Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DNA damage checkpoint protein rad24

Gene

rad24

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

Functioni

Required for the DNA damage checkpoint that ensures that DNA damage is repaired before mitosis is attempted. Acts as a negative regulator of meiosis by antagonizing the function of mei2. It inhibits the association of meiRNA (a non-coding RNA molecule required for the nuclear mei2 dot formation) to the phosphorylated but not to the unphosphorylated form of mei2 in vitro.1 Publication

GO - Molecular functioni

  • protein phosphatase inhibitor activity Source: PomBase

GO - Biological processi

  • cellular protein localization Source: PomBase
  • cytokinesis checkpoint Source: PomBase
  • cytoplasmic sequestering of protein Source: PomBase
  • meiotic cell cycle Source: UniProtKB-KW
  • mitotic DNA damage checkpoint Source: PomBase
  • negative regulation of catalytic activity Source: GOC
  • negative regulation of G2/M transition of mitotic cell cycle Source: PomBase
  • negative regulation of induction of conjugation with cellular fusion Source: PomBase
  • negative regulation of sequence-specific DNA binding transcription factor activity Source: PomBase
  • negative regulation of transcription from RNA polymerase II promoter Source: PomBase
  • positive regulation of septation initiation signaling Source: PomBase
Complete GO annotation...

Keywords - Biological processi

Cell cycle, DNA damage, Meiosis

Enzyme and pathway databases

ReactomeiR-SPO-3371453. Regulation of HSF1-mediated heat shock response.
R-SPO-3371511. HSF1 activation.
R-SPO-5625740. RHO GTPases activate PKNs.
R-SPO-75035. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA damage checkpoint protein rad24
Gene namesi
Name:rad24
ORF Names:SPAC8E11.02c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC8E11.02c.
PomBaseiSPAC8E11.02c. rad24.

Subcellular locationi

GO - Cellular componenti

  • cell division site Source: PomBase
  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • mitotic spindle pole body Source: PomBase
  • spindle midzone Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 270270DNA damage checkpoint protein rad24PRO_0000058717Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei34 – 341Phosphoserine1 Publication
Modified residuei66 – 661Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP42656.
PRIDEiP42656.

PTM databases

iPTMnetiP42656.
SwissPalmiP42656.

Interactioni

Subunit structurei

Binds preferentially to mei2 phosphorylated by ran1/pat1.

Binary interactionsi

WithEntry#Exp.IntActNotes
clp1Q9P7H13EBI-704791,EBI-704737

Protein-protein interaction databases

BioGridi278511. 78 interactions.
IntActiP42656. 3 interactions.
MINTiMINT-132194.

Structurei

3D structure databases

ProteinModelPortaliP42656.
SMRiP42656. Positions 6-234.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the 14-3-3 family.Curated

Phylogenomic databases

HOGENOMiHOG000240379.
InParanoidiP42656.
KOiK06630.
OMAiELSNICH.
OrthoDBiEOG7TXKTD.
PhylomeDBiP42656.

Family and domain databases

InterProiIPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view]
PANTHERiPTHR18860. PTHR18860. 1 hit.
PfamiPF00244. 14-3-3. 1 hit.
[Graphical view]
PIRSFiPIRSF000868. 14-3-3. 1 hit.
PRINTSiPR00305. 1433ZETA.
SMARTiSM00101. 14_3_3. 1 hit.
[Graphical view]
SUPFAMiSSF48445. SSF48445. 1 hit.
PROSITEiPS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P42656-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTTSREDAV YLAKLAEQAE RYEGMVENMK SVASTDQELT VEERNLLSVA
60 70 80 90 100
YKNVIGARRA SWRIVSSIEQ KEESKGNTAQ VELIKEYRQK IEQELDTICQ
110 120 130 140 150
DILTVLEKHL IPNAASAESK VFYYKMKGDY YRYLAEFAVG EKRQHSADQS
160 170 180 190 200
LEGYKAASEI ATAELAPTHP IRLGLALNFS VFYYEILNSP DRACYLAKQA
210 220 230 240 250
FDEAISELDS LSEESYKDST LIMQLLRDNL TLWTSDAEYS AAAAGGNTEG
260 270
AQENAPSNAP EGEAEPKADA
Length:270
Mass (Da):30,082
Last modified:July 15, 1998 - v2
Checksum:i1401DD425A1A872F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti219 – 2191S → F in BAA24800 (PubMed:12242289).Curated
Sequence conflicti264 – 2641A → R in CAA55795 (PubMed:8036497).Curated
Sequence conflicti269 – 2702DA → THR in CAA55795 (PubMed:8036497).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79206 Genomic DNA. Translation: CAA55795.1.
AB010899 mRNA. Translation: BAA24800.1.
AB008545 Genomic DNA. Translation: BAA28672.1.
CU329670 Genomic DNA. Translation: CAA17023.1.
PIRiT39156.
T43316.
T45211.
RefSeqiNP_594167.1. NM_001019591.2.

Genome annotation databases

EnsemblFungiiSPAC8E11.02c.1; SPAC8E11.02c.1:pep; SPAC8E11.02c.
GeneIDi2542029.
KEGGispo:SPAC8E11.02c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79206 Genomic DNA. Translation: CAA55795.1.
AB010899 mRNA. Translation: BAA24800.1.
AB008545 Genomic DNA. Translation: BAA28672.1.
CU329670 Genomic DNA. Translation: CAA17023.1.
PIRiT39156.
T43316.
T45211.
RefSeqiNP_594167.1. NM_001019591.2.

3D structure databases

ProteinModelPortaliP42656.
SMRiP42656. Positions 6-234.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278511. 78 interactions.
IntActiP42656. 3 interactions.
MINTiMINT-132194.

PTM databases

iPTMnetiP42656.
SwissPalmiP42656.

Proteomic databases

MaxQBiP42656.
PRIDEiP42656.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC8E11.02c.1; SPAC8E11.02c.1:pep; SPAC8E11.02c.
GeneIDi2542029.
KEGGispo:SPAC8E11.02c.

Organism-specific databases

EuPathDBiFungiDB:SPAC8E11.02c.
PomBaseiSPAC8E11.02c. rad24.

Phylogenomic databases

HOGENOMiHOG000240379.
InParanoidiP42656.
KOiK06630.
OMAiELSNICH.
OrthoDBiEOG7TXKTD.
PhylomeDBiP42656.

Enzyme and pathway databases

ReactomeiR-SPO-3371453. Regulation of HSF1-mediated heat shock response.
R-SPO-3371511. HSF1 activation.
R-SPO-5625740. RHO GTPases activate PKNs.
R-SPO-75035. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.

Miscellaneous databases

NextBioi20803107.
PROiP42656.

Family and domain databases

InterProiIPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view]
PANTHERiPTHR18860. PTHR18860. 1 hit.
PfamiPF00244. 14-3-3. 1 hit.
[Graphical view]
PIRSFiPIRSF000868. 14-3-3. 1 hit.
PRINTSiPR00305. 1433ZETA.
SMARTiSM00101. 14_3_3. 1 hit.
[Graphical view]
SUPFAMiSSF48445. SSF48445. 1 hit.
PROSITEiPS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "14-3-3 protein homologs required for the DNA damage checkpoint in fission yeast."
    Ford J.C., Al-Khodairy F., Fotou E., Sheldrick K.S., Griffiths D.J.F., Carr A.M.
    Science 265:533-535(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The 14-3-3 proteins Rad24 and Rad25 negatively regulate Byr2 by affecting its localization in Schizosaccharomyces pombe."
    Ozoe F., Kurokawa R., Kobayashi Y., Jeong H.T., Tanaka K., Sen K., Nakagawa T., Matsuda H., Kawamukai M.
    Mol. Cell. Biol. 22:7105-7119(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. Yoneki T., Fukushima K., Nojima H.
    Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "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.
  5. "14-3-3 protein interferes with the binding of RNA to the phosphorylated form of fission yeast meiotic regulator Mei2p."
    Sato M., Watanabe Y., Akiyoshi Y., Yamamoto M.
    Curr. Biol. 12:141-145(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MEI2.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34 AND SER-66, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiRAD24_SCHPO
AccessioniPrimary (citable) accession number: P42656
Secondary accession number(s): O42704, O42879
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 15, 1998
Last modified: April 13, 2016
This is version 132 of the entry and version 2 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.