GenomeNet

Database: UniProt
Entry: A0A3Q1M5X3_BOVIN
LinkDB: A0A3Q1M5X3_BOVIN
Original site: A0A3Q1M5X3_BOVIN 
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
//
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