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
//