ID A0A3Q1M5X3_BOVIN Unreviewed; 2721 AA.
AC A0A3Q1M5X3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=ASH1 like histone lysine methyltransferase {ECO:0000313|Ensembl:ENSBTAP00000065339.1};
GN Name=ASH1L {ECO:0000313|Ensembl:ENSBTAP00000065339.1,
GN ECO:0000313|VGNC:VGNC:50606};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000065339.1, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000065339.1, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000065339.1,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000065339.1}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000065339.1};
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR Ensembl; ENSBTAT00000070269.1; ENSBTAP00000065339.1; ENSBTAG00000003954.6.
DR VEuPathDB; HostDB:ENSBTAG00000003954; -.
DR VGNC; VGNC:50606; ASH1L.
DR GeneTree; ENSGT00940000156698; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000003954; Expressed in neutrophil and 111 other cell types or tissues.
DR ExpressionAtlas; A0A3Q1M5X3; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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; 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:SF1; HISTONE-LYSINE N-METHYLTRANSFERASE ASH1L; 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; 4.
DR SMART; SM00570; AWS; 1.
DR SMART; SM00439; BAH; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 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; 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|PROSITE-ProRule:PRU00035};
KW 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:UP000009136};
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 1843..1894
FT /note="AWS"
FT /evidence="ECO:0000259|PROSITE:PS51215"
FT DOMAIN 1897..2013
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 2021..2037
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT DOMAIN 2215..2285
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 2413..2550
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT REGION 317..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1059..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1396..1527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1733..1763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2040..2094
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2577..2609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2625..2670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..657
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..753
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..1030
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1046
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1396..1456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1470..1527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2041..2058
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2061..2078
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2590..2609
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2631..2670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2721 AA; 305273 MW; 22FD61C713DA4A5B CRC64;
MTDYINATSS TLVGSRDPDL KDRALLNGGT SVTEKLAQLI ATCPPSKSSK TKPKKLATGT
TAGLVSKDLI RKAGVGSVAG IIHKDLIKKP TISTAVGLVT KDPGKKPVFN ATVGLVNKDS
VKKLGTGTTT VFINKDLGKK PGAITTVGLL SKDTGKKLGI GIVPGLVNKE PGKKLGLGTV
VGLVNKDLGK KLGSTVGLVA KDCAKKIVAN STVGLVNKDI GKKLVSCPMT GLVNKDAINL
KAEALLPTQE PLKASCSTNI ISHESQDLSE SLKDGATSKT FEKNVTRQSK ESILEKFSVR
KEIINLEKEM FNEGTCIQQD SFSSSERGSY ETSKHEKQPP VYCTSPDFQM GVASDASTAK
SPFSAVGESN LPSPSPTVSV NPLSRSPPET SSQMTPNPLL LSPTTELMEE ISESVGKNQF
TSESTHLNIG HRSMGHSMNI ECKGIDKELN DSKTTHIDIS RINSSLGKKP SLTSESSIHT
ITPSVVNFTS LFSNKPFLKL GAVSASDKHC QVAESLSTTL QSKPLKKRKG RKPRWTKVVA
RSTCRSPKGL ELERSELFKN VTCSSLSNSN SEPAKFMKNI GPSSFVDHDF LKRRLPKLSK
STAPSLALLT DSEKPSHKSF ATHKLSSSMC VSSDLLSDIY KPKRGRPKSK EMPQLEGPPK
RTLKIPASKV FSLQSKEEQE PPILQPEIEI PSFKQSLSVS PFPKKRGRPK RQMRSPVKMK
PPVLSVAPFV ATESPSKLES ESDNHRSSSD FFESEDQLQD PDDLDDSHRP TVCSMSDLEM
EPDKKITKRN NGQLMKTIIR KINKMKTLKR KKLLNQILSS SVESSNKGKV QSKLHNTVSS
LAATFGSKLG QQINVSKKGT IYIGKRRGRK PKTVLNGILS GSPTSLAVLE QTAQQAAGSA
LGQILPPLLP SSASSSEILP SPICSQSSGT SGGQSPVSSD AGFVEPSSVP YLHLHSRQGS
MIQTLAMKKA SKGRRRLSPP TLLPNSPSHL SELTSLKEAT PSPISESHSD ETIPSDSGIG
TDNNSTSDRA EKFCGQKKRR HSFEHVSLIP PETSTVLSSL KEKHKHKCKR RNHDYLSYDK
MKRQKRKRKK KYPQLRNRQD PDFIADLEEL ISRLSEIRIT HRSHHFIPRD LLPTIFRINF
NSFYTHPSFP LDPLHYIRKP DLKKKRGRPP KMREAMAEMP FMHSLSFPLS STGFYPSYGM
PYSPSPLTAA PIGLGYYGRY PPTLYPPPPS PSFTTPLPPP SYMHAGHLLL NPTKYHKKKH
KLLRQEAFLT TSRTPLLSMS TYPSVPPEMA YGWMVEHKHR HRHKHREHRS SEQPQVSMDA
GSSRSVLESL KRYRFGKDTV GERYKHKEKH RCHMSCPHLS PSKSLINREE QWVHREPSES
SPLALGLQTP LQIDCSESSP SLSLGGFTPN SDPASSDEHT NLFTSAIGSC RVSNPNSSGR
KKLTDSPGLF SAQDTSLNRP HRKEPLPSSE RAVQTLTGSQ PASDKSSQRP SESTNCSPAR
KRSSSESTSS TVNGVPSRSP RLVSSGDDSV DSLLQRMVQH EDQEPLEKNI DAVIASASVP
PSSSPVHSLS KERTLGKPDS LLVPAVPSDS CSSSISLLSE KLPSSHSPHH IKRSVVEAMQ
RQARKMCNYD KILATKKNLD HVNKILKAKK LQRQARTGNN FVKRRPGRPR KCPLQAVVSM
QAFQAAQFVG SELNEGEEGT ALHLGPDTVT DVIEAVVQSV NLNPDHKKGL KRKSWLLEEQ
TKKKQKPFPE EEEEEENAKS PKSRLIQLKK EKLEYTPGEH EYGLFPAPIH VGKYLRQKRI
DFQLPYDILW QWKHNQLYKK PDVPLYKKIR SNVYVDVKPL SGYEATTCNC KKPDDDTKKG
CVDDCLNRMI FAECSPNTCP CGEQCCNQRI QRHEWVQCLE RFRAEEKGWG IRTKEPLKAG
QFIIEYLGEV VSEQEFRNRM IEQYHNHSDH YCLNLDSGMV IDSYRMGNEA RFINHSCDPN
CEMQKWSVNG VYRIGLYALK DMPAGTELTY DYNFHSFNVE KQQLCKCGFE KCRGIIGGKS
QRMNGLTSNK SSQPVTSHKK SGRSKEKRKS KHKLKKRRGH LSEEPSENIN TPTRLTPQLQ
MKPMSNRERN FVLKHHVFLV RNWEKIRQKQ EEVKHTSDNI HSASLYTRWN GICRDDGNIK
SDVFMTQFSA LQTARSVRTR RLAAAEENIE VARAARLAQI FKEICDGIIS YKDSSRQSLA
APLLNLPPKK KNADYYEKIS DPLDLSTIEK QILIGYYKTV EAFDADMLKV FRNAEKYYGR
KSPVGRDVCR LRKAYYNARH EASAQIDEIV GETASEADSS ETSVSEKENG HEKDDDVIRC
ICGLYKDEGL MIQCDKCMVW QHCDCMGVNS DVEHYLCEQC DPRPVDREVP MIPRPHYTQP
GCVYFICLLR DDLLLRQGDC VYLMRDSRRT PDGHPVRQSY RLLSHINRDK LDIFRIEKLW
KNEKEERFAF GHHYFRPHET HHSPSRRFYH NELFRVPLYE IIPLEAVVGT CCVLDLYTYC
KGRPKGVKEQ DVYICDYRLD KSAHLFYKIH RNRYPVCTKP YAFDHFPKKL TPKRDFSPHY
VPDNYKRNGG RSSWKSERSK PPLKDLGQED DALPLIEEVL ASQEQAANEM PSLEEPEREG
ATAENSESEK KKEESSQEPQ VACTPEERRH NQRERLNQIL LNLLEKIPGK NAIDVTYLLE
EGSGRKLRRR TLFIPENSFR K
//