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Q9NQR1

- SETD8_HUMAN

UniProt

Q9NQR1 - SETD8_HUMAN

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Protein
N-lysine methyltransferase SETD8
Gene
SETD8, KMT5A, PRSET7, SET07, SET8
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Protein-lysine N-methyltransferase that monomethylates both histones and non-histone proteins. Specifically monomethylates 'Lys-20' of histone H4 (H4K20me1). H4K20me1 is enriched during mitosis and represents a specific tag for epigenetic transcriptional repression. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. Required for cell proliferation, probably by contributing to the maintenance of proper higher-order structure of DNA during mitosis. Involved in chromosome condensation and proper cytokinesis. Nucleosomes are preferred as substrate compared to free histones. Mediates monomethylation of p53/TP53 at 'Lys-382', leading to repress p53/TP53-target genes. Plays a negative role in TGF-beta response regulation and a positive role in cell migration.8 Publications

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei312 – 3121S-adenosyl-L-methionine

GO - Molecular functioni

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

GO - Biological processi

  1. histone lysine methylation Source: GOC
  2. mitotic cell cycle Source: Reactome
  3. mitotic nuclear division Source: UniProtKB-KW
  4. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  5. negative regulation of transcription, DNA-templated Source: UniProtKB
  6. peptidyl-lysine monomethylation Source: UniProtKB
  7. regulation of DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
  8. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Repressor, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Transcription, Transcription regulation

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi2.1.1.43. 2681.
ReactomeiREACT_172744. Condensation of Prophase Chromosomes.

Names & Taxonomyi

Protein namesi
Recommended name:
N-lysine methyltransferase SETD8 (EC:2.1.1.-)
Alternative name(s):
H4-K20-HMTase SETD8
Histone-lysine N-methyltransferase SETD8 (EC:2.1.1.43)
Lysine N-methyltransferase 5A
PR/SET domain-containing protein 07
Short name:
PR-Set7
Short name:
PR/SET07
SET domain-containing protein 8
Gene namesi
Name:SETD8
Synonyms:KMT5A, PRSET7, SET07, SET8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:29489. SETD8.

Subcellular locationi

Nucleus. Chromosome
Note: Specifically localizes to mitotic chromosomes. Colocalized with SIRT2 at mitotic foci. Associates with chromosomes during mitosis; association is increased in a H2O(2)-induced oxidative stress-dependent manner. Associates with silent chromatin on euchromatic arms. Not associated with constitutive heterochromatin.2 Publications

GO - Cellular componenti

  1. chromosome Source: UniProtKB-SubCell
  2. nucleolus Source: HPA
  3. nucleoplasm Source: Reactome
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi172 – 1721K → Q: Inhibits the interaction with SIRT2. Increases the number of mitotic foci formation. Does not change methyltransferase activity.
Mutagenesisi172 – 1721K → R: Increases the interaction with SIRT2. Reduces the number of mitotic foci formation. Does not change methyltransferase activity.
Mutagenesisi286 – 2861Y → A or F: Strongly reduces affinity for histone H4 and abolishes methyltransferase activity. 1 Publication
Mutagenesisi300 – 3001E → A: Strongly reduces affinity for histone H4. 1 Publication
Mutagenesisi311 – 3111C → A: Strongly reduces affinity for histone H4. 1 Publication
Mutagenesisi336 – 3361R → G: Abolishes methyltransferase activity. 2 Publications
Mutagenesisi340 – 3401H → A: Strongly decreases methyltransferase activity. 1 Publication
Mutagenesisi375 – 3751Y → A: Strongly reduces affinity for histone H4 and methyltransferase activity. 1 Publication
Mutagenesisi375 – 3751Y → F: Alters methyltransferase activity, so that both monomethylation and dimethylation take place. 1 Publication
Mutagenesisi379 – 3791D → A or N: Abolishes histone H4 binding and methyltransferase activity. 4 Publications
Mutagenesisi385 – 3939Missing: Abolishes methyltransferase activity. 1 Publication
Mutagenesisi388 – 3881H → A or E: Strongly reduces affinity for histone H4. 1 Publication
Mutagenesisi388 – 3881H → F: Increases affinity for histone H4. 1 Publication

Organism-specific databases

PharmGKBiPA143485616.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 393393N-lysine methyltransferase SETD8
PRO_0000186081Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei100 – 1001Phosphoserine2 Publications
Modified residuei172 – 1721N6-acetyllysine

Post-translational modificationi

Acetylated at Lys-172; does not change methyltransferase activity. Deacetylated at Lys-172 by SIRT2; does not change methyltransferase activity.
Ubiquitinated and degraded by the DCX(DTL) complex Inferred.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9NQR1.
PaxDbiQ9NQR1.
PRIDEiQ9NQR1.

PTM databases

PhosphoSiteiQ9NQR1.

Expressioni

Developmental stagei

Not detected during G1 phase. First detected during S through G2 phases, and peaks during mitosis (at protein level).1 Publication

Inductioni

By HCFC1 C-terminal chain, independently of HCFC1 N-terminal chain. Transiently induced by TGF-beta and during the cell cycle.2 Publications

Gene expression databases

ArrayExpressiQ9NQR1.
BgeeiQ9NQR1.
CleanExiHS_SETD8.
GenevestigatoriQ9NQR1.

Organism-specific databases

HPAiHPA053747.

Interactioni

Subunit structurei

Interacts with L3MBTL1. Isoform 2 interacts with SIRT2 (phosphorylated form); the interaction is direct, stimulates SETD8-mediated methyltransferase activity at histone H4 'Lys-20' (H4K20me1) and is increased in a H2O(2)-induced oxidative stress-dependent manner.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
HIST2H4BP628055EBI-1268946,EBI-302023
TWIST1Q156725EBI-1268946,EBI-1797287

Protein-protein interaction databases

BioGridi132490. 25 interactions.
DIPiDIP-39133N.
IntActiQ9NQR1. 3 interactions.
MINTiMINT-3072203.
STRINGi9606.ENSP00000332995.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi236 – 25318
Beta strandi259 – 2646
Turni265 – 2673
Beta strandi268 – 2758
Beta strandi282 – 2854
Beta strandi288 – 2925
Helixi293 – 30311
Helixi306 – 3094
Helixi310 – 3123
Beta strandi313 – 3186
Beta strandi321 – 3266
Helixi335 – 3373
Beta strandi345 – 3539
Beta strandi356 – 36510
Helixi382 – 3876
Helixi389 – 3924

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZKKX-ray1.45A/B/C/D231-393[»]
2BQZX-ray1.50A/E233-393[»]
3F9WX-ray1.60A/B/C/D232-393[»]
3F9XX-ray1.25A/B/C/D232-393[»]
3F9YX-ray1.50A/B232-393[»]
3F9ZX-ray1.60A/B/C/D232-393[»]
4IJ8X-ray2.00A/B232-393[»]
ProteinModelPortaliQ9NQR1.
SMRiQ9NQR1. Positions 233-393.

Miscellaneous databases

EvolutionaryTraceiQ9NQR1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini257 – 378122SET
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni267 – 2693S-adenosyl-L-methionine binding
Regioni339 – 3402S-adenosyl-L-methionine binding

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili134 – 16330 Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi6 – 6762Ala-rich
Add
BLAST
Compositional biasi29 – 324Poly-Arg

Domaini

Although the SET domain contains the active site of enzymatic activity, both sequences upstream and downstream of the SET domain are required for methyltransferase activity.

Sequence similaritiesi

Contains 1 SET domain.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG2940.
HOGENOMiHOG000020818.
HOVERGENiHBG067546.
InParanoidiQ9NQR1.
KOiK11428.
OMAiCSGMRSP.
OrthoDBiEOG70KGRN.
PhylomeDBiQ9NQR1.
TreeFamiTF335181.

Family and domain databases

InterProiIPR016858. Hist_H4-K20_MeTrfase.
IPR001214. SET_dom.
[Graphical view]
PfamiPF00856. SET. 1 hit.
[Graphical view]
PIRSFiPIRSF027717. Histone_H4-K20_mtfrase. 1 hit.
SMARTiSM00317. SET. 1 hit.
[Graphical view]
PROSITEiPS51571. SAM_MT43_PR_SET. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NQR1-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MGEGGAAAAL VAAAAAAAAA AAAVVAGQRR RRLGRRARCH GPGRAAGGKM    50
SKPCAVEAAA AAVAATAPGP EMVERRGPGR PRTDGENVFT GQSKIYSYMS 100
PNKCSGMRFP LQEENSVTHH EVKCQGKPLA GIYRKREEKR NAGNAVRSAM 150
KSEEQKIKDA RKGPLVPFPN QKSEAAEPPK TPPSSCDSTN AAIAKQALKK 200
PIKGKQAPRK KAQGKTQQNR KLTDFYPVRR SSRKSKAELQ SEERKRIDEL 250
IESGKEEGMK IDLIDGKGRG VIATKQFSRG DFVVEYHGDL IEITDAKKRE 300
ALYAQDPSTG CYMYYFQYLS KTYCVDATRE TNRLGRLINH SKCGNCQTKL 350
HDIDGVPHLI LIASRDIAAG EELLYDYGDR SKASIEAHPW LKH 393
Length:393
Mass (Da):42,890
Last modified:November 15, 2002 - v3
Checksum:i2DCD9B697834B5BD
GO
Isoform 2 (identifier: Q9NQR1-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-41: Missing.
     42-57: PGRAAGGKMSKPCAVE → MARGRKMSKPRAVEAA

Show »
Length:352
Mass (Da):39,223
Checksum:iE0DA1AB9881EE4E6
GO

Sequence cautioni

The sequence AAL40879.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4141Missing in isoform 2.
VSP_002226Add
BLAST
Alternative sequencei42 – 5716PGRAA…PCAVE → MARGRKMSKPRAVEAA in isoform 2.
VSP_002227Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti162 – 1632KG → RR in AAF97812. 1 Publication
Sequence conflicti281 – 2811D → A in AAF97812. 1 Publication
Sequence conflicti343 – 3431C → R in AAF97812. 1 Publication
Sequence conflicti357 – 3571P → R in AAH50346. 1 Publication
Sequence conflicti373 – 3731L → P in AAF97812. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY064546 mRNA. Translation: AAL40879.1. Different initiation.
AY102937 mRNA. Translation: AAM47033.1.
AF287261 mRNA. Translation: AAF97812.2.
AK292645 mRNA. Translation: BAF85334.1.
BC050346 mRNA. Translation: AAH50346.1.
CCDSiCCDS9247.1. [Q9NQR1-2]
RefSeqiNP_065115.3. NM_020382.3. [Q9NQR1-2]
UniGeneiHs.443735.
Hs.572262.

Genome annotation databases

EnsembliENST00000330479; ENSP00000332995; ENSG00000183955. [Q9NQR1-2]
ENST00000402868; ENSP00000384629; ENSG00000183955. [Q9NQR1-2]
GeneIDi387893.
KEGGihsa:387893.
UCSCiuc001uew.3. human. [Q9NQR1-2]

Polymorphism databases

DMDMi25091219.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY064546 mRNA. Translation: AAL40879.1 . Different initiation.
AY102937 mRNA. Translation: AAM47033.1 .
AF287261 mRNA. Translation: AAF97812.2 .
AK292645 mRNA. Translation: BAF85334.1 .
BC050346 mRNA. Translation: AAH50346.1 .
CCDSi CCDS9247.1. [Q9NQR1-2 ]
RefSeqi NP_065115.3. NM_020382.3. [Q9NQR1-2 ]
UniGenei Hs.443735.
Hs.572262.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ZKK X-ray 1.45 A/B/C/D 231-393 [» ]
2BQZ X-ray 1.50 A/E 233-393 [» ]
3F9W X-ray 1.60 A/B/C/D 232-393 [» ]
3F9X X-ray 1.25 A/B/C/D 232-393 [» ]
3F9Y X-ray 1.50 A/B 232-393 [» ]
3F9Z X-ray 1.60 A/B/C/D 232-393 [» ]
4IJ8 X-ray 2.00 A/B 232-393 [» ]
ProteinModelPortali Q9NQR1.
SMRi Q9NQR1. Positions 233-393.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 132490. 25 interactions.
DIPi DIP-39133N.
IntActi Q9NQR1. 3 interactions.
MINTi MINT-3072203.
STRINGi 9606.ENSP00000332995.

Chemistry

BindingDBi Q9NQR1.
ChEMBLi CHEMBL1795176.
GuidetoPHARMACOLOGYi 2704.

PTM databases

PhosphoSitei Q9NQR1.

Polymorphism databases

DMDMi 25091219.

Proteomic databases

MaxQBi Q9NQR1.
PaxDbi Q9NQR1.
PRIDEi Q9NQR1.

Protocols and materials databases

DNASUi 387893.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000330479 ; ENSP00000332995 ; ENSG00000183955 . [Q9NQR1-2 ]
ENST00000402868 ; ENSP00000384629 ; ENSG00000183955 . [Q9NQR1-2 ]
GeneIDi 387893.
KEGGi hsa:387893.
UCSCi uc001uew.3. human. [Q9NQR1-2 ]

Organism-specific databases

CTDi 387893.
GeneCardsi GC12P123868.
H-InvDB HIX0037637.
HGNCi HGNC:29489. SETD8.
HPAi HPA053747.
MIMi 607240. gene.
neXtProti NX_Q9NQR1.
PharmGKBi PA143485616.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2940.
HOGENOMi HOG000020818.
HOVERGENi HBG067546.
InParanoidi Q9NQR1.
KOi K11428.
OMAi CSGMRSP.
OrthoDBi EOG70KGRN.
PhylomeDBi Q9NQR1.
TreeFami TF335181.

Enzyme and pathway databases

BRENDAi 2.1.1.43. 2681.
Reactomei REACT_172744. Condensation of Prophase Chromosomes.

Miscellaneous databases

EvolutionaryTracei Q9NQR1.
GeneWikii SETD8.
GenomeRNAii 387893.
NextBioi 101711.
PROi Q9NQR1.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NQR1.
Bgeei Q9NQR1.
CleanExi HS_SETD8.
Genevestigatori Q9NQR1.

Family and domain databases

InterProi IPR016858. Hist_H4-K20_MeTrfase.
IPR001214. SET_dom.
[Graphical view ]
Pfami PF00856. SET. 1 hit.
[Graphical view ]
PIRSFi PIRSF027717. Histone_H4-K20_mtfrase. 1 hit.
SMARTi SM00317. SET. 1 hit.
[Graphical view ]
PROSITEi PS51571. SAM_MT43_PR_SET. 1 hit.
PS50280. SET. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "PR-Set7 is a nucleosome-specific methyltransferase that modifies lysine 20 of histone H4 and is associated with silent chromatin."
    Nishioka K., Rice J.C., Sarma K., Erdjument-Bromage H., Werner J., Wang Y., Chuikov S., Valenzuela P., Tempst P., Steward R., Lis J.T., Allis C.D., Reinberg D.
    Mol. Cell 9:1201-1213(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 108-131; 220-231 AND 349-393, FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-336.
    Tissue: Cervix carcinoma.
  2. "Purification and functional characterization of SET8, a nucleosomal histone H4-lysine 20-specific methyltransferase."
    Fang J., Feng Q., Ketel C.S., Wang H., Cao R., Xia L., Erdjument-Bromage H., Tempst P., Simon J.A., Zhang Y.
    Curr. Biol. 12:1086-1099(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 83-103; 109-134; 141-151; 162-172; 221-230; 245-260; 280-297 AND 350-393, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-340 AND 385-ILE--HIS-393.
  3. "A novel PR/SET domain-containing gene, SET07, as a candidate tumor suppressor."
    Tain F., Huang S.
    Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Thymus.
  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] (ISOFORM 2).
    Tissue: Testis.
  6. "Mitotic-specific methylation of histone H4 Lys 20 follows increased PR-Set7 expression and its localization to mitotic chromosomes."
    Rice J.C., Nishioka K., Sarma K., Steward R., Reinberg D., Allis C.D.
    Genes Dev. 16:2225-2230(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
  7. "A switch in mitotic histone H4 lysine 20 methylation status is linked to M phase defects upon loss of HCF-1."
    Julien E., Herr W.
    Mol. Cell 14:713-725(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  8. "SET8 recognizes the sequence RHRK20VLRDN within the N terminus of histone H4 and mono-methylates lysine 20."
    Yin Y., Liu C., Tsai S.N., Zhou B., Ngai S.M., Zhu G.
    J. Biol. Chem. 280:30025-30031(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY.
  9. "A trans-tail histone code defined by monomethylated H4 Lys-20 and H3 Lys-9 demarcates distinct regions of silent chromatin."
    Sims J.K., Houston S.I., Magazinnik T., Rice J.C.
    J. Biol. Chem. 281:12760-12766(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Modulation of p53 function by SET8-mediated methylation at lysine 382."
    Shi X., Kachirskaia I., Yamaguchi H., West L.E., Wen H., Wang E.W., Dutta S., Appella E., Gozani O.
    Mol. Cell 27:636-646(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-379.
  11. "Histone H4 lysine 20 monomethylation promotes transcriptional repression by L3MBTL1."
    Kalakonda N., Fischle W., Boccuni P., Gurvich N., Hoya-Arias R., Zhao X., Miyata Y., Macgrogan D., Zhang J., Sims J.K., Rice J.C., Nimer S.D.
    Oncogene 27:4293-4304(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH L3MBTL1.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "The MBT repeats of L3MBTL1 link SET8-mediated p53 methylation at lysine 382 to target gene repression."
    West L.E., Roy S., Lachmi-Weiner K., Hayashi R., Shi X., Appella E., Kutateladze T.G., Gozani O.
    J. Biol. Chem. 285:37725-37732(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-379.
  14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "The tumor suppressor SirT2 regulates cell cycle progression and genome stability by modulating the mitotic deposition of H4K20 methylation."
    Serrano L., Martinez-Redondo P., Marazuela-Duque A., Vazquez B.N., Dooley S.J., Voigt P., Beck D.B., Kane-Goldsmith N., Tong Q., Rabanal R.M., Fondevila D., Munoz P., Kruger M., Tischfield J.A., Vaquero A.
    Genes Dev. 27:639-653(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-172, DEACETYLATION AT LYS-172 BY SIRT2, INTERACTION WITH SIRT2, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-172, MASS SPECTROMETRY (ISOFORM 2).
  16. "CRL1-FBXO11 promotes Cdt2 ubiquitylation and degradation and regulates Pr-Set7/Set8-mediated cellular migration."
    Abbas T., Mueller A.C., Shibata E., Keaton M., Rossi M., Dutta A.
    Mol. Cell 49:1147-1158(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION, UBIQUITINATION, MUTAGENESIS OF ARG-336 AND ASP-379.
  17. Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 233-393 IN COMPLEX WITH HISTONE H4 AND S-ADENOSYLMETHIONINE, FUNCTION.
  18. "Structural and functional analysis of SET8, a histone H4 'Lys-20' methyltransferase."
    Couture J.-F., Collazo E., Brunzelle J.S., Trievel R.C.
    Genes Dev. 19:1455-1465(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 231-393 IN COMPLEX WITH HISTONE H4 AND S-ADENOSYLMETHIONINE, FUNCTION, MUTAGENESIS OF TYR-286; GLU-300; CYS-311; TYR-375; ASP-379 AND HIS-388.

Entry informationi

Entry nameiSETD8_HUMAN
AccessioniPrimary (citable) accession number: Q9NQR1
Secondary accession number(s): A8K9D0, Q86W83, Q8TD09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 15, 2002
Last modified: September 3, 2014
This is version 134 of the entry and version 3 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

Caution

It is uncertain whether Met-1 or Met-72 is the initiator.

Keywords - Technical termi

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

Documents

  1. Human chromosome 12
    Human chromosome 12: 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

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