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Q53H47

- SETMR_HUMAN

UniProt

Q53H47 - SETMR_HUMAN

Protein

Histone-lysine N-methyltransferase SETMAR

Gene

SETMAR

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 2 (16 Apr 2014)
      Previous versions | rss
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    Functioni

    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.5 Publications

    Catalytic activityi

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

    Cofactori

    Binds 1 magnesium 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. endonuclease activity Source: UniProtKB
    2. histone-lysine N-methyltransferase activity Source: UniProtKB-EC
    3. protein binding Source: UniProtKB
    4. protein homodimerization activity Source: UniProtKB
    5. structure-specific DNA binding Source: UniProtKB
    6. transposase activity Source: UniProtKB
    7. zinc ion binding Source: InterPro

    GO - Biological processi

    1. DNA catabolic process, endonucleolytic Source: UniProtKB
    2. DNA double-strand break processing Source: UniProtKB
    3. DNA integration Source: InterPro
    4. negative regulation of cell cycle arrest Source: UniProtKB
    5. negative regulation of chromosome organization Source: UniProtKB
    6. positive regulation of double-strand break repair via nonhomologous end joining Source: UniProtKB
    7. transposition, DNA-mediated Source: UniProtKB

    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 SETMAR
    Alternative name(s):
    SET domain and mariner transposase fusion gene-containing protein
    Short name:
    HsMar1
    Short name:
    Metnase
    Including the following 2 domains:
    Mariner transposase Hsmar1 (EC:3.1.-.-)
    Gene namesi
    Name:SETMAR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:10762. SETMAR.

    Subcellular locationi

    Nucleus Curated. Chromosome Curated

    GO - Cellular componenti

    1. chromosome Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB

    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

    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 residuei508 – 5081Phosphoserine3 Publications

    Keywords - PTMi

    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

    ArrayExpressiQ53H47.
    BgeeiQ53H47.
    CleanExiHS_SETMAR.
    GenevestigatoriQ53H47.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi112317. 8 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 – 334
    Beta strandi35 – 373
    Beta strandi40 – 434
    Turni84 – 863
    Helixi88 – 903
    Helixi133 – 1353
    Beta strandi141 – 1455
    Beta strandi147 – 15711
    Beta strandi164 – 1674
    Beta strandi170 – 1734
    Helixi175 – 1828
    Beta strandi194 – 1985
    Beta strandi206 – 21611
    Helixi218 – 2214
    Beta strandi229 – 24113
    Beta strandi243 – 2508
    Beta strandi257 – 2604
    Beta strandi270 – 27910
    Helixi466 – 48520
    Helixi489 – 4913
    Beta strandi492 – 50312
    Beta strandi530 – 5389
    Beta strandi541 – 5477
    Helixi556 – 57318
    Helixi574 – 5763
    Beta strandi584 – 5863
    Helixi591 – 5944
    Helixi598 – 6058
    Helixi617 – 6193
    Helixi621 – 6244
    Helixi626 – 6349
    Helixi642 – 65413
    Helixi660 – 6667
    Helixi668 – 67710
    Turni678 – 6803

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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 no transposase activity because the active site contains an Asn in position 610 instead of a Asp residue.
    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.
    HOGENOMiHOG000154295.
    HOVERGENiHBG093941.
    InParanoidiQ53H47.
    KOiK11433.
    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. Align

    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

    MFAEAAKTTR PCGMAEFKEK PEAPTEQLDV ACGQENLPVG AWPPGAAPAP    50
    FQYTPDHVVG PGADIDPTQI TFPGCICVKT PCLPGTCSCL RHGENYDDNS 100
    CLRDIGSGGK YAEPVFECNV LCRCSDHCRN RVVQKGLQFH FQVFKTHKKG 150
    WGLRTLEFIP KGRFVCEYAG EVLGFSEVQR RIHLQTKSDS NYIIAIREHV 200
    YNGQVMETFV DPTYIGNIGR FLNHSCEPNL LMIPVRIDSM VPKLALFAAK 250
    DIVPEEELSY DYSGRYLNLT VSEDKERLDH GKLRKPCYCG AKSCTAFLPF 300
    DSSLYCPVEK SNISCGNEKE PSMCGSAPSV FPSCKRLTLE TMKMMLDKKQ 350
    IRAIFLFEFK MGRKAAETTR NINNAFGPGT ANERTVQWWF KKFCKGDESL 400
    EDEERSGRPS EVDNDQLRAI IEADPLTTTR EVAEELNVNH STVVRHLKQI 450
    GKVKKLDKWV PHELTENQKN RRFEVSSSLI LRNHNEPFLD RIVTCDEKWI 500
    LYDNRRRSAQ WLDQEEAPKH FPKPILHPKK VMVTIWWSAA GLIHYSFLNP 550
    GETITSEKYA QEIDEMNQKL QRLQLALVNR KGPILLHDNA RPHVAQPTLQ 600
    KLNELGYEVL PHPPYSPDLL PTNYHVFKHL NNFLQGKRFH NQQDAENAFQ 650
    EFVESQSTDF YATGINQLIS RWQKCVDCNG SYFD 684
    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.
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS2563.2. [Q53H47-1 ]
    CCDS58814.1. [Q53H47-3 ]
    CCDS63528.1. [Q53H47-2 ]
    RefSeqi NP_001230652.1. NM_001243723.1. [Q53H47-3 ]
    NP_001263254.1. NM_001276325.1. [Q53H47-2 ]
    NP_006506.3. NM_006515.3. [Q53H47-1 ]
    UniGenei Hs.475300.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3BO5 X-ray 1.59 A 15-303 [» ]
    3F2K X-ray 1.85 A/B 459-684 [» ]
    3K9J X-ray 1.90 A/B 446-684 [» ]
    3K9K X-ray 2.55 A/B 446-684 [» ]
    ProteinModelPortali Q53H47.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112317. 8 interactions.
    IntActi Q53H47. 1 interaction.
    MINTi MINT-4826518.
    STRINGi 9606.ENSP00000373354.

    Chemistry

    ChEMBLi CHEMBL2189111.

    PTM databases

    PhosphoSitei Q53H47.

    Polymorphism databases

    DMDMi 74740552.

    Proteomic databases

    MaxQBi Q53H47.
    PaxDbi Q53H47.
    PRIDEi Q53H47.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000358065 ; ENSP00000373354 ; ENSG00000170364 . [Q53H47-1 ]
    ENST00000425863 ; ENSP00000403145 ; ENSG00000170364 . [Q53H47-3 ]
    ENST00000430981 ; ENSP00000403000 ; ENSG00000170364 . [Q53H47-2 ]
    GeneIDi 6419.
    KEGGi hsa:6419.
    UCSCi uc010hbx.3. human. [Q53H47-1 ]

    Organism-specific databases

    CTDi 6419.
    GeneCardsi GC03P004344.
    HGNCi HGNC:10762. SETMAR.
    MIMi 609834. gene.
    neXtProti NX_Q53H47.
    PharmGKBi PA35680.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2940.
    HOGENOMi HOG000154295.
    HOVERGENi HBG093941.
    InParanoidi Q53H47.
    KOi K11433.
    OrthoDBi EOG744T8D.
    PhylomeDBi Q53H47.
    TreeFami TF352220.

    Miscellaneous databases

    EvolutionaryTracei Q53H47.
    GeneWikii SETMAR.
    GenomeRNAii 6419.
    NextBioi 24930.
    PROi Q53H47.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q53H47.
    Bgeei Q53H47.
    CleanExi HS_SETMAR.
    Genevestigatori Q53H47.

    Family and domain databases

    InterProi IPR003616. 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 ]
    Pfami PF01498. HTH_Tnp_Tc3_2. 1 hit.
    PF05033. Pre-SET. 1 hit.
    PF00856. SET. 1 hit.
    PF01359. Transposase_1. 1 hit.
    [Graphical view ]
    SMARTi SM00508. PostSET. 1 hit.
    SM00468. PreSET. 1 hit.
    SM00317. SET. 1 hit.
    [Graphical view ]
    PROSITEi PS50868. POST_SET. 1 hit.
    PS50867. PRE_SET. 1 hit.
    PS50280. SET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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, 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 (1.59 ANGSTROMS) OF 459-684 IN COMPLEXES WITH S-ADENOSYL-L-HOMOCYSTEINE; ZINC AND MAGNESIUM IONS.
    14. "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: October 1, 2014
    This is version 90 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