SETD7_MOUSE
ID SETD7_MOUSE Reviewed; 366 AA.
AC Q8VHL1; Q6ZPJ6; Q80UU3; Q8C7Y6;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Histone-lysine N-methyltransferase SETD7;
DE EC=2.1.1.364 {ECO:0000250|UniProtKB:Q8WTS6};
DE AltName: Full=Histone H3-K4 methyltransferase SETD7;
DE Short=H3-K4-HMTase SETD7;
DE AltName: Full=SET domain-containing protein 7;
DE AltName: Full=SET7/9;
GN Name=Setd7; Synonyms=Kiaa1717, Set7, Set9;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreas;
RX PubMed=11779497; DOI=10.1016/s1097-2765(01)00405-1;
RA Wang H., Cao R., Xia L., Erdjument-Bromage H., Borchers C., Tempst P.,
RA Zhang Y.;
RT "Purification and functional characterization of a histone H3-lysine 4-
RT specific methyltransferase.";
RL Mol. Cell 8:1207-1217(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Brain, and Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129/Sv X 129SvCp; TISSUE=Embryonic stem cell;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION.
RX PubMed=12711597; DOI=10.1074/jbc.m303423200;
RA Chakrabarti S.K., Francis J., Ziesmann S.M., Garmey J.C., Mirmira R.G.;
RT "Covalent histone modifications underlie the developmental regulation of
RT insulin gene transcription in pancreatic beta cells.";
RL J. Biol. Chem. 278:23617-23623(2003).
RN [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=15975555; DOI=10.1016/j.bbrc.2005.06.003;
RA Jeong K.S., Park J.H., Lee S.;
RT "The analysis of X-chromosome inactivation-related gene expression from
RT single mouse embryo with sex-determination.";
RL Biochem. Biophys. Res. Commun. 333:803-807(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, and Spleen;
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 expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Histone methyltransferase that specifically monomethylates
CC 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag
CC for epigenetic transcriptional activation. Plays a central role in the
CC transcriptional activation of genes such as collagenase or insulin.
CC Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate
CC transcription. Has also methyltransferase activity toward non-histone
CC proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and
CC binding the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-
CC 189' of TAF10, leading to increase the affinity of TAF10 for RNA
CC polymerase II. Monomethylates 'Lys-372' of p53/TP53, stabilizing
CC p53/TP53 and increasing p53/TP53-mediated transcriptional activation.
CC {ECO:0000269|PubMed:12711597}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(4)-[histone H3] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60264, Rhea:RHEA-COMP:15543, Rhea:RHEA-COMP:15547,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.364;
CC Evidence={ECO:0000250|UniProtKB:Q8WTS6, ECO:0000255|PROSITE-
CC ProRule:PRU00910};
CC -!- SUBUNIT: Interacts with IPF1/PDX-1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed during all pre-implementation stages in
CC both male and female embryos. {ECO:0000269|PubMed:15975555}.
CC -!- DOMAIN: The SET domain is necessary but not sufficient for histone
CC methyltransferase activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. SET7 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00910}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98238.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF448509; AAL56578.1; -; mRNA.
DR EMBL; AK129428; BAC98238.1; ALT_INIT; mRNA.
DR EMBL; AK048924; BAC33493.1; -; mRNA.
DR EMBL; AK147422; BAE27903.1; -; mRNA.
DR EMBL; AK147413; BAE27897.1; -; mRNA.
DR EMBL; AK147667; BAE28059.1; -; mRNA.
DR EMBL; AK170161; BAE41607.1; -; mRNA.
DR EMBL; BC050190; AAH50190.1; -; mRNA.
DR CCDS; CCDS17341.1; -.
DR RefSeq; NP_542983.3; NM_080793.5.
DR AlphaFoldDB; Q8VHL1; -.
DR SMR; Q8VHL1; -.
DR BioGRID; 215865; 6.
DR IntAct; Q8VHL1; 1.
DR STRING; 10090.ENSMUSP00000043492; -.
DR iPTMnet; Q8VHL1; -.
DR PhosphoSitePlus; Q8VHL1; -.
DR EPD; Q8VHL1; -.
DR MaxQB; Q8VHL1; -.
DR PaxDb; Q8VHL1; -.
DR PeptideAtlas; Q8VHL1; -.
DR PRIDE; Q8VHL1; -.
DR ProteomicsDB; 261171; -.
DR Antibodypedia; 16193; 542 antibodies from 40 providers.
DR DNASU; 73251; -.
DR Ensembl; ENSMUST00000037141; ENSMUSP00000043492; ENSMUSG00000037111.
DR GeneID; 73251; -.
DR KEGG; mmu:73251; -.
DR UCSC; uc008peb.1; mouse.
DR CTD; 80854; -.
DR MGI; MGI:1920501; Setd7.
DR VEuPathDB; HostDB:ENSMUSG00000037111; -.
DR eggNOG; KOG1079; Eukaryota.
DR GeneTree; ENSGT00390000004827; -.
DR HOGENOM; CLU_803117_0_0_1; -.
DR InParanoid; Q8VHL1; -.
DR OMA; NGIRITH; -.
DR OrthoDB; 675418at2759; -.
DR PhylomeDB; Q8VHL1; -.
DR TreeFam; TF106392; -.
DR BRENDA; 2.1.1.364; 3474.
DR Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR BioGRID-ORCS; 73251; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Setd7; mouse.
DR PRO; PR:Q8VHL1; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q8VHL1; protein.
DR Bgee; ENSMUSG00000037111; Expressed in triceps brachii and 215 other tissues.
DR Genevisible; Q8VHL1; MM.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0002039; F:p53 binding; ISO:MGI.
DR GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0070828; P:heterochromatin organization; IMP:MGI.
DR GO; GO:0034968; P:histone lysine methylation; IEA:InterPro.
DR GO; GO:0018027; P:peptidyl-lysine dimethylation; ISS:UniProtKB.
DR GO; GO:0018022; P:peptidyl-lysine methylation; IDA:MGI.
DR GO; GO:0018026; P:peptidyl-lysine monomethylation; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0006479; P:protein methylation; IDA:MGI.
DR GO; GO:0051570; P:regulation of histone H3-K9 methylation; IDA:MGI.
DR CDD; cd10530; SET_SETD7; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR017155; Hist-Lys_N-MeTrfase_SET.
DR InterPro; IPR003409; MORN.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR044436; SETD7_SET.
DR Pfam; PF02493; MORN; 4.
DR Pfam; PF00856; SET; 1.
DR PIRSF; PIRSF037249; Histone_Lys_mtfrase_SET; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51577; SAM_MT43_SET7; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW Activator; Chromatin regulator; Chromosome; Methyltransferase; Nucleus;
KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..366
FT /note="Histone-lysine N-methyltransferase SETD7"
FT /id="PRO_0000186055"
FT REPEAT 36..58
FT /note="MORN 1"
FT REPEAT 59..81
FT /note="MORN 2"
FT REPEAT 106..128
FT /note="MORN 3"
FT DOMAIN 214..336
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 226..228
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00910"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 256..258
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 266..268
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 296..297
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00910"
FT BINDING 317
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 335
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 356
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT CONFLICT 77
FT /note="E -> V (in Ref. 4; AAH50190)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="L -> I (in Ref. 1; AAL56578)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 366 AA; 40506 MW; C826EAFCB4B9D345 CRC64;
MDSDDEVVEE AVEGHLDDDG LPHGFCTVTY SSTDRFEGNF VHGEKNGRGK FFFFDGSTLE
GYYVDDALQG QGVYTYEDGG VLQGTYVDGE LNGPAQEYDS DGRLIFKGQY KDNNRHGVCW
IHYPDGGSLV GEVNEDGEMT GEKIAYVYPD QRTALYGKFI DGEMLEGKLA TLMATEEGRP
HFEVTSGSSV YHFDKSTSSC ISSDALLPDP YESERVYVAD SLISSAGEGL FSKVAVGPNT
VMSFYNGVRI THQEVDSRDW ALNGNTLSLD EETVIDVPEP YNHVSKYCAS LGHKANHSFT
PNCVYDLFVH PRFGPIKCIR TLRAVEAEEE LTVAYGYDHS PPGKSGPEAP EWYQVELKAF
QATQQK
