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Database: UniProt
Entry: Q8CFT2
LinkDB: Q8CFT2
Original site: Q8CFT2 
ID   SET1B_MOUSE             Reviewed;        1985 AA.
AC   Q8CFT2; Q80TK9; Q8CFQ8; Q8CGD1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   13-FEB-2019, entry version 130.
DE   RecName: Full=Histone-lysine N-methyltransferase SETD1B;
DE            EC=2.1.1.43;
DE   AltName: Full=SET domain-containing protein 1B;
GN   Name=Setd1b; Synonyms=Kiaa1076, Set1b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 883-1985 (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Eye, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1090-1985 (ISOFORM 2).
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=17355966; DOI=10.1074/jbc.M609809200;
RA   Lee J.-H., Tate C.M., You J.-S., Skalnik D.G.;
RT   "Identification and characterization of the human Set1B histone H3-
RT   Lys4 methyltransferase complex.";
RL   J. Biol. Chem. 282:13419-13428(2007).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1283; SER-1301; SER-1678
RP   AND SER-1682, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
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. The non-overlapping localization with SETD1B suggests
CC       that SETD1A and SETD1B make non-redundant contributions to the
CC       epigenetic control of chromatin structure and gene expression (By
CC       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   -!- SUBUNIT: Component of the SET1 complex, at least composed of the
CC       catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5,
CC       ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30. Interacts with HCFC1. and
CC       ASH2L/ASH2. Interacts (via the RRM domain) with WDR82. Interacts
CC       (via the RRM domain) with hyperphosphorylated C-terminal domain
CC       (CTD) of RNA polymerase II large subunit (POLR2A) only in the
CC       presence of WDR82. Binds specifically to CTD heptad repeats
CC       phosphorylated on 'Ser-5' of each heptad. Interacts with RBM15 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Chromosome
CC       {ECO:0000250}. Note=Localizes to a largely non-overlapping set of
CC       euchromatic nuclear speckles with SETD1A, suggesting that SETD1A
CC       and SETD1B each bind to a unique set of target genes.
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8CFT2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CFT2-2; Sequence=VSP_030851;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC       {ECO:0000269|PubMed:17355966}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
DR   EMBL; AC158114; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC038367; AAH38367.2; -; mRNA.
DR   EMBL; BC040775; AAH40775.1; -; mRNA.
DR   EMBL; BC041681; AAH41681.1; -; mRNA.
DR   EMBL; AK122435; BAC65717.1; -; mRNA.
DR   CCDS; CCDS59684.1; -. [Q8CFT2-1]
DR   RefSeq; NP_001035488.2; NM_001040398.2. [Q8CFT2-1]
DR   UniGene; Mm.250391; -.
DR   ProteinModelPortal; Q8CFT2; -.
DR   SMR; Q8CFT2; -.
DR   BioGrid; 228940; 2.
DR   STRING; 10090.ENSMUSP00000133933; -.
DR   iPTMnet; Q8CFT2; -.
DR   PhosphoSitePlus; Q8CFT2; -.
DR   PaxDb; Q8CFT2; -.
DR   PeptideAtlas; Q8CFT2; -.
DR   PRIDE; Q8CFT2; -.
DR   Ensembl; ENSMUST00000056053; ENSMUSP00000134686; ENSMUSG00000038384. [Q8CFT2-1]
DR   Ensembl; ENSMUST00000163030; ENSMUSP00000133933; ENSMUSG00000038384. [Q8CFT2-1]
DR   Ensembl; ENSMUST00000174836; ENSMUSP00000134461; ENSMUSG00000038384. [Q8CFT2-2]
DR   GeneID; 208043; -.
DR   KEGG; mmu:208043; -.
DR   UCSC; uc008zng.2; mouse. [Q8CFT2-1]
DR   CTD; 23067; -.
DR   MGI; MGI:2652820; Setd1b.
DR   eggNOG; KOG1080; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000154575; -.
DR   HOVERGEN; HBG055596; -.
DR   InParanoid; Q8CFT2; -.
DR   KO; K11422; -.
DR   OMA; MLQQDNG; -.
DR   OrthoDB; 1234689at2759; -.
DR   TreeFam; TF106436; -.
DR   Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR   Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR   PRO; PR:Q8CFT2; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   Bgee; ENSMUSG00000038384; Expressed in 243 organ(s), highest expression level in mesenteric lymph node.
DR   ExpressionAtlas; Q8CFT2; baseline and differential.
DR   Genevisible; Q8CFT2; MM.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; ISS:UniProtKB.
DR   GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IEA:Ensembl.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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; Alternative splicing; Chromatin regulator; Chromosome;
KW   Complete proteome; Methyltransferase; Nucleus; Phosphoprotein;
KW   Reference proteome; RNA-binding; S-adenosyl-L-methionine;
KW   Transcription; Transcription regulation; Transferase.
FT   CHAIN         1   1985       Histone-lysine N-methyltransferase
FT                                SETD1B.
FT                                /FTId=PRO_0000316994.
FT   DOMAIN       92    180       RRM. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00176}.
FT   DOMAIN     1846   1963       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     1969   1985       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   COMPBIAS    373   1690       Pro-rich.
FT   COMPBIAS   1031   1179       Ser-rich.
FT   COMPBIAS   1059   1331       Glu-rich.
FT   MOD_RES     977    977       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9UPS6}.
FT   MOD_RES     985    985       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9UPS6}.
FT   MOD_RES    1022   1022       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9UPS6}.
FT   MOD_RES    1283   1283       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1301   1301       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1354   1354       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9UPS6}.
FT   MOD_RES    1678   1678       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1682   1682       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   VAR_SEQ    1139   1179       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:12693553}.
FT                                /FTId=VSP_030851.
FT   CONFLICT   1222   1222       A -> V (in Ref. 3; BAC65717).
FT                                {ECO:0000305}.
FT   CONFLICT   1411   1411       S -> G (in Ref. 3; BAC65717).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1985 AA;  215352 MW;  760EA261769292EC CRC64;
     MENSHPHHHH QQPPPQPGPS GERRNHHWRS YKLMIDPALK KGHHKLYRYD GQHFSLAMSS
     NRPVEIVEDP RVVGIWTKNK ELELSVPKFK IDEFYVGPVP PKQVTFAKLN DNVRENFLRD
     MCKKYGEVEE VEILYNPKTK KHLGIAKVVF ATVRGAKEAV QHLHSTSVMG NIIHVELDTK
     GETRMRFYEL LVTGRYTPQT LPVGELDAIS PIVSETLQLS DALKRLKDGS LSAGCGSGSS
     SVTPNSGGTP FSQDTAYSSC RLDTPNSYGQ GTPITPRLGT PFSQDSSYSS RQPTPSYLFS
     QDPTATFKAR RHESKFTDAY NRRHEHHYVH NSAVAGATAP FRGSSDLSFG TVGSSGTPFK
     AQSQDATTFA HTPPPAQTAT ASGFKSAFSP YQTPAPPFPP PPEEPTATAA FGSRDSGEFR
     RAPAPPPLPP AEPPAKEKPG TPPGPPPPDS NSMELGGRPT FGWSPEPCDS PGTPTLESSP
     AGPEKPHDSL DSRIEMLLKE QRTKLPFLRE QDSDTEIQME GSPISSSSSQ LSPLSHFGTN
     SQPGFRGPSP PSSRPSSTGL EDISPTPLPD SDEDEDLGLG LGPRPPPEPG PPDPMGLLGQ
     TAEVDLDLAG DRTPTSERMD EGQQSSGEDM EISDDEMPSA PITSADCPKP MVVTPGAGAV
     AAPNVLAPNL PLPPPPGFPP LPPPPPPPPP QPGFPMPPPL PPPPPPPPPA HPAVTVPPPP
     LPAPPGVPPP PILPPLPPFP PGLFPVMQVD MSHVLGGQWG GMPMSFQMQT QMLSRLMTGQ
     GACPYPPFMA AAAAAASAGL QFVNLPPYRS PFSLSNSGPG RGQHWPPLPK FDPSVPPPGY
     IPRQEDPHKA TVDGVLLVVL KELKAIMKRD LNRKMVEVVA FRAFDEWWDK KERMAKASLT
     PVKSGEHKDE DRPKPKDRIA SCLLESWGKG EGLGYEGLGL GIGLRGAIRL PSFKVKRKEP
     PDTASSGDQK RLRPSTSVDE EDEESERERD RDIADAPCEL TKRDPKSVGV RRRPGRPLEL
     DSGGEEDEKE SLSASSSSSA SSSSGSSTTS PSSSASDKEE EDRESTEEEE EEEEEEAEEE
     EEEGPRSRIS SPSSSSSSDK DDEDDNEADS DGQIDSDIDD QGAPLSEASE KDNGDSEEEE
     TESITTSKAP AESSSSSSES SGSSEFESSS ESESSSSSSE DEEEMTVPGV EEEEEEEEEE
     EKETAMAAAT VVAMAEESMP PAGGQDFEQD RAEVPLGPRG PMRESLGTEE EVDIEAEDEV
     PEMQAPELEE PPLPMGARKL EGSPEPPEEP GPNTQGDMLL SPELPARETE EAQLPSPPEH
     GPESDLDMEP EPPPMLSLPL QPPLPPPRLL RPPSPPPEPE TPEPPKPPVP LEPPPEDHPP
     RTPGLCGSLA KSQSTETVPA TPGGEPPLSG SSSGLSLSSP QVPGSPFSYP SPSPGLSSGG
     LPRTPGRDFS FTPTFPEPSG PLLLPVCPLP TGRRDERTGP LASPVLLETG LPLPLPLPLP
     LPLALPVPVL RAQPRPPPQL PPLLPATLAP CPTPIKRKPG RPRRSPPSML SLDGPLVRPP
     PGPALGRDLL LLPGQPPAPI FPSAHDPRAV TLDFRNTGIP APPPPLPPQP PPPPPPPPVE
     STKLPFKELD NQWPSEAIPP GPRRDEVTEE YVDLAKVRGP WRRPPKKRHE DLVAPSASPE
     PSPPQPLFRP RSEFEEMTIL YDIWNGGIDE EDIRFLCVTY ERLLQQDNGM DWLNDTLWVY
     HPSTSLSSAK KKKREDGIRE HVTGCARSEG FYTIDKKDKL RYLNSSRAST DEPPMDTQGM
     SIPAQPHAST RAGSERRSEQ RRLLSSFTGS CDSDLLKFNQ LKFRKKKLKF CKSHIHDWGL
     FAMEPIAADE MVIEYVGQNI RQVIADMREK RYEDEGIGSS YMFRVDHDTI IDATKCGNFA
     RFINHSCNPN CYAKVITVES QKKIVIYSKQ HINVNEEITY DYKFPIEDVK IPCLCGSENC
     RGTLN
//
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