関: ubiquitin-conjugating enzyme E2

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any of several complex proteins that are produced by cells and act as catalysts in specific biochemical reactions

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/01/23 02:25:11」(JST)

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Ubiquitin-conjugating enzymes, also known as E2 enzymes and more rarely as ubiquitin-carrier enzymes, perform the second step in the ubiquitination reaction that targets a protein for degradation via the proteasome.The ubiquitination process covalently attaches ubiquitin, a short protein of 76 amino acids, to a lysine residue on the target protein. Once a protein has been tagged with one ubiquitin molecule, additional rounds of ubiquitination form a polyubiquitin chain that is recognized by the proteasome's 19S regulatory particle, triggering the ATP-dependent unfolding of the target protein that allows passage into the proteasome's 20S core particle, where proteases degrade the target into short peptide fragments for recycling by the cell.

Relationships

A ubiquitin-activating enzyme or E1 first activates the ubiquitin by covalently attaching the molecule to its active site cysteine residue. The activated ubiquitin is then transferred to an E2 cysteine. Once conjugated to ubiquitin, the E2 molecule binds one of several ubiquitin ligases or E3s via a structurally conserved binding region. The E3 molecule is responsible for binding the target protein substrate and transferring the ubiquitin from the E2 cysteine to a lysine residue on the target protein.^[1]

Schematic diagram of the ubiquitylation system.

A particular cell usually contains only a few types of E1 molecule, a greater diversity of E2s, and a very large variety of E3s. The E3 molecules responsible for substrate identification and binding are thus the mechanisms of substrate specificity in proteasomal degradation. Each type of E2 can associate with many E3s.^[2]

Isozymes

The following human genes encode ubiquitin-conjugating enzymes:

UBE2A
UBE2B
UBE2C
UBE2D1, UBE2D2, UBE2D3, UBE2D4 (the latter putative)
UBE2E1, UBE2E2, UBE2E3
UBE2F (putative)
UBE2G1, UBE2G2
UBE2H
UBE2I
UBE2J1, UBE2J2
UBE2K
UBE2L3, UBE2L6; (UBE2L1, UBE2L2, UBE2L4 are pseudogenes)
UBE2M
UBE2N
UBE2O
UBE2Q1, UBE2Q2
UBE2R1 (CDC34), UBE2R2
UBE2S
UBE2T (putative)
UBE2U (putative)
UBE2V1, UBE2V2
UBE2W (putative)
UBE2Z
ATG3
BIRC6
UFC1

References

^ Nandi D, Tahiliani P, Kumar A, Chandu D (2006). "The ubiquitin-proteasome system". Journal of biosciences 31 (1): 137–55. doi:10.1007/BF02705243. PMID 16595883.
^ Risseeuw EP, Daskalchuk TE, Banks TW, Liu E, Cotelesage J, Hellmann H, Estelle M, Somers DE, Crosby WL (2003). "Protein interaction analysis of SCF ubiquitin E3 ligase subunits from Arabidopsis". The Plant journal : for cell and molecular biology 34 (6): 753–67. doi:10.1046/j.1365-313X.2003.01768.x. PMID 12795696.

External links

Eukaryotic Linear Motif resource motif class MOD_SUMO
Ubiquitin-Conjugating Enzymes at the US National Library of Medicine Medical Subject Headings (MeSH)

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English Journal

Role of a non-canonical surface of Rad6 in ubiquitin conjugating activity.

Kumar P1, Magala P2, Geiger-Schuller KR3, Majumdar A4, Tolman JR2, Wolberger C5.
Nucleic acids research.Nucleic Acids Res.2015 Aug 18. pii: gkv845. [Epub ahead of print]
Rad6 is a yeast E2 ubiquitin conjugating enzyme that monoubiquitinates histone H2B in conjunction with the E3, Bre1, but can non-specifically modify histones on its own. We determined the crystal structure of a Rad6∼Ub thioester mimic, which revealed a network of interactions in the crystal in whi
PMID 26286193

Rad18 and Rnf8 facilitate homologous recombination by two distinct mechanisms, promoting Rad51 focus formation and suppressing the toxic effect of nonhomologous end joining.

Kobayashi S1, Kasaishi Y1, Nakada S2, Takagi T3, Era S1, Motegi A1, Chiu RK4, Takeda S1, Hirota K5.
Oncogene.Oncogene.2015 Aug 13;34(33):4403-11. doi: 10.1038/onc.2014.371. Epub 2014 Nov 24.
The E2 ubiquitin conjugating enzyme Ubc13 and the E3 ubiquitin ligases Rad18 and Rnf8 promote homologous recombination (HR)-mediated double-strand break (DSB) repair by enhancing polymerization of the Rad51 recombinase at γ-ray-induced DSB sites. To analyze functional interactions between the three
PMID 25417706

A Ubl/ubiquitin switch in the activation of Parkin.

Sauvé V1, Lilov A1, Seirafi M1, Vranas M2, Rasool S3, Kozlov G1, Sprules T4, Wang J5, Trempe JF6, Gehring K7.
The EMBO journal.EMBO J.2015 Aug 7. pii: e201592237. [Epub ahead of print]
Mutations in Parkin and PINK1 cause an inherited early-onset form of Parkinson's disease. The two proteins function together in a mitochondrial quality control pathway whereby PINK1 accumulates on damaged mitochondria and activates Parkin to induce mitophagy. How PINK1 kinase activity releases the a
PMID 26254305

Japanese Journal

NBS1 Recruits RAD18 via a RAD6-like Domain and Regulates Pol η-Dependent Translesion DNA Synthesis.

Yanagihara Hiromi,Kobayashi Junya,Tateishi Satoshi,Kato Akihiro,Matsuura Shinya,Tauchi Hiroshi,Yamada Kouichi,Takezawa Jun,Sugasawa Kaoru,Masutani Chikahide,Hanaoka Fumio,Weemaes Corry M,Mori Toshio,Zou Lee,Komatsu Kenshi
Molecular cell 43(5), 788-797, 2011-09-02
… While the ubiquitin-conjugating enzyme RAD6 and ubiquitin ligase RAD18 are known to monoubiquitinate PCNA, how they are regulated by DNA damage is not fully understood. …
NAID 120003338825

Cadmium toxicity is caused by accumulation of p53 through the down-regulation of Ube2d family genes in vitro and in vivo

TOKUMOTO Maki,FUJIWARA Yasuyuki,SHIMADA Akinori,HASEGAWA Tatsuya,SEKO Yoshiyuki,NAGASE Hisamitsu,SATOH Masahiko
Journal of toxicological sciences 36(2), 191-200, 2011-04-01
… Previously, we found that the expression of Ube2d4 gene, which is a member of the ubiquitin-conjugating enzyme Ube2d family, is suppressed by Cd in NRK-52E rat renal tubular epithelial cells. … To investigate the mechanisms of Cd-induced renal toxicity, we examined the effects of Cd on the ubiquitin-proteasome system, particularly the expression and function of Ube2d family members in the NRK-52E cells and mice. …
NAID 10028101239

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「ubiquitin-conjugating enzyme E2」

Ubiquitin-conjugating enzyme, E2
Identifiers
Symbol	UBQ-conjugat_E2
Pfam	PF00179
InterPro	IPR000608
SMART	SM00212
PROSITE	PDOC00163
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

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PMC	articles
PubMed	articles
NCBI	proteins

Ubiquitin—protein ligase
Identifiers
EC number	6.3.2.19
CAS number	74812-49-0
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
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PMC	articles
PubMed	articles
NCBI	proteins

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関: ubiquitin-conjugating enzyme

[Nandi-1] Nandi D, Tahiliani P, Kumar A, Chandu D (2006). "The ubiquitin-proteasome system". Journal of biosciences 31 (1): 137–55. doi:10.1007/BF02705243. PMID 16595883.

[Risseeuw-2] Risseeuw EP, Daskalchuk TE, Banks TW, Liu E, Cotelesage J, Hellmann H, Estelle M, Somers DE, Crosby WL (2003). "Protein interaction analysis of SCF ubiquitin E3 ligase subunits from Arabidopsis". The Plant journal : for cell and molecular biology 34 (6): 753–67. doi:10.1046/j.1365-313X.2003.01768.x. PMID 12795696.

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ubiquitin-conjugating enzyme