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Database: UniProt/SWISS-PROT
Entry: SE1BA_DANRE
LinkDB: SE1BA_DANRE
Original site: 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   05-DEC-2018, entry version 87.
DE   RecName: Full=Histone-lysine N-methyltransferase SETD1B-A;
DE            EC=2.1.1.43;
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   Cyprinidae; 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.,
RA   Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L.,
RA   McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C.,
RA   Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T.,
RA   Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T.,
RA   Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F.,
RA   Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H.,
RA   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., Eliott D., Threadgold G.,
RA   Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B.,
RA   Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S.,
RA   Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C.,
RA   Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H.,
RA   Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C.,
RA   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.,
RA   Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S.,
RA   Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R.,
RA   Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R.,
RA   Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R.,
RA   Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A.,
RA   Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Osoegawa K., Zhu B., Rapp A., Widaa S.,
RA   Langford C., Yang F., Carter N.P., Harrow J., Ning Z., Herrero J.,
RA   Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C.,
RA   Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H.,
RA   Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J.,
RA   Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the
RT   human 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.,
RA   Chen Y., Chen S.-J., Huang Q.-H., Liu T.X., Chen Z.;
RT   "Genome-wide survey and developmental expression mapping of zebrafish
RT   SET domain-containing genes.";
RL   PLoS ONE 3:E1499-E1499(2008).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1138, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18307296; DOI=10.1021/pr700667w;
RA   Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B.,
RA   den Hertog J., Slijper M., Heck A.J.R.;
RT   "Online automated in vivo zebrafish phosphoproteomics: from large-
RT   scale analysis down to a single embryo.";
RL   J. Proteome Res. 7:1555-1564(2008).
CC   -!- FUNCTION: Histone methyltransferase that specifically methylates
CC       'Lys-4' of histone H3, when part of the SET1 histone
CC       methyltransferase (HMT) complex, but not if the neighboring 'Lys-
CC       9' residue is already methylated. H3 'Lys-4' methylation
CC       represents a specific tag for epigenetic transcriptional
CC       activation (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Chromosome
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
DR   EMBL; BX088560; CAK10781.2; -; Genomic_DNA.
DR   EMBL; DQ851809; ABI34481.1; -; mRNA.
DR   RefSeq; NP_001038599.2; NM_001045134.2.
DR   UniGene; Dr.80156; -.
DR   ProteinModelPortal; 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   eggNOG; COG2940; LUCA.
DR   HOGENOM; HOG000168216; -.
DR   HOVERGEN; HBG055596; -.
DR   InParanoid; Q1LY77; -.
DR   KO; K11422; -.
DR   PhylomeDB; Q1LY77; -.
DR   PRO; PR:Q1LY77; -.
DR   Proteomes; UP000000437; 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; IEA:InterPro.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase 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:0051568; P:histone H3-K4 methylation; IEA:InterPro.
DR   CDD; cd12549; RRM_Set1B; 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; IPR034468; Set1B_RRM.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR037842; SETD1B.
DR   PANTHER; PTHR22884:SF475; PTHR22884:SF475; 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   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; Complete proteome;
KW   Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW   RNA-binding; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN         1   1844       Histone-lysine N-methyltransferase
FT                                SETD1B-A.
FT                                /FTId=PRO_0000316996.
FT   DOMAIN      128    216       RRM. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00176}.
FT   DOMAIN     1705   1822       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     1828   1844       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   COMPBIAS    375    786       Pro-rich.
FT   COMPBIAS    952   1116       Glu-rich.
FT   COMPBIAS   1000   1080       Ser-rich.
FT   COMPBIAS   1172   1435       Pro-rich.
FT   MOD_RES    1138   1138       Phosphoserine.
FT                                {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
//
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