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Protein

Histone-lysine N-methyltransferase SETD7

Gene

Setd7

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Histone methyltransferase that specifically monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes such as collagenase or insulin. Recruited by IPF1/PDX-1 to the insulin promoter, leading to activate transcription. Has also methyltransferase activity toward non-histone proteins such as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189' of TAF10, leading to increase the affinity of TAF10 for RNA polymerase II. Monomethylates 'Lys-372' of p53/TP53, stabilizing p53/TP53 and increasing p53/TP53-mediated transcriptional activation.1 Publication

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei245 – 2451SubstrateBy similarity
Binding sitei317 – 3171SubstrateBy similarity
Binding sitei335 – 3351Substrate; via carbonyl oxygenBy similarity
Binding sitei356 – 3561S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • cellular response to DNA damage stimulus Source: MGI
  • heterochromatin organization Source: MGI
  • negative regulation of transferase activity Source: MGI
  • peptidyl-lysine dimethylation Source: UniProtKB
  • peptidyl-lysine methylation Source: MGI
  • peptidyl-lysine monomethylation Source: UniProtKB
  • regulation of histone H3-K9 methylation Source: MGI
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Methyltransferase, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

ReactomeiREACT_278269. PKMTs methylate histone lysines.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase SETD7 (EC:2.1.1.43)
Alternative name(s):
Histone H3-K4 methyltransferase SETD7
Short name:
H3-K4-HMTase SETD7
SET domain-containing protein 7
SET7/9
Gene namesi
Name:Setd7
Synonyms:Kiaa1717, Set7, Set9
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1920501. Setd7.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 366366Histone-lysine N-methyltransferase SETD7PRO_0000186055Add
BLAST

Proteomic databases

MaxQBiQ8VHL1.
PaxDbiQ8VHL1.
PRIDEiQ8VHL1.

PTM databases

PhosphoSiteiQ8VHL1.

Expressioni

Developmental stagei

Expressed during all pre-implementation stages in both male and female embryos.1 Publication

Gene expression databases

BgeeiQ8VHL1.
GenevestigatoriQ8VHL1.

Interactioni

Subunit structurei

Interacts with IPF1/PDX-1.By similarity

Protein-protein interaction databases

BioGridi215865. 1 interaction.
IntActiQ8VHL1. 1 interaction.
MINTiMINT-4114741.

Structurei

3D structure databases

ProteinModelPortaliQ8VHL1.
SMRiQ8VHL1. Positions 52-344.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati36 – 5823MORN 1Add
BLAST
Repeati59 – 8123MORN 2Add
BLAST
Repeati106 – 12823MORN 3Add
BLAST
Domaini214 – 336123SETPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni226 – 2283S-adenosyl-L-methionine bindingPROSITE-ProRule annotation
Regioni256 – 2583Substrate bindingBy similarity
Regioni266 – 2683Substrate bindingBy similarity
Regioni296 – 2972S-adenosyl-L-methionine bindingPROSITE-ProRule annotation

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi51 – 544Poly-Phe

Domaini

The SET domain is necessary but not sufficient for histone methyltransferase activity.By similarity

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET7 subfamily.PROSITE-ProRule annotation
Contains 3 MORN repeats.Curated
Contains 1 SET domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG4642.
GeneTreeiENSGT00390000004827.
HOGENOMiHOG000074731.
HOVERGENiHBG028309.
InParanoidiQ8VHL1.
KOiK11431.
OMAiGSSVYHF.
OrthoDBiEOG7M98G8.
PhylomeDBiQ8VHL1.
TreeFamiTF106392.

Family and domain databases

InterProiIPR017155. Hist-Lys_N-MeTrfase_SET.
IPR003409. MORN.
IPR001214. SET_dom.
[Graphical view]
PfamiPF02493. MORN. 4 hits.
PF00856. SET. 1 hit.
[Graphical view]
PIRSFiPIRSF037249. Histone_Lys_mtfrase_SET. 1 hit.
SMARTiSM00317. SET. 1 hit.
[Graphical view]
PROSITEiPS51577. SAM_MT43_SET7. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8VHL1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSDDEVVEE AVEGHLDDDG LPHGFCTVTY SSTDRFEGNF VHGEKNGRGK
60 70 80 90 100
FFFFDGSTLE GYYVDDALQG QGVYTYEDGG VLQGTYVDGE LNGPAQEYDS
110 120 130 140 150
DGRLIFKGQY KDNNRHGVCW IHYPDGGSLV GEVNEDGEMT GEKIAYVYPD
160 170 180 190 200
QRTALYGKFI DGEMLEGKLA TLMATEEGRP HFEVTSGSSV YHFDKSTSSC
210 220 230 240 250
ISSDALLPDP YESERVYVAD SLISSAGEGL FSKVAVGPNT VMSFYNGVRI
260 270 280 290 300
THQEVDSRDW ALNGNTLSLD EETVIDVPEP YNHVSKYCAS LGHKANHSFT
310 320 330 340 350
PNCVYDLFVH PRFGPIKCIR TLRAVEAEEE LTVAYGYDHS PPGKSGPEAP
360
EWYQVELKAF QATQQK
Length:366
Mass (Da):40,506
Last modified:February 5, 2008 - v2
Checksum:iC826EAFCB4B9D345
GO

Sequence cautioni

The sequence BAC98238.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti77 – 771E → V in AAH50190 (PubMed:15489334).Curated
Sequence conflicti165 – 1651L → I in AAL56578 (PubMed:11779497).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF448509 mRNA. Translation: AAL56578.1.
AK129428 mRNA. Translation: BAC98238.1. Different initiation.
AK048924 mRNA. Translation: BAC33493.1.
AK147422 mRNA. Translation: BAE27903.1.
AK147413 mRNA. Translation: BAE27897.1.
AK147667 mRNA. Translation: BAE28059.1.
AK170161 mRNA. Translation: BAE41607.1.
BC050190 mRNA. Translation: AAH50190.1.
CCDSiCCDS17341.1.
RefSeqiNP_542983.3. NM_080793.5.
UniGeneiMm.192111.

Genome annotation databases

EnsembliENSMUST00000037141; ENSMUSP00000043492; ENSMUSG00000037111.
GeneIDi73251.
KEGGimmu:73251.
UCSCiuc008peb.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF448509 mRNA. Translation: AAL56578.1.
AK129428 mRNA. Translation: BAC98238.1. Different initiation.
AK048924 mRNA. Translation: BAC33493.1.
AK147422 mRNA. Translation: BAE27903.1.
AK147413 mRNA. Translation: BAE27897.1.
AK147667 mRNA. Translation: BAE28059.1.
AK170161 mRNA. Translation: BAE41607.1.
BC050190 mRNA. Translation: AAH50190.1.
CCDSiCCDS17341.1.
RefSeqiNP_542983.3. NM_080793.5.
UniGeneiMm.192111.

3D structure databases

ProteinModelPortaliQ8VHL1.
SMRiQ8VHL1. Positions 52-344.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi215865. 1 interaction.
IntActiQ8VHL1. 1 interaction.
MINTiMINT-4114741.

PTM databases

PhosphoSiteiQ8VHL1.

Proteomic databases

MaxQBiQ8VHL1.
PaxDbiQ8VHL1.
PRIDEiQ8VHL1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000037141; ENSMUSP00000043492; ENSMUSG00000037111.
GeneIDi73251.
KEGGimmu:73251.
UCSCiuc008peb.1. mouse.

Organism-specific databases

CTDi80854.
MGIiMGI:1920501. Setd7.
RougeiSearch...

Phylogenomic databases

eggNOGiCOG4642.
GeneTreeiENSGT00390000004827.
HOGENOMiHOG000074731.
HOVERGENiHBG028309.
InParanoidiQ8VHL1.
KOiK11431.
OMAiGSSVYHF.
OrthoDBiEOG7M98G8.
PhylomeDBiQ8VHL1.
TreeFamiTF106392.

Enzyme and pathway databases

ReactomeiREACT_278269. PKMTs methylate histone lysines.

Miscellaneous databases

ChiTaRSiSetd7. mouse.
NextBioi337766.
PROiQ8VHL1.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VHL1.
GenevestigatoriQ8VHL1.

Family and domain databases

InterProiIPR017155. Hist-Lys_N-MeTrfase_SET.
IPR003409. MORN.
IPR001214. SET_dom.
[Graphical view]
PfamiPF02493. MORN. 4 hits.
PF00856. SET. 1 hit.
[Graphical view]
PIRSFiPIRSF037249. Histone_Lys_mtfrase_SET. 1 hit.
SMARTiSM00317. SET. 1 hit.
[Graphical view]
PROSITEiPS51577. SAM_MT43_SET7. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase."
    Wang H., Cao R., Xia L., Erdjument-Bromage H., Borchers C., Tempst P., Zhang Y.
    Mol. Cell 8:1207-1217(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Pancreas.
  2. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryonic tail.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6 and NOD.
    Tissue: Brain and Cerebellum.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: 129/Sv X 129SvCp.
    Tissue: Embryonic stem cell.
  5. "Covalent histone modifications underlie the developmental regulation of insulin gene transcription in pancreatic beta cells."
    Chakrabarti S.K., Francis J., Ziesmann S.M., Garmey J.C., Mirmira R.G.
    J. Biol. Chem. 278:23617-23623(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "The analysis of X-chromosome inactivation-related gene expression from single mouse embryo with sex-determination."
    Jeong K.S., Park J.H., Lee S.
    Biochem. Biophys. Res. Commun. 333:803-807(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiSETD7_MOUSE
AccessioniPrimary (citable) accession number: Q8VHL1
Secondary accession number(s): Q6ZPJ6, Q80UU3, Q8C7Y6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: February 5, 2008
Last modified: April 1, 2015
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.