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Protein

Mst2 complex subunit nto1

Gene

nto1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Component of the mst2 complex which is a highly specific H3 lysine 14 (H3K14) acetyltransferase that functions together with gcn5 to regulate global levels of H3K14 acetylation (H3K14ac), critical for DNA damage checkpoint activation.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri194 – 24451PHD-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

DNA damage

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-SPO-114608. Platelet degranulation.
R-SPO-6804758. Regulation of TP53 Activity through Acetylation.

Names & Taxonomyi

Protein namesi
Recommended name:
Mst2 complex subunit nto1
Gene namesi
Name:nto1
ORF Names:SPBC17D11.04c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC17D11.04c.
PomBaseiSPBC17D11.04c. nto1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • Mst2 histone acetyltransferase complex Source: PomBase
  • NuA3 histone acetyltransferase complex Source: PomBase
  • nuclear chromatin Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 767767Mst2 complex subunit nto1PRO_0000303918Add
BLAST

Proteomic databases

MaxQBiO74759.

Interactioni

Subunit structurei

Component of the mst2 complex composed of at least eaf6, mst2, nto1, pdp3, ptf1, ptf2 and tfg3.1 Publication

Protein-protein interaction databases

BioGridi276615. 67 interactions.
MINTiMINT-4680521.

Structurei

3D structure databases

ProteinModelPortaliO74759.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Contains 1 PHD-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri194 – 24451PHD-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

InParanoidiO74759.
OMAiFNERITR.
OrthoDBiEOG7DC2D3.
PhylomeDBiO74759.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR019542. Enhancer_polycomb-like_N.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF10513. EPL1. 1 hit.
[Graphical view]
SMARTiSM00249. PHD. 2 hits.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O74759-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQTFRLTSTG RNILRPDELA FQPREEIPYK SFHPDLQIDE PLEILEGDHT
60 70 80 90 100
QYAGLRDSLV TYKSENSYVL KALLNAKIEN VKPVGVQTEN INPQEKKFGY
110 120 130 140 150
KTAKQLDWSP DEYFKFVAIH PYSKTSFPVS YDLDELDTMW LTYYNEFQLS
160 170 180 190 200
SNSEWENVSK EFLEIVLTII EREWLYLEAW MPKIEPVRVE DELDGRCVIC
210 220 230 240 250
NEAECENSNA IVFCDNCNTS VHQNCYGIPF VPEGQWFCKK CLLAPHEVIC
260 270 280 290 300
CAFCPDRDGA FCTTLDGRWC HTICAIAIPE ISFHDTSRLD LVRNIASIPK
310 320 330 340 350
SRWKLVCCIC KLRWGTCVQC SDKNCYAAYH ITCARRAGFF YKIYSHSASY
360 370 380 390 400
DSVDMETYCD KHTPPDYLNG LMKRLFPLAE LYYKRMATDV PLNFQATKAP
410 420 430 440 450
DFVPEGPWKS HPLPAFIVDK VTKVLLSYNV KRQDLPSIVT DICKFYHMKR
460 470 480 490 500
RSRKDAPLLK SQLLMDSLEN LPVRASKDRV RSLEVAKALQ DQYQSLLTLV
510 520 530 540 550
ESTAKRQLLK CQLSNLRKKF LNLNYFPAQR LLQDTLVKII DLDVDGLFNM
560 570 580 590 600
PLDNGWIGWV ELKRQVFSYQ IGSISSLEKK LEPIWDVDGV IQCIDDMEQL
610 620 630 640 650
TAMVQFAQKT EGEVKKLFIK AKIYFESLSL DERGNLKVPS LGINGLEYDN
660 670 680 690 700
WPGLNELEMS QLDIPSQGNL KSLHDFIEGL DLNEKIGKFP ISMFQNQVAQ
710 720 730 740 750
FSTIEIPKMS GRANGMHNFH SEDVTGQSNH ALPNSVTKKN GTKQPYTKNS
760
LPFNERITRS KAKKNYS
Length:767
Mass (Da):88,257
Last modified:November 1, 1998 - v1
Checksum:i94664AA082E74245
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA21075.1.
PIRiT39715.
RefSeqiNP_596378.1. NM_001022299.2.

Genome annotation databases

EnsemblFungiiSPBC17D11.04c.1; SPBC17D11.04c.1:pep; SPBC17D11.04c.
GeneIDi2540077.
KEGGispo:SPBC17D11.04c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA21075.1.
PIRiT39715.
RefSeqiNP_596378.1. NM_001022299.2.

3D structure databases

ProteinModelPortaliO74759.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276615. 67 interactions.
MINTiMINT-4680521.

Proteomic databases

MaxQBiO74759.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC17D11.04c.1; SPBC17D11.04c.1:pep; SPBC17D11.04c.
GeneIDi2540077.
KEGGispo:SPBC17D11.04c.

Organism-specific databases

EuPathDBiFungiDB:SPBC17D11.04c.
PomBaseiSPBC17D11.04c. nto1.

Phylogenomic databases

InParanoidiO74759.
OMAiFNERITR.
OrthoDBiEOG7DC2D3.
PhylomeDBiO74759.

Enzyme and pathway databases

ReactomeiR-SPO-114608. Platelet degranulation.
R-SPO-6804758. Regulation of TP53 Activity through Acetylation.

Miscellaneous databases

PROiO74759.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR019542. Enhancer_polycomb-like_N.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF10513. EPL1. 1 hit.
[Graphical view]
SMARTiSM00249. PHD. 2 hits.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  3. "Histone H3 lysine 14 acetylation is required for activation of a DNA damage checkpoint in fission yeast."
    Wang Y., Kallgren S.P., Reddy B.D., Kuntz K., Lopez-Maury L., Thompson J., Watt S., Ma C., Hou H., Shi Y., Yates J.R. III, Bahler J., O'Connell M.J., Jia S.
    J. Biol. Chem. 287:4386-4393(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MST2 COMPLEX, FUNCTION.

Entry informationi

Entry nameiNTO1_SCHPO
AccessioniPrimary (citable) accession number: O74759
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: November 1, 1998
Last modified: June 8, 2016
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. 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.