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Q8WTS6

- SETD7_HUMAN

UniProt

Q8WTS6 - SETD7_HUMAN

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Protein

Histone-lysine N-methyltransferase SETD7

Gene

SETD7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein 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.6 Publications

Catalytic activityi

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

Kineticsi

  1. KM=29 µM for histone H31 Publication
  2. KM=12 µM for TAF101 Publication
  3. KM=69 µM for p53/TP531 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei245 – 2451Substrate
Binding sitei317 – 3171Substrate
Binding sitei335 – 3351Substrate; via carbonyl oxygen
Binding sitei356 – 3561S-adenosyl-L-methionine; via carbonyl oxygen2 PublicationsPROSITE-ProRule annotation

GO - Molecular functioni

  1. histone-lysine N-methyltransferase activity Source: UniProtKB
  2. p53 binding Source: UniProtKB
  3. protein-lysine N-methyltransferase activity Source: UniProtKB

GO - Biological processi

  1. chromatin modification Source: UniProtKB
  2. peptidyl-lysine dimethylation Source: UniProtKB
  3. peptidyl-lysine monomethylation Source: UniProtKB
  4. regulation of transcription, DNA-templated Source: UniProtKB-KW
  5. 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

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
Lysine N-methyltransferase 7
SET domain-containing protein 7
SET7/9
Gene namesi
Name:SETD7
Synonyms:KIAA1717, KMT7, SET7, SET9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:30412. SETD7.

Subcellular locationi

GO - Cellular componenti

  1. chromosome Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi220 – 2201E → A: Increases near-attack conformations. 1 Publication
Mutagenesisi228 – 2281E → A: Increases near-attack conformations. 1 Publication
Mutagenesisi245 – 2451Y → A: Significantly reduces the monomethyltransferase activity but increases the dimethyltransferase activity. 2 Publications
Mutagenesisi294 – 2941K → A: Significantly reduces the catalytic activity. 1 Publication
Mutagenesisi297 – 2971H → A or G: Abolishes methyltransferase activity. 5 Publications
Mutagenesisi317 – 3171K → A: Induces a reduction in methyltransferase activity toward TAF10 but an increased methyltransferase activity for H3 and p53/TP53. 1 Publication

Organism-specific databases

PharmGKBiPA143485615.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 366366Histone-lysine N-methyltransferase SETD7PRO_0000186054Add
BLAST

Proteomic databases

MaxQBiQ8WTS6.
PaxDbiQ8WTS6.
PeptideAtlasiQ8WTS6.
PRIDEiQ8WTS6.

PTM databases

PhosphoSiteiQ8WTS6.

Expressioni

Tissue specificityi

Widely expressed. Expressed in pancreatic islets.

Gene expression databases

BgeeiQ8WTS6.
CleanExiHS_SETD7.
ExpressionAtlasiQ8WTS6. baseline and differential.
GenevestigatoriQ8WTS6.

Organism-specific databases

HPAiHPA058111.

Interactioni

Subunit structurei

Interacts with IPF1/PDX-1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Foxo3Q9WVH45EBI-1268586,EBI-6127038From a different organism.
HIST1H3DP684314EBI-1268586,EBI-79722
Hist1h3iP684332EBI-1268586,EBI-79743From a different organism.
RB1P064004EBI-1268586,EBI-491274
RELAQ0420610EBI-1268586,EBI-73886
RelaQ042072EBI-1268586,EBI-644400From a different organism.
SERTAD1Q9UHV22EBI-1268586,EBI-748601
TAF10Q129622EBI-1268586,EBI-708376
TP53P046376EBI-1268586,EBI-366083

Protein-protein interaction databases

BioGridi123332. 34 interactions.
DIPiDIP-29045N.
IntActiQ8WTS6. 14 interactions.
MINTiMINT-6615937.
STRINGi9606.ENSP00000274031.

Structurei

Secondary structure

1
366
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi54 – 563
Beta strandi61 – 644
Beta strandi67 – 759
Beta strandi81 – 877
Beta strandi90 – 989
Beta strandi100 – 1023
Beta strandi104 – 1118
Helixi114 – 1163
Beta strandi119 – 1224
Beta strandi128 – 1314
Beta strandi135 – 1373
Beta strandi141 – 1477
Beta strandi151 – 16010
Beta strandi163 – 17614
Beta strandi179 – 1846
Beta strandi186 – 1883
Turni203 – 2064
Helixi210 – 2134
Beta strandi216 – 2205
Turni224 – 2263
Beta strandi228 – 2347
Beta strandi241 – 2455
Beta strandi248 – 2503
Helixi252 – 2565
Helixi260 – 2623
Beta strandi266 – 2683
Beta strandi270 – 2723
Beta strandi274 – 2763
Turni279 – 2824
Turni284 – 2863
Helixi292 – 2943
Beta strandi295 – 3006
Beta strandi302 – 3109
Turni311 – 3133
Beta strandi314 – 32310
Beta strandi330 – 3334
Beta strandi338 – 3403
Beta strandi344 – 3463
Helixi351 – 36313

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H3IX-ray2.10A/B52-344[»]
1MT6X-ray2.20A58-337[»]
1MUFX-ray2.26A81-337[»]
1N6AX-ray1.70A108-366[»]
1N6CX-ray2.30A70-366[»]
1O9SX-ray1.75A/B108-366[»]
1XQHX-ray1.75A/E108-366[»]
2F69X-ray1.30A110-366[»]
3CBMX-ray1.69A111-366[»]
3CBOX-ray1.65A111-366[»]
3CBPX-ray1.42A111-366[»]
3M53X-ray1.85A110-366[»]
3M54X-ray1.60A110-366[»]
3M55X-ray1.55A110-366[»]
3M56X-ray1.65A110-366[»]
3M57X-ray1.70A110-366[»]
3M58X-ray1.40A110-366[»]
3M59X-ray1.70A110-366[»]
3M5AX-ray1.75A110-366[»]
3OS5X-ray1.69A111-366[»]
3VUZX-ray2.50A111-366[»]
3VV0X-ray2.00A111-366[»]
4E47X-ray2.00A/B/C/D109-366[»]
4J7FX-ray1.59A110-366[»]
4J7IX-ray2.56A110-366[»]
4J83X-ray1.70A110-366[»]
4J8OX-ray1.63A110-366[»]
4JDSX-ray1.70A/B/C/D109-366[»]
4JLGX-ray1.90A/B109-366[»]
ProteinModelPortaliQ8WTS6.
SMRiQ8WTS6. Positions 52-344.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8WTS6.

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 binding
Regioni256 – 2583Substrate binding
Regioni266 – 2683Substrate binding
Regioni296 – 2972S-adenosyl-L-methionine binding

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.

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.
InParanoidiQ8WTS6.
KOiK11431.
OMAiGSSVYHF.
PhylomeDBiQ8WTS6.
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.

Q8WTS6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDSDDEMVEE AVEGHLDDDG LPHGFCTVTY SSTDRFEGNF VHGEKNGRGK
60 70 80 90 100
FFFFDGSTLE GYYVDDALQG QGVYTYEDGG VLQGTYVDGE LNGPAQEYDT
110 120 130 140 150
DGRLIFKGQY KDNIRHGVCW IYYPDGGSLV GEVNEDGEMT GEKIAYVYPD
160 170 180 190 200
ERTALYGKFI DGEMIEGKLA TLMSTEEGRP HFELMPGNSV YHFDKSTSSC
210 220 230 240 250
ISTNALLPDP YESERVYVAE SLISSAGEGL FSKVAVGPNT VMSFYNGVRI
260 270 280 290 300
THQEVDSRDW ALNGNTLSLD EETVIDVPEP YNHVSKYCAS LGHKANHSFT
310 320 330 340 350
PNCIYDMFVH PRFGPIKCIR TLRAVEADEE LTVAYGYDHS PPGKSGPEAP
360
EWYQVELKAF QATQQK
Length:366
Mass (Da):40,721
Last modified:March 1, 2002 - v1
Checksum:i73A1217079E3BA13
GO

Sequence cautioni

The sequence BAB21808.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF448510 mRNA. Translation: AAL56579.1.
AF462150 mRNA. Translation: AAL69901.1.
AB051504 mRNA. Translation: BAB21808.1. Different initiation.
AC112236 Genomic DNA. No translation available.
AC114743 Genomic DNA. Translation: AAY40937.1.
BC121055 mRNA. Translation: AAI21056.1.
BC121056 mRNA. Translation: AAI21057.1.
CCDSiCCDS3748.1.
RefSeqiNP_085151.1. NM_030648.2.
UniGeneiHs.480792.

Genome annotation databases

EnsembliENST00000274031; ENSP00000274031; ENSG00000145391.
GeneIDi80854.
KEGGihsa:80854.
UCSCiuc003ihw.3. human.

Polymorphism databases

DMDMi25091217.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF448510 mRNA. Translation: AAL56579.1 .
AF462150 mRNA. Translation: AAL69901.1 .
AB051504 mRNA. Translation: BAB21808.1 . Different initiation.
AC112236 Genomic DNA. No translation available.
AC114743 Genomic DNA. Translation: AAY40937.1 .
BC121055 mRNA. Translation: AAI21056.1 .
BC121056 mRNA. Translation: AAI21057.1 .
CCDSi CCDS3748.1.
RefSeqi NP_085151.1. NM_030648.2.
UniGenei Hs.480792.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1H3I X-ray 2.10 A/B 52-344 [» ]
1MT6 X-ray 2.20 A 58-337 [» ]
1MUF X-ray 2.26 A 81-337 [» ]
1N6A X-ray 1.70 A 108-366 [» ]
1N6C X-ray 2.30 A 70-366 [» ]
1O9S X-ray 1.75 A/B 108-366 [» ]
1XQH X-ray 1.75 A/E 108-366 [» ]
2F69 X-ray 1.30 A 110-366 [» ]
3CBM X-ray 1.69 A 111-366 [» ]
3CBO X-ray 1.65 A 111-366 [» ]
3CBP X-ray 1.42 A 111-366 [» ]
3M53 X-ray 1.85 A 110-366 [» ]
3M54 X-ray 1.60 A 110-366 [» ]
3M55 X-ray 1.55 A 110-366 [» ]
3M56 X-ray 1.65 A 110-366 [» ]
3M57 X-ray 1.70 A 110-366 [» ]
3M58 X-ray 1.40 A 110-366 [» ]
3M59 X-ray 1.70 A 110-366 [» ]
3M5A X-ray 1.75 A 110-366 [» ]
3OS5 X-ray 1.69 A 111-366 [» ]
3VUZ X-ray 2.50 A 111-366 [» ]
3VV0 X-ray 2.00 A 111-366 [» ]
4E47 X-ray 2.00 A/B/C/D 109-366 [» ]
4J7F X-ray 1.59 A 110-366 [» ]
4J7I X-ray 2.56 A 110-366 [» ]
4J83 X-ray 1.70 A 110-366 [» ]
4J8O X-ray 1.63 A 110-366 [» ]
4JDS X-ray 1.70 A/B/C/D 109-366 [» ]
4JLG X-ray 1.90 A/B 109-366 [» ]
ProteinModelPortali Q8WTS6.
SMRi Q8WTS6. Positions 52-344.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123332. 34 interactions.
DIPi DIP-29045N.
IntActi Q8WTS6. 14 interactions.
MINTi MINT-6615937.
STRINGi 9606.ENSP00000274031.

Chemistry

BindingDBi Q8WTS6.
ChEMBLi CHEMBL5523.

PTM databases

PhosphoSitei Q8WTS6.

Polymorphism databases

DMDMi 25091217.

Proteomic databases

MaxQBi Q8WTS6.
PaxDbi Q8WTS6.
PeptideAtlasi Q8WTS6.
PRIDEi Q8WTS6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000274031 ; ENSP00000274031 ; ENSG00000145391 .
GeneIDi 80854.
KEGGi hsa:80854.
UCSCi uc003ihw.3. human.

Organism-specific databases

CTDi 80854.
GeneCardsi GC04M140417.
HGNCi HGNC:30412. SETD7.
HPAi HPA058111.
MIMi 606594. gene.
neXtProti NX_Q8WTS6.
PharmGKBi PA143485615.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG4642.
GeneTreei ENSGT00390000004827.
HOGENOMi HOG000074731.
HOVERGENi HBG028309.
InParanoidi Q8WTS6.
KOi K11431.
OMAi GSSVYHF.
PhylomeDBi Q8WTS6.
TreeFami TF106392.

Miscellaneous databases

EvolutionaryTracei Q8WTS6.
GeneWikii SETD7.
GenomeRNAii 80854.
NextBioi 71300.
PROi Q8WTS6.
SOURCEi Search...

Gene expression databases

Bgeei Q8WTS6.
CleanExi HS_SETD7.
ExpressionAtlasi Q8WTS6. baseline and differential.
Genevestigatori Q8WTS6.

Family and domain databases

InterProi IPR017155. Hist-Lys_N-MeTrfase_SET.
IPR003409. MORN.
IPR001214. SET_dom.
[Graphical view ]
Pfami PF02493. MORN. 4 hits.
PF00856. SET. 1 hit.
[Graphical view ]
PIRSFi PIRSF037249. Histone_Lys_mtfrase_SET. 1 hit.
SMARTi SM00317. SET. 1 hit.
[Graphical view ]
PROSITEi PS51577. SAM_MT43_SET7. 1 hit.
PS50280. SET. 1 hit.
[Graphical view ]
ProtoNeti Search...

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], PROTEIN SEQUENCE OF 35-44; 108-115; 144-152; 234-258 AND 345-358, MUTAGENESIS OF HIS-297.
    Tissue: Brain.
  2. "Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation."
    Nishioka K., Chuikov S., Sarma K., Erdjument-Bromage H., Allis C.D., Tempst P., Reinberg D.
    Genes Dev. 16:479-489(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 36-45; 104-115; 144-152; 159-169; 201-250 AND 324-358, MUTAGENESIS OF HIS-297.
    Tissue: Cervix carcinoma.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
    DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. "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].
  6. "Cascade of distinct histone modifications during collagenase gene activation."
    Martens J.H., Verlaan M., Kalkhoven E., Zantema A.
    Mol. Cell. Biol. 23:1808-1816(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Gene-specific modulation of TAF10 function by SET9-mediated methylation."
    Kouskouti A., Scheer E., Staub A., Tora L., Talianidis I.
    Mol. Cell 14:175-182(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF HIS-297.
  8. "Pdx-1 links histone H3-Lys-4 methylation to RNA polymerase II elongation during activation of insulin transcription."
    Francis J., Chakrabarti S.K., Garmey J.C., Mirmira R.G.
    J. Biol. Chem. 280:36244-36253(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH IPF1, MUTAGENESIS OF HIS-297.
  9. Cited for: FUNCTION.
  10. "Catalytic mechanism and product specificity of the histone lysine methyltransferase SET7/9: an ab initio QM/MM-FE study with multiple initial structures."
    Hu P., Zhang Y.
    J. Am. Chem. Soc. 128:1272-1278(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF GLU-220; GLU-228; TYR-245 AND LYS-294.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Crystal structure and functional analysis of the histone methyltransferase SET7/9."
    Wilson J., Jing C., Walker P., Martin S., Howell S., Blackburn G., Gamblin S., Xiao B.
    Cell 111:105-115(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 52-344.
  13. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
  14. "Structure and catalytic mechanism of the human histone methyltransferase SET7/9."
    Xiao B., Jing C., Wilson J.R., Walker P.A., Vasisht N., Kelly G., Howell S., Taylor I.A., Blackburn G.M., Gamblin S.J.
    Nature 421:652-656(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 108-366 IN COMPLEX WITH S-ADENOSYL-L-METHIONINE AND HISTONE PEPTIDE, FUNCTION, MUTAGENESIS OF TYR-245.
  15. "Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet."
    Kwon T., Chang J.H., Kwak E., Lee C.W., Joachimiak A., Kim Y.C., Lee J., Cho Y.
    EMBO J. 22:292-303(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 70-366 IN COMPLEX WITH S-ADENOSYL-L-METHIONINE.
  16. Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 108-366, FUNCTION, MUTAGENESIS OF HIS-297.
  17. "Structural basis for the methylation site specificity of SET7/9."
    Couture J.-F., Collazo E., Hauk G., Trievel R.C.
    Nat. Struct. Mol. Biol. 13:140-146(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 110-366, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-317.

Entry informationi

Entry nameiSETD7_HUMAN
AccessioniPrimary (citable) accession number: Q8WTS6
Secondary accession number(s): B5WWL3
, Q0VAH3, Q4W5A9, Q9C0E6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: March 1, 2002
Last modified: October 29, 2014
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Monomethyltransferase activity is achieved by disrupting the formation at near-attack conformations for the dimethylation reaction.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3