UBE2D2

From Wikipedia, the free encyclopedia

Ubiquitin-conjugating enzyme E2D 2

PDB rendering based on 1ur6.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1UR6, 1W4U, 2C4O, 2CLW, 2ESK, 2ESO, 2ESP, 2ESQ, 3A33, 3JVZ, 3JW0, 3L1Y, 3TGD, 3ZNI, 4A49, 4A4B, 4A4C, 4AUQ, 4DDG, 4LDT

Identifiers

Symbols

UBE2D2; E2(17)KB2; PUBC1; UBC4; UBC4/5; UBCH5B

External IDs

OMIM: 602962 MGI: 1930715 HomoloGene: 2506 GeneCards: UBE2D2 Gene

EC number

6.3.2.19

Gene Ontology
Molecular function	• ubiquitin-protein ligase activity • protein binding • ATP binding
Cellular component	• nucleoplasm • cytosol
Biological process	• protein polyubiquitination • toll-like receptor signaling pathway • MyD88-independent toll-like receptor signaling pathway • cellular protein modification process • ubiquitin-dependent protein catabolic process • protein ubiquitination • cellular response to stress • toll-like receptor 3 signaling pathway • toll-like receptor 4 signaling pathway • TRIF-dependent toll-like receptor signaling pathway • innate immune response • regulation of transcription from RNA polymerase II promoter in response to hypoxia • protein K48-linked ubiquitination • cellular response to hypoxia
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 5:
138.91 – 139.01 Mb

Chr 18:
35.77 – 35.81 Mb

PubMed search

Ubiquitin-conjugating enzyme E2 D2 is a protein that in humans is encoded by the UBE2D2 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. 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 PJA1,^[3] Baculoviral IAP repeat-containing protein 3,^[4] PJA2,^[3] UBE3A^[5]^[6] and NEDD4.^[5]^[6]

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: UBE2D2 ubiquitin-conjugating enzyme E2D 2 (UBC4/5 homolog, yeast)".
↑ 3.0 3.1 Yu, Ping; Chen Yiwang, Tagle Danilo A, Cai Tao (Jun 2002). "PJA1, encoding a RING-H2 finger ubiquitin ligase, is a novel human X chromosome gene abundantly expressed in brain". Genomics (United States) 79 (6): 869–74. doi:10.1006/geno.2002.6770. ISSN 0888-7543. PMID 12036302. Cite uses deprecated parameters (help)
↑ Mace, Peter D; Linke Katrin, Feltham Rebecca, Schumacher Frances-Rose, Smith Clyde A, Vaux David L, Silke John, Day Catherine L (Nov 2008). "Structures of the cIAP2 RING domain reveal conformational changes associated with ubiquitin-conjugating enzyme (E2) recruitment". J. Biol. Chem. (United States) 283 (46): 31633–40. doi:10.1074/jbc.M804753200. ISSN 0021-9258. PMID 18784070. Cite uses deprecated parameters (help)
↑ 5.0 5.1 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 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)
↑ 6.0 6.1 Hatakeyama, S; Jensen J P, Weissman A M (Jun 1997). "Subcellular localization and ubiquitin-conjugating enzyme (E2) interactions of mammalian HECT family ubiquitin protein ligases". J. Biol. Chem. (UNITED STATES) 272 (24): 15085–92. doi:10.1074/jbc.272.24.15085. ISSN 0021-9258. PMID 9182527. Cite uses deprecated parameters (help)

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. doi:10.1073/pnas.92.8.3264. PMC 42146. 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. doi:10.1073/pnas.91.19.8797. PMC 44693. PMID 8090726.
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. doi:10.1074/jbc.272.24.15085. 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. 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.
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. doi:10.1126/science.286.5438.309. 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. doi:10.1128/MCB.20.13.4691-4698.2000. PMC 85887. 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. PMC 64697. 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. 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.
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. doi:10.1016/S0014-4827(03)00187-3. 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. PMC 2394340. 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. 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.
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.

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°)

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UBE2D2

Interactions

References

Further reading