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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).1 Publication10 Publications

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)DescriptionActionsGraphical viewLength
Metal bindingi75Zinc 11
Metal bindingi75Zinc 21
Metal bindingi77Zinc 11
Metal bindingi82Zinc 11
Metal bindingi82Zinc 31
Metal bindingi87Zinc 11
Metal bindingi89Zinc 21
Metal bindingi118Zinc 21
Metal bindingi118Zinc 31
Metal bindingi122Zinc 21
Metal bindingi124Zinc 31
Metal bindingi128Zinc 31
Binding sitei192S-adenosyl-L-methionine1
Binding sitei220S-adenosyl-L-methioninePROSITE-ProRule annotation1
Metal bindingi226Zinc 41
Metal bindingi287Zinc 41
Metal bindingi289Zinc 41
Metal bindingi294Zinc 41
Metal bindingi496Magnesium1
Metal bindingi588Magnesium1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi364 – 395H-T-H motifBy similarityAdd BLAST32
DNA bindingi428 – 448H-T-H motifAdd BLAST21

GO - Molecular functioni

  • DNA topoisomerase binding Source: UniProtKB
  • double-stranded DNA binding Source: UniProtKB
  • endonuclease activity Source: UniProtKB
  • histone methyltransferase activity (H3-K36 specific) Source: UniProtKB
  • histone methyltransferase activity (H3-K4 specific) Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • single-stranded DNA binding Source: UniProtKB
  • single-stranded DNA endodeoxyribonuclease activity Source: UniProtKB
  • structure-specific DNA binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cell proliferation Source: UniProtKB
  • DNA catabolic process, endonucleolytic Source: UniProtKB
  • DNA double-strand break processing Source: UniProtKB
  • DNA integration Source: UniProtKB
  • double-strand break repair via nonhomologous end joining Source: UniProtKB
  • histone H3-K36 dimethylation Source: UniProtKB
  • histone H3-K36 methylation Source: UniProtKB
  • histone H3-K4 methylation Source: UniProtKB
  • mitotic DNA integrity checkpoint Source: UniProtKB
  • negative regulation of cell cycle arrest Source: UniProtKB
  • negative regulation of chromosome organization Source: UniProtKB
  • nucleic acid phosphodiester bond hydrolysis Source: UniProtKB
  • positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity Source: UniProtKB
  • positive regulation of double-strand break repair via nonhomologous end joining Source: UniProtKB
  • replication fork processing Source: UniProtKB
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

Enzyme and pathway databases

BioCyciZFISH:HS10111-MONOMER.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:10762. SETMAR.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi223N → S: Reduces activity in double-strand break repair. 1 Publication1
Mutagenesisi261D → S: Reduces activity in double-strand break repair. 1 Publication1
Mutagenesisi445R → A: Abolishes TIR-specific DNA-binding. 1 Publication1
Mutagenesisi473F → K: Abolishes homodimerization and DNA-binding and reduces cleavage of single-stranded DNA. 1 Publication1
Mutagenesisi496D → A: Abolishes DNA cleavage. 1 Publication1
Mutagenesisi503D → S: Reduces activity in double-strand break repair. 1 Publication1
Mutagenesisi508S → 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 Publication1
Mutagenesisi623N → D or E: Loss of function in DNA repair. Altered DNA-binding properties. 1 Publication1

Organism-specific databases

DisGeNETi6419.
OpenTargetsiENSG00000170364.
PharmGKBiPA35680.

Chemistry databases

ChEMBLiCHEMBL2189111.

Polymorphism and mutation databases

DMDMi74740552.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002595261 – 684Histone-lysine N-methyltransferase SETMARAdd BLAST684

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei498N6-methyllysine1 Publication1
Modified residuei508Phosphoserine; by CHEK1Combined sources1 Publication1

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

EPDiQ53H47.
MaxQBiQ53H47.
PaxDbiQ53H47.
PeptideAtlasiQ53H47.
PRIDEiQ53H47.

PTM databases

iPTMnetiQ53H47.
PhosphoSitePlusiQ53H47.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000170364.
CleanExiHS_SETMAR.
ExpressionAtlasiQ53H47. baseline and differential.
GenevisibleiQ53H47. HS.

Organism-specific databases

HPAiHPA057999.

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

GO - Molecular functioni

  • DNA topoisomerase binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi112317. 17 interactors.
IntActiQ53H47. 3 interactors.
MINTiMINT-4826518.
STRINGi9606.ENSP00000373354.

Chemistry databases

BindingDBiQ53H47.

Structurei

Secondary structure

1684
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni30 – 33Combined sources4
Beta strandi35 – 37Combined sources3
Beta strandi40 – 43Combined sources4
Turni84 – 86Combined sources3
Helixi88 – 90Combined sources3
Helixi133 – 135Combined sources3
Beta strandi141 – 145Combined sources5
Beta strandi147 – 157Combined sources11
Beta strandi164 – 167Combined sources4
Beta strandi170 – 173Combined sources4
Helixi175 – 182Combined sources8
Beta strandi194 – 198Combined sources5
Beta strandi206 – 216Combined sources11
Helixi218 – 221Combined sources4
Beta strandi229 – 241Combined sources13
Beta strandi243 – 250Combined sources8
Beta strandi257 – 260Combined sources4
Beta strandi270 – 279Combined sources10
Helixi466 – 485Combined sources20
Helixi489 – 491Combined sources3
Beta strandi492 – 503Combined sources12
Beta strandi530 – 538Combined sources9
Beta strandi541 – 547Combined sources7
Helixi556 – 573Combined sources18
Helixi574 – 576Combined sources3
Beta strandi584 – 586Combined sources3
Helixi591 – 594Combined sources4
Helixi598 – 605Combined sources8
Helixi617 – 619Combined sources3
Helixi621 – 624Combined sources4
Helixi626 – 634Combined sources9
Helixi642 – 654Combined sources13
Helixi660 – 666Combined sources7
Helixi668 – 677Combined sources10
Turni678 – 680Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ53H47.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini73 – 136Pre-SETPROSITE-ProRule annotationAdd BLAST64
Domaini139 – 263SETPROSITE-ProRule annotationAdd BLAST125
Domaini283 – 299Post-SETPROSITE-ProRule annotationAdd BLAST17

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 345Histone-lysine N-methyltransferaseAdd BLAST345
Regioni149 – 151S-adenosyl-L-methionine binding3
Regioni223 – 224S-adenosyl-L-methionine binding2
Regioni346 – 684Mariner transposase Hsmar1Add BLAST339

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

eggNOGiKOG1082. Eukaryota.
COG2940. LUCA.
GeneTreeiENSGT00780000121845.
HOGENOMiHOG000154295.
HOVERGENiHBG093941.
InParanoidiQ53H47.
KOiK11433.
OMAiRRRSAQW.
OrthoDBiEOG091G0Y4N.
PhylomeDBiQ53H47.
TreeFamiTF352220.

Family and domain databases

InterProiIPR003616. Post-SET_dom.
IPR007728. Pre-SET_dom.
IPR001214. SET_dom.
IPR001888. Transposase_1.
[Graphical view]
PfamiPF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
PF01359. Transposase_1. 1 hit.
[Graphical view]
SMARTiSM00468. 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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAY29570 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAD96454 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti91R → H in BAG63636 (PubMed:14702039).Curated1
Sequence conflicti343K → E in AAC52010 (PubMed:9461395).Curated1
Sequence conflicti439N → D in AAC52010 (PubMed:9461395).Curated1
Sequence conflicti465T → S in AAC52010 (PubMed:9461395).Curated1
Sequence conflicti484H → N in AAC52010 (PubMed:9461395).Curated1
Sequence conflicti508S → P in AAC52010 (PubMed:9461395).Curated1
Sequence conflicti514Q → R in AAC52010 (PubMed:9461395).Curated1
Sequence conflicti525I → N in AAC52010 (PubMed:9461395).Curated1
Sequence conflicti528P → Q in AAC52010 (PubMed:9461395).Curated1
Sequence conflicti535I → V in AAC52010 (PubMed:9461395).Curated1
Sequence conflicti562E → Q in AAC52010 (PubMed:9461395).Curated1
Sequence conflicti567 – 568NQ → HR in AAC52010 (PubMed:9461395).Curated2
Sequence conflicti575L → P in AAC52010 (PubMed:9461395).Curated1
Sequence conflicti620L → S in AAC52010 (PubMed:9461395).Curated1
Sequence conflicti623N → D in AAC52010 (PubMed:9461395).Curated1
Sequence conflicti626V → F in AAC52010 (PubMed:9461395).Curated1
Sequence conflicti631N → D in AAC52010 (PubMed:9461395).Curated1
Sequence conflicti656Q → R in AAC52010 (PubMed:9461395).Curated1
Sequence conflicti667Q → K in AAC52010 (PubMed:9461395).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_054089163 – 301Missing in isoform 3. CuratedAdd BLAST139
Alternative sequenceiVSP_021440341 – 365TMKMM…MGRKA → VSLFSDKQLAPPYSGRQWLA SFTSA in isoform 2. 2 PublicationsAdd BLAST25
Alternative sequenceiVSP_021441366 – 684Missing in isoform 2. 2 PublicationsAdd BLAST319

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_001307606.1. NM_001320677.1.
NP_001307607.1. NM_001320678.1.
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.
UCSCiuc003bpw.6. human. [Q53H47-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Protein Spotlight

Taming genes - Issue 167 of February 2015

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_001307606.1. NM_001320677.1.
NP_001307607.1. NM_001320678.1.
NP_006506.3. NM_006515.3. [Q53H47-1]
UniGeneiHs.475300.

3D structure databases

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

Protein-protein interaction databases

BioGridi112317. 17 interactors.
IntActiQ53H47. 3 interactors.
MINTiMINT-4826518.
STRINGi9606.ENSP00000373354.

Chemistry databases

BindingDBiQ53H47.
ChEMBLiCHEMBL2189111.

PTM databases

iPTMnetiQ53H47.
PhosphoSitePlusiQ53H47.

Polymorphism and mutation databases

DMDMi74740552.

Proteomic databases

EPDiQ53H47.
MaxQBiQ53H47.
PaxDbiQ53H47.
PeptideAtlasiQ53H47.
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.
UCSCiuc003bpw.6. human. [Q53H47-1]

Organism-specific databases

CTDi6419.
DisGeNETi6419.
GeneCardsiSETMAR.
HGNCiHGNC:10762. SETMAR.
HPAiHPA057999.
MIMi609834. gene.
neXtProtiNX_Q53H47.
OpenTargetsiENSG00000170364.
PharmGKBiPA35680.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1082. Eukaryota.
COG2940. LUCA.
GeneTreeiENSGT00780000121845.
HOGENOMiHOG000154295.
HOVERGENiHBG093941.
InParanoidiQ53H47.
KOiK11433.
OMAiRRRSAQW.
OrthoDBiEOG091G0Y4N.
PhylomeDBiQ53H47.
TreeFamiTF352220.

Enzyme and pathway databases

BioCyciZFISH:HS10111-MONOMER.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000170364.
CleanExiHS_SETMAR.
ExpressionAtlasiQ53H47. baseline and differential.
GenevisibleiQ53H47. HS.

Family and domain databases

InterProiIPR003616. Post-SET_dom.
IPR007728. Pre-SET_dom.
IPR001214. SET_dom.
IPR001888. Transposase_1.
[Graphical view]
PfamiPF05033. Pre-SET. 1 hit.
PF00856. SET. 1 hit.
PF01359. Transposase_1. 1 hit.
[Graphical view]
SMARTiSM00468. 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...

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: November 2, 2016
This is version 111 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. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  5. SIMILARITY comments
    Index of protein domains and families

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 one 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.