SE1BA_DANRE
ID SE1BA_DANRE Reviewed; 1844 AA.
AC Q1LY77; A5XCC0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Histone-lysine N-methyltransferase SETD1B-A;
DE EC=2.1.1.354 {ECO:0000250|UniProtKB:Q9UPS6};
DE AltName: Full=SET domain-containing protein 1B-A;
GN Name=setd1ba; Synonyms=setd1b; ORFNames=si:dkey-237o15.4;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1585-1740.
RX PubMed=18231586; DOI=10.1371/journal.pone.0001499;
RA Sun X.-J., Xu P.-F., Zhou T., Hu M., Fu C.-T., Zhang Y., Jin Y., Chen Y.,
RA Chen S.-J., Huang Q.-H., Liu T.X., Chen Z.;
RT "Genome-wide survey and developmental expression mapping of zebrafish SET
RT domain-containing genes.";
RL PLoS ONE 3:E1499-E1499(2008).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1138, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18307296; DOI=10.1021/pr700667w;
RA Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA Slijper M., Heck A.J.R.;
RT "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT analysis down to a single embryo.";
RL J. Proteome Res. 7:1555-1564(2008).
CC -!- FUNCTION: Histone methyltransferase that specifically methylates 'Lys-
CC 4' of histone H3, when part of the SET1 histone methyltransferase (HMT)
CC complex, but not if the neighboring 'Lys-9' residue is already
CC methylated. H3 'Lys-4' methylation represents a specific tag for
CC epigenetic transcriptional activation. {ECO:0000250|UniProtKB:Q9UPS6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537, Rhea:RHEA-
CC COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.354;
CC Evidence={ECO:0000250|UniProtKB:Q9UPS6};
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Chromosome
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; BX088560; CAK10781.2; -; Genomic_DNA.
DR EMBL; DQ851809; ABI34481.1; -; mRNA.
DR RefSeq; NP_001038599.2; NM_001045134.2.
DR AlphaFoldDB; Q1LY77; -.
DR SMR; Q1LY77; -.
DR STRING; 7955.ENSDARP00000080600; -.
DR iPTMnet; Q1LY77; -.
DR PaxDb; Q1LY77; -.
DR PRIDE; Q1LY77; -.
DR GeneID; 567970; -.
DR KEGG; dre:567970; -.
DR CTD; 567970; -.
DR ZFIN; ZDB-GENE-050309-289; setd1ba.
DR eggNOG; KOG1080; Eukaryota.
DR InParanoid; Q1LY77; -.
DR OrthoDB; 1234689at2759; -.
DR PhylomeDB; Q1LY77; -.
DR Reactome; R-DRE-3214841; PKMTs methylate histone lysines.
DR Reactome; R-DRE-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR PRO; PR:Q1LY77; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IBA:GO_Central.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:ZFIN.
DR GO; GO:0051568; P:histone H3-K4 methylation; IBA:GO_Central.
DR Gene3D; 2.170.270.10; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR024657; COMPASS_Set1_N-SET.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR044570; Set1-like.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR037842; SETD1B.
DR PANTHER; PTHR45814; PTHR45814; 1.
DR PANTHER; PTHR45814:SF1; PTHR45814:SF1; 1.
DR Pfam; PF11764; N-SET; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM01291; N-SET; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW Activator; Chromatin regulator; Chromosome; Methyltransferase; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; S-adenosyl-L-methionine;
KW Transcription; Transcription regulation; Transferase.
FT CHAIN 1..1844
FT /note="Histone-lysine N-methyltransferase SETD1B-A"
FT /id="PRO_0000316996"
FT DOMAIN 128..216
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 1705..1822
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 1828..1844
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 18..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1160..1341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1367..1499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1647..1678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..396
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..481
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..859
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..1010
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1037
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1059
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1247
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1251..1272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1279..1313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1381..1404
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1432..1451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1479..1493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1647..1674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1138
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
SQ SEQUENCE 1844 AA; 204141 MW; 020BC92CCB797E27 CRC64;
MCWKVEIVVY CKRQKPQTRG TQYVPGERNK LNEDHGRRQS SSLANGMDNS HPICSSGEKR
SHHWRSYKLI IDPALKKGSH KVYRYDGHQF STPSFGMSPV DIVRDPRIGR LWTKYKETDL
PVPKFKIDEC YVGRVPPKEV TFAKLNDNVR EGFLTDMCKK FGDIEEVEIL YNPKNKKHLG
IAKVVFETVK AAKDAVQNLH NTSVMGNIIH VELDPKGENR QRYFQRLING SYTPLTLPVG
GEEACDVSPR SLAEALMACE PSRRLFEGGS SVVAGTTPSG TNTPMSLDTA YSSLRQDTPQ
SQGTPHTPRP SGTPFSQDSS YSSRQGTPAF QANRAESSGG YKSRRHETKF QDAYNRRPER
RYVHGPTQRG NTEQPPSFKQ HQPPEPPSPA FTHTPPPPTS ANFKTAYSQY QPPIPQEYTV
ASYHQPVQRE LDYRRPPQAP PPPSTDFLPV RDRPTTPPIP EPPPAPETQP TTPPSSTPEP
CPSPTQESER NSLDSRIEML LKPFLNERGD SDAEVRMDGS PISSSSSQLS PIPPQRPSRP
SSTGLEDISP TPLPDSEDDE PIRGTASLLA NSRGMSPTNM HSKSCVGEPR TAIDKMDTGH
QSSGEDMEIS DDEMPGTPIA SGDCDKNIVV NSALSLIQTI PMPPPGFPPL PHAAGFPLPP
HHLPHHSTVS HLPSHHPMLH PLHSYGMMHF LPVDLLSSLP QLLQMPFQMQ TQMLSRMAQS
QHPYAYPYPA PSANPAAMPF GGPYPPLSVV SAPADTLHGQ PWPLPSMPQF NPAVPPPGYE
PQKEDPHKAT IDGVLMAIVK ELKAIMKKDL NRKMVEVVAF RKFDEWWDKQ ELSAKATLTP
VKTGEGKDEE KERAKPKETM SSHLPWNKGE GLGFEGMGLG IGLRGIRLPS FKVKRKQPPE
PTSTSDNKRV RPSTPVDDEL EDEESERMGR TDGSRVDPAG SSSKRRPARP LELDSEGEEE
EETSGKEESS LSDHEEEPVD DASERLSSGK DLEEEDEKKS ESHSSESESS DSSDDEASSS
SSSKSGSDSS GSESSSDYES SSEEEEEEEE EEERIVGMDD EEDVDARTST SSSTTSTSSS
DEEEVVEVKA PSTPTGPPPE EEPNELGRLE AVDEAEIDHK PSMVSLIKTK VEEVRPPSPK
GLPADELDVD LEVKIPVPKT EASLEEVGNL RPPTPTGSFA DSDQDTRPKI PTEDFPRTPG
HEGPVPLESE TTVPRSLPTP SMHLPLPPSH VPDPQSLLPP PETLPDMPVR GRLPTEEDIP
RTPGRDLMDR ARGLGKLQST DTVPVTPGSD TPLTGNSLSS PHILGSPFSY PAQSPVLSAG
IPRTPGRDLT FAPAFPDSAG LSAGLPIHRK ASSEILEEKP LFKEPLLSAS PQASLPNNAA
SSPFPGPPLP TASLPEPALP PQGSPPASIE NSFPASPKEL PVPMIDVPVP LDDTPSKKKL
VRSKNKKGIQ DSEEPQVTLI EASSLPELPV NNQYPDLPSE SIKEEDGEPA FSEKEESQVP
TIIPKVEETS FYVEEPIQKT RRQRRGWQEL LLSMHSPVAS PRRPSFMPRS DFEEMTILYD
IWNDGIDEED IRYLKITYDK MLQQDNAHDW LNDTLWVHHP PTNMGSATGV KKKRKEDGIR
DHVTGCARSE GYYKIDKKDK MKYLNSSRLQ SEEPDVDTQG KSIPAQPQVS TRAGSERRSE
QRRLLSSFSC DSDLLKFNQL KFRKKKIRFC RSHIHDWGLF AMEPIAADEM VIEYVGQNIR
QVIADMREKR YEDEGIGSSY MFRVDHDTII DATKCGNFAR FINHSCNPNC YAKVITVESQ
KKIVIYSRQP INVNEEITYD YKFPIEDEKI PCLCGAENCR GTLN
