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Database: UniProt
Entry: E9PYH6
LinkDB: E9PYH6
Original site: E9PYH6 
ID   SET1A_MOUSE             Reviewed;        1716 AA.
AC   E9PYH6;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   05-APR-2011, sequence version 1.
DT   10-APR-2019, entry version 75.
DE   RecName: Full=Histone-lysine N-methyltransferase SETD1A;
DE            EC=2.1.1.43 {ECO:0000250|UniProtKB:O15047};
DE   AltName: Full=SET domain-containing protein 1A;
GN   Name=Setd1a;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH NAP1L1.
RX   PubMed=29490266; DOI=10.1016/j.celrep.2018.02.019;
RA   Qiao H., Li Y., Feng C., Duo S., Ji F., Jiao J.;
RT   "Nap1l1 controls embryonic neural progenitor cell proliferation and
RT   differentiation in the developing brain.";
RL   Cell Rep. 22:2279-2293(2018).
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.
CC       {ECO:0000269|PubMed:29490266}.
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         Evidence={ECO:0000250|UniProtKB:O15047};
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.
CC       Interacts with ASH2/ASH2L, CXXC1/CFP1, WDR5 and RBBP5. Interacts
CC       (via the RRM domain) with WDR82. Interacts (via the RRM domain)
CC       with hyperphosphorylated C-terminal domain (CTD) of RNA polymerase
CC       II large subunit (POLR2A) only in the presence of WDR82. Binds
CC       specifically to CTD heptad repeats phosphorylated on 'Ser-5' of
CC       each heptad. Interacts with ZNF335. Interacts with SUPT6H (By
CC       similarity). Interacts with NAP1L1 (PubMed:29490266).
CC       {ECO:0000250|UniProtKB:O15047, ECO:0000269|PubMed:29490266}.
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle
CC       {ECO:0000250|UniProtKB:O15047}. Chromosome
CC       {ECO:0000250|UniProtKB:O15047}. Note=Localizes to a largely non-
CC       overlapping set of euchromatic nuclear speckles with SETD1B,
CC       suggesting that SETD1A and SETD1B each bind to a unique set of
CC       target genes. {ECO:0000250|UniProtKB:O15047}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
DR   EMBL; AC149222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS40144.1; -.
DR   RefSeq; NP_821172.2; NM_178029.3.
DR   RefSeq; XP_017177700.1; XM_017322211.1.
DR   RefSeq; XP_017177701.1; XM_017322212.1.
DR   RefSeq; XP_017177702.1; XM_017322213.1.
DR   RefSeq; XP_017177703.1; XM_017322214.1.
DR   UniGene; Mm.435494; -.
DR   ProteinModelPortal; E9PYH6; -.
DR   SMR; E9PYH6; -.
DR   IntAct; E9PYH6; 1.
DR   STRING; 10090.ENSMUSP00000047672; -.
DR   iPTMnet; E9PYH6; -.
DR   PhosphoSitePlus; E9PYH6; -.
DR   jPOST; E9PYH6; -.
DR   MaxQB; E9PYH6; -.
DR   PaxDb; E9PYH6; -.
DR   PeptideAtlas; E9PYH6; -.
DR   PRIDE; E9PYH6; -.
DR   Ensembl; ENSMUST00000047075; ENSMUSP00000047672; ENSMUSG00000042308.
DR   Ensembl; ENSMUST00000047157; ENSMUSP00000037600; ENSMUSG00000042308.
DR   GeneID; 233904; -.
DR   KEGG; mmu:233904; -.
DR   UCSC; uc009jwt.1; mouse.
DR   CTD; 9739; -.
DR   MGI; MGI:2446244; Setd1a.
DR   eggNOG; KOG1080; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000162290; -.
DR   InParanoid; E9PYH6; -.
DR   KO; K11422; -.
DR   OMA; RIWTRLE; -.
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   Proteomes; UP000000589; Chromosome 7.
DR   Bgee; ENSMUSG00000042308; Expressed in 231 organ(s), highest expression level in cumulus cell.
DR   ExpressionAtlas; E9PYH6; baseline and differential.
DR   GO; GO:0035097; C:histone methyltransferase complex; ISO:MGI.
DR   GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
DR   GO; GO:0005719; C:nuclear euchromatin; IDA:BHF-UCL.
DR   GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; ISO:MGI.
DR   GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR   GO; GO:1990188; F:euchromatin binding; IDA:BHF-UCL.
DR   GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); ISO:MGI.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008134; F:transcription factor binding; ISO:MGI.
DR   GO; GO:0048096; P:chromatin-mediated maintenance of transcription; NAS:BHF-UCL.
DR   GO; GO:0051568; P:histone H3-K4 methylation; IMP:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:ParkinsonsUK-UCL.
DR   GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IMP:MGI.
DR   GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:MGI.
DR   GO; GO:1902275; P:regulation of chromatin organization; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0045646; P:regulation of erythrocyte differentiation; IMP:ParkinsonsUK-UCL.
DR   GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; ISO:MGI.
DR   GO; GO:0019827; P:stem cell population maintenance; IMP:MGI.
DR   CDD; cd12548; RRM_Set1A; 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; IPR034467; Set1A_RRM.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR037841; SETD1A.
DR   PANTHER; PTHR22884:SF295; PTHR22884:SF295; 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   1716       Histone-lysine N-methyltransferase
FT                                SETD1A.
FT                                /FTId=PRO_0000445151.
FT   DOMAIN       84    172       RRM. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00176}.
FT   DOMAIN     1577   1694       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     1700   1716       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   REGION     1424   1459       Interaction with CFP1.
FT                                {ECO:0000250|UniProtKB:O15047}.
FT   REGION     1459   1546       Interaction with ASH2L, RBBP5 and WDR5.
FT                                {ECO:0000250|UniProtKB:O15047}.
FT   MOTIF      1307   1311       HCFC1-binding motif (HBM).
FT                                {ECO:0000250|UniProtKB:O15047}.
FT   MOD_RES     477    477       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O15047}.
FT   MOD_RES     521    521       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O15047}.
FT   MOD_RES     578    578       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O15047}.
FT   MOD_RES     930    930       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O15047}.
FT   MOD_RES    1110   1110       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O15047}.
SQ   SEQUENCE   1716 AA;  186060 MW;  F578D5A2276F2D73 CRC64;
     MDQEGGGDGQ KAPSFQWRNY KLIVDPALDP ALRRPSQKVY RYDGVHFSVS DSKYTPVEDL
     QDPRCHVRSK ARDFSLPVPK FKLDEFYIGQ IPLKEVTFAR LNDNVRETFL KDMCRKYGEV
     EEVEILLHPR TRKHLGLARV LFTSTRGAKE TVKNLHLTSV MGNIIHAQLD IKGQQRMKYY
     ELIVNGSYTP QTVPTGGKAL SEKFQGSGAA AETTEARRRS SSDTAAYPAG TTVGGTPGNG
     TPCSQDTNFS SSRQDTPSSF GQFTPQSSQG TPYTSRGSTP YSQDSAYSSS TTSTSFKPRR
     SENSYQDSFS RRHFSTSSAP ATTATATSAT AAATAASSSS SSSSSSSSSS SSSSSASQFR
     GSDSSYPAYY ESWNRYQRHT SYPPRRATRE DPSGASFAEN TAERFPPSYT SYLAPEPNRS
     TDQDYRPPAS EAPPPEPPEP GGGGGGSGGG GGGGGGGGGG APSPEREEAR TPPRPASPAR
     SGSPAPETTN ESVPFAQHSS LDSRIEMLLK EQRSKFSFLA SDTEEEEENS SAGPGARDAG
     AEVPSGAGHG PCTPPPAPAN FEDVAPTGSG EPGAARESPK ANGQNQASPC SSGEDMEISD
     DDRGGSPPPA PTPPQQPPPP PPPPPPPPPP YLASLPLGYP PHQPAYLLPP RPDGPPPPEY
     PPPPPPPPPH IYDFVNSLEL MDRLGAQWGG MPMSFQMQTQ MLTRLHQLRQ GKGLTAASAG
     PPGGAFGEAF LPFPPPQEAA YGLPYALYTQ GQEGRGSYSR EAYHLPLPMA AEPLPSSSVS
     GEEARLPHRE EAEIAESKVL PSAGTVGRVL ATLVQEMKSI MQRDLNRKMV ENVAFGAFDQ
     WWESKEEKAK PFQNAAKQQA KEEDKEKMKL KEPGMLSLVD WAKSGGITGI EAFAFGSGLR
     GALRLPSFKV KRKEPSEISE ASEEKRPRPS TPAEEDEDDP EREKEAGEPG RPGTKPPKRD
     EERGKTQGKH RKSFTLDSEG EEASQESSSE KDEDDDDEDE EDEEQEEAVD ATKKEAEASD
     GEDEDSDSSS QCSLYADSDG ENGSTSDSES GSSSSSSSSS SSSSSSSSSE SSSEEEEQSA
     VIPSASPPRE VPEPLPAPDE KPETDGLVDS PVMPLSEKET LPTQPAGPAE EPPPSVPQPP
     AEPPAGPPDA APRLDERPSS PIPLLPPPKK RRKTVSFSAA EEAPVPEPST AAPLQAKSSG
     PVSRKVPRVV ERTIRNLPLD HASLVKSWPE EVARGGRNRA GGRVRSTEEE EATESGTEVD
     LAVLADLALT PARRGLATLP TGDDSEATET SDEAERPSPL LSHILLEHNY ALAIKPPPTT
     PAPRPLEPAP ALAALFSSPA DEVLEAPEVV VAEAEEPKQQ LQQQHPEQEG EEEEEDEEEE
     SESSESSSSS SSDEEGAIRR RSLRSHTRRR RPPLPPPPPP PPSFEPRSEF EQMTILYDIW
     NSGLDLEDMS YLRLTYERLL QQTSGADWLN DTHWVQHTIT NLSTPKRKRR PQDGPREHQT
     GSARSEGYYP ISKKEKDKYL DVCPVSARQL EGGDTQGTNR VLSERRSEQR RLLSAIGTSA
     IMDSDLLKLN QLKFRKKKLR FGRSRIHEWG LFAMEPIAAD EMVIEYVGQN IRQMVADMRE
     KRYVQEGIGS SYLFRVDHDT IIDATKCGNL ARFINHCCTP NCYAKVITIE SQKKIVIYSK
     QPIGVDEEIT YDYKFPLEDN KIPCLCGTES CRGSLN
//
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