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Q53H47

- SETMR_HUMAN

UniProt

Q53H47 - SETMR_HUMAN

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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

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-methionine By similarity
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 motif By similarityAdd
BLAST
DNA bindingi428 – 44821H-T-H motif1 PublicationAdd
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
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 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 Inferred. Chromosome Inferred

GO - Cellular componenti

  1. chromosome Source: UniProtKB-SubCell
  2. nucleus 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

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.

Miscellaneous databases

EvolutionaryTraceiQ53H47.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini73 – 13664Pre-SETAdd
BLAST
Domaini139 – 263125SETAdd
BLAST
Domaini283 – 29917Post-SETAdd
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.
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.

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei163 – 301139Missing in isoform 3. VSP_054089Add
BLAST
Alternative sequencei341 – 36525TMKMM…MGRKA → VSLFSDKQLAPPYSGRQWLA SFTSA in isoform 2. VSP_021440Add
BLAST
Alternative sequencei366 – 684319Missing in isoform 2. VSP_021441Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911R → H in BAG63636. 1 Publication
Sequence conflicti343 – 3431K → E in AAC52010. 1 Publication
Sequence conflicti439 – 4391N → D in AAC52010. 1 Publication
Sequence conflicti465 – 4651T → S in AAC52010. 1 Publication
Sequence conflicti484 – 4841H → N in AAC52010. 1 Publication
Sequence conflicti508 – 5081S → P in AAC52010. 1 Publication
Sequence conflicti514 – 5141Q → R in AAC52010. 1 Publication
Sequence conflicti525 – 5251I → N in AAC52010. 1 Publication
Sequence conflicti528 – 5281P → Q in AAC52010. 1 Publication
Sequence conflicti535 – 5351I → V in AAC52010. 1 Publication
Sequence conflicti562 – 5621E → Q in AAC52010. 1 Publication
Sequence conflicti567 – 5682NQ → HR in AAC52010. 1 Publication
Sequence conflicti575 – 5751L → P in AAC52010. 1 Publication
Sequence conflicti620 – 6201L → S in AAC52010. 1 Publication
Sequence conflicti623 – 6231N → D in AAC52010. 1 Publication
Sequence conflicti626 – 6261V → F in AAC52010. 1 Publication
Sequence conflicti631 – 6311N → D in AAC52010. 1 Publication
Sequence conflicti656 – 6561Q → R in AAC52010. 1 Publication
Sequence conflicti667 – 6671Q → K in AAC52010. 1 Publication

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.
ENST00000425863; ENSP00000403145; ENSG00000170364.
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 .
ENST00000425863 ; ENSP00000403145 ; ENSG00000170364 .
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

« 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, 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: September 3, 2014
This is version 89 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

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