• postreplication repair • protein K63-linked ubiquitination • regulation of DNA repair • DNA double-strand break processing • positive regulation of DNA repair • stimulatory C-type lectin receptor signaling pathway • proteolysis • cellular response to DNA damage stimulus • Fc-epsilon receptor signaling pathway • global genome nucleotide-excision repair • positive regulation of histone modification • cellular protein modification process • positive regulation of ubiquitin-protein transferase activity • protein ubiquitination • regulation of histone ubiquitination • positive regulation of I-kappaB kinase/NF-kappaB signaling • T cell receptor signaling pathway • double-strand break repair via nonhomologous end joining • nucleotide-binding oligomerization domain containing signaling pathway • histone ubiquitination • DNA repair • double-strand break repair via homologous recombination • activation of MAPK activity • JNK cascade • positive regulation of NF-kappaB transcription factor activity • ubiquitin-dependent protein catabolic process • interleukin-1-mediated signaling pathway
Sources:Amigo / QuickGO
Orthologs
Species
Human
Mouse
Entrez
7334
93765
Ensembl
ENSG00000177889
ENSMUSG00000074781
UniProt
P61088
P61089
RefSeq (mRNA)
NM_003348
NM_080560
RefSeq (protein)
NP_003339
NP_542127
Location (UCSC)
Chr 12: 93.41 – 93.44 Mb
Chr 10: 95.52 – 95.55 Mb
PubMed search
[3]
[4]
Wikidata
View/Edit Human
View/Edit Mouse
Ubiquitin-conjugating enzyme E2 N is a protein that in humans is encoded by the UBE2N gene.[5][6]
Contents
1Function
2Interactions
3References
4Further reading
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. Studies in mouse suggest that this protein plays a role in DNA postreplication repair.[6]
Interactions
UBE2N has been shown to interact with:
AURKA,[7]
HLTF,[8]
TRAF2,[9]
TRAF6,[9] and
UBE2V1.[9]
References
^ abcGRCh38: Ensembl release 89: ENSG00000177889 - Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000074781 - Ensembl, May 2017
^Yamaguchi T, Kim NS, Sekine S, Seino H, Osaka F, Yamao F, Kato S (February 1997). "Cloning and expression of cDNA encoding a human ubiquitin-conjugating enzyme similar to the Drosophila bendless gene product". J Biochem. 120 (3): 494–97. doi:10.1093/oxfordjournals.jbchem.a021440. PMID 8902611.
^Ewart-Toland A, Briassouli P, de Koning JP, Mao JH, Yuan J, Chan F, MacCarthy-Morrogh L, Ponder BA, Nagase H, Burn J, Ball S, Almeida M, Linardopoulos S, Balmain A (August 2003). "Identification of Stk6/STK15 as a candidate low-penetrance tumor-susceptibility gene in mouse and human". Nat. Genet. 34 (4): 403–12. doi:10.1038/ng1220. PMID 12881723.
^Unk I, Hajdú I, Fátyol K, Hurwitz J, Yoon JH, Prakash L, Prakash S, Haracska L (March 2008). "Human HLTF functions as a ubiquitin ligase for proliferating cell nuclear antigen polyubiquitination". Proc. Natl. Acad. Sci. U.S.A. 105 (10): 3768–73. doi:10.1073/pnas.0800563105. PMC 2268824. PMID 18316726.
^ abcDeng L, Wang C, Spencer E, Yang L, Braun A, You J, Slaughter C, Pickart C, Chen ZJ (October 2000). "Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain". Cell. 103 (2): 351–61. doi:10.1016/s0092-8674(00)00126-4. PMID 11057907.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
Hofmann RM, Pickart CM (1999). "Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair". Cell. 96 (5): 645–53. doi:10.1016/S0092-8674(00)80575-9. PMID 10089880.
Deng L, Wang C, Spencer E, Yang L, Braun A, You J, Slaughter C, Pickart C, Chen ZJ (2000). "Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain". Cell. 103 (2): 351–61. doi:10.1016/S0092-8674(00)00126-4. PMID 11057907.
Ashley C, Pastushok L, McKenna S, Ellison MJ, Xiao W (2002). "Roles of mouse UBC13 in DNA postreplication repair and Lys63-linked ubiquitination". Gene. 285 (1–2): 183–91. doi:10.1016/S0378-1119(02)00409-2. PMID 12039045.
McKenna S, Moraes T, Pastushok L, Ptak C, Xiao W, Spyracopoulos L, Ellison MJ (2003). "An NMR-based model of the ubiquitin-bound human ubiquitin conjugation complex Mms2.Ubc13. The structural basis for lysine 63 chain catalysis". J. Biol. Chem. 278 (15): 13151–8. doi:10.1074/jbc.M212353200. PMID 12569095.
Anandasabapathy N, Ford GS, Bloom D, Holness C, Paragas V, Seroogy C, Skrenta H, Hollenhorst M, Fathman CG, Soares L (2003). "GRAIL: an E3 ubiquitin ligase that inhibits cytokine gene transcription is expressed in anergic CD4+ T cells". Immunity. 18 (4): 535–47. doi:10.1016/S1074-7613(03)00084-0. PMID 12705856.
Ewart-Toland A, Briassouli P, de Koning JP, Mao JH, Yuan J, Chan F, MacCarthy-Morrogh L, Ponder BA, Nagase H, Burn J, Ball S, Almeida M, Linardopoulos S, Balmain A (2003). "Identification of Stk6/STK15 as a candidate low-penetrance tumor-susceptibility gene in mouse and human". Nat. Genet. 34 (4): 403–12. doi:10.1038/ng1220. PMID 12881723.
Bothos J, Summers MK, Venere M, Scolnick DM, Halazonetis TD (2003). "The Chfr mitotic checkpoint protein functions with Ubc13-Mms2 to form Lys63-linked polyubiquitin chains". Oncogene. 22 (46): 7101–7. doi:10.1038/sj.onc.1206831. PMID 14562038.
Zhou H, Wertz I, O'Rourke K, Ultsch M, Seshagiri S, Eby M, Xiao W, Dixit VM (2004). "Bcl10 activates the NF-kappaB pathway through ubiquitination of NEMO". Nature. 427 (6970): 167–71. doi:10.1038/nature02273. PMID 14695475.
Sun L, Deng L, Ea CK, Xia ZP, Chen ZJ (2004). "The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes". Mol. Cell. 14 (3): 289–301. doi:10.1016/S1097-2765(04)00236-9. PMID 15125833.
Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM (2004). "Functional proteomics mapping of a human signaling pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
Pastushok L, Moraes TF, Ellison MJ, Xiao W (2005). "A single Mms2 "key" residue insertion into a Ubc13 pocket determines the interface specificity of a human Lys63 ubiquitin conjugation complex". J. Biol. Chem. 280 (18): 17891–900. doi:10.1074/jbc.M410469200. PMID 15749714.
Takeuchi T, Yokosawa H (2005). "ISG15 modification of Ubc13 suppresses its ubiquitin-conjugating activity". Biochem. Biophys. Res. Commun. 336 (1): 9–13. doi:10.1016/j.bbrc.2005.08.034. PMID 16112642.
Zou W, Papov V, Malakhova O, Kim KI, Dao C, Li J, Zhang DE (2005). "ISG15 modification of ubiquitin E2 Ubc13 disrupts its ability to form thioester bond with ubiquitin". Biochem. Biophys. Res. Commun. 336 (1): 61–8. doi:10.1016/j.bbrc.2005.08.038. PMID 16122702.
‹ The template below (PDB Gallery) is being considered for deletion. See templates for discussion to help reach a consensus. ›
v
t
e
PDB gallery
1j7d: Crystal Structure of hMms2-hUbc13
2c2v: CRYSTAL STRUCTURE OF THE CHIP-UBC13-UEV1A COMPLEX
v
t
e
Posttranslational modification
Chaperones/ protein folding
Heat shock proteins/ Chaperonins
Hsp10/GroES
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
Deubiquitinating enzyme: Ataxin 3
USP6
CYLD
ATG3
BIRC6
UFC1
Other
Ubiquitin-like modifiers
SUMO protein
ISG15
URM1
NEDD8
FAT10
ATG8
ATG12
FUB1
MUB
UFM1
UBL5
Prokaryotic ubiquitin-like protein
This article on a gene on human chromosome 12 is a stub. You can help Wikipedia by expanding it.
This article is part of a series on Information security Related security categories Internet security Cyberwarfare Computer security Mobile security Network security Threats Computer crime Vulnerability Eavesdropping Malware Spyware Ransomware Trojans Viruses Worms Rootkits Bootkits Keyloggers Screen scrapers Exploits Backdoors Logic bombs Payloads Denial of service Defenses Computer access control Application security Antivirus software Secure coding Secure by default Secure by design Secure operating systems Authentication Multi-factor authentication Authorization Data-centric security Encryption Firewall Intrusion detection system Mobile secure gateway Runtime application self-protection (RASP) v t e Information security , sometimes shortened to InfoSec , is the practice of preventing unauthorized access, use, disclosure, disruption, modification, inspection, recording or destruction of information. Th...
For Lambak Kiri public housing area, see Lambak Kiri Landless Indigenous Citizens' Housing Scheme. Village in Brunei-Muara, Brunei Lambak Kiri Village Location in Brunei Coordinates: 4°59′26″N 114°57′04″E / 4.990472°N 114.951114°E / 4.990472; 114.951114 Coordinates: 4°59′26″N 114°57′04″E / 4.990472°N 114.951114°E / 4.990472; 114.951114 Country Brunei District Brunei-Muara Mukim Berakas A Government • Village head Hamdani Omar Postcode BB1214 Lambak Kiri is a populated place in Brunei-Muara District, Brunei. It is officially a village subdivision under Berakas A, a mukim in the district. Lambak Kiri may also refer to the greater area which includes the Lambak Kiri public housing area of the Landless Indigenous Citizens' Housing Scheme (Malay: Skim Tanah Kurnia Rakyat Jati ), although the latter is a separate subdivision. Contents 1 Name 2 Administration 3 See also 4 References Name ...
Comments
Post a Comment