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Database: UniProt
Entry: A0A1S3WEI7_ERIEU
LinkDB: A0A1S3WEI7_ERIEU
Original site: A0A1S3WEI7_ERIEU 
ID   A0A1S3WEI7_ERIEU        Unreviewed;      2995 AA.
AC   A0A1S3WEI7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   SubName: Full=Histone-lysine N-methyltransferase ASH1L isoform X2 {ECO:0000313|RefSeq:XP_016044697.1};
GN   Name=ASH1L {ECO:0000313|RefSeq:XP_016044697.1};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016044697.1};
RN   [1] {ECO:0000313|RefSeq:XP_016044697.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   RefSeq; XP_016044697.1; XM_016189211.1.
DR   GeneID; 103115552; -.
DR   CTD; 55870; -.
DR   OrthoDB; 2882778at2759; -.
DR   Proteomes; UP000079721; Unplaced.
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: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; 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:UP000079721};
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          2117..2168
FT                   /note="AWS"
FT                   /evidence="ECO:0000259|PROSITE:PS51215"
FT   DOMAIN          2171..2287
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          2295..2311
FT                   /note="Post-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50868"
FT   DOMAIN          2489..2559
FT                   /note="Bromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50014"
FT   DOMAIN          2687..2824
FT                   /note="BAH"
FT                   /evidence="ECO:0000259|PROSITE:PS51038"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          120..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          535..585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          823..843
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          876..951
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1097..1123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1148..1228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1240..1278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1486..1505
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1522..1542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1575..1705
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1909..1941
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2314..2367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2851..2883
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2903..2945
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..145
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..582
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        823..839
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        920..935
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1162..1211
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1212..1227
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1575..1637
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1654..1699
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1909..1934
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2315..2332
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2335..2352
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2864..2883
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2904..2930
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2995 AA;  336436 MW;  D697FAAE079E9E46 CRC64;
     MDHRNTAMLG LGSDSEGFSR KSPSAINTGT LVSKREIELE SNTKEEEDLL KWNRERKTEA
     GKDDCLAAAQ QQFSVKETNF SEGNLKLKIG LQAKRTKKPP KNLENYVCRP AIKTTIKHPR
     KTLKSGKMTD EKNEHCPSKR DSSKLYKKAG DSAAIECHSE ESIHLHSQGE NNSLSKKLSP
     VHSEMTDYMN AASLVGSRDP DFKDRALLNG GTTVTEKLAQ LIATCPPSKS SKTKPKKLVT
     GTTAGLVSKD LIRKASVSTV AGIIHKDLIK KPTISTAVGL VTKDPGKKSV FNATVGLVNK
     DSMKKLGTGT TTVFINKDLG KKPGTITTVG LLSKDSGKKL GIGIVPGLVN KESGKKLGLG
     TVVGLVNKDL GKKLGSTVGL MAKDCAKKIV ASSAMGLINK DIGKKIVSCP MAGLISRDSI
     NLKAEALLPP QELHKVSCST NISSHENQDI SESMKDSATG KIFEKNVLRQ SKENILEKFS
     VRREINNLEK QMFNEGTCIQ QDSFSPIERG PYEISKHEKQ PPVYCTSPDF QMGGASDMST
     AKSPFSAVGE SNLPSPSPTV SVNPLTRNSP ETSSQMAHNP LHLSPTTDLM EDISESVGKR
     QFTSESTHLN ISHRSMGHSI NIECKGIDKE LNDSRTTHID IPRISSSLGK KPSLTSESSI
     HTITPSVVNF TSLFSNKPFL KLGAVAASDK HCQVTESLSS SLQSKPLKKR KGRKPRWTKV
     VARSTCRSPK GLELERSELF KNVSCSSLSS SNSEQAKFMK NIGSSSFVDH DFLKRRLPKL
     SKSTTPSLAL LTDSEKTSHK SFATHKLSSS MCVSSDLLSD IYKPKRGRPK SKEMPQLEGP
     PKRTLKIPAS KVFSLQSKEE QEPPILQPEI EIPSFKQSIS LSPFPKKRGR PKRQMRSPVK
     MKPPVLSVAP FVATESPSKI ESESDNHRSS SDFFESEDQL QDPDDLDDSH RSTVCSMSDL
     EMEPDKKITK RNNGQLMKTI IRKINKMKTL KRKKLLNQIL SSSVESSKGK VQSKLHNTVS
     SLAATFGSKL GQQINVSKKG TIYIGKRRGR KPKTVLNGLL SGSPTSLAVL EQTAQQAAGS
     ALGQILPPLL PSSASSSEIL PSPICSQSSG TSGGQSPVSS DAGFVEPSSL PYLHLHSRQG
     SMIQTLAMKK ASKGRRRLSP PTLLPNSPSH LSELTSLKEA TPSPISESHS DETIPSDSGI
     GTDNNSTSDR AEKFCGQKKR RHSFEHVSLI PPETSTVLSS LKEKHKHKCK RRNHDYLSYD
     KMKRQKRKRK KKYPQLRNRQ DPDFIADLEE LISRLSEIRI THRSHHFIPR DLLPTIFRIN
     FNSFYTHPSF PLDPLHYIRK PDLKKKRGRP PKMREAMAEM PFMHSLSFPL SSTGFYPSYG
     MPYSPSPLTA APIGLGYYGR YTPTIYPPPP SPSFTTPLPP PSYMHAGHLL LNPTKYHKKK
     HKLLRQEAFL TTSRTPLLSM STYPSVPPEM AYGWMVEHKH RHRHKHREHR SSEQPQVSMD
     TGSSRSVLES LKRYRFGKDT VGERYKHKDK HRCHMSYPHL SPSKSLINRE EQWVHREPSE
     SSSLTLGLQT PLQIDCSESS PSLSLGGFTP NSDPASNDEH TNLFTSAIGS CRVSNPNSSG
     RKKLTDSPGL FSAQDTSLNR PHRKEPLPSS ERAVPTLTGA QPASDKSSHR PSESTNCSPT
     RRRSSSESTS STVNGVPSRS PRLVVSGDES VDSLLQRMVQ HEDQDPLEKN IDAVIASVSV
     PPSSSPGHIH NKERTLSKSD SLLVPAVPSD SCSNSISLLS EKLPSSCSPH HIKRSVVEAM
     QRQARKMCNY DKILATKKNL DHVNKILKAK KLQRQARTGN NFVKRRPGRP RKCPLQAVVS
     MQAFQAAQFV NSELNEVEEG TALHLNPDTV TDVIEAVVQS VNLNPEHKKG LKRKSWLLDE
     QTKKKQKPFP EGGGGEEENT KSFSDAAVEI LSPPEVPAKP SEPENTLQSV LSLIPREKKT
     PRPPKKKYQK AGLYSDVYKT ADPKSRLIQL KKEKLEYTPG EHEYGLFPAP IHVVQVVGDY
     PSSSVCKAES SPGQNTPSSQ AALTPRKYLR QKRIDFQLPY DILWQWKHNQ LYKKPDVPLY
     KKIRSNVYVD VKPLSGYEAT TCNCKKPDDD IRKGCMDDCL NRMIFAECSP NTCPCGEQCC
     NQRIQRHEWV QCLERFRAEE KGWGIRTKEP LKAGQFIIEY LGEVVSEQEF RNRMIEQYHN
     HSDHYCLNLD SGMVIDSYRM GNEARFINHS CDPNCEMQKW SVNGVYRIGL YALKDMPAGT
     ELTYDYNFHS FNVEKQQLCK CGFEKCRGII GGKSQRMNGL TSSKTSQPMN THKKSGRSKE
     KRKSKHKLKK RRGHLSEEPS ESINTPTRLT PQLQMKPMSN RERNFVLKHH VFLVRNWEKI
     RQKQEEVKHT NDNIHSASLY TRWNGMCRDD GNIKSDVFMT QFSALQTARS VRTRRLAAAE
     ENIEVARAAR LAQIFKEICD GIISYKDSSR QALAAPLLNL PPKKKNADYY EKISDPLDLV
     TIEKQILIGY YKTVEAFDAD MLKVFRNAEK YYGRKSPIGR DVCRLRKAYY NARHEASAQI
     DEIVGETASE ADSSETSVSE KENGHEKDDD VIRCICGLYK DEGLMIQCDK CMVWQHCDCM
     GVNSDVEHYL CEQCDPRPVD REVPMIPRPH YAQPGCVYFI CLLRDDLLLR QGDCVYLMRD
     SRRTSDGHPV RQSYRLLSHI NRDKLDIFRI EKLWKNEKEE RFAFGHHYFR PHETHHSPSR
     RFYHNELFRV PLYEIIPLEA VVGTCCVLDL YTYCKGRPKG VKEQDVYICD YRLDKSAHLF
     YKIHRNRYPV CTKPYAFDHF PKKLTPKRDF SPHYVPDNYK RNGGRSSWKS ERSKPPLKDL
     GQEDDALPLI EEVLASQEQA ANEMPGLEER EQEGGTTDIS ENEKKTEENS QEPQPACTPE
     ERRHNQRERL NQILLNLLEK IPGKNAIDVT YLLEEGSGRK LRRRTLFMPE HSFRK
//
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