Reviewed,
UniProtKB/Swiss-Prot Q53H47 (SETMR_HUMAN)
Last modified
June 16, 2009.
Version 41.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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Names and origin
| Protein names | Recommended 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 |
| ||
| Organism | Homo sapiens (Human) | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 671 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
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. |
Ontologies
| Keywords | |
|---|---|
| Biological process | DNA damage DNA repair |
| Cellular component | Nucleus |
| Coding sequence diversity | Alternative splicing |
| Domain | Coiled coil |
| Ligand | DNA-binding |
| Molecular function | Chromatin regulator Methyltransferase Transferase |
| PTM | Phosphoprotein |
| Technical term | 3D-structure |
| Gene Ontology (GO) | |
| Biological process | DNA repair Inferred from electronic annotation. Source: UniProtKB-KW chromatin modificationInferred from electronic annotation. Source: UniProtKB-KW transposition, DNA-mediated Ref.5Traceable author statement. Source: UniProtKB |
| Cellular component | nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | DNA binding Inferred from electronic annotation. Source: UniProtKB-KW histone-lysine N-methyltransferase activityInferred from electronic annotation. Source: EC transposase activity Ref.5Traceable author statement. Source: UniProtKB zinc ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
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. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 671 | 671 | Histone-lysine N-methyltransferase SETMAR | PRO_0000259526 | |||||
Regions | |||||||||
| Domain | 60 – 123 | 64 | Pre-SET | ||||||
| Domain | 125 – 254 | 130 | SET | ||||||
| Domain | 270 – 286 | 17 | Post-SET | ||||||
| Region | 1 – 332 | 332 | Histone-lysine N-methyltransferase | ||||||
| Region | 333 – 671 | 339 | Mariner transposase Hsmar1 | ||||||
| Coiled coil | 539 – 569 | 31 | Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 325 | 1 | Phosphothreonine Ref.6 | ||||||
| Modified residue | 328 | 1 | Phosphothreonine Ref.6 | ||||||
Natural variations | |||||||||
| Alternative sequence | 328 – 352 | 25 | TMKMM…MGRKA → VSLFSDKQLAPPYSGRQWLA SFTSA in isoform 2. | VSP_021440 | |||||
| Alternative sequence | 353 – 671 | 319 | Missing in isoform 2. | VSP_021441 | |||||
Experimental info | |||||||||
| Mutagenesis | 210 | 1 | N → S: Reduces activity in double strand break repair. Ref.1 | ||||||
| Mutagenesis | 248 | 1 | D → S: Reduces activity in double strand break repair. Ref.1 | ||||||
| Mutagenesis | 490 | 1 | D → S: Reduces activity in double strand break repair. Ref.1 | ||||||
| Sequence conflict | 330 | 1 | K → E in AAC52010. Ref.5 | ||||||
| Sequence conflict | 426 | 1 | N → D in AAC52010. Ref.5 | ||||||
| Sequence conflict | 452 | 1 | T → S in AAC52010. Ref.5 | ||||||
| Sequence conflict | 471 | 1 | H → N in AAC52010. Ref.5 | ||||||
| Sequence conflict | 495 | 1 | S → P in AAC52010. Ref.5 | ||||||
| Sequence conflict | 501 | 1 | Q → R in AAC52010. Ref.5 | ||||||
| Sequence conflict | 512 | 1 | I → N in AAC52010. Ref.5 | ||||||
| Sequence conflict | 515 | 1 | P → Q in AAC52010. Ref.5 | ||||||
| Sequence conflict | 522 | 1 | I → V in AAC52010. Ref.5 | ||||||
| Sequence conflict | 549 | 1 | E → Q in AAC52010. Ref.5 | ||||||
| Sequence conflict | 554 – 555 | 2 | NQ → HR in AAC52010. Ref.5 | ||||||
| Sequence conflict | 562 | 1 | L → P in AAC52010. Ref.5 | ||||||
| Sequence conflict | 607 | 1 | L → S in AAC52010. Ref.5 | ||||||
| Sequence conflict | 610 | 1 | N → D in AAC52010. Ref.5 | ||||||
| Sequence conflict | 613 | 1 | V → F in AAC52010. Ref.5 | ||||||
| Sequence conflict | 618 | 1 | N → D in AAC52010. Ref.5 | ||||||
| Sequence conflict | 643 | 1 | Q → R in AAC52010. Ref.5 | ||||||
| Sequence conflict | 654 | 1 | Q → K in AAC52010. Ref.5 | ||||||
Sequences
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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. |
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. | |||||||||||||||||||
| IPI | IPI00171821. IPI00879669. | ||||||||||||||||||
| RefSeq | NP_006506.3. | ||||||||||||||||||
| UniGene | Hs.475300 | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
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| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| IntAct | Q53H47. 1 interaction. | ||||||||||||||||||
PTM databases | |||||||||||||||||||
| PhosphoSite | Q53H47. | ||||||||||||||||||
Proteomic databases | |||||||||||||||||||
| PRIDE | Q53H47. | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| Ensembl | ENSG00000170364. Homo sapiens. [Contig view] | ||||||||||||||||||
| GeneID | 6419. | ||||||||||||||||||
| KEGG | hsa:6419. | ||||||||||||||||||
| NMPDR | fig|9606.3.peg.22044. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| GeneCards | GC03P004320. | ||||||||||||||||||
| H-InvDB | HIX0003012. | ||||||||||||||||||
| HGNC | HGNC:10762. SETMAR. | ||||||||||||||||||
| MIM | 609834. gene. | ||||||||||||||||||
| PharmGKB | PA35680. | ||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| HOVERGEN | Q53H47. | ||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||
| BRENDA | 2.1.1.43. 247. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| ArrayExpress | Q53H47. | ||||||||||||||||||
| Bgee | Q53H47. | ||||||||||||||||||
| CleanEx | HS_SETMAR. | ||||||||||||||||||
| GermOnline | ENSG00000170364. Homo sapiens. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR003616. Post-SET_Zn_bd. IPR007728. Pre-SET_Zn_bd. IPR003606. Pre-SET_Zn_bd_sub. IPR001214. SET. IPR001888. Transposase_1. [Graphical view] | ||||||||||||||||||
| Pfam | PF05033. Pre-SET. 1 hit. PF00856. SET. 1 hit. PF01359. Transposase_1. 1 hit. [Graphical view] | ||||||||||||||||||
| SMART | SM00508. PostSET. 1 hit. SM00468. PreSET. 1 hit. SM00317. SET. 1 hit. [Graphical view] | ||||||||||||||||||
| PROSITE | PS50868. POST_SET. 1 hit. PS50867. PRE_SET. 1 hit. PS50280. SET. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other Resources | |||||||||||||||||||
| NextBio | 24930. | ||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||
Entry information
| Entry name | SETMR_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q53H47 Secondary accession number(s): Q13579, Q1G668, Q96F41 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
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 |

Clusters with


