ID H0V809_CAVPO Unreviewed; 1762 AA.
AC H0V809;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=histone acetyltransferase {ECO:0000256|ARBA:ARBA00013184};
DE EC=2.3.1.48 {ECO:0000256|ARBA:ARBA00013184};
GN Name=KAT6B {ECO:0000313|Ensembl:ENSCPOP00000005892.3};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000005892.3, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000005892.3}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000005892.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000256|ARBA:ARBA00000780};
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC {ECO:0000256|ARBA:ARBA00010107}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAKN02021289; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02021290; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02021291; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02021292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02021293; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02021294; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_013012206.1; XM_013156752.1.
DR STRING; 10141.ENSCPOP00000025577; -.
DR Ensembl; ENSCPOT00000006610.3; ENSCPOP00000005892.3; ENSCPOG00000006544.4.
DR Ensembl; ENSCPOT00000035709.1; ENSCPOP00000025577.1; ENSCPOG00000006544.4.
DR GeneID; 100723383; -.
DR CTD; 23522; -.
DR VEuPathDB; HostDB:ENSCPOG00000006544; -.
DR eggNOG; KOG2747; Eukaryota.
DR GeneTree; ENSGT00940000157372; -.
DR HOGENOM; CLU_001232_1_1_1; -.
DR OMA; AFQHQSG; -.
DR TreeFam; TF106483; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000006544; Expressed in pituitary gland and 13 other cell types or tissues.
DR GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IEA:Ensembl.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0036408; F:histone H3K14 acetyltransferase activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR CDD; cd15527; PHD2_KAT6A_6B; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 3.30.60.60; N-acetyl transferase-like; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR002717; HAT_MYST-type.
DR InterPro; IPR005818; Histone_H1/H5_H15.
DR InterPro; IPR048589; SAMD1-like_WH.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR InterPro; IPR040706; Zf-MYST.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR PANTHER; PTHR10615:SF73; HISTONE ACETYLTRANSFERASE KAT6B; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF21524; SAMD1_WH; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SMART; SM00526; H15; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS51504; H15; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 103..176
FT /note="H15"
FT /evidence="ECO:0000259|PROSITE:PS51504"
FT DOMAIN 213..272
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 269..320
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 423..697
FT /note="MYST-type HAT"
FT /evidence="ECO:0000259|PROSITE:PS51726"
FT REGION 72..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 900..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1178..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1280..1311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 702..729
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 736..750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..804
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..839
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..871
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..940
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1046
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1070
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1098
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1125
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1141
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1225..1244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 599
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602717-51"
SQ SEQUENCE 1762 AA; 197373 MW; 85DE4A9559F0A777 CRC64;
MVKLANPLYT EWILEAIQKI KKQKQRPSEE RICHAVSASH GLDKKTVSEQ LELSVQDGSV
LKVTNKGLAS YKDPDNPGRF SAVKPGTFPK SSKGSRGSCN DLRNVDWNKL LRRAIEGLEE
PNGSSLKNIE KYLRSQSDLS STTTNPAFQQ RLRLGAKRAV NNGRLLKDGP QYRVNYGGSD
GKAAPQCPSA FPSSLPPVSL LPHEKDQPRA DPIPICSFCL GTKESNREKK PEELLSCADC
GSSGHPSCLK FCPELTTNVK ALRWQCIECK TCSACRIQGK NADNMLFCDS CDRGFHMECC
DPPLSRMPKG MWICQVCRPK KKGRKLLHEK AAQIKRRYAK PIGRPKNKLK QRLLSVTSDE
GSMNAFTGRG SPDTEIKISI KQENTDVNVI GNKDVVTEED LDVFKQAQEL SWEKIECESG
VEDCGRYPSV IEFGKYEIQT WYSSPYPQEY ARLPKLYLCE FCLKYMKSKN ILLRHSKKCG
WFHPPANEIY RRKDLSVFEV DGNMSKIYCQ NLCLLAKLFL DHKTLYYDVE PFLFYVLTKN
DEKGCHLVGY FSKEKLCQQK YNVSCIMIMP QHQRQGFGRF LIDFSYLLSR REGQAGSPEK
PLSDLGRLSY LAYWKSVILE YLCHHHERHI SIKAISRATG MCPHDIATTL QHLHMIDKRD
GRFVIIRREK LILDHMEKLK TCSRVNELDP ECLRWTPILI SNVAVSEEER EAEKEAERLM
EQASCWEKED QEILSSRANS RQSPAKVQSK NKYLHSPEGR PGAGERGQLM ELAKESSEEE
EEEEEEEEEE EEEEEEEEDE EEEENIRSSP PRLTKPQSVA IKRKRPFVLK KKRGRKRRRI
NSSVTTETIS ETTEVLNEPF DHSDEERPMP QLEPTCELEV EEESRKPVLR KAFQHQLGKK
RQAELEEEKD NHCFKNSDPC RNNTDEDANN LKEGSKDNPE TLKCKQTWPK GTKRGLSKWR
QSKERKTGFK LNLYTPPETP MEPDEQVTVE EQQEISEDKS SPTLAEMEQE VKETSEAPLP
RDGNRREESC TPGSPHESPG EKSDDLIKPE EEEEEEEEEE EEEEEEEGIV EKDPDGSKNQ
EKVEPEISVA KEDHVHLDDH EEEEEEDEEP AHNEDHDADD EDDSHMESAG AEKEELPREA
FKAVLENQEA FLDLSVQPSY SNSEVLMDCG VDVAASCHSE PKELAGDTET APESDGEPPE
EQAQKQDQKD GEEVDAEFKE ANTATLEIDS ETVQAVQSLT QENREQDDTF QDCAETQEAC
RSLQNYTHAD QSPQIAATLD DCQQSDHSSP VSSVHSHPSQ SVRSVNSPSV PAMENSYAQI
SPDQSAISVP SLQNMETSPM MDVPSVSDHS QQVVDSGFSD LGSIESTTEN YENPSSYDST
MGGSICGNGS SQNSCSYSNL TSSNLTQSSC AVTQQMSNMS GSCSMLQQTS ISSPPTCSVK
SPQGCVGERP PSSSQQLAQC SMAANFSPPM QLADIPEAGN ANIGLYERMG QSDFGAGHYP
QPSATFSLAK LQQLTNTLID HSLPYSHSAA VTSYANSASL STPLSNTGLV QLSQSPHSVP
GGPQAQATMT PPPNLTPPPM NLPPPLLQRN MAASNIGISH SQRLQTQIAS KGHISMRTKS
ASLSPAAATH QSQIYGRSQT VAMQGPARTL TMQRGMNMSV NLMPAPAYNV NSVNMNTLNA
MNGYSMSQPM MNSGYHSNHG YMNQTPQYPM QMQMGMMGTQ PYAQQPMQTP PHSNMMYTAP
GHHGYMNTGM SKQSLNGSYM RR
//
