SETMAR
Histone-lysine N-methyltransferase SETMAR
Also known as: metnase, SETMR_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q53H47
- Gene
- SETMAR
- Ensembl
- ENSG00000170364
- Chromosome
- 3
- Canonical length
- 684 aa
- Protein class
- Enzymes, Metabolic proteins, Predicted intracellular proteins
- Subcellular location
- Nucleoli
- Quaternary structure
- Homodimer
OverviewNCBI Gene
This gene encodes a fusion protein that contains an N-terminal histone-lysine N-methyltransferase domain and a C-terminal mariner transposase domain. The encoded protein binds DNA and functions in DNA repair activities including non-homologous end joining and double strand break repair. The SET domain portion of this protein specifically methylates histone H3 lysines 4 and 36. This gene exists as a fusion gene only in anthropoid primates, other organisms lack mariner transposase domain. Alternate splicing results in multiple transcript variants. [provided by RefSeq, Jan 2013]
Canonical amino-acid sequenceUniProt
684 residues, UniProt reviewed canonical sequence.
>Q53H47|SETMAR
1 MFAEAAKTTR PCGMAEFKEK PEAPTEQLDV ACGQENLPVG AWPPGAAPAP FQYTPDHVVG
61 PGADIDPTQI TFPGCICVKT PCLPGTCSCL RHGENYDDNS CLRDIGSGGK YAEPVFECNV
121 LCRCSDHCRN RVVQKGLQFH FQVFKTHKKG WGLRTLEFIP KGRFVCEYAG EVLGFSEVQR
181 RIHLQTKSDS NYIIAIREHV YNGQVMETFV DPTYIGNIGR FLNHSCEPNL LMIPVRIDSM
241 VPKLALFAAK DIVPEEELSY DYSGRYLNLT VSEDKERLDH GKLRKPCYCG AKSCTAFLPF
301 DSSLYCPVEK SNISCGNEKE PSMCGSAPSV FPSCKRLTLE TMKMMLDKKQ IRAIFLFEFK
361 MGRKAAETTR NINNAFGPGT ANERTVQWWF KKFCKGDESL EDEERSGRPS EVDNDQLRAI
421 IEADPLTTTR EVAEELNVNH STVVRHLKQI GKVKKLDKWV PHELTENQKN RRFEVSSSLI
481 LRNHNEPFLD RIVTCDEKWI LYDNRRRSAQ WLDQEEAPKH FPKPILHPKK VMVTIWWSAA
541 GLIHYSFLNP GETITSEKYA QEIDEMNQKL QRLQLALVNR KGPILLHDNA RPHVAQPTLQ
601 KLNELGYEVL PHPPYSPDLL PTNYHVFKHL NNFLQGKRFH NQQDAENAFQ EFVESQSTDF
661 YATGINQLIS RWQKCVDCNG SYFDLocalizationUniProt · AlphaFold · HPA
Whether an antibody against SETMAR can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Intracellular
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.35
- Highest tissue expression
- 13 nTPM
Expression across tissuesHPA
Tissue
- ovary: 13 nTPM
- endometrium: 12 nTPM
- smooth muscle: 11 nTPM
- blood vessel: 9.6 nTPM
- breast: 9.5 nTPM
- fallopian tube: 9.5 nTPM
Single-cell type
- epicardial cells: 43 nCPM
- adipocytes: 36 nCPM
- sertoli cells: 35 nCPM
- cytotrophoblasts: 34 nCPM
- cardiomyocytes: 30 nCPM
- breast myoepithelial cells: 28 nCPM
Immune cell
- naive CD8 T-cell: 1.8 nTPM
- naive CD4 T-cell: 1.6 nTPM
- naive B-cell: 1.3 nTPM
- intermediate monocyte: 1 nTPM
- memory B-cell: 1 nTPM
- memory CD4 T-cell: 1 nTPM
Brain region
- white matter: 15 nTPM
- basal ganglia: 12 nTPM
- thalamus: 12 nTPM
- pons: 11 nTPM
- medulla oblongata: 11 nTPM
- cerebellum: 9.8 nTPM
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 1.13
- gnomAD pLI
- 0
- gnomAD missense Z
- 0.26
- DepMap mean gene effect
- 0.08
- DepMap dependency class
- none
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 4% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- cell population proliferation
- DNA catabolic process
- DNA double-strand break processing
- DNA integration
- double-strand break repair via nonhomologous end joining
- methylation
- nucleic acid metabolic process
- positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity
- positive regulation of double-strand break repair via nonhomologous end joining
- replication fork processing
- mitotic DNA integrity checkpoint signaling
- negative regulation of chromosome organization
Molecular functions
- DNA binding
- DNA topoisomerase binding
- double-stranded DNA binding
- endonuclease activity
- histone H3K36 dimethyltransferase activity
- histone H3K36 methyltransferase activity
- histone H3K4 methyltransferase activity
- protein homodimerization activity
- single-stranded DNA binding
- single-stranded DNA endodeoxyribonuclease activity
- zinc ion binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
- SET domain
- Post-SET domain
- Pre-SET domain
- Winged helix-like DNA-binding domain superfamily
- Ribonuclease H superfamily
- Mos1 transposase, HTH domain
- SET domain superfamily
- Transposase-Methyltransferase Hybrid
- SET domain
- Pre-SET motif
- HTH domain in Mos1 transposase
- Transposase, type 1
- Transposase (partial DDE domain)
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of SETMAR in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads SETMAR as an antibody target. Whether an autoantibody or antibody against SETMAR could matter depends on whether native SETMAR is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
SETMAR is annotated as predominantly intracellular. Intracellular proteins are common autoantibody markers, becoming visible to the immune system after cell injury or altered processing, but are usually markers of disease rather than direct drivers.
Annotation status
The present source text does not explicitly label SETMAR as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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