GCN5L2: Difference between revisions

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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}} __NOTOC__
{{PBB_Controls
'''Histone acetyltransferase KAT2A''' is an [[enzyme]] that in humans is encoded by the ''KAT2A'' [[gene]].<ref name="pmid8552087">{{cite journal | vauthors = Candau R, Moore PA, Wang L, Barlev N, Ying CY, Rosen CA, Berger SL | title = Identification of human proteins functionally conserved with the yeast putative adaptors ADA2 and GCN5 | journal = Mol Cell Biol | volume = 16 | issue = 2 | pages = 593–602 | date = February 1996 | pmid = 8552087 | pmc = 231038 | doi =  10.1128/mcb.16.2.593}}</ref><ref name="entrez">{{cite web | title = Entrez Gene: GCN5L2 GCN5 general control of amino-acid synthesis 5-like 2 (yeast)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2648| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Interactions ==
{{GNF_Protein_box
| image = PBB_Protein_GCN5L2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1f68.
| PDB = {{PDB2|1f68}}, {{PDB2|1z4r}}
| Name = GCN5 general control of amino-acid synthesis 5-like 2 (yeast)
| HGNCid = 4201
| Symbol = GCN5L2
| AltSymbols =; GCN5; MGC102791; PCAF-b; hGCN5
| OMIM = 602301
| ECnumber = 
| Homologene = 41343
| MGIid = 1343101
| GeneAtlas_image1 = PBB_GE_GCN5L2_202182_at_tn.png
| Function = {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0004402 |text = histone acetyltransferase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008080 |text = N-acetyltransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0042826 |text = histone deacetylase binding}}
| Component = {{GNF_GO|id=GO:0000123 |text = histone acetyltransferase complex}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0001756 |text = somitogenesis}} {{GNF_GO|id=GO:0006338 |text = chromatin remodeling}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006357 |text = regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006473 |text = protein amino acid acetylation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2648
    | Hs_Ensembl = ENSG00000108773
    | Hs_RefseqProtein = NP_066564
    | Hs_RefseqmRNA = NM_021078
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 17
    | Hs_GenLoc_start = 37518655
    | Hs_GenLoc_end = 37526901
    | Hs_Uniprot = Q92830
    | Mm_EntrezGene = 14534
    | Mm_Ensembl = ENSMUSG00000020918
    | Mm_RefseqmRNA = NM_001038010
    | Mm_RefseqProtein = NP_001033099
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 100520836
    | Mm_GenLoc_end = 100528555
    | Mm_Uniprot = Q99KW4
  }}
}}
'''GCN5 general control of amino-acid synthesis 5-like 2 (yeast)''', also known as '''GCN5L2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GCN5L2 GCN5 general control of amino-acid synthesis 5-like 2 (yeast)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2648| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
GCN5L2 has been shown to [[Protein-protein interaction|interact]] with:
{{PBB_Summary
* [[DDB1]],<ref name = pmid11564863/>
| section_title =  
* [[Ku70]],<ref name = pmid9488450>{{cite journal | vauthors = Barlev NA, Poltoratsky V, Owen-Hughes T, Ying C, Liu L, Workman JL, Berger SL | title = Repression of GCN5 histone acetyltransferase activity via bromodomain-mediated binding and phosphorylation by the Ku-DNA-dependent protein kinase complex | journal = Mol. Cell. Biol. | volume = 18 | issue = 3 | pages = 1349–58 | date = March 1998 | pmid = 9488450 | pmc = 108848 | doi =  10.1128/mcb.18.3.1349}}</ref>
| summary_text =  
* [[Ku80]],<ref name = pmid9488450/>
}}
* [[TADA2L]],<ref name = pmid9488450/><ref name = pmid8972232>{{cite journal | vauthors = Wang L, Mizzen C, Ying C, Candau R, Barlev N, Brownell J, Allis CD, Berger SL | title = Histone acetyltransferase activity is conserved between yeast and human GCN5 and is required for complementation of growth and transcriptional activation | journal = Mol. Cell. Biol. | volume = 17 | issue = 1 | pages = 519–27 | date = January 1997 | pmid = 8972232 | pmc = 231776 | doi = 10.1128/mcb.17.1.519}}</ref>
* [[TAF9]],<ref name = pmid11564863>{{cite journal | vauthors = Martinez E, Palhan VB, Tjernberg A, Lymar ES, Gamper AM, Kundu TK, Chait BT, Roeder RG | title = Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo | journal = Mol. Cell. Biol. | volume = 21 | issue = 20 | pages = 6782–95 | date = October 2001 | pmid = 11564863 | pmc = 99856 | doi = 10.1128/MCB.21.20.6782-6795.2001 }}</ref> and
* [[Transcription initiation protein SPT3 homolog]].<ref name = pmid11564863/><ref name = pmid11406595>{{cite journal | vauthors = Brand M, Moggs JG, Oulad-Abdelghani M, Lejeune F, Dilworth FJ, Stevenin J, Almouzni G, Tora L | title = UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation | journal = EMBO J. | volume = 20 | issue = 12 | pages = 3187–96 | date = June 2001 | pmid = 11406595 | pmc = 150203 | doi = 10.1093/emboj/20.12.3187 }}</ref>


==References==
== References ==
{{reflist|2}}
{{reflist}}
==Further reading==
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Berry R, Stevens TJ, Walter NA, Wilcox AS, Rubano T, Hopkins JA, Weber J, Goold R, Soares MB, Sikela JM | title = Gene-based sequence-tagged-sites (STSs) as the basis for a human gene map. | journal = Nat. Genet. | volume = 10 | issue = 4 | pages = 415–23 | year = 1995 | pmid = 7670491 | doi = 10.1038/ng0895-415 }}
| citations =
* {{cite journal | vauthors = Yang XJ, Ogryzko VV, Nishikawa J, Howard BH, Nakatani Y | title = A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. | journal = Nature | volume = 382 | issue = 6589 | pages = 319–24 | year = 1996 | pmid = 8684459 | doi = 10.1038/382319a0 }}
*{{cite journal | author=Berry R, Stevens TJ, Walter NA, ''et al.'' |title=Gene-based sequence-tagged-sites (STSs) as the basis for a human gene map. |journal=Nat. Genet. |volume=10 |issue= 4 |pages= 415-23 |year= 1995 |pmid= 7670491 |doi= 10.1038/ng0895-415 }}
* {{cite journal | vauthors = Wang L, Mizzen C, Ying C, Candau R, Barlev N, Brownell J, Allis CD, Berger SL | title = Histone acetyltransferase activity is conserved between yeast and human GCN5 and is required for complementation of growth and transcriptional activation. | journal = Mol. Cell. Biol. | volume = 17 | issue = 1 | pages = 519–27 | year = 1997 | pmid = 8972232 | pmc = 231776 | doi = 10.1128/mcb.17.1.519}}
*{{cite journal | author=Candau R, Moore PA, Wang L, ''et al.'' |title=Identification of human proteins functionally conserved with the yeast putative adaptors ADA2 and GCN5. |journal=Mol. Cell. Biol. |volume=16 |issue= 2 |pages= 593-602 |year= 1996 |pmid= 8552087 |doi= }}
* {{cite journal | vauthors = Carter KC, Wang L, Shell BK, Zamir I, Berger SL, Moore PA | title = The human transcriptional adaptor genes TADA2L and GCN5L2 colocalize to chromosome 17q12-q21 and display a similar tissue expression pattern. | journal = Genomics | volume = 40 | issue = 3 | pages = 497–500 | year = 1997 | pmid = 9073520 | doi = 10.1006/geno.1996.4605 }}
*{{cite journal | author=Yang XJ, Ogryzko VV, Nishikawa J, ''et al.'' |title=A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A. |journal=Nature |volume=382 |issue= 6589 |pages= 319-24 |year= 1996 |pmid= 8684459 |doi= 10.1038/382319a0 }}
* {{cite journal | vauthors = Barlev NA, Poltoratsky V, Owen-Hughes T, Ying C, Liu L, Workman JL, Berger SL | title = Repression of GCN5 histone acetyltransferase activity via bromodomain-mediated binding and phosphorylation by the Ku-DNA-dependent protein kinase complex. | journal = Mol. Cell. Biol. | volume = 18 | issue = 3 | pages = 1349–58 | year = 1998 | pmid = 9488450 | pmc = 108848 | doi = 10.1128/mcb.18.3.1349}}
*{{cite journal | author=Wang L, Mizzen C, Ying C, ''et al.'' |title=Histone acetyltransferase activity is conserved between yeast and human GCN5 and is required for complementation of growth and transcriptional activation. |journal=Mol. Cell. Biol. |volume=17 |issue= 1 |pages= 519-27 |year= 1997 |pmid= 8972232 |doi= }}
* {{cite journal | vauthors = Smith ER, Belote JM, Schiltz RL, Yang XJ, Moore PA, Berger SL, Nakatani Y, Allis CD | title = Cloning of Drosophila GCN5: conserved features among metazoan GCN5 family members. | journal = Nucleic Acids Res. | volume = 26 | issue = 12 | pages = 2948–54 | year = 1998 | pmid = 9611240 | pmc = 147644 | doi = 10.1093/nar/26.12.2948 }}
*{{cite journal | author=Carter KC, Wang L, Shell BK, ''et al.'' |title=The human transcriptional adaptor genes TADA2L and GCN5L2 colocalize to chromosome 17q12-q21 and display a similar tissue expression pattern. |journal=Genomics |volume=40 |issue= 3 |pages= 497-500 |year= 1997 |pmid= 9073520 |doi= 10.1006/geno.1996.4605 }}
* {{cite journal | vauthors = Randhawa GS, Bell DW, Testa JR, Feinberg AP | title = Identification and mapping of human histone acetylation modifier gene homologues. | journal = Genomics | volume = 51 | issue = 2 | pages = 262–9 | year = 1998 | pmid = 9722949 | doi = 10.1006/geno.1998.5370 }}
*{{cite journal | author=Barlev NA, Poltoratsky V, Owen-Hughes T, ''et al.'' |title=Repression of GCN5 histone acetyltransferase activity via bromodomain-mediated binding and phosphorylation by the Ku-DNA-dependent protein kinase complex. |journal=Mol. Cell. Biol. |volume=18 |issue= 3 |pages= 1349-58 |year= 1998 |pmid= 9488450 |doi= }}
* {{cite journal | vauthors = Xu W, Edmondson DG, Roth SY | title = Mammalian GCN5 and P/CAF acetyltransferases have homologous amino-terminal domains important for recognition of nucleosomal substrates. | journal = Mol. Cell. Biol. | volume = 18 | issue = 10 | pages = 5659–69 | year = 1998 | pmid = 9742083 | pmc = 109152 | doi = }}
*{{cite journal | author=Smith ER, Belote JM, Schiltz RL, ''et al.'' |title=Cloning of Drosophila GCN5: conserved features among metazoan GCN5 family members. |journal=Nucleic Acids Res. |volume=26 |issue= 12 |pages= 2948-54 |year= 1998 |pmid= 9611240 |doi= }}
* {{cite journal | vauthors = Brand M, Yamamoto K, Staub A, Tora L | title = Identification of TATA-binding protein-free TAFII-containing complex subunits suggests a role in nucleosome acetylation and signal transduction. | journal = J. Biol. Chem. | volume = 274 | issue = 26 | pages = 18285–9 | year = 1999 | pmid = 10373431 | doi = 10.1074/jbc.274.26.18285 }}
*{{cite journal | author=Randhawa GS, Bell DW, Testa JR, Feinberg AP |title=Identification and mapping of human histone acetylation modifier gene homologues. |journal=Genomics |volume=51 |issue= 2 |pages= 262-9 |year= 1998 |pmid= 9722949 |doi= 10.1006/geno.1998.5370 }}
* {{cite journal | vauthors = McMahon SB, Wood MA, Cole MD | title = The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc. | journal = Mol. Cell. Biol. | volume = 20 | issue = 2 | pages = 556–62 | year = 2000 | pmid = 10611234 | pmc = 85131 | doi = 10.1128/MCB.20.2.556-562.2000 }}
*{{cite journal | author=Xu W, Edmondson DG, Roth SY |title=Mammalian GCN5 and P/CAF acetyltransferases have homologous amino-terminal domains important for recognition of nucleosomal substrates. |journal=Mol. Cell. Biol. |volume=18 |issue= 10 |pages= 5659-69 |year= 1998 |pmid= 9742083 |doi= }}
* {{cite journal | vauthors = Kurooka H, Honjo T | title = Functional interaction between the mouse notch1 intracellular region and histone acetyltransferases PCAF and GCN5. | journal = J. Biol. Chem. | volume = 275 | issue = 22 | pages = 17211–20 | year = 2000 | pmid = 10747963 | doi = 10.1074/jbc.M000909200 }}
*{{cite journal | author=Brand M, Yamamoto K, Staub A, Tora L |title=Identification of TATA-binding protein-free TAFII-containing complex subunits suggests a role in nucleosome acetylation and signal transduction. |journal=J. Biol. Chem. |volume=274 |issue= 26 |pages= 18285-9 |year= 1999 |pmid= 10373431 |doi= }}
* {{cite journal | vauthors = Hudson BP, Martinez-Yamout MA, Dyson HJ, Wright PE | title = Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain. | journal = J. Mol. Biol. | volume = 304 | issue = 3 | pages = 355–70 | year = 2000 | pmid = 11090279 | doi = 10.1006/jmbi.2000.4207 }}
*{{cite journal | author=McMahon SB, Wood MA, Cole MD |title=The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc. |journal=Mol. Cell. Biol. |volume=20 |issue= 2 |pages= 556-62 |year= 2000 |pmid= 10611234 |doi= }}
* {{cite journal | vauthors = Col E, Caron C, Seigneurin-Berny D, Gracia J, Favier A, Khochbin S | title = The histone acetyltransferase, hGCN5, interacts with and acetylates the HIV transactivator, Tat. | journal = J. Biol. Chem. | volume = 276 | issue = 30 | pages = 28179–84 | year = 2001 | pmid = 11384967 | doi = 10.1074/jbc.M101385200 }}
*{{cite journal | author=Kurooka H, Honjo T |title=Functional interaction between the mouse notch1 intracellular region and histone acetyltransferases PCAF and GCN5. |journal=J. Biol. Chem. |volume=275 |issue= 22 |pages= 17211-20 |year= 2000 |pmid= 10747963 |doi= 10.1074/jbc.M000909200 }}
* {{cite journal | vauthors = Brand M, Moggs JG, Oulad-Abdelghani M, Lejeune F, Dilworth FJ, Stevenin J, Almouzni G, Tora L | title = UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation. | journal = EMBO J. | volume = 20 | issue = 12 | pages = 3187–96 | year = 2001 | pmid = 11406595 | pmc = 150203 | doi = 10.1093/emboj/20.12.3187 }}
*{{cite journal | author=Hudson BP, Martinez-Yamout MA, Dyson HJ, Wright PE |title=Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain. |journal=J. Mol. Biol. |volume=304 |issue= 3 |pages= 355-70 |year= 2000 |pmid= 11090279 |doi= 10.1006/jmbi.2000.4207 }}
* {{cite journal | vauthors = Gangloff YG, Pointud JC, Thuault S, Carré L, Romier C, Muratoglu S, Brand M, Tora L, Couderc JL, Davidson I | title = The TFIID components human TAF(II)140 and Drosophila BIP2 (TAF(II)155) are novel metazoan homologues of yeast TAF(II)47 containing a histone fold and a PHD finger. | journal = Mol. Cell. Biol. | volume = 21 | issue = 15 | pages = 5109–21 | year = 2001 | pmid = 11438666 | pmc = 87236 | doi = 10.1128/MCB.21.15.5109-5121.2001 }}
*{{cite journal | author=Col E, Caron C, Seigneurin-Berny D, ''et al.'' |title=The histone acetyltransferase, hGCN5, interacts with and acetylates the HIV transactivator, Tat. |journal=J. Biol. Chem. |volume=276 |issue= 30 |pages= 28179-84 |year= 2001 |pmid= 11384967 |doi= 10.1074/jbc.M101385200 }}
* {{cite journal | vauthors = Martinez E, Palhan VB, Tjernberg A, Lymar ES, Gamper AM, Kundu TK, Chait BT, Roeder RG | title = Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo. | journal = Mol. Cell. Biol. | volume = 21 | issue = 20 | pages = 6782–95 | year = 2001 | pmid = 11564863 | pmc = 99856 | doi = 10.1128/MCB.21.20.6782-6795.2001 }}
*{{cite journal | author=Brand M, Moggs JG, Oulad-Abdelghani M, ''et al.'' |title=UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation. |journal=EMBO J. |volume=20 |issue= 12 |pages= 3187-96 |year= 2001 |pmid= 11406595 |doi= 10.1093/emboj/20.12.3187 }}
* {{cite journal | vauthors = Yanagisawa J, Kitagawa H, Yanagida M, Wada O, Ogawa S, Nakagomi M, Oishi H, Yamamoto Y, Nagasawa H, McMahon SB, Cole MD, Tora L, Takahashi N, Kato S | title = Nuclear receptor function requires a TFTC-type histone acetyl transferase complex. | journal = Mol. Cell | volume = 9 | issue = 3 | pages = 553–62 | year = 2002 | pmid = 11931763 | doi = 10.1016/S1097-2765(02)00478-1 }}
*{{cite journal | author=Gangloff YG, Pointud JC, Thuault S, ''et al.'' |title=The TFIID components human TAF(II)140 and Drosophila BIP2 (TAF(II)155) are novel metazoan homologues of yeast TAF(II)47 containing a histone fold and a PHD finger. |journal=Mol. Cell. Biol. |volume=21 |issue= 15 |pages= 5109-21 |year= 2001 |pmid= 11438666 |doi= 10.1128/MCB.21.15.5109-5121.2001 }}
* {{cite journal | vauthors = Brès V, Kiernan R, Emiliani S, Benkirane M | title = Tat acetyl-acceptor lysines are important for human immunodeficiency virus type-1 replication. | journal = J. Biol. Chem. | volume = 277 | issue = 25 | pages = 22215–21 | year = 2002 | pmid = 11956210 | doi = 10.1074/jbc.M201895200 }}
*{{cite journal | author=Martinez E, Palhan VB, Tjernberg A, ''et al.'' |title=Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo. |journal=Mol. Cell. Biol. |volume=21 |issue= 20 |pages= 6782-95 |year= 2001 |pmid= 11564863 |doi= 10.1128/MCB.21.20.6782-6795.2001 }}
* {{cite journal | vauthors = Col E, Gilquin B, Caron C, Khochbin S | title = Tat-controlled protein acetylation. | journal = J. Biol. Chem. | volume = 277 | issue = 40 | pages = 37955–60 | year = 2002 | pmid = 12154097 | doi = 10.1074/jbc.M206694200 }}
*{{cite journal  | author=Yanagisawa J, Kitagawa H, Yanagida M, ''et al.'' |title=Nuclear receptor function requires a TFTC-type histone acetyl transferase complex. |journal=Mol. Cell |volume=9 |issue= 3 |pages= 553-62 |year= 2002 |pmid= 11931763 |doi=  }}
*{{cite journal | author=Brès V, Kiernan R, Emiliani S, Benkirane M |title=Tat acetyl-acceptor lysines are important for human immunodeficiency virus type-1 replication. |journal=J. Biol. Chem. |volume=277 |issue= 25 |pages= 22215-21 |year= 2002 |pmid= 11956210 |doi= 10.1074/jbc.M201895200 }}
*{{cite journal | author=Col E, Gilquin B, Caron C, Khochbin S |title=Tat-controlled protein acetylation. |journal=J. Biol. Chem. |volume=277 |issue= 40 |pages= 37955-60 |year= 2002 |pmid= 12154097 |doi= 10.1074/jbc.M206694200 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
== External links ==
{{WikiDoc Sources}}
* {{FactorBook|GCN5}}
 
{{PDB Gallery|geneid=2648}}
 
 
{{gene-17-stub}}

Latest revision as of 08:42, 31 August 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

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UniProt

n/a

n/a

RefSeq (mRNA)

n/a

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Histone acetyltransferase KAT2A is an enzyme that in humans is encoded by the KAT2A gene.[1][2]

Interactions

GCN5L2 has been shown to interact with:

References

  1. ↑ Candau R, Moore PA, Wang L, Barlev N, Ying CY, Rosen CA, Berger SL (February 1996). "Identification of human proteins functionally conserved with the yeast putative adaptors ADA2 and GCN5". Mol Cell Biol. 16 (2): 593–602. doi:10.1128/mcb.16.2.593. PMC 231038. PMID 8552087.
  2. ↑ "Entrez Gene: GCN5L2 GCN5 general control of amino-acid synthesis 5-like 2 (yeast)".
  3. ↑ 3.0 3.1 3.2 Martinez E, Palhan VB, Tjernberg A, Lymar ES, Gamper AM, Kundu TK, Chait BT, Roeder RG (October 2001). "Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo". Mol. Cell. Biol. 21 (20): 6782–95. doi:10.1128/MCB.21.20.6782-6795.2001. PMC 99856. PMID 11564863.
  4. ↑ 4.0 4.1 4.2 Barlev NA, Poltoratsky V, Owen-Hughes T, Ying C, Liu L, Workman JL, Berger SL (March 1998). "Repression of GCN5 histone acetyltransferase activity via bromodomain-mediated binding and phosphorylation by the Ku-DNA-dependent protein kinase complex". Mol. Cell. Biol. 18 (3): 1349–58. doi:10.1128/mcb.18.3.1349. PMC 108848. PMID 9488450.
  5. ↑ Wang L, Mizzen C, Ying C, Candau R, Barlev N, Brownell J, Allis CD, Berger SL (January 1997). "Histone acetyltransferase activity is conserved between yeast and human GCN5 and is required for complementation of growth and transcriptional activation". Mol. Cell. Biol. 17 (1): 519–27. doi:10.1128/mcb.17.1.519. PMC 231776. PMID 8972232.
  6. ↑ Brand M, Moggs JG, Oulad-Abdelghani M, Lejeune F, Dilworth FJ, Stevenin J, Almouzni G, Tora L (June 2001). "UV-damaged DNA-binding protein in the TFTC complex links DNA damage recognition to nucleosome acetylation". EMBO J. 20 (12): 3187–96. doi:10.1093/emboj/20.12.3187. PMC 150203. PMID 11406595.

Further reading

External links


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