Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Histone-lysine N-methyltransferase SETMAR

Gene

SETMAR

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protein derived from the fusion of a methylase with the transposase of an Hsmar1 transposon that plays a role in DNA double-strand break repair, stalled replication fork restart and DNA integration. DNA-binding protein, it is indirectly recruited to sites of DNA damage through protein-protein interactions. Has also kept a sequence-specific DNA-binding activity recognizing the 19-mer core of the 5'-terminal inverted repeats (TIRs) of the Hsmar1 element and displays a DNA nicking and end joining activity (PubMed:16332963, PubMed:16672366, PubMed:17877369, PubMed:17403897, PubMed:18263876, PubMed:22231448, PubMed:24573677, PubMed:20521842). In parallel, has a histone methyltransferase activity and methylates 'Lys-4' and 'Lys-36' of histone H3. Specifically mediates dimethylation of H3 'Lys-36' at sites of DNA double-strand break and may recruit proteins required for efficient DSB repair through non-homologous end-joining (PubMed:16332963, PubMed:21187428, PubMed:22231448). Also regulates replication fork processing, promoting replication fork restart and regulating DNA decatenation through stimulation of the topoisomerase activity of TOP2A (PubMed:18790802, PubMed:20457750).10 Publications1 Publication

Catalytic activityi

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

Cofactori

Mg2+Note: Binds 1 Mg2+ ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi75 – 751Zinc 1
Metal bindingi75 – 751Zinc 2
Metal bindingi77 – 771Zinc 1
Metal bindingi82 – 821Zinc 1
Metal bindingi82 – 821Zinc 3
Metal bindingi87 – 871Zinc 1
Metal bindingi89 – 891Zinc 2
Metal bindingi118 – 1181Zinc 2
Metal bindingi118 – 1181Zinc 3
Metal bindingi122 – 1221Zinc 2
Metal bindingi124 – 1241Zinc 3
Metal bindingi128 – 1281Zinc 3
Binding sitei192 – 1921S-adenosyl-L-methionine
Binding sitei220 – 2201S-adenosyl-L-methioninePROSITE-ProRule annotation
Metal bindingi226 – 2261Zinc 4
Metal bindingi287 – 2871Zinc 4
Metal bindingi289 – 2891Zinc 4
Metal bindingi294 – 2941Zinc 4
Metal bindingi496 – 4961Magnesium
Metal bindingi588 – 5881Magnesium

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi364 – 39532H-T-H motifBy similarityAdd
BLAST
DNA bindingi428 – 44821H-T-H motifAdd
BLAST

GO - Molecular functioni

  1. DNA topoisomerase binding Source: UniProtKB
  2. double-stranded DNA binding Source: UniProtKB
  3. endonuclease activity Source: UniProtKB
  4. histone methyltransferase activity (H3-K36 specific) Source: UniProtKB
  5. histone methyltransferase activity (H3-K4 specific) Source: UniProtKB
  6. protein homodimerization activity Source: UniProtKB
  7. single-stranded DNA binding Source: UniProtKB
  8. single-stranded DNA endodeoxyribonuclease activity Source: UniProtKB
  9. structure-specific DNA binding Source: UniProtKB
  10. transposase activity Source: InterPro
  11. zinc ion binding Source: InterPro

GO - Biological processi

  1. cell proliferation Source: UniProtKB
  2. DNA catabolic process, endonucleolytic Source: UniProtKB
  3. DNA double-strand break processing Source: UniProtKB
  4. DNA integration Source: UniProtKB
  5. double-strand break repair via nonhomologous end joining Source: UniProtKB
  6. histone H3-K36 dimethylation Source: UniProtKB
  7. histone H3-K36 methylation Source: UniProtKB
  8. histone H3-K4 methylation Source: UniProtKB
  9. mitotic DNA integrity checkpoint Source: UniProtKB
  10. negative regulation of cell cycle arrest Source: UniProtKB
  11. negative regulation of chromosome organization Source: UniProtKB
  12. nucleic acid phosphodiester bond hydrolysis Source: UniProtKB
  13. positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity Source: UniProtKB
  14. positive regulation of double-strand break repair via nonhomologous end joining Source: UniProtKB
  15. replication fork processing Source: UniProtKB
  16. transposition, DNA-mediated Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Endonuclease, Hydrolase, Methyltransferase, Nuclease, Transferase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding, Magnesium, Metal-binding, S-adenosyl-L-methionine, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase SETMARCurated
Alternative name(s):
SET domain and mariner transposase fusion proteinCurated
Short name:
Metnase1 Publication
Including the following 2 domains:
Histone-lysine N-methyltransferaseCurated (EC:2.1.1.431 Publication)
Transposon Hsmar1 transposase1 Publication (EC:3.1.-.-1 Publication)
Gene namesi
Name:SETMARImported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:10762. SETMAR.

Subcellular locationi

Nucleus 1 Publication. Chromosome 2 Publications
Note: Recruited on damaged DNA at sites of double-strand break.1 Publication

GO - Cellular componenti

  1. nucleus Source: UniProtKB
  2. site of double-strand break Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi223 – 2231N → S: Reduces activity in double-strand break repair. 1 Publication
Mutagenesisi261 – 2611D → S: Reduces activity in double-strand break repair. 1 Publication
Mutagenesisi445 – 4451R → A: Abolishes TIR-specific DNA-binding. 1 Publication
Mutagenesisi473 – 4731F → K: Abolishes homodimerization and DNA-binding and reduces cleavage of single-stranded DNA. 1 Publication
Mutagenesisi496 – 4961D → A: Abolishes DNA cleavage. 1 Publication
Mutagenesisi503 – 5031D → S: Reduces activity in double-strand break repair. 1 Publication
Mutagenesisi508 – 5081S → A: Prevents phosphorylation. Impairs recruitment to damaged DNA and double-strand break repair. Impairs interaction with histone H3 and its methylation. Allows replication fork restart. 1 Publication
Mutagenesisi623 – 6231N → D or E: Loss of function in DNA repair. Altered DNA-binding properties. 1 Publication

Organism-specific databases

PharmGKBiPA35680.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 684684Histone-lysine N-methyltransferase SETMARPRO_0000259526Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei498 – 4981N6-methyllysine1 Publication
Modified residuei508 – 5081Phosphoserine; by CHEK14 Publications

Post-translational modificationi

Methylated. Methylation regulates activity in DNA decatenation.1 Publication
Phosphorylated at Ser-508 by CHEK1 and dephosphorylated by protein phosphatase 2A/PP2A. Phosphorylation at Ser-508 is enhanced by DNA damage and promotes recruitment to damaged DNA. It stimulates DNA repair and impairs replication fork restart.1 Publication

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

MaxQBiQ53H47.
PaxDbiQ53H47.
PRIDEiQ53H47.

PTM databases

PhosphoSiteiQ53H47.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ53H47.
CleanExiHS_SETMAR.
ExpressionAtlasiQ53H47. baseline and differential.
GenevestigatoriQ53H47.

Interactioni

Subunit structurei

Homodimer (PubMed:20521842). Interacts with PRPF19; required for SETMAR recruitment to damaged DNA sites (PubMed:18263876). Interacts with PCNA (PubMed:20457750). Interacts with TOP2A; stimulates TOP2A topoisomerase activity (PubMed:18790802, PubMed:20457750). May interact with RAD9A and/or RAD9B (PubMed:20457750).4 Publications

Protein-protein interaction databases

BioGridi112317. 11 interactions.
IntActiQ53H47. 1 interaction.
MINTiMINT-4826518.
STRINGi9606.ENSP00000373354.

Structurei

Secondary structure

1
684
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni30 – 334Combined sources
Beta strandi35 – 373Combined sources
Beta strandi40 – 434Combined sources
Turni84 – 863Combined sources
Helixi88 – 903Combined sources
Helixi133 – 1353Combined sources
Beta strandi141 – 1455Combined sources
Beta strandi147 – 15711Combined sources
Beta strandi164 – 1674Combined sources
Beta strandi170 – 1734Combined sources
Helixi175 – 1828Combined sources
Beta strandi194 – 1985Combined sources
Beta strandi206 – 21611Combined sources
Helixi218 – 2214Combined sources
Beta strandi229 – 24113Combined sources
Beta strandi243 – 2508Combined sources
Beta strandi257 – 2604Combined sources
Beta strandi270 – 27910Combined sources
Helixi466 – 48520Combined sources
Helixi489 – 4913Combined sources
Beta strandi492 – 50312Combined sources
Beta strandi530 – 5389Combined sources
Beta strandi541 – 5477Combined sources
Helixi556 – 57318Combined sources
Helixi574 – 5763Combined sources
Beta strandi584 – 5863Combined sources
Helixi591 – 5944Combined sources
Helixi598 – 6058Combined sources
Helixi617 – 6193Combined sources
Helixi621 – 6244Combined sources
Helixi626 – 6349Combined sources
Helixi642 – 65413Combined sources
Helixi660 – 6667Combined sources
Helixi668 – 67710Combined sources
Turni678 – 6803Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BO5X-ray1.59A15-303[»]
3F2KX-ray1.85A/B459-684[»]
3K9JX-ray1.90A/B446-684[»]
3K9KX-ray2.55A/B446-684[»]
ProteinModelPortaliQ53H47.
SMRiQ53H47. Positions 25-303, 347-684.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ53H47.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini73 – 13664Pre-SETPROSITE-ProRule annotationAdd
BLAST
Domaini139 – 263125SETPROSITE-ProRule annotationAdd
BLAST
Domaini283 – 29917Post-SETPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 345345Histone-lysine N-methyltransferaseAdd
BLAST
Regioni149 – 1513S-adenosyl-L-methionine binding
Regioni223 – 2242S-adenosyl-L-methionine binding
Regioni346 – 684339Mariner transposase Hsmar1Add
BLAST

Domaini

The mariner transposase Hsmar1 region mediates DNA-binding. It has retained some of the nucleases activity but has lost its transposase activity because the active site contains an Asn in position 610 instead of an Asp residue.1 Publication
In the pre-SET domain, Cys residues bind 3 zinc ions that are arranged in a triangular cluster; some of these Cys residues contribute to the binding of two zinc ions within the cluster.

Sequence similaritiesi

In the N-terminal section; belongs to the class V-like SAM-binding methyltransferase superfamily.Curated
In the C-terminal section; belongs to the mariner transposase family.Curated
Contains 1 post-SET domain.PROSITE-ProRule annotation
Contains 1 pre-SET domain.PROSITE-ProRule annotation
Contains 1 SET domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG2940.
GeneTreeiENSGT00780000121845.
HOGENOMiHOG000154295.
HOVERGENiHBG093941.
InParanoidiQ53H47.
KOiK11433.
OMAiRRRSAQW.
OrthoDBiEOG744T8D.
PhylomeDBiQ53H47.
TreeFamiTF352220.

Family and domain databases

InterProiIPR003616. Post-SET_dom.
IPR007728. Pre-SET_dom.
IPR003606. Pre-SET_Zn-bd_sub.
IPR001214. SET_dom.
IPR001888. Transposase_1.
IPR002492. Transposase_Tc1-like.
[Graphical view]
PfamiPF01498. HTH_Tnp_Tc3_2. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
PF01359. Transposase_1. 1 hit.
[Graphical view]
SMARTiSM00508. PostSET. 1 hit.
SM00468. PreSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
PROSITEiPS50868. POST_SET. 1 hit.
PS50867. PRE_SET. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q53H47-1) [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

        10         20         30         40         50
MFAEAAKTTR PCGMAEFKEK PEAPTEQLDV ACGQENLPVG AWPPGAAPAP
60 70 80 90 100
FQYTPDHVVG PGADIDPTQI TFPGCICVKT PCLPGTCSCL RHGENYDDNS
110 120 130 140 150
CLRDIGSGGK YAEPVFECNV LCRCSDHCRN RVVQKGLQFH FQVFKTHKKG
160 170 180 190 200
WGLRTLEFIP KGRFVCEYAG EVLGFSEVQR RIHLQTKSDS NYIIAIREHV
210 220 230 240 250
YNGQVMETFV DPTYIGNIGR FLNHSCEPNL LMIPVRIDSM VPKLALFAAK
260 270 280 290 300
DIVPEEELSY DYSGRYLNLT VSEDKERLDH GKLRKPCYCG AKSCTAFLPF
310 320 330 340 350
DSSLYCPVEK SNISCGNEKE PSMCGSAPSV FPSCKRLTLE TMKMMLDKKQ
360 370 380 390 400
IRAIFLFEFK MGRKAAETTR NINNAFGPGT ANERTVQWWF KKFCKGDESL
410 420 430 440 450
EDEERSGRPS EVDNDQLRAI IEADPLTTTR EVAEELNVNH STVVRHLKQI
460 470 480 490 500
GKVKKLDKWV PHELTENQKN RRFEVSSSLI LRNHNEPFLD RIVTCDEKWI
510 520 530 540 550
LYDNRRRSAQ WLDQEEAPKH FPKPILHPKK VMVTIWWSAA GLIHYSFLNP
560 570 580 590 600
GETITSEKYA QEIDEMNQKL QRLQLALVNR KGPILLHDNA RPHVAQPTLQ
610 620 630 640 650
KLNELGYEVL PHPPYSPDLL PTNYHVFKHL NNFLQGKRFH NQQDAENAFQ
660 670 680
EFVESQSTDF YATGINQLIS RWQKCVDCNG SYFD
Length:684
Mass (Da):78,034
Last modified:April 16, 2014 - v2
Checksum:iBB9460455C0BDBFA
GO
Isoform 2 (identifier: Q53H47-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     341-365: TMKMMLDKKQIRAIFLFEFKMGRKA → VSLFSDKQLAPPYSGRQWLASFTSA
     366-684: Missing.

Note: No experimental confirmation available.

Show »
Length:365
Mass (Da):40,510
Checksum:iE1FFA86B6E63F8E4
GO
Isoform 3 (identifier: Q53H47-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     163-301: Missing.

Show »
Length:545
Mass (Da):62,124
Checksum:i8F570F8A67A495C7
GO

Sequence cautioni

The sequence AAH11635.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAY29570.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAD96454.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911R → H in BAG63636 (PubMed:14702039).Curated
Sequence conflicti343 – 3431K → E in AAC52010 (PubMed:9461395).Curated
Sequence conflicti439 – 4391N → D in AAC52010 (PubMed:9461395).Curated
Sequence conflicti465 – 4651T → S in AAC52010 (PubMed:9461395).Curated
Sequence conflicti484 – 4841H → N in AAC52010 (PubMed:9461395).Curated
Sequence conflicti508 – 5081S → P in AAC52010 (PubMed:9461395).Curated
Sequence conflicti514 – 5141Q → R in AAC52010 (PubMed:9461395).Curated
Sequence conflicti525 – 5251I → N in AAC52010 (PubMed:9461395).Curated
Sequence conflicti528 – 5281P → Q in AAC52010 (PubMed:9461395).Curated
Sequence conflicti535 – 5351I → V in AAC52010 (PubMed:9461395).Curated
Sequence conflicti562 – 5621E → Q in AAC52010 (PubMed:9461395).Curated
Sequence conflicti567 – 5682NQ → HR in AAC52010 (PubMed:9461395).Curated
Sequence conflicti575 – 5751L → P in AAC52010 (PubMed:9461395).Curated
Sequence conflicti620 – 6201L → S in AAC52010 (PubMed:9461395).Curated
Sequence conflicti623 – 6231N → D in AAC52010 (PubMed:9461395).Curated
Sequence conflicti626 – 6261V → F in AAC52010 (PubMed:9461395).Curated
Sequence conflicti631 – 6311N → D in AAC52010 (PubMed:9461395).Curated
Sequence conflicti656 – 6561Q → R in AAC52010 (PubMed:9461395).Curated
Sequence conflicti667 – 6671Q → K in AAC52010 (PubMed:9461395).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei163 – 301139Missing in isoform 3. CuratedVSP_054089Add
BLAST
Alternative sequencei341 – 36525TMKMM…MGRKA → VSLFSDKQLAPPYSGRQWLA SFTSA in isoform 2. 2 PublicationsVSP_021440Add
BLAST
Alternative sequencei366 – 684319Missing in isoform 2. 2 PublicationsVSP_021441Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK222734 mRNA. Translation: BAD96454.1. Different initiation.
AK302296 mRNA. Translation: BAG63636.1.
AC023483 Genomic DNA. No translation available.
AC034191 Genomic DNA. No translation available.
BC011635 mRNA. Translation: AAH11635.1. Different initiation.
AY952295 mRNA. Translation: AAY29570.1. Different initiation.
DQ341316 Genomic DNA. Translation: ABC72087.1.
U52077 Genomic DNA. Translation: AAC52010.1.
CCDSiCCDS2563.2. [Q53H47-1]
CCDS58814.1. [Q53H47-3]
CCDS63528.1. [Q53H47-2]
RefSeqiNP_001230652.1. NM_001243723.1. [Q53H47-3]
NP_001263254.1. NM_001276325.1. [Q53H47-2]
NP_006506.3. NM_006515.3. [Q53H47-1]
UniGeneiHs.475300.

Genome annotation databases

EnsembliENST00000358065; ENSP00000373354; ENSG00000170364. [Q53H47-1]
ENST00000425863; ENSP00000403145; ENSG00000170364. [Q53H47-3]
ENST00000430981; ENSP00000403000; ENSG00000170364. [Q53H47-2]
GeneIDi6419.
KEGGihsa:6419.
UCSCiuc010hbx.3. human. [Q53H47-1]

Polymorphism databases

DMDMi74740552.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK222734 mRNA. Translation: BAD96454.1. Different initiation.
AK302296 mRNA. Translation: BAG63636.1.
AC023483 Genomic DNA. No translation available.
AC034191 Genomic DNA. No translation available.
BC011635 mRNA. Translation: AAH11635.1. Different initiation.
AY952295 mRNA. Translation: AAY29570.1. Different initiation.
DQ341316 Genomic DNA. Translation: ABC72087.1.
U52077 Genomic DNA. Translation: AAC52010.1.
CCDSiCCDS2563.2. [Q53H47-1]
CCDS58814.1. [Q53H47-3]
CCDS63528.1. [Q53H47-2]
RefSeqiNP_001230652.1. NM_001243723.1. [Q53H47-3]
NP_001263254.1. NM_001276325.1. [Q53H47-2]
NP_006506.3. NM_006515.3. [Q53H47-1]
UniGeneiHs.475300.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BO5X-ray1.59A15-303[»]
3F2KX-ray1.85A/B459-684[»]
3K9JX-ray1.90A/B446-684[»]
3K9KX-ray2.55A/B446-684[»]
ProteinModelPortaliQ53H47.
SMRiQ53H47. Positions 25-303, 347-684.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112317. 11 interactions.
IntActiQ53H47. 1 interaction.
MINTiMINT-4826518.
STRINGi9606.ENSP00000373354.

Chemistry

BindingDBiQ53H47.
ChEMBLiCHEMBL2189111.

PTM databases

PhosphoSiteiQ53H47.

Polymorphism databases

DMDMi74740552.

Proteomic databases

MaxQBiQ53H47.
PaxDbiQ53H47.
PRIDEiQ53H47.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000358065; ENSP00000373354; ENSG00000170364. [Q53H47-1]
ENST00000425863; ENSP00000403145; ENSG00000170364. [Q53H47-3]
ENST00000430981; ENSP00000403000; ENSG00000170364. [Q53H47-2]
GeneIDi6419.
KEGGihsa:6419.
UCSCiuc010hbx.3. human. [Q53H47-1]

Organism-specific databases

CTDi6419.
GeneCardsiGC03P004344.
HGNCiHGNC:10762. SETMAR.
MIMi609834. gene.
neXtProtiNX_Q53H47.
PharmGKBiPA35680.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2940.
GeneTreeiENSGT00780000121845.
HOGENOMiHOG000154295.
HOVERGENiHBG093941.
InParanoidiQ53H47.
KOiK11433.
OMAiRRRSAQW.
OrthoDBiEOG744T8D.
PhylomeDBiQ53H47.
TreeFamiTF352220.

Miscellaneous databases

EvolutionaryTraceiQ53H47.
GeneWikiiSETMAR.
GenomeRNAii6419.
NextBioi24930.
PROiQ53H47.
SOURCEiSearch...

Gene expression databases

BgeeiQ53H47.
CleanExiHS_SETMAR.
ExpressionAtlasiQ53H47. baseline and differential.
GenevestigatoriQ53H47.

Family and domain databases

InterProiIPR003616. Post-SET_dom.
IPR007728. Pre-SET_dom.
IPR003606. Pre-SET_Zn-bd_sub.
IPR001214. SET_dom.
IPR001888. Transposase_1.
IPR002492. Transposase_Tc1-like.
[Graphical view]
PfamiPF01498. HTH_Tnp_Tc3_2. 1 hit.
PF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
PF01359. Transposase_1. 1 hit.
[Graphical view]
SMARTiSM00508. PostSET. 1 hit.
SM00468. PreSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
PROSITEiPS50868. POST_SET. 1 hit.
PS50867. PRE_SET. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORMS 1 AND 2).
  2. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-684 (ISOFORM 2).
    Tissue: Uterus.
  4. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-684 (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, MUTAGENESIS OF ASN-223; ASP-261 AND ASP-503.
  5. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 341-684, FUNCTION, DNA-BINDING.
  6. "Molecular evolution of an ancient mariner transposon, Hsmar1, in the human genome."
    Robertson H.M., Zumpano K.L.
    Gene 205:203-217(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 342-684.
  7. "Biochemical characterization of a SET and transposase fusion protein, Metnase: its DNA binding and DNA cleavage activity."
    Roman Y., Oshige M., Lee Y.J., Goodwin K., Georgiadis M.M., Hromas R.A., Lee S.H.
    Biochemistry 46:11369-11376(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA CLEAVAGE ACTIVITY, MUTAGENESIS OF ARG-445 AND ASP-496.
  8. "The ancient mariner sails again: transposition of the human Hsmar1 element by a reconstructed transposase and activities of the SETMAR protein on transposon ends."
    Miskey C., Papp B., Mates L., Sinzelle L., Keller H., Izsvak Z., Ivics Z.
    Mol. Cell. Biol. 27:4589-4600(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, LACK OF TRANSPOSASE ACTIVITY, DOMAIN.
  9. "Human Pso4 is a metnase (SETMAR)-binding partner that regulates metnase function in DNA repair."
    Beck B.D., Park S.J., Lee Y.J., Roman Y., Hromas R.A., Lee S.H.
    J. Biol. Chem. 283:9023-9030(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PRPF19, SUBCELLULAR LOCATION.
  10. "The SET and transposase domain protein Metnase enhances chromosome decatenation: regulation by automethylation."
    Williamson E.A., Rasila K.K., Corwin L.K., Wray J., Beck B.D., Severns V., Mobarak C., Lee S.H., Nickoloff J.A., Hromas R.
    Nucleic Acids Res. 36:5822-5831(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TOP2A, METHYLATION AT LYS-498, SUBCELLULAR LOCATION.
  11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: FUNCTION, INTERACTION WITH PCNA; RAD9A; RAD9B AND TOP2A.
  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-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: FUNCTION.
  16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Chk1 phosphorylation of Metnase enhances DNA repair but inhibits replication fork restart."
    Hromas R., Williamson E.A., Fnu S., Lee Y.J., Park S.J., Beck B.D., You J.S., Leitao A., Laitao A., Nickoloff J.A., Lee S.H.
    Oncogene 31:4245-4254(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-508 BY CHEK1, DEPHOSPHORYLATION BY PP2A, MUTAGENESIS OF SER-508, SUBCELLULAR LOCATION.
  18. "The DDN catalytic motif is required for Metnase functions in non-homologous end joining (NHEJ) repair and replication restart."
    Kim H.S., Chen Q., Kim S.K., Nickoloff J.A., Hromas R., Georgiadis M.M., Lee S.H.
    J. Biol. Chem. 289:10930-10938(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASN-623.
  19. "The crystal structure of transposase domain of human histone-lysine N-methyltransferase SETMAR."
    Structural genomics consortium (SGC)
    Submitted (AUG-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 15-303, X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 459-684 IN COMPLEXES WITH S-ADENOSYL-L-HOMOCYSTEINE; ZINC AND MAGNESIUM IONS.
  20. "Crystal structure of the human Hsmar1-derived transposase domain in the DNA repair enzyme Metnase."
    Goodwin K.D., He H., Imasaki T., Lee S.H., Georgiadis M.M.
    Biochemistry 49:5705-5713(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 446-684, FUNCTION, SUBUNIT, MUTAGENESIS OF PHE-473.

Entry informationi

Entry nameiSETMR_HUMAN
AccessioniPrimary (citable) accession number: Q53H47
Secondary accession number(s): B4DY74
, E7EN68, Q13579, Q1G668, Q96F41
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: April 16, 2014
Last modified: February 4, 2015
This is version 94 of the entry and version 2 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

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.

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.