UBE2D3

From Wikipedia, the free encyclopedia

Ubiquitin-conjugating enzyme E2D 3

PDB rendering based on 1ur6.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1X23, 2FUH, 3L1Z, 3RPG, 3UGB

Identifiers

Symbols

UBE2D3; E2(17)KB3; UBC4/5; UBCH5C

External IDs

OMIM: 602963 MGI: 1913355 HomoloGene: 123914 GeneCards: UBE2D3 Gene

EC number

6.3.2.19

Gene Ontology
Molecular function	• ubiquitin-protein ligase activity • protein binding • ATP binding
Cellular component	• nucleoplasm • cytosol • plasma membrane • endosome membrane
Biological process	• negative regulation of transcription from RNA polymerase II promoter • protein polyubiquitination • toll-like receptor signaling pathway • MyD88-independent toll-like receptor signaling pathway • DNA repair • transcription, DNA-dependent • transcription initiation from RNA polymerase II promoter • cellular protein modification process • ubiquitin-dependent protein catabolic process • protein monoubiquitination • apoptotic process • transforming growth factor beta receptor signaling pathway • gene expression • protein ubiquitination • BMP signaling pathway • negative regulation of type I interferon production • cellular response to stress • toll-like receptor 3 signaling pathway • toll-like receptor 4 signaling pathway • TRIF-dependent toll-like receptor signaling pathway • proteasomal ubiquitin-dependent protein catabolic process • innate immune response • regulation of transcription from RNA polymerase II promoter in response to hypoxia • protein K48-linked ubiquitination • protein K11-linked ubiquitination • cellular response to hypoxia
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 4:
103.72 – 103.79 Mb

Chr 3:
135.44 – 135.47 Mb

PubMed search

Ubiquitin-conjugating enzyme E2 D3 is a protein that in humans is encoded by the UBE2D3 gene.^[1]^[2]

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. Multiple spliced transcript variants have been found for this gene, but the full-length nature of some variants has not been determined.^[2]

Interactions

UBE2D3 has been shown to interact with NEDD4.^[3]^[4]

References

↑ Jensen JP, Bates PW, Yang M, Vierstra RD, Weissman AM (Jan 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.
↑ 2.0 2.1 "Entrez Gene: UBE2D3 ubiquitin-conjugating enzyme E2D 3 (UBC4/5 homolog, yeast)".
↑ 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 Cells (ENGLAND) 3 (11): 751–63. doi:10.1046/j.1365-2443.1998.00227.x. ISSN 1356-9597. PMID 9990509. Cite uses deprecated parameters (help)
↑ Wang, Xinjiang; Shi Yuji, Wang Junru, Huang Guochang, Jiang Xuejun (Sep 2008). "Crucial role of the C-terminus of PTEN in antagonizing NEDD4-1-mediated PTEN ubiquitination and degradation". Biochem. J. (England) 414 (2): 221–9. doi:10.1042/BJ20080674. PMID 18498243. Cite uses deprecated parameters (help)

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. doi:10.1073/pnas.91.19.8797. PMC 44693. PMID 8090726.
Rogakou EP, Pilch DR, Orr AH, et al. (1998). "DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139.". J. Biol. Chem. 273 (10): 5858–68. doi:10.1074/jbc.273.10.5858. PMID 9488723.
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. doi:10.1046/j.1365-2443.1998.00227.x. 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. doi:10.1074/jbc.274.21.14823. PMID 10329681.
Orian A, Gonen H, Bercovich B, et al. (2000). "SCF(beta)(-TrCP) ubiquitin ligase-mediated processing of NF-kappaB p105 requires phosphorylation of its C-terminus by IkappaB kinase.". EMBO J. 19 (11): 2580–91. doi:10.1093/emboj/19.11.2580. PMC 212749. PMID 10835356.
Coleman CS, Pegg AE (2001). "Polyamine analogues inhibit the ubiquitination of spermidine/spermine N1-acetyltransferase and prevent its targeting to the proteasome for degradation.". Biochem. J. 358 (Pt 1): 137–45. doi:10.1042/0264-6021:3580137. PMC 1222041. PMID 11485561.
Chen A, Kleiman FE, Manley JL, et al. (2002). "Autoubiquitination of the BRCA1*BARD1 RING ubiquitin ligase.". J. Biol. Chem. 277 (24): 22085–92. doi:10.1074/jbc.M201252200. PMID 11927591.
Obin M, Lee BY, Meinke G, et al. (2003). "Ubiquitylation of the transducin betagamma subunit complex. Regulation by phosducin.". J. Biol. Chem. 277 (46): 44566–75. doi:10.1074/jbc.M205308200. PMID 12215439.
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. PMC 139241. 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.
Brzovic PS, Keeffe JR, Nishikawa H, et al. (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.
Tang ED, Wang CY, Xiong Y, Guan KL (2003). "A role for NF-kappaB essential modifier/IkappaB kinase-gamma (NEMO/IKKgamma) ubiquitination in the activation of the IkappaB kinase complex by tumor necrosis factor-alpha.". J. Biol. Chem. 278 (39): 37297–305. doi:10.1074/jbc.M303389200. PMID 12867425.
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. PMC 2394340. PMID 14562029.
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. doi:10.1016/S0888-7543(03)00235-0. 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.
Saville MK, Sparks A, Xirodimas DP, et al. (2004). "Regulation of p53 by the ubiquitin-conjugating enzymes UbcH5B/C in vivo.". J. Biol. Chem. 279 (40): 42169–81. doi:10.1074/jbc.M403362200. PMID 15280377.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.

PDB gallery

1ur6: NMR BASED STRUCTURAL MODEL OF THE UBCH5B-CNOT4 COMPLEX

1w4u: NMR SOLUTION STRUCTURE OF THE UBIQUITIN CONJUGATING ENZYME UBCH5B

1x23: Crystal structure of ubch5c

1z2u: The 1.1A crystallographic structure of ubiquitin-conjugating enzyme (ubc-2) from Caenorhabditis elegans: functional and evolutionary significance

2c4o: CRYSTAL STRUCTURE OF HUMAN UBIQUITIN-CONJUGATING ENZYME UBCH5B

2esk: Human Ubiquitin-Conjugating Enzyme (E2) UbcH5b, wild-type

2eso: Human Ubiquitin-Conjugating Enzyme (E2) UbcH5b mutant Ile37Ala

2esp: Human ubiquitin-conjugating enzyme (E2) UbcH5b mutant Ile88Ala

2esq: Human Ubiquitin-Conjugating Enzyme (E2) UbcH5b mutant Ser94Gly

2fuh: Solution Structure of the UbcH5c/Ub Non-covalent Complex

Posttranslational modification

Chaperones/
protein folding

Heat shock proteins/ Chaperonins	Hsp10/GroES Early pregnancy factor Hsp27 Hsp47 HSP60/GroEL Hsp40/DnaJ A1 A2 A3 B1 B2 B11 B4 B6 B9 C1 C3 C5 C6 C7 C10 C11 C13 C14 C19 Hsp70 1A 1B 1L 2 4 4L 5 6 7 8 9 12A 14 Hsp90 α₁ α₂ β ER TRAP1

Other	Alpha crystallin Clusterin Survival of motor neuron SMN1 SMN2

Protein targeting

Signal peptide Mitochondrial targeting signal

Ubiquitin

E1 Ubiquitin-activating enzyme
- UBA1
- UBA2
- UBA3
- UBA5
- UBA6
- UBA7
- ATG7
- NAE1
- SAE1

E2 Ubiquitin-conjugating enzyme
- A
- B
- C
- D1
- D2
- D3
- E1
- E2
- E3
- G1
- G2
- H
- I
- J1
- J2
- K
- L1
- L2
- L3
- L4
- L6
- M
- N
- O
- Q1
- Q2
- R1 (CDC34)
- R2
- S
- V1
- V2
- Z

E3 Ubiquitin ligase
- VHL
- Cullin
- CBL
- MDM2
- FANCL
- UBR1

ATG3
BIRC6
UFC1

Other

Ubiquitin-like modifiers
- SUMO protein
- ISG15
- URM1
- NEDD8
- FAT10
- ATG8
- ATG12
- FUB1
- MUB
- UFM1
- UBL5

See also: posttranslational modification disorders
B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)

This article is issued from Wikipedia. The text is available under the Creative Commons Attribution/Share Alike; additional terms may apply for the media files.

UBE2D3

Interactions

References

Further reading