UBE2D2

Ubiquitin-conjugating enzyme E2 D2 is a protein that in humans is encoded by the UBE2D2 gene.[5][6]

UBE2D2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1UR6, 1W4U, 2CLW, 2ESK, 2ESO, 2ESP, 2ESQ, 3A33, 3JVZ, 3JW0, 3L1Y, 3TGD, 3ZNI, 4A49, 4A4B, 4A4C, 4AUQ, 4DDG, 4LDT, 4V3K, 4V3L, 4WZ3, 5D1L, 5D1K, 5D0M, 5D0K, 5D1M, 5EDV
Identifiers
Aliases	UBE2D2, E2(17)KB2, PUBC1, UBC4, UBC4/5, UBCH4, UBCH5B, ubiquitin conjugating enzyme E2 D2
External IDs	OMIM: 602962 MGI: 1930715 HomoloGene: 2506 GeneCards: UBE2D2
EC number	2.3.2.24
Gene location (Human) Chr. Chromosome 5 (human)[1] Band 5q31.2 Start 139,526,431 bp[1] End 139,628,434 bp[1]
Gene location (Mouse) Chr. Chromosome 18 (mouse)[2] Band 18|18 B2 Start 35,771,558 bp[2] End 35,809,494 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • transferase activity • nucleotide binding • ubiquitin-protein transferase activity • GO:0001948 protein binding • ATP binding • ubiquitin conjugating enzyme activity • ubiquitin protein ligase binding Cellular component • cytosol • ubiquitin ligase complex • nucleoplasm • extracellular exosome • macromolecular complex Biological process • ubiquitin-dependent protein catabolic process • protein polyubiquitination • stimulatory C-type lectin receptor signaling pathway • TRIF-dependent toll-like receptor signaling pathway • Fc-epsilon receptor signaling pathway • protein K48-linked ubiquitination • cellular protein modification process • regulation of transcription from RNA polymerase II promoter in response to hypoxia • T cell receptor signaling pathway • protein autoubiquitination • protein ubiquitination • MyD88-independent toll-like receptor signaling pathway • protein targeting to peroxisome • protein K11-linked ubiquitination Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	7322	56550
Ensembl	ENSG00000131508	ENSMUSG00000091896
UniProt	P62837	P62838
RefSeq (mRNA)	NM_003339 NM_181838	NM_019912
RefSeq (protein)	NP_003330 NP_862821	NP_064296
Location (UCSC)	Chr 5: 139.53 – 139.63 Mb	Chr 18: 35.77 – 35.81 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[6]

Interactions

UBE2D2 has been shown to interact with:

• Baculoviral IAP repeat-containing protein 3,[7]
• NEDD4,[8][9]
• PJA1,[10]
• PJA2,[10] and
• UBE3A.[8][9]

References

1. GRCh38: Ensembl release 89: ENSG00000131508 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000091896 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. "Entrez Gene: UBE2D2 ubiquitin-conjugating enzyme E2D 2 (UBC4/5 homolog, yeast)".
7. 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.
8. 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.
9. 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.
10. 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

• Rolfe M, Beer-Romero P, Glass S, Eckstein J, Berdo I, Theodoras A, Pagano M, Draetta G (Apr 1995). "Reconstitution of p53-ubiquitinylation reactions from purified components: the role of human ubiquitin-conjugating enzyme UBC4 and E6-associated protein (E6AP)". Proceedings of the National Academy of Sciences of the United States of America. 92 (8): 3264–8. doi:10.1073/pnas.92.8.3264. PMC 42146. PMID 7724550.
• Scheffner M, Huibregtse JM, Howley PM (Sep 1994). "Identification of a human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53". Proceedings of the National Academy of Sciences of the United States of America. 91 (19): 8797–801. doi:10.1073/pnas.91.19.8797. PMC 44693. PMID 8090726.
• 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.
• 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.
• Gonen H, Bercovich B, Orian A, Carrano A, Takizawa C, Yamanaka K, Pagano M, Iwai K, Ciechanover A (May 1999). "Identification of the ubiquitin carrier proteins, E2s, involved in signal-induced conjugation and subsequent degradation of IkappaBalpha". The Journal of Biological Chemistry. 274 (21): 14823–30. doi:10.1074/jbc.274.21.14823. PMID 10329681.
• Joazeiro CA, Wing SS, Huang H, Leverson JD, Hunter T, Liu YC (Oct 1999). "The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase". Science. 286 (5438): 309–12. doi:10.1126/science.286.5438.309. PMID 10514377.
• Tongaonkar P, Chen L, Lambertson D, Ko B, Madura K (Jul 2000). "Evidence for an interaction between ubiquitin-conjugating enzymes and the 26S proteasome". Molecular and Cellular Biology. 20 (13): 4691–8. doi:10.1128/MCB.20.13.4691-4698.2000. PMC 85887. PMID 10848595.
• 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 (Jul 2000). "SCF(beta-TRCP) and phosphorylation dependent ubiquitinationof I kappa B alpha catalyzed by Ubc3 and Ubc4". Oncogene. 19 (31): 3529–36. doi:10.1038/sj.onc.1203647. PMID 10918611.
• Fang S, Ferrone M, Yang C, Jensen JP, Tiwari S, Weissman AM (Dec 2001). "The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum". Proceedings of the National Academy of Sciences of the United States of America. 98 (25): 14422–7. doi:10.1073/pnas.251401598. PMC 64697. PMID 11724934.
• 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.
• Xia Y, Pao GM, Chen HW, Verma IM, Hunter T (Feb 2003). "Enhancement of BRCA1 E3 ubiquitin ligase activity through direct interaction with the BARD1 protein". The Journal of Biological Chemistry. 278 (7): 5255–63. doi:10.1074/jbc.M204591200. PMID 12431996.
• Takeyama K, Aguiar RC, Gu L, He C, Freeman GJ, Kutok JL, Aster JC, Shipp MA (Jun 2003). "The BAL-binding protein BBAP and related Deltex family members exhibit ubiquitin-protein isopeptide ligase activity". The Journal of Biological Chemistry. 278 (24): 21930–7. doi:10.1074/jbc.M301157200. PMID 12670957.
• Xu L, Yang L, Moitra PK, Hashimoto K, Rallabhandi P, Kaul S, Meroni G, Jensen JP, Weissman AM, D'Arpa P (Aug 2003). "BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite motif protein, TRIM5delta". Experimental Cell Research. 288 (1): 84–93. doi:10.1016/S0014-4827(03)00187-3. PMID 12878161.
• Subramaniam V, Li H, Wong M, Kitching R, Attisano L, Wrana J, Zubovits J, Burger AM, Seth A (Oct 2003). "The RING-H2 protein RNF11 is overexpressed in breast cancer and is a target of Smurf2 E3 ligase". British Journal of Cancer. 89 (8): 1538–44. doi:10.1038/sj.bjc.6601301. PMC 2394340. PMID 14562029.
• Shimura H, Schwartz D, Gygi SP, Kosik KS (Feb 2004). "CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival". The Journal of Biological Chemistry. 279 (6): 4869–76. doi:10.1074/jbc.M305838200. PMID 14612456.
• Lehner B, Semple JI, Brown SE, Counsell D, Campbell RD, Sanderson CM (Jan 2004). "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". Genomics. 83 (1): 153–67. doi:10.1016/S0888-7543(03)00235-0. PMID 14667819.
• Winkler GS, Albert TK, Dominguez C, Legtenberg YI, Boelens R, Timmers HT (Mar 2004). "An altered-specificity ubiquitin-conjugating enzyme/ubiquitin-protein ligase pair". Journal of Molecular Biology. 337 (1): 157–65. doi:10.1016/j.jmb.2004.01.031. PMID 15001359.