UBE2D2

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Ubiquitin-conjugating enzyme E2D 2 (UBC4/5 homolog, yeast)
PDB rendering based on 1ur6.
Available structures: 1ur6, 1w4u, 1x23, 1z2u, 2c4o, 2esk, 2eso, 2esp, 2esq, 2fuh
Identifiers
Symbol(s) UBE2D2; UBC4/5; E2(17)KB2; PUBC1; UBC4; UBCH5B
External IDs OMIM: 602962 MGI: 1930715 HomoloGene: 86060
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 7322 56550
Ensembl ENSG00000131508 n/a
Refseq NM_003339 (mRNA)
NP_003330 (protein)		 NM_019912 (mRNA)
NP_064296 (protein)
Location Chr 5: 138.92 - 138.99 Mb n/a
Pubmed search [1] [2]

Ubiquitin-conjugating enzyme E2D 2 (UBC4/5 homolog, yeast), also known as UBE2D2, is a human gene.[1]

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.[1]

[edit] References

  1. ^ a b Entrez Gene: UBE2D2 ubiquitin-conjugating enzyme E2D 2 (UBC4/5 homolog, yeast).

[edit] Further reading

  • Rolfe M, Beer-Romero P, Glass S, et al. (1995). "Reconstitution of p53-ubiquitinylation reactions from purified components: the role of human ubiquitin-conjugating enzyme UBC4 and E6-associated protein (E6AP).". Proc. Natl. Acad. Sci. U.S.A. 92 (8): 3264-8. PMID 7724550. 
  • Scheffner M, Huibregtse JM, Howley PM (1994). "Identification of a human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53.". Proc. Natl. Acad. Sci. U.S.A. 91 (19): 8797-801. PMID 8090726. 
  • Jensen JP, Bates PW, Yang M, et al. (1996). "Identification of a family of closely related human ubiquitin conjugating enzymes.". J. Biol. Chem. 270 (51): 30408-14. PMID 8530467. 
  • Hatakeyama S, Jensen JP, Weissman AM (1997). "Subcellular localization and ubiquitin-conjugating enzyme (E2) interactions of mammalian HECT family ubiquitin protein ligases.". J. Biol. Chem. 272 (24): 15085-92. PMID 9182527. 
  • Anan T, Nagata Y, Koga H, et al. (1999). "Human ubiquitin-protein ligase Nedd4: expression, subcellular localization and selective interaction with ubiquitin-conjugating enzymes.". Genes Cells 3 (11): 751-63. PMID 9990509. 
  • Gonen H, Bercovich B, Orian A, et al. (1999). "Identification of the ubiquitin carrier proteins, E2s, involved in signal-induced conjugation and subsequent degradation of IkappaBalpha.". J. Biol. Chem. 274 (21): 14823-30. PMID 10329681. 
  • Joazeiro CA, Wing SS, Huang H, et al. (1999). "The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase.". Science 286 (5438): 309-12. PMID 10514377. 
  • Tongaonkar P, Chen L, Lambertson D, et al. (2000). "Evidence for an interaction between ubiquitin-conjugating enzymes and the 26S proteasome.". Mol. Cell. Biol. 20 (13): 4691-8. PMID 10848595. 
  • Strack P, Caligiuri M, Pelletier M, et al. (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, et al. (2002). "The tumor autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum.". Proc. Natl. Acad. Sci. U.S.A. 98 (25): 14422-7. doi:10.1073/pnas.251401598. PMID 11724934. 
  • Yu P, Chen Y, Tagle DA, Cai T (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, et al. (2003). "Enhancement of BRCA1 E3 ubiquitin ligase activity through direct interaction with the BARD1 protein.". J. Biol. Chem. 278 (7): 5255-63. doi:10.1074/jbc.M204591200. PMID 12431996. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932. 
  • Takeyama K, Aguiar RC, Gu L, et al. (2003). "The BAL-binding protein BBAP and related Deltex family members exhibit ubiquitin-protein isopeptide ligase activity.". J. Biol. Chem. 278 (24): 21930-7. doi:10.1074/jbc.M301157200. PMID 12670957. 
  • Xu L, Yang L, Moitra PK, et al. (2003). "BTBD1 and BTBD2 colocalize to cytoplasmic bodies with the RBCC/tripartite motif protein, TRIM5delta.". Exp. Cell Res. 288 (1): 84-93. PMID 12878161. 
  • Subramaniam V, Li H, Wong M, et al. (2003). "The RING-H2 protein RNF11 is overexpressed in breast cancer and is a target of Smurf2 E3 ligase.". Br. J. Cancer 89 (8): 1538-44. doi:10.1038/sj.bjc.6601301. PMID 14562029. 
  • Shimura H, Schwartz D, Gygi SP, Kosik KS (2004). "CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival.". J. Biol. Chem. 279 (6): 4869-76. doi:10.1074/jbc.M305838200. PMID 14612456. 
  • Lehner B, Semple JI, Brown SE, et al. (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. PMID 14667819. 
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40-5. doi:10.1038/ng1285. PMID 14702039. 
  • Winkler GS, Albert TK, Dominguez C, et al. (2004). "An altered-specificity ubiquitin-conjugating enzyme/ubiquitin-protein ligase pair.". J. Mol. Biol. 337 (1): 157-65. doi:10.1016/j.jmb.2004.01.031. PMID 15001359. 
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