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Reviewed, UniProtKB/Swiss-Prot Q53H47 (SETMR_HUMAN)

Last modified June 16, 2009. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Histone-lysine N-methyltransferase SETMAR
    EC=2.1.1.43
Alternative name(s):
    SET domain and mariner transposase fusion gene-containing protein
      Short name=Metnase
      Short name=Hsmar1
Including the following 2 domains:
    1- Recommended name:
            Histone-lysine N-methyltransferase
    2- Recommended name:
            Mariner transposase Hsmar1
Gene names
Name: SETMAR
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length671 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Histone methyltransferase that methylates 'Lys-4' and 'Lys-36' of histone H3, 2 specific tags for epigenetic transcriptional activation. Specifically mediates dimethylation of H3 'Lys-36'. Binds DNA. May play a role in non-homologous end-joining repair. Ref.1 Ref.4

Catalytic activity

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

Subcellular location

Nucleus Probable.

Tissue specificity

Widely expressed, with highest expression in placenta and ovary and lowest expression in skeletal muscle. Ref.1

Domain

The mariner transposase Hsmar1 region mediates DNA-binding. It has no transposase activity because the active site contains an Asn in position 610 instead of a Asp residue.

Miscellaneous

The mariner transposase region in only present in primates and appeared 40-58 million years ago, after the insertion of a transposon downstream of a preexisting SET gene, followed by the de novo exonization of previously non-coding sequence and the creation of a new intron.

Sequence similarities

In the N-terminal section; belongs to the histone-lysine methyltransferase family.

In the C-terminal section; belongs to the mariner transposase family.

Contains 1 post-SET domain.

Contains 1 pre-SET domain.

Contains 1 SET domain.

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Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   LigandDNA-binding
   Molecular functionChromatin regulator
Methyltransferase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processDNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin modification

Inferred from electronic annotation. Source: UniProtKB-KW

transposition, DNA-mediated Ref.5

Traceable author statement. Source: UniProtKB

   Cellular componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

histone-lysine N-methyltransferase activity

Inferred from electronic annotation. Source: EC

transposase activity Ref.5

Traceable author statement. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q53H47-1)

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: Q53H47-2)

The sequence of this isoform differs from the canonical sequence as follows:
     328-352: TMKMMLDKKQIRAIFLFEFKMGRKA → VSLFSDKQLAPPYSGRQWLASFTSA
     353-671: Missing.
Note: No experimental confirmation available.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 671671Histone-lysine N-methyltransferase SETMAR
PRO_0000259526

Regions

Domain60 – 12364Pre-SET
Domain125 – 254130SET
Domain270 – 28617Post-SET
Region1 – 332332Histone-lysine N-methyltransferase
Region333 – 671339Mariner transposase Hsmar1
Coiled coil539 – 56931 Potential

Amino acid modifications

Modified residue3251Phosphothreonine Ref.6
Modified residue3281Phosphothreonine Ref.6

Natural variations

Alternative sequence328 – 35225TMKMM…MGRKA → VSLFSDKQLAPPYSGRQWLA SFTSA in isoform 2.
VSP_021440
Alternative sequence353 – 671319Missing in isoform 2.
VSP_021441

Experimental info

Mutagenesis2101N → S: Reduces activity in double strand break repair. Ref.1
Mutagenesis2481D → S: Reduces activity in double strand break repair. Ref.1
Mutagenesis4901D → S: Reduces activity in double strand break repair. Ref.1
Sequence conflict3301K → E in AAC52010. Ref.5
Sequence conflict4261N → D in AAC52010. Ref.5
Sequence conflict4521T → S in AAC52010. Ref.5
Sequence conflict4711H → N in AAC52010. Ref.5
Sequence conflict4951S → P in AAC52010. Ref.5
Sequence conflict5011Q → R in AAC52010. Ref.5
Sequence conflict5121I → N in AAC52010. Ref.5
Sequence conflict5151P → Q in AAC52010. Ref.5
Sequence conflict5221I → V in AAC52010. Ref.5
Sequence conflict5491E → Q in AAC52010. Ref.5
Sequence conflict554 – 5552NQ → HR in AAC52010. Ref.5
Sequence conflict5621L → P in AAC52010. Ref.5
Sequence conflict6071L → S in AAC52010. Ref.5
Sequence conflict6101N → D in AAC52010. Ref.5
Sequence conflict6131V → F in AAC52010. Ref.5
Sequence conflict6181N → D in AAC52010. Ref.5
Sequence conflict6431Q → R in AAC52010. Ref.5
Sequence conflict6541Q → K in AAC52010. Ref.5

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Sequences

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

Last modified May 24, 2005. Version 1.
Checksum: A0349ADF2F12D920

FASTA67176,669
        10         20         30         40         50         60 
MAEFKEKPEA PTEQLDVACG QENLPVGAWP PGAAPAPFQY TPDHVVGPGA DIDPTQITFP 

        70         80         90        100        110        120 
GCICVKTPCL PGTCSCLRHG ENYDDNSCLR DIGSGGKYAE PVFECNVLCR CSDHCRNRVV 

       130        140        150        160        170        180 
QKGLQFHFQV FKTHKKGWGL RTLEFIPKGR FVCEYAGEVL GFSEVQRRIH LQTKSDSNYI 

       190        200        210        220        230        240 
IAIREHVYNG QVMETFVDPT YIGNIGRFLN HSCEPNLLMI PVRIDSMVPK LALFAAKDIV 

       250        260        270        280        290        300 
PEEELSYDYS GRYLNLTVSE DKERLDHGKL RKPCYCGAKS CTAFLPFDSS LYCPVEKSNI 

       310        320        330        340        350        360 
SCGNEKEPSM CGSAPSVFPS CKRLTLETMK MMLDKKQIRA IFLFEFKMGR KAAETTRNIN 

       370        380        390        400        410        420 
NAFGPGTANE RTVQWWFKKF CKGDESLEDE ERSGRPSEVD NDQLRAIIEA DPLTTTREVA 

       430        440        450        460        470        480 
EELNVNHSTV VRHLKQIGKV KKLDKWVPHE LTENQKNRRF EVSSSLILRN HNEPFLDRIV 

       490        500        510        520        530        540 
TCDEKWILYD NRRRSAQWLD QEEAPKHFPK PILHPKKVMV TIWWSAAGLI HYSFLNPGET 

       550        560        570        580        590        600 
ITSEKYAQEI DEMNQKLQRL QLALVNRKGP ILLHDNARPH VAQPTLQKLN ELGYEVLPHP 

       610        620        630        640        650        660 
PYSPDLLPTN YHVFKHLNNF LQGKRFHNQQ DAENAFQEFV ESQSTDFYAT GINQLISRWQ 

       670 
KCVDCNGSYF D

« Hide

Isoform 2.

Checksum: 053C81EE8219AE96
Show »

FASTA35239,146

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References

« Hide 'large scale' references
[1]"The SET domain protein Metnase mediates foreign DNA integration and links integration to nonhomologous end-joining repair."
Lee S.-H., Oshige M., Durant S.T., Rasila K.K., Williamson E.A., Ramsey H., Kwan L., Nickoloff J.A., Hromas R.
Proc. Natl. Acad. Sci. U.S.A. 102:18075-18080(2005) [PubMed: 16332963] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF ASN-210; ASP-248 AND ASP-490.
[2]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Dermoid cancer.
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Uterus.
[4]"Birth of a chimeric primate gene by capture of the transposase gene from a mobile element."
Cordaux R., Udit S., Batzer M.A., Feschotte C.
Proc. Natl. Acad. Sci. U.S.A. 103:8101-8106(2006) [PubMed: 16672366] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 328-671, FUNCTION, DNA-BINDING.
[5]"Molecular evolution of an ancient mariner transposon, Hsmar1, in the human genome."
Robertson H.M., Zumpano K.L.
Gene 205:203-217(1997) [PubMed: 9461395] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.
Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-325 AND THR-328, MASS SPECTROMETRY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AY952295 mRNA. Translation: AAY29570.1.
AK222734 mRNA. Translation: BAD96454.1.
BC011635 mRNA. Translation: AAH11635.1.
DQ341316 Genomic DNA. Translation: ABC72087.1.
U52077 Genomic DNA. Translation: AAC52010.1.
IPIIPI00171821.
IPI00879669.
RefSeqNP_006506.3.
UniGeneHs.475300

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
3BO5X-ray1.59A2-290[»]
3F2KX-ray1.85A/B446-671[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ53H47. 1 interaction.

PTM databases

PhosphoSiteQ53H47.

Proteomic databases

PRIDEQ53H47.

Genome annotation databases

EnsemblENSG00000170364. Homo sapiens. [Contig view]
GeneID6419.
KEGGhsa:6419.
NMPDRfig|9606.3.peg.22044.

Organism-specific databases

GeneCardsGC03P004320.
H-InvDBHIX0003012.
HGNCHGNC:10762. SETMAR.
MIM609834. gene.
PharmGKBPA35680.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ53H47.

Enzyme and pathway databases

BRENDA2.1.1.43. 247.

Gene expression databases

ArrayExpressQ53H47.
BgeeQ53H47.
CleanExHS_SETMAR.
GermOnlineENSG00000170364. Homo sapiens.

Family and domain databases

InterProIPR003616. Post-SET_Zn_bd.
IPR007728. Pre-SET_Zn_bd.
IPR003606. Pre-SET_Zn_bd_sub.
IPR001214. SET.
IPR001888. Transposase_1.
[Graphical view]
PfamPF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
PF01359. Transposase_1. 1 hit.
[Graphical view]
SMARTSM00508. PostSET. 1 hit.
SM00468. PreSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
PROSITEPS50868. POST_SET. 1 hit.
PS50867. PRE_SET. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio24930.
SOURCESearch...

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Entry information

Entry nameSETMR_HUMAN
AccessionPrimary (citable) accession number: Q53H47
Secondary accession number(s): Q13579, Q1G668, Q96F41
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: May 24, 2005
Last modified: June 16, 2009
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents