GCN5L2

GCN5L2

GCN5 general control of amino-acid synthesis 5-like 2 (yeast), also known as GCN5L2, is a human gene.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 = ]

PBB_Summary
section_title =
summary_text =

References

Further reading

PBB_Further_reading
citations =
*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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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 | 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

PBB_Controls
update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes


Wikimedia Foundation. 2010.

Игры ⚽ Поможем написать реферат

Look at other dictionaries:

  • GCN5L2 — Histona acetiltransferasa KAT2A Estructura tridimensional de la proteína GCN5L2. HUGO …   Wikipedia Español

  • DDB1 — Damage specific DNA binding protein 1, 127kDa PDB rendering based on 2b5l …   Wikipedia

  • TADA2L — Transcriptional adaptor 2 (ADA2 homolog, yeast) like, also known as TADA2L, is a human gene.cite web | title = Entrez Gene: TADA2L transcriptional adaptor 2 (ADA2 homolog, yeast) like| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene… …   Wikipedia

  • Ku70 — Estructura tridimensional de la proteína Ku70. HUGO 4055 …   Wikipedia Español

  • Ku80 — Estructura tridimensional de la proteína Ku80. HUGO 12833 …   Wikipedia Español

  • Ku80 — Связать? Ku80  белок, закодированный у человека геном XRCC5.[1] Вместе с белком Ku70 белок Ku80 образует гетеродимер, связывающийся с концами двунитевых разрывов в ДНК, и требуется для репарации ДНК путем негомологичного соединения концов… …   Википедия

Share the article and excerpts

Direct link
Do a right-click on the link above
and select “Copy Link”