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Database: UniProt
Entry: G3NGA8_GASAC
LinkDB: G3NGA8_GASAC
Original site: G3NGA8_GASAC 
ID   G3NGA8_GASAC            Unreviewed;      2094 AA.
AC   G3NGA8;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Ash1 (absent, small, or homeotic)-like (Drosophila) {ECO:0000313|Ensembl:ENSGACP00000004363.3};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000004363.3, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000004363.3, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000004363.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   STRING; 69293.ENSGACP00000004363; -.
DR   Ensembl; ENSGACT00000004377.3; ENSGACP00000004363.3; ENSGACG00000003327.3.
DR   eggNOG; KOG1083; Eukaryota.
DR   GeneTree; ENSGT00940000156698; -.
DR   InParanoid; G3NGA8; -.
DR   OMA; DKDNGHE; -.
DR   TreeFam; TF106416; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000003327; Expressed in telencephalon and 13 other cell types or tissues.
DR   GO; GO:0005694; C:chromosome; IEA:UniProt.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0140938; F:histone H3 methyltransferase activity; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:UniProt.
DR   CDD; cd04717; BAH_polybromo; 1.
DR   CDD; cd05525; Bromo_ASH1; 1.
DR   CDD; cd15548; PHD_ASH1L; 1.
DR   CDD; cd19174; SET_ASH1L; 1.
DR   Gene3D; 2.30.30.490; -; 1.
DR   Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR   InterPro; IPR006560; AWS_dom.
DR   InterPro; IPR001025; BAH_dom.
DR   InterPro; IPR043151; BAH_sf.
DR   InterPro; IPR043320; Bromo_ASH1L.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR043319; PHD_ASH1L.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46147; HISTONE-LYSINE N-METHYLTRANSFERASE ASH1; 1.
DR   PANTHER; PTHR46147:SF2; SET-BINDING PROTEIN; 1.
DR   Pfam; PF17907; AWS; 1.
DR   Pfam; PF01426; BAH; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF20826; PHD_5; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00384; AT_hook; 5.
DR   SMART; SM00570; AWS; 1.
DR   SMART; SM00439; BAH; 1.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS51215; AWS; 1.
DR   PROSITE; PS51038; BAH; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
PE   4: Predicted;
KW   Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW   ProRule:PRU00035}; Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          1211..1262
FT                   /note="AWS"
FT                   /evidence="ECO:0000259|PROSITE:PS51215"
FT   DOMAIN          1265..1381
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          1389..1405
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   DOMAIN          1574..1644
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          1780..1917
FT                   /note="BAH"
FT                   /evidence="ECO:0000259|PROSITE:PS51038"
FT   REGION          1..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          171..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          281..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          529..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          616..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          702..741
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          801..859
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          950..1111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1428..1456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1673..1698
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1954..2046
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..240
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        302..332
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..634
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        821..843
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        844..859
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        990..1004
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1078..1094
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1677..1698
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1968..2020
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2021..2040
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2094 AA;  237317 MW;  CBCB01CC563EEA13 CRC64;
     KRGRPKSIMP RLDGPARGCL PNKLVPSKVF SSLLKSKEEQ DPPVLHPEVD LNPPKPMPRK
     RGRPKRLPPT LPQEGQPPTL APEAGDMGDK RFRTKGNGQL IMKTIIGKIN KMKSMRRKRI
     LSQILLGPRP EDTPKCTTSG VVGSVEAATQ SLSSLAASFG GKLGPQINVS KKGTIYMGKR
     RGRKPKSASN STTPPPEPFL SPNTTSPLHH HQSHQHHQLS SSEVFPSPSL SQSSGGHSPI
     SDASFVEPGS VHFAAASQKK SSYRGYQHDH HYRQHYHYHR LSPSRPLHPT SPAPLSELKE
     ATPSPVSESH SEETVPSDSG IGTDNNSTSD RGEKAGGLGG ARSSPDPRRP HPAAPASSLI
     GHKDKHKHKC KRRTHGCPGY DKLKRQKRKR KKKFLQLRSR RHDPDFLAEL EEIVVRLSEI
     RITHRGPPPH HYVHRDLLPT IFRVNFGSFY SHPAYSCDPL HYVRKPDMKK KRGRPPKLRE
     SMSEVPFVPG LGFPLSSGGF YHPSYAVPYS SGPLGLGYYR GYPPASALYP HPHHQSPHTA
     PSHHSHHSPS FPPPPPTSYM HHHHPSHLLL NPSKFHKKKH KLLRQDYLGG GRSPVLYPPM
     SSELSFNWHH KHKHRHKHRE RCSEDDREEA ARAGSASRAR MAESLQRCRF GRDAASTKRY
     KRKESSMSCL GPSRLALGNG SKGHQPVESW FRMGSSKASY SKLSRSHVAP GQAGCSDSED
     EEPLSPTEDV EPGAHDSPNR TNLFASALTR TTLKGGKNRK TEAVTESSAF SRIDRPIRKD
     LGGKTLKEGD IACQTFSGIR MQDPAPQQWP SEGLTECPLT KTDLSGGSLR SSLQNGTTKG
     GHSSSESDES ETKLKKRNVE NEDEAIVLSY CSSIQGVALS PPEGPDVPMH HRQQHHHLQP
     SMFHSHGSAS SSCLSPSQDC CLDASPPHHS HRAQPSKHSL HHVNKILRAK KLQRQARTGN
     NVVKKRGPGR PRKHPLPSPL PSPPPAVELN QVRHRDRVTE RPVGGRGWEG DTVTDAIEAV
     VQGQRRKSQK RKQWAGDEEE EEEEDEDEED GEKPSHGSLS SAMESKPDGQ CSPDRPTTAP
     PEQAPPMPVI PQREKRPARP PKKKFQKAGL YSNVYKTEDP RSQLLQLKKE KLEYIPGEHE
     FGLFPSPIHF NFLPCFVFSG KYLRQKRIDF QLPYDILWLW KHDQLYKRPD VPLYKKIRSN
     VYVDVKPLSG YETTTCSCKQ REDSTEKGCL DECLNRMSYA ECSPSTCPSG DQCDNQHIQR
     HDWVQCLERF RAEGKGWGIR TKETLRSGQF IIEYLGEVVS EQEFRSRMME QYFAHSGQYC
     LNLDSGMVID SYRMGNEARF INHSCEPNCE MQKWSVNGVY RIGLFALKDI NSGIELTYDY
     NFHSFNTEEQ QACKCGSESC RGIIGGKSQR INGLPGKTGG TRRLGRLKEK RKSKHQLKKR
     VSEEESSDSN KFYPHLMKPM SNRERNFVLK HRVFLLRNWE KMREKQELLK REGERERDPG
     SLSLYTRWGG VIRDDGNIKS DVFLTQFSAL QTSRSVRTRR LAAAEENTEV TRTARLAHIF
     KEICDMITSY KDSAGQTLAA PLVNLPSRKR NSQYYEKVSD PLDLSTIEKQ ILTGHYKTVE
     AFDTDMLKVF RNAEKYYGRK SSVGRDVCRL RKAYYSARHE AAVQIDEIVG ETASEADSSD
     SLERDHGHHH GGGGPGPHDK DDDVIRCICG MYKDEGLMIQ CEKCMVWQHF DCMRLESEVE
     HYLCELCDPR PVDREVPMIP QPSYAQAGSV YYICLLRDEL LLHQGDCVYL MRDSRRTPEG
     QPVRQSYRLL SHVNRDKLDI FRIEKLWKNE KGERFAFGHH YFRPHETHHS PSRRFYQNEL
     FRMPLYEIIP LEAVVATCCV LDLYTYCKGR PKGVKEQDVY ICDYRLDKSA HLFYKIHRNR
     FPVCTKLYAF NHFPKRLAPK RDFSPHYVPD NYKRNGGRSA WKSDLPKGAA GCEDDDSPRE
     RADDFPPEAE GGRGEEDDAD KNPDEPELSA KPRGAERERD GEGDEDEDEK EEEEEGQESE
     ERDAQRDRLN KILLDLLYRS PNKNAIDVSY LLEEGAGRRL RRRALGFGDF VGRK
//
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