GenomeNet

Database: UniProt
Entry: Q8VHL1
LinkDB: Q8VHL1
Original site: Q8VHL1 
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   16-JAN-2019, entry version 131.
DE   RecName: Full=Histone-lysine N-methyltransferase SETD7;
DE            EC=2.1.1.43;
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   4-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:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   project: 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.,
RA   Mirmira R.G.;
RT   "Covalent histone modifications underlie the developmental regulation
RT   of 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
RT   from 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Histone methyltransferase that specifically
CC       monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation
CC       represents a specific tag for epigenetic transcriptional
CC       activation. Plays a central role in the transcriptional activation
CC       of genes such as collagenase or insulin. Recruited by IPF1/PDX-1
CC       to the insulin promoter, leading to activate transcription. Has
CC       also methyltransferase activity toward non-histone proteins such
CC       as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding
CC       the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189'
CC       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
CC       activation. {ECO:0000269|PubMed:12711597}.
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:0000255|PROSITE-ProRule:PRU00910};
CC   -!- SUBUNIT: Interacts with IPF1/PDX-1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome
CC       {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during all pre-implementation
CC       stages in both male and female embryos.
CC       {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
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. SET7 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00910}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98238.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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   UniGene; Mm.192111; -.
DR   ProteinModelPortal; Q8VHL1; -.
DR   SMR; Q8VHL1; -.
DR   BioGrid; 215865; 4.
DR   IntAct; Q8VHL1; 2.
DR   MINT; Q8VHL1; -.
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   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   eggNOG; KOG1079; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00390000004827; -.
DR   HOGENOM; HOG000074731; -.
DR   HOVERGEN; HBG028309; -.
DR   InParanoid; Q8VHL1; -.
DR   KO; K11431; -.
DR   OMA; SSVYHFD; -.
DR   OrthoDB; 675418at2759; -.
DR   PhylomeDB; Q8VHL1; -.
DR   TreeFam; TF106392; -.
DR   Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR   ChiTaRS; Setd7; mouse.
DR   PRO; PR:Q8VHL1; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   Bgee; ENSMUSG00000037111; Expressed in 247 organ(s), highest expression level in quadriceps femoris.
DR   Genevisible; Q8VHL1; MM.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
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; ISS:UniProtKB.
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: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:0051570; P:regulation of histone H3-K9 methylation; IDA:MGI.
DR   GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR   InterPro; IPR017155; Hist-Lys_N-MeTrfase_SET.
DR   InterPro; IPR003409; MORN.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF02493; MORN; 4.
DR   Pfam; PF00856; SET; 1.
DR   PIRSF; PIRSF037249; Histone_Lys_mtfrase_SET; 1.
DR   PROSITE; PS51577; SAM_MT43_SET7; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   Activator; Chromatin regulator; Chromosome; Complete proteome;
KW   Methyltransferase; Nucleus; Reference proteome; Repeat;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase.
FT   CHAIN         1    366       Histone-lysine N-methyltransferase SETD7.
FT                                /FTId=PRO_0000186055.
FT   REPEAT       36     58       MORN 1.
FT   REPEAT       59     81       MORN 2.
FT   REPEAT      106    128       MORN 3.
FT   DOMAIN      214    336       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   REGION      226    228       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00910}.
FT   REGION      256    258       Substrate binding. {ECO:0000250}.
FT   REGION      266    268       Substrate binding. {ECO:0000250}.
FT   REGION      296    297       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00910}.
FT   COMPBIAS     51     54       Poly-Phe.
FT   BINDING     245    245       Substrate. {ECO:0000250}.
FT   BINDING     317    317       Substrate. {ECO:0000250}.
FT   BINDING     335    335       Substrate; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   BINDING     356    356       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   CONFLICT     77     77       E -> V (in Ref. 4; AAH50190).
FT                                {ECO:0000305}.
FT   CONFLICT    165    165       L -> I (in Ref. 1; AAL56578).
FT                                {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
//
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