004.01.031 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{PDB Gallery|geneid=7322}}
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{{Gene-5-stub}}

Latest revision as of 02:03, 27 October 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

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

Ubiquitin-conjugating enzyme E2 D2 is a protein that in humans is encoded by the UBE2D2 gene.[1][2]

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 functions in the ubiquitination of the tumor-suppressor protein p53, which is induced by an E3 ubiquitin-protein ligase. Two alternatively spliced transcript variants have been found for this gene and they encode distinct isoforms.[2]

Interactions

UBE2D2 has been shown to interact with:

References

  1. Jensen JP, Bates PW, Yang M, Vierstra RD, Weissman AM (Dec 1995). "Identification of a family of closely related human ubiquitin conjugating enzymes". The Journal of Biological Chemistry. 270 (51): 30408–14. doi:10.1074/jbc.270.51.30408. PMID 8530467.
  2. 2.0 2.1 "Entrez Gene: UBE2D2 ubiquitin-conjugating enzyme E2D 2 (UBC4/5 homolog, yeast)".
  3. Mace PD, Linke K, Feltham R, Schumacher FR, Smith CA, Vaux DL, Silke J, Day CL (Nov 2008). "Structures of the cIAP2 RING domain reveal conformational changes associated with ubiquitin-conjugating enzyme (E2) recruitment". The Journal of Biological Chemistry. 283 (46): 31633–40. doi:10.1074/jbc.M804753200. PMID 18784070.
  4. 4.0 4.1 Anan T, Nagata Y, Koga H, Honda Y, Yabuki N, Miyamoto C, Kuwano A, Matsuda I, Endo F, Saya H, Nakao M (Nov 1998). "Human ubiquitin-protein ligase Nedd4: expression, subcellular localization and selective interaction with ubiquitin-conjugating enzymes". Genes to Cells. 3 (11): 751–63. doi:10.1046/j.1365-2443.1998.00227.x. PMID 9990509.
  5. 5.0 5.1 Hatakeyama S, Jensen JP, Weissman AM (Jun 1997). "Subcellular localization and ubiquitin-conjugating enzyme (E2) interactions of mammalian HECT family ubiquitin protein ligases". The Journal of Biological Chemistry. 272 (24): 15085–92. doi:10.1074/jbc.272.24.15085. PMID 9182527.
  6. 6.0 6.1 Yu P, Chen Y, Tagle DA, Cai T (Jun 2002). "PJA1, encoding a RING-H2 finger ubiquitin ligase, is a novel human X chromosome gene abundantly expressed in brain". Genomics. 79 (6): 869–74. doi:10.1006/geno.2002.6770. PMID 12036302.

Further reading