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   27-MAR-2024, entry version 111.
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   -!- SUBUNIT: Component of the SET1B/COMPASS complex.
CC       {ECO:0000250|UniProtKB:Q9UPS6}.
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q9UPS6}.
CC       Chromosome {ECO:0000250|UniProtKB:Q9UPS6}.
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.ENSDARP00000130529; -.
DR   iPTMnet; Q1LY77; -.
DR   PaxDb; 7955-ENSDARP00000080600; -.
DR   GeneID; 567970; -.
DR   KEGG; dre:567970; -.
DR   AGR; ZFIN:ZDB-GENE-050309-289; -.
DR   CTD; 567970; -.
DR   ZFIN; ZDB-GENE-050309-289; setd1ba.
DR   eggNOG; KOG1080; Eukaryota.
DR   InParanoid; Q1LY77; -.
DR   OrthoDB; 950362at2759; -.
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   Reactome; R-DRE-9772755; Formation of WDR5-containing histone-modifying complexes.
DR   PRO; PR:Q1LY77; -.
DR   Proteomes; UP000000437; Alternate scaffold 10.
DR   Proteomes; UP000000437; Chromosome 10.
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 H3K4 methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0140999; F:histone H3K4 trimethyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:ZFIN.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd12549; RRM_Set1B; 1.
DR   CDD; cd19169; SET_SETD1; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 2.170.270.10; SET domain; 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; IPR034468; Set1B_RRM.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR037841; SET_SETD1A/B.
DR   PANTHER; PTHR45814; HISTONE-LYSINE N-METHYLTRANSFERASE SETD1; 1.
DR   PANTHER; PTHR45814:SF1; HISTONE-LYSINE N-METHYLTRANSFERASE SETD1B; 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; RNA-binding domain, RBD; 1.
DR   SUPFAM; SSF82199; SET domain; 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   MOTIF           1678..1683
FT                   /note="RxxxRR motif"
FT                   /evidence="ECO:0000250|UniProtKB:P38827"
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   BINDING         1821
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
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
//