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Q9NQR1 (SETD8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SETD8
Synonyms:KMT5A, PRSET7, SET07, SET8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.7 Ref.9 Ref.10 Ref.15 Ref.16 Ref.17

Catalytic activity

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. Ref.1 Ref.2 Ref.8

Subunit structure

Interacts with L3MBTL1. Ref.11

Subcellular location

Nucleus. Chromosome. Note: Specifically localizes to mitotic chromosomes. Associates with silent chromatin on euchromatic arms. Not associated with constitutive heterochromatin. Ref.1 Ref.6

Developmental stage

Not detected during G1 phase. First detected during S through G2 phases, and peaks during mitosis (at protein level). Ref.6

Induction

By HCFC1 C-terminal chain, independently of HCFC1 N-terminal chain. Transiently induced by TGF-beta and during the cell cycle. Ref.7 Ref.15

Domain

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.

Post-translational modification

Ubiquitinated and degraded by the DCX(DTL) complex Probable. Ref.15

Sequence similarities

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. PR/SET subfamily.

Contains 1 SET domain.

Caution

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

Sequence caution

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

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
Transcription
Transcription regulation
   Cellular componentChromosome
Nucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   LigandS-adenosyl-L-methionine
   Molecular functionChromatin regulator
Methyltransferase
Repressor
Transferase
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processhistone lysine methylation

Inferred from direct assay Ref.10. Source: GOC

mitotic cell cycle

Traceable author statement. Source: Reactome

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.10. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 18474616. Source: UniProtKB

peptidyl-lysine monomethylation

Inferred from direct assay Ref.10. Source: UniProtKB

regulation of DNA damage response, signal transduction by p53 class mediator

Inferred from mutant phenotype Ref.10. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchromosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionhistone-lysine N-methyltransferase activity

Inferred from direct assay Ref.10. Source: UniProtKB

p53 binding

Inferred from physical interaction Ref.10. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.11. Source: UniProtKB

protein-lysine N-methyltransferase activity

Inferred from direct assay Ref.10. Source: UniProtKB

transcription corepressor activity

Inferred from direct assay Ref.11. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HIST2H4BP628055EBI-1268946,EBI-302023
TWIST1Q156725EBI-1268946,EBI-1797287

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NQR1-1)

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.
Isoform 2 (identifier: Q9NQR1-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 393393N-lysine methyltransferase SETD8
PRO_0000186081

Regions

Domain257 – 378122SET
Region267 – 2693S-adenosyl-L-methionine binding
Region339 – 3402S-adenosyl-L-methionine binding
Coiled coil134 – 16330 Potential
Compositional bias6 – 6762Ala-rich
Compositional bias29 – 324Poly-Arg

Sites

Binding site3121S-adenosyl-L-methionine

Amino acid modifications

Modified residue1001Phosphoserine Ref.12 Ref.14

Natural variations

Alternative sequence1 – 4141Missing in isoform 2.
VSP_002226
Alternative sequence42 – 5716PGRAA…PCAVE → MARGRKMSKPRAVEAA in isoform 2.
VSP_002227

Experimental info

Mutagenesis2861Y → A or F: Strongly reduces affinity for histone H4 and abolishes methyltransferase activity. Ref.17
Mutagenesis3001E → A: Strongly reduces affinity for histone H4. Ref.17
Mutagenesis3111C → A: Strongly reduces affinity for histone H4. Ref.17
Mutagenesis3361R → G: Abolishes methyltransferase activity. Ref.1 Ref.15
Mutagenesis3401H → A: Strongly decreases methyltransferase activity. Ref.2
Mutagenesis3751Y → A: Strongly reduces affinity for histone H4 and methyltransferase activity. Ref.17
Mutagenesis3751Y → F: Alters methyltransferase activity, so that both monomethylation and dimethylation take place. Ref.17
Mutagenesis3791D → A or N: Abolishes histone H4 binding and methyltransferase activity. Ref.10 Ref.13 Ref.15 Ref.17
Mutagenesis385 – 3939Missing: Abolishes methyltransferase activity. Ref.2
Mutagenesis3881H → A or E: Strongly reduces affinity for histone H4. Ref.17
Mutagenesis3881H → F: Increases affinity for histone H4. Ref.17
Sequence conflict162 – 1632KG → RR in AAF97812. Ref.3
Sequence conflict2811D → A in AAF97812. Ref.3
Sequence conflict3431C → R in AAF97812. Ref.3
Sequence conflict3571P → R in AAH50346. Ref.5
Sequence conflict3731L → P in AAF97812. Ref.3

Secondary structure

............................ 393
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 15, 2002. Version 3.
Checksum: 2DCD9B697834B5BD

FASTA39342,890
        10         20         30         40         50         60 
MGEGGAAAAL VAAAAAAAAA AAAVVAGQRR RRLGRRARCH GPGRAAGGKM SKPCAVEAAA 

        70         80         90        100        110        120 
AAVAATAPGP EMVERRGPGR PRTDGENVFT GQSKIYSYMS PNKCSGMRFP LQEENSVTHH 

       130        140        150        160        170        180 
EVKCQGKPLA GIYRKREEKR NAGNAVRSAM KSEEQKIKDA RKGPLVPFPN QKSEAAEPPK 

       190        200        210        220        230        240 
TPPSSCDSTN AAIAKQALKK PIKGKQAPRK KAQGKTQQNR KLTDFYPVRR SSRKSKAELQ 

       250        260        270        280        290        300 
SEERKRIDEL IESGKEEGMK IDLIDGKGRG VIATKQFSRG DFVVEYHGDL IEITDAKKRE 

       310        320        330        340        350        360 
ALYAQDPSTG CYMYYFQYLS KTYCVDATRE TNRLGRLINH SKCGNCQTKL HDIDGVPHLI 

       370        380        390 
LIASRDIAAG EELLYDYGDR SKASIEAHPW LKH 

« Hide

Isoform 2 [UniParc].

Checksum: E0DA1AB9881EE4E6
Show »

FASTA35239,223

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"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.
[16]"Specificity and mechanism of the histone methyltransferase Pr-Set7."
Xiao B., Jing C., Kelly G., Walker P.A., Muskett F.W., Frenkiel T.A., Martin S.R., Sarma K., Reinberg D., Gamblin S.J., Wilson J.R.
Genes Dev. 19:1444-1454(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 233-393 IN COMPLEX WITH HISTONE H4 AND S-ADENOSYLMETHIONINE, FUNCTION.
[17]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS9247.1. [Q9NQR1-2]
RefSeqNP_065115.3. NM_020382.3. [Q9NQR1-2]
UniGeneHs.443735.
Hs.572262.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ9NQR1.
SMRQ9NQR1. Positions 233-393.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid132490. 25 interactions.
DIPDIP-39133N.
IntActQ9NQR1. 3 interactions.
MINTMINT-3072203.
STRING9606.ENSP00000332995.

Chemistry

BindingDBQ9NQR1.
ChEMBLCHEMBL1795176.
GuidetoPHARMACOLOGY2704.

PTM databases

PhosphoSiteQ9NQR1.

Polymorphism databases

DMDM25091219.

Proteomic databases

MaxQBQ9NQR1.
PaxDbQ9NQR1.
PRIDEQ9NQR1.

Protocols and materials databases

DNASU387893.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000330479; ENSP00000332995; ENSG00000183955. [Q9NQR1-2]
ENST00000402868; ENSP00000384629; ENSG00000183955. [Q9NQR1-2]
GeneID387893.
KEGGhsa:387893.
UCSCuc001uew.3. human. [Q9NQR1-2]

Organism-specific databases

CTD387893.
GeneCardsGC12P123868.
H-InvDBHIX0037637.
HGNCHGNC:29489. SETD8.
HPAHPA053747.
MIM607240. gene.
neXtProtNX_Q9NQR1.
PharmGKBPA143485616.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2940.
HOGENOMHOG000020818.
HOVERGENHBG067546.
InParanoidQ9NQR1.
KOK11428.
OMACSGMRSP.
OrthoDBEOG70KGRN.
PhylomeDBQ9NQR1.
TreeFamTF335181.

Enzyme and pathway databases

BRENDA2.1.1.43. 2681.
ReactomeREACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.

Gene expression databases

ArrayExpressQ9NQR1.
BgeeQ9NQR1.
CleanExHS_SETD8.
GenevestigatorQ9NQR1.

Family and domain databases

InterProIPR016858. Hist_H4-K20_MeTrfase.
IPR001214. SET_dom.
[Graphical view]
PfamPF00856. SET. 1 hit.
[Graphical view]
PIRSFPIRSF027717. Histone_H4-K20_mtfrase. 1 hit.
SMARTSM00317. SET. 1 hit.
[Graphical view]
PROSITEPS51571. SAM_MT43_PR_SET. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9NQR1.
GeneWikiSETD8.
GenomeRNAi387893.
NextBio101711.
PROQ9NQR1.
SOURCESearch...

Entry information

Entry nameSETD8_HUMAN
AccessionPrimary (citable) accession number: Q9NQR1
Secondary accession number(s): A8K9D0, Q86W83, Q8TD09
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 15, 2002
Last modified: July 9, 2014
This is version 133 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM