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Histone acetyltransferase KAT5 (EC 2.3.1.48) (60 kDa Tat-interactive protein) (Tip60) (Histone acetyltransferase HTATIP) (Lysine acetyltransferase 5)

 KAT5_RAT                Reviewed;         513 AA.
Q99MK2; Q5XI16;
28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
11-JUL-2006, sequence version 2.
22-NOV-2017, entry version 127.
RecName: Full=Histone acetyltransferase KAT5;
EC=2.3.1.48 {ECO:0000250|UniProtKB:Q92993};
AltName: Full=60 kDa Tat-interactive protein;
Short=Tip60;
AltName: Full=Histone acetyltransferase HTATIP;
AltName: Full=Lysine acetyltransferase 5;
Name=Kat5; Synonyms=Htatip, Tip60, Tip60b;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 63-506 (ISOFORM 2), AND INTERACTION WITH
APP.
PubMed=11441186; DOI=10.1126/science.1058783;
Cao X., Suedhof T.C.;
"A transcriptionally active complex of APP with Fe65 and histone
acetyltransferase Tip60.";
Science 293:115-120(2001).
[3]
INTERACTION WITH APBB1.
PubMed=19282473; DOI=10.1073/pnas.0810869106;
Stante M., Minopoli G., Passaro F., Raia M., Vecchio L.D., Russo T.;
"Fe65 is required for Tip60-directed histone H4 acetylation at DNA
strand breaks.";
Proc. Natl. Acad. Sci. U.S.A. 106:5093-5098(2009).
-!- FUNCTION: Catalytic subunit of the NuA4 histone acetyltransferase
complex which is involved in transcriptional activation of select
genes principally by acetylation of nucleosomal histones H4 and
H2A. This modification may both alter nucleosome - DNA
interactions and promote interaction of the modified histones with
other proteins which positively regulate transcription. This
complex may be required for the activation of transcriptional
programs associated with oncogene and proto-oncogene mediated
growth induction, tumor suppressor mediated growth arrest and
replicative senescence, apoptosis, and DNA repair. The NuA4
complex ATPase and helicase activities seem to be, at least in
part, contributed by the association of RUVBL1 and RUVBL2 with
EP400. NuA4 may also play a direct role in DNA repair when
recruited to sites of DNA damage. Directly acetylates and
activates ATM. Relieves NR1D2-mediated inhibition of APOC3
expression by acetylating NR1D2. Component of a SWR1-like complex
that specifically mediates the removal of histone H2A.Z/H2AFZ from
the nucleosome. Promotes FOXP3 acetylation and positively
regulates its transcriptional repressor activity (By similarity).
{ECO:0000250|UniProtKB:Q92993, ECO:0000303|PubMed:19282473}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + [protein]-L-lysine = CoA +
[protein]-N(6)-acetyl-L-lysine. {ECO:0000250|UniProtKB:Q92993}.
-!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex
which contains the catalytic subunit KAT5/TIP60 and the subunits
EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49,
RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX,
MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6 (By similarity).
HTATTIP/TIP60, EPC1, and ING3 together constitute a minimal HAT
complex termed Piccolo NuA4 (By similarity). The NuA4 complex
interacts with MYC (By similarity). Interacts with ATM (By
similarity). Interacts with JADE1 (By similarity). Interacts with
PLA2G4A/CPLA2, EDNRA and HDAC7 (By similarity). Interacts with
TRIM24 and TRIM68 (By similarity). Forms a complex with SENP6 and
UBE2I in response to UV irradiation. Identified in a complex with
HINT1 (By similarity). Interacts with ATF2 and CUL3. Interacts
with NR1D2 (via N-terminus). Component of a SWR1-like complex (By
similarity). Interacts with the cytoplasmic tail of APP and
APBB1/FE65. Interacts with FOXP3 (By similarity). Interacts with
ZBTB49 (By similarity). {ECO:0000250|UniProtKB:Q92993,
ECO:0000269|PubMed:11441186, ECO:0000269|PubMed:19282473}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92993}.
Nucleus, nucleolus {ECO:0000250|UniProtKB:Q92993}. Cytoplasm,
perinuclear region {ECO:0000250|UniProtKB:Q92993}. Note=Upon
stimulation with EDN1, it is exported from the nucleus to the
perinuclear region. {ECO:0000250|UniProtKB:Q92993}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q99MK2-1; Sequence=Displayed;
Name=2;
IsoId=Q99MK2-2; Sequence=VSP_019781;
-!- PTM: Sumoylated by UBE2I at Lys-430 and Lys-451, leading to
increase of its histone acetyltransferase activity in UV-induced
DNA damage response, as well as its translocation to nuclear
bodies. {ECO:0000250}.
-!- PTM: Phosphorylated. The phosphorylated form has a higher
activity. {ECO:0000250|UniProtKB:Q9H7Z6}.
-!- PTM: Ubiquitinated by MDM2, leading to its proteasome-dependent
degradation. {ECO:0000250}.
-!- PTM: Autoacetylation at Lys-327 is required for proper function.
{ECO:0000250|UniProtKB:Q9H7Z6}.
-!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}.
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EMBL; BC083879; AAH83879.1; -; mRNA.
EMBL; AF333984; AAK20836.1; -; mRNA.
RefSeq; NP_001005872.1; NM_001005872.1. [Q99MK2-1]
UniGene; Rn.6629; -.
ProteinModelPortal; Q99MK2; -.
SMR; Q99MK2; -.
BioGrid; 251357; 1.
STRING; 10116.ENSRNOP00000039632; -.
ChEMBL; CHEMBL1932911; -.
iPTMnet; Q99MK2; -.
PhosphoSitePlus; Q99MK2; -.
PaxDb; Q99MK2; -.
GeneID; 192218; -.
KEGG; rno:192218; -.
UCSC; RGD:621061; rat. [Q99MK2-1]
CTD; 10524; -.
RGD; 621061; Kat5.
eggNOG; KOG2747; Eukaryota.
eggNOG; COG5027; LUCA.
HOGENOM; HOG000182457; -.
InParanoid; Q99MK2; -.
KO; K11304; -.
PhylomeDB; Q99MK2; -.
PRO; PR:Q99MK2; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISS:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IDA:RGD.
GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0032777; C:Piccolo NuA4 histone acetyltransferase complex; ISS:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:RGD.
GO; GO:0000812; C:Swr1 complex; ISS:UniProtKB.
GO; GO:0005667; C:transcription factor complex; ISO:RGD.
GO; GO:0003682; F:chromatin binding; IDA:RGD.
GO; GO:0004402; F:histone acetyltransferase activity; ISO:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0043274; F:phospholipase binding; IPI:RGD.
GO; GO:0032403; F:protein complex binding; IPI:RGD.
GO; GO:0070491; F:repressing transcription factor binding; ISO:RGD.
GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IDA:RGD.
GO; GO:0006915; P:apoptotic process; IEP:RGD.
GO; GO:0071392; P:cellular response to estradiol stimulus; ISO:RGD.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:RGD.
GO; GO:0071481; P:cellular response to X-ray; IEP:RGD.
GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; ISS:UniProtKB.
GO; GO:0006302; P:double-strand break repair; ISO:RGD.
GO; GO:0016573; P:histone acetylation; IMP:RGD.
GO; GO:0043967; P:histone H4 acetylation; NAS:UniProtKB.
GO; GO:0032703; P:negative regulation of interleukin-2 production; ISO:RGD.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISO:RGD.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
GO; GO:1901985; P:positive regulation of protein acetylation; ISO:RGD.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:RGD.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:RGD.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
GO; GO:0009408; P:response to heat; IEP:RGD.
GO; GO:0010212; P:response to ionizing radiation; ISO:RGD.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00024; CHROMO; 1.
InterPro; IPR016181; Acyl_CoA_acyltransferase.
InterPro; IPR016197; Chromo-like_dom_sf.
InterPro; IPR000953; Chromo/chromo_shadow_dom.
InterPro; IPR002717; HAT_MYST-type.
InterPro; IPR025995; Tudor-knot.
Pfam; PF01853; MOZ_SAS; 1.
Pfam; PF11717; Tudor-knot; 1.
SMART; SM00298; CHROMO; 1.
SUPFAM; SSF54160; SSF54160; 1.
SUPFAM; SSF55729; SSF55729; 1.
PROSITE; PS51726; MYST_HAT; 1.
1: Evidence at protein level;
Acetylation; Activator; Acyltransferase; Alternative splicing;
Complete proteome; Cytoplasm; Isopeptide bond; Metal-binding; Nucleus;
Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Transferase; Ubl conjugation; Zinc;
Zinc-finger.
CHAIN 1 513 Histone acetyltransferase KAT5.
/FTId=PRO_0000051582.
DOMAIN 227 504 MYST-type HAT. {ECO:0000255|PROSITE-
ProRule:PRU01063}.
ZN_FING 260 285 C2HC MYST-type. {ECO:0000255|PROSITE-
ProRule:PRU01063}.
REGION 368 513 Interaction with ATF2. {ECO:0000250}.
REGION 370 372 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:Q9H7Z6}.
REGION 377 383 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:Q9H7Z6}.
ACT_SITE 403 403 Proton donor/acceptor.
{ECO:0000250|UniProtKB:Q9H7Z6}.
BINDING 407 407 Acetyl-CoA.
{ECO:0000250|UniProtKB:Q9H7Z6}.
BINDING 416 416 Acetyl-CoA.
{ECO:0000250|UniProtKB:Q9H7Z6}.
MOD_RES 52 52 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q92993}.
MOD_RES 86 86 Phosphoserine.
{ECO:0000250|UniProtKB:Q92993}.
MOD_RES 90 90 Phosphoserine.
{ECO:0000250|UniProtKB:Q92993}.
MOD_RES 199 199 Phosphoserine.
{ECO:0000250|UniProtKB:Q92993}.
MOD_RES 327 327 N6-acetyllysine; by autocatalysis.
{ECO:0000250|UniProtKB:Q92993}.
CROSSLNK 430 430 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 451 451 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
VAR_SEQ 96 147 Missing (in isoform 2).
{ECO:0000303|PubMed:11441186}.
/FTId=VSP_019781.
SEQUENCE 513 AA; 58598 MW; EACEE4D544C0DB60 CRC64;
MAEVGEIIEG CRLPVLRRNQ DNEDEWPLAE ILSVKDISGR KLFYVHYIDF NKRLDEWVTH
ERLDLKKIQF PKKEAKTPTK NGLPGSRPGS PEREVPASAQ ASGKTLPIPV QITLRFNLPK
EREAIPGGEP DQPLSSSSCL QPNHRSTKRK VEVVSPATPV PSETAPASVF PQNGSARRAV
AAQPGRKRKS NCLGTDEDSQ DSSDGIPSAP RMTGSLVSDR SHDDIVTRMK NIECIELGRH
RLKPWYFSPY PQELTTLPVL YLCEFCLKYG RSLKCLQRHL TKCDLRHPPG NEIYRKGTIS
FFEIDGRKNK SYSQNLCLLA KCFLDHKTLY YDTDPFLFYV MTEYDCKGFH IVGYFSKEKE
STEDYNVACI LTLPPYQRRG YGKLLIEFSY ELSKVEGKTG TPEKPLSDLG LLSYRSYWSQ
TILEILMGLK SESGERPQIT INEISEITSI KKEDVISTLQ YLNLINYYKG QYILTLSEDI
VDGHERAMLK RLLRIDSKCL HFTPKDWSKR GKW


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