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Q53H47 (SETMR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone-lysine N-methyltransferase SETMAR
Alternative name(s):
SET domain and mariner transposase fusion gene-containing protein
Short name=HsMar1
Short name=Metnase

Including the following 2 domains:

  1. Histone-lysine N-methyltransferase
    EC=2.1.1.43
  2. Mariner transposase Hsmar1
    EC=3.1.-.-
Gene names
Name:SETMAR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length684 AA.
Sequence statusComplete.
Protein existenceEvidence 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'. Has sequence-specific DNA-binding activity and recognizes the 19-mer core of the 5'-terminal inverted repeats (TIRs) of the Hsmar1 element. Has DNA nicking activity. Has in vivo end joining activity and may mediate genomic integration of foreign DNA. Ref.4 Ref.5 Ref.7 Ref.8

Catalytic activity

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

Cofactor

Binds 1 magnesium ion per subunit.

Subcellular location

Nucleus Probable. Chromosome Probable.

Tissue specificity

Widely expressed, with highest expression in placenta and ovary and lowest expression in skeletal muscle. Ref.4

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 class V-like SAM-binding methyltransferase superfamily.

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.

Sequence caution

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

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

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

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentChromosome
Nucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   LigandDNA-binding
Magnesium
Metal-binding
S-adenosyl-L-methionine
   Molecular functionChromatin regulator
Endonuclease
Hydrolase
Methyltransferase
Nuclease
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processDNA catabolic process, endonucleolytic

Inferred from direct assay PubMed 20521842PubMed 21491884. Source: UniProtKB

DNA double-strand break processing

Inferred from direct assay PubMed 21491884. Source: UniProtKB

DNA integration

Inferred from electronic annotation. Source: InterPro

negative regulation of cell cycle arrest

Inferred from mutant phenotype PubMed 19390626. Source: UniProtKB

negative regulation of chromosome organization

Inferred from direct assay PubMed 20620605. Source: UniProtKB

positive regulation of double-strand break repair via nonhomologous end joining

Inferred from direct assay PubMed 20620605PubMed 21491884. Source: UniProtKB

transposition, DNA-mediated

Traceable author statement Ref.6. Source: UniProtKB

   Cellular_componentchromosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred by curator PubMed 21491884. Source: UniProtKB

   Molecular_functionendonuclease activity

Inferred from direct assay PubMed 20620605PubMed 21491884. Source: UniProtKB

histone-lysine N-methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein homodimerization activity

Inferred from physical interaction PubMed 20521842. Source: UniProtKB

structure-specific DNA binding

Inferred from direct assay PubMed 20521842. Source: UniProtKB

transposase activity

Traceable author statement PubMed 21491884Ref.6. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 3 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:
     341-365: TMKMMLDKKQIRAIFLFEFKMGRKA → VSLFSDKQLAPPYSGRQWLASFTSA
     366-684: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q53H47-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 684684Histone-lysine N-methyltransferase SETMAR
PRO_0000259526

Regions

Domain73 – 13664Pre-SET
Domain139 – 263125SET
Domain283 – 29917Post-SET
DNA binding364 – 39532H-T-H motif By similarity
DNA binding428 – 44821H-T-H motif Ref.5
Region1 – 345345Histone-lysine N-methyltransferase
Region346 – 684339Mariner transposase Hsmar1
Coiled coil552 – 58231 Potential

Sites

Metal binding4961Magnesium
Metal binding5881Magnesium

Amino acid modifications

Modified residue5081Phosphoserine Ref.9 Ref.11 Ref.12

Natural variations

Alternative sequence163 – 301139Missing in isoform 3.
VSP_054089
Alternative sequence341 – 36525TMKMM…MGRKA → VSLFSDKQLAPPYSGRQWLA SFTSA in isoform 2.
VSP_021440
Alternative sequence366 – 684319Missing in isoform 2.
VSP_021441

Experimental info

Mutagenesis2231N → S: Reduces activity in double strand break repair. Ref.4
Mutagenesis2611D → S: Reduces activity in double strand break repair. Ref.4
Mutagenesis4451R → A: Abolishes TIR-specific DNA-binding. Ref.7
Mutagenesis4961D → A: Abolishes DNA cleavage. Ref.7
Mutagenesis5031D → S: Reduces activity in double strand break repair. Ref.4
Sequence conflict911R → H in BAG63636. Ref.1
Sequence conflict3431K → E in AAC52010. Ref.6
Sequence conflict4391N → D in AAC52010. Ref.6
Sequence conflict4651T → S in AAC52010. Ref.6
Sequence conflict4841H → N in AAC52010. Ref.6
Sequence conflict5081S → P in AAC52010. Ref.6
Sequence conflict5141Q → R in AAC52010. Ref.6
Sequence conflict5251I → N in AAC52010. Ref.6
Sequence conflict5281P → Q in AAC52010. Ref.6
Sequence conflict5351I → V in AAC52010. Ref.6
Sequence conflict5621E → Q in AAC52010. Ref.6
Sequence conflict567 – 5682NQ → HR in AAC52010. Ref.6
Sequence conflict5751L → P in AAC52010. Ref.6
Sequence conflict6201L → S in AAC52010. Ref.6
Sequence conflict6231N → D in AAC52010. Ref.6
Sequence conflict6261V → F in AAC52010. Ref.6
Sequence conflict6311N → D in AAC52010. Ref.6
Sequence conflict6561Q → R in AAC52010. Ref.6
Sequence conflict6671Q → K in AAC52010. Ref.6

Secondary structure

.................................................................... 684
Helix Strand Turn

Details...

Sequences

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

Last modified April 16, 2014. Version 2.
Checksum: BB9460455C0BDBFA

FASTA68478,034
        10         20         30         40         50         60 
MFAEAAKTTR PCGMAEFKEK PEAPTEQLDV ACGQENLPVG AWPPGAAPAP FQYTPDHVVG 

        70         80         90        100        110        120 
PGADIDPTQI TFPGCICVKT PCLPGTCSCL RHGENYDDNS CLRDIGSGGK YAEPVFECNV 

       130        140        150        160        170        180 
LCRCSDHCRN RVVQKGLQFH FQVFKTHKKG WGLRTLEFIP KGRFVCEYAG EVLGFSEVQR 

       190        200        210        220        230        240 
RIHLQTKSDS NYIIAIREHV YNGQVMETFV DPTYIGNIGR FLNHSCEPNL LMIPVRIDSM 

       250        260        270        280        290        300 
VPKLALFAAK DIVPEEELSY DYSGRYLNLT VSEDKERLDH GKLRKPCYCG AKSCTAFLPF 

       310        320        330        340        350        360 
DSSLYCPVEK SNISCGNEKE PSMCGSAPSV FPSCKRLTLE TMKMMLDKKQ IRAIFLFEFK 

       370        380        390        400        410        420 
MGRKAAETTR NINNAFGPGT ANERTVQWWF KKFCKGDESL EDEERSGRPS EVDNDQLRAI 

       430        440        450        460        470        480 
IEADPLTTTR EVAEELNVNH STVVRHLKQI GKVKKLDKWV PHELTENQKN RRFEVSSSLI 

       490        500        510        520        530        540 
LRNHNEPFLD RIVTCDEKWI LYDNRRRSAQ WLDQEEAPKH FPKPILHPKK VMVTIWWSAA 

       550        560        570        580        590        600 
GLIHYSFLNP GETITSEKYA QEIDEMNQKL QRLQLALVNR KGPILLHDNA RPHVAQPTLQ 

       610        620        630        640        650        660 
KLNELGYEVL PHPPYSPDLL PTNYHVFKHL NNFLQGKRFH NQQDAENAFQ EFVESQSTDF 

       670        680 
YATGINQLIS RWQKCVDCNG SYFD 

« Hide

Isoform 2 [UniParc].

Checksum: E1FFA86B6E63F8E4
Show »

FASTA36540,510
Isoform 3 [UniParc].

Checksum: 8F570F8A67A495C7
Show »

FASTA54562,124

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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, 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.
[9]"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.
[10]"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].
[11]"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.
[12]"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].
[13]"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 (1.85 ANGSTROMS) OF 459-684 IN COMPLEX WITH MAGNESIUM IONS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001230652.1. NM_001243723.1.
NP_001263254.1. NM_001276325.1.
NP_006506.3. NM_006515.3.
UniGeneHs.475300.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BO5X-ray1.59A15-303[»]
3F2KX-ray1.85A/B459-684[»]
3K9JX-ray1.90A/B446-684[»]
3K9KX-ray2.55A/B446-684[»]
ProteinModelPortalQ53H47.
SMRQ53H47. Positions 12-290, 334-671.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112317. 8 interactions.
IntActQ53H47. 1 interaction.
MINTMINT-4826518.
STRING9606.ENSP00000373354.

Chemistry

ChEMBLCHEMBL2189111.

PTM databases

PhosphoSiteQ53H47.

Polymorphism databases

DMDM74740552.

Proteomic databases

PaxDbQ53H47.
PRIDEQ53H47.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000358065; ENSP00000373354; ENSG00000170364.
ENST00000425863; ENSP00000403145; ENSG00000170364.
GeneID6419.
KEGGhsa:6419.
UCSCuc010hbx.3. human. [Q53H47-1]

Organism-specific databases

CTD6419.
GeneCardsGC03P004344.
HGNCHGNC:10762. SETMAR.
MIM609834. gene.
neXtProtNX_Q53H47.
PharmGKBPA35680.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2940.
HOGENOMHOG000154295.
HOVERGENHBG093941.
InParanoidQ53H47.
KOK11433.
OrthoDBEOG744T8D.
PhylomeDBQ53H47.
TreeFamTF352220.

Gene expression databases

ArrayExpressQ53H47.
BgeeQ53H47.
CleanExHS_SETMAR.
GenevestigatorQ53H47.

Family and domain databases

InterProIPR003616. 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]
PfamPF01498. HTH_Tnp_Tc3_2. 1 hit.
PF05033. 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

EvolutionaryTraceQ53H47.
GeneWikiSETMAR.
GenomeRNAi6419.
NextBio24930.
PROQ53H47.
SOURCESearch...

Entry information

Entry nameSETMR_HUMAN
AccessionPrimary (citable) accession number: Q53H47
Secondary accession number(s): B4DY74 expand/collapse secondary AC list , E7EN68, Q13579, Q1G668, Q96F41
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: April 16, 2014
Last modified: April 16, 2014
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 3

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