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P87074

- RHP9_SCHPO

UniProt

P87074 - RHP9_SCHPO

Protein

DNA repair protein rhp9

Gene

rhp9

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    Essential for cell cycle arrest at the G1 and G2 stages following DNA damage by X-, and UV-irradiation, or inactivation of DNA ligase. Plays a role in the response to DNA damage.3 Publications

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. protein binding Source: IntAct

    GO - Biological processi

    1. mitotic G2 DNA damage checkpoint Source: PomBase
    2. negative regulation of DNA replication Source: UniProtKB-KW
    3. telomere maintenance Source: PomBase

    Keywords - Molecular functioni

    DNA replication inhibitor

    Keywords - Biological processi

    Cell cycle, DNA damage

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA repair protein rhp9
    Alternative name(s):
    RAD9 homolog
    Gene namesi
    Name:rhp9
    Synonyms:crb2
    ORF Names:SPBC342.05
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome II

    Organism-specific databases

    PomBaseiSPBC342.05.

    Subcellular locationi

    Nucleus 3 Publications
    Note: Recruited to sites of DNA damage, such as double stand breaks.

    GO - Cellular componenti

    1. nuclear chromatin Source: PomBase
    2. nucleus Source: PomBase
    3. site of double-strand break Source: PomBase

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi215 – 2151T → A: Reduces hyper-phosphorylation in response to DNA damage. Impairs checkpoint response after DNA damage. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 778778DNA repair protein rhp9PRO_0000097328Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei215 – 2151Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Subunit structurei

    Interacts with sad1. Interacts with histone H4 that has been dimethylated at 'Lys-20'.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-768448,EBI-768448
    chk1P342084EBI-768448,EBI-768535
    rad3Q020993EBI-768448,EBI-768555
    rad4P323722EBI-768448,EBI-768521

    Protein-protein interaction databases

    BioGridi277508. 115 interactions.
    IntActiP87074. 5 interactions.
    MINTiMINT-1179460.
    STRINGi4896.SPBC342.05-1.

    Structurei

    Secondary structure

    1
    778
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi182 – 1843
    Helixi237 – 2393
    Helixi362 – 3643
    Beta strandi365 – 3695
    Beta strandi372 – 3743
    Beta strandi377 – 38610
    Beta strandi395 – 4006
    Beta strandi405 – 4095
    Beta strandi412 – 4165
    Beta strandi423 – 4264
    Beta strandi434 – 4407
    Helixi449 – 4513
    Beta strandi459 – 4646
    Beta strandi467 – 4726
    Helixi473 – 4753
    Beta strandi476 – 4783
    Helixi480 – 4834
    Turni539 – 5424
    Beta strandi543 – 5475
    Helixi558 – 56710
    Helixi578 – 5803
    Turni584 – 5874
    Helixi599 – 6035
    Beta strandi605 – 6106
    Helixi618 – 6269
    Helixi634 – 6429
    Helixi649 – 6513
    Beta strandi652 – 6587
    Turni659 – 6624
    Beta strandi663 – 6664
    Helixi678 – 6847
    Turni688 – 6914
    Beta strandi693 – 6964
    Helixi714 – 72613
    Beta strandi730 – 7323
    Beta strandi743 – 7464
    Beta strandi748 – 7503
    Helixi763 – 77210

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FHDX-ray2.40A/B/C358-507[»]
    2VXBX-ray2.30A/B538-778[»]
    2VXCX-ray3.10A/B537-778[»]
    4BU0X-ray1.50B/C180-193[»]
    4BU1X-ray2.10C/D229-241[»]
    ProteinModelPortaliP87074.
    SMRiP87074. Positions 358-505, 538-778.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP87074.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini535 – 653119BRCTPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni376 – 40328Interaction with dimethylated histone H4By similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 1 BRCT domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG323789.
    OrthoDBiEOG75J0WC.
    PhylomeDBiP87074.

    Family and domain databases

    Gene3Di3.40.50.10190. 1 hit.
    InterProiIPR001357. BRCT_dom.
    [Graphical view]
    PfamiPF00533. BRCT. 1 hit.
    [Graphical view]
    SMARTiSM00292. BRCT. 1 hit.
    [Graphical view]
    SUPFAMiSSF52113. SSF52113. 1 hit.
    PROSITEiPS50172. BRCT. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P87074-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEVNDTSLHK GFGLDINSQR VFGAQAAISR NNYSKVNASI NPSPPRSNDN    50
    SNKEFSYSKD VNNNGAVEEL SLTQLFEVPS QAAFAKQSSQ DISDDELIQH 100
    DSRKVISSPY SPKQTHTVLK RLYDRQSVIS DHEKLLTPQN VSNSSQILSP 150
    FTSLLPSTLS TLKDTPLSVS QNEKNLETVG EVLVPETVAQ HRTKFYDYTL 200
    DEMENETESG QVETTPTRLA TSLGSPVLYG RVESTPPAFL PETSEKQYKR 250
    KFSFTEPSSE KVDNTETKFS KKTKNINDEN FPNPFNVISS YETSASPSTV 300
    IDQSSQVSSI FVNKRLRKSV NNQAISRSDS LSLDTPKIDS LFTRASIKPL 350
    KPSQSPNSRR SFKNRVLAFF KGYPSFYYPA TLVAPVHSAV TSSIMYKVQF 400
    DDATMSTVNS NQIKRFFLKK GDVVQSTRLG KIKHTVVKTF RSTNEQLSLI 450
    AVDALNNDMV ILAHGEIEVT VPISTIYVAP VNIRRFQGRD LSFSTLKDMK 500
    FEETSFLPSH DSQRNRSSLK ERDSSFVKKN LDSESNQLIF DDCVFAFSGP 550
    VHEDAYDRSA LETVVQDHGG LVLDTGLRPL FNDPFKSKQK KLRHLKPQKR 600
    SKSWNQAFVV SDTFSRKVKY LEALAFNIPC VHPQFIKQCL KMNRVVDFSP 650
    YLLASGYSHR LDCTLSQRIE PFDTTDSLYD RLLARKGPLF GKKILFIIPE 700
    AKSWQKKIEN TEQGQKALAH VYHALALGAD VEIRPNVAHL ECDLILTMDG 750
    NIVDETNCPV VDPEWIVECL ISQSDIST 778
    Length:778
    Mass (Da):87,462
    Last modified:July 1, 1997 - v1
    Checksum:i5E35178828E6E42A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti76 – 761F → C in BAA13093. (PubMed:9407031)Curated
    Sequence conflicti84 – 841F → C in BAA13093. (PubMed:9407031)Curated
    Sequence conflicti162 – 1632LK → YR in BAA13093. (PubMed:9407031)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y09431 Genomic DNA. Translation: CAA70582.1.
    D86478 Genomic DNA. Translation: BAA13093.1.
    CU329671 Genomic DNA. Translation: CAB46775.1.
    PIRiT43223.
    T45221.
    RefSeqiNP_596748.1. NM_001023768.2.

    Genome annotation databases

    EnsemblFungiiSPBC342.05.1; SPBC342.05.1:pep; SPBC342.05.
    GeneIDi2540992.
    KEGGispo:SPBC342.05.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y09431 Genomic DNA. Translation: CAA70582.1 .
    D86478 Genomic DNA. Translation: BAA13093.1 .
    CU329671 Genomic DNA. Translation: CAB46775.1 .
    PIRi T43223.
    T45221.
    RefSeqi NP_596748.1. NM_001023768.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FHD X-ray 2.40 A/B/C 358-507 [» ]
    2VXB X-ray 2.30 A/B 538-778 [» ]
    2VXC X-ray 3.10 A/B 537-778 [» ]
    4BU0 X-ray 1.50 B/C 180-193 [» ]
    4BU1 X-ray 2.10 C/D 229-241 [» ]
    ProteinModelPortali P87074.
    SMRi P87074. Positions 358-505, 538-778.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 277508. 115 interactions.
    IntActi P87074. 5 interactions.
    MINTi MINT-1179460.
    STRINGi 4896.SPBC342.05-1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPBC342.05.1 ; SPBC342.05.1:pep ; SPBC342.05 .
    GeneIDi 2540992.
    KEGGi spo:SPBC342.05.

    Organism-specific databases

    PomBasei SPBC342.05.

    Phylogenomic databases

    eggNOGi NOG323789.
    OrthoDBi EOG75J0WC.
    PhylomeDBi P87074.

    Miscellaneous databases

    EvolutionaryTracei P87074.
    NextBioi 20802107.
    PROi P87074.

    Family and domain databases

    Gene3Di 3.40.50.10190. 1 hit.
    InterProi IPR001357. BRCT_dom.
    [Graphical view ]
    Pfami PF00533. BRCT. 1 hit.
    [Graphical view ]
    SMARTi SM00292. BRCT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52113. SSF52113. 1 hit.
    PROSITEi PS50172. BRCT. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of the Schizosaccharomyces pombe rhp9 gene: a gene required for the DNA damage checkpoint but not the replication checkpoint."
      Willson J., Wilson S., Warr N., Watts F.Z.
      Nucleic Acids Res. 25:2138-2145(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
      Strain: 972 / ATCC 24843.
    2. "Damage and replication checkpoint control in fission yeast is ensured by interactions of Crb2, a protein with BRCT motif, with Cut5 and Chk1."
      Saka Y., Esashi F., Matsusaka T., Mochida S., Yanagida M.
      Genes Dev. 11:3387-3400(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
      Strain: 972 / ATCC 24843.
    3. "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.
    4. "Two-hybrid search for proteins that interact with Sad1 and Kms1, two membrane-bound components of the spindle pole body in fission yeast."
      Miki F., Kurabayashi A., Tange Y., Okazaki K., Shimanuki M., Niwa O.
      Mol. Genet. Genomics 270:449-461(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SAD1, SUBCELLULAR LOCATION.
    5. "Methylation of histone H4 lysine 20 controls recruitment of Crb2 to sites of DNA damage."
      Sanders S.L., Portoso M., Mata J., Baehler J., Allshire R.C., Kouzarides T.
      Cell 119:603-614(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
    6. "Cooperative control of Crb2 by ATM family and Cdc2 kinases is essential for the DNA damage checkpoint in fission yeast."
      Nakamura T.M., Moser B.A., Du L.-L., Russell P.
      Mol. Cell. Biol. 25:10721-10730(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-215, MUTAGENESIS OF THR-215.
    7. "Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair."
      Botuyan M.V., Lee J., Ward I.M., Kim J.-E., Thompson J.R., Chen J., Mer G.
      Cell 127:1361-1373(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 358-507, INTERACTION WITH HISTONE H4.

    Entry informationi

    Entry nameiRHP9_SCHPO
    AccessioniPrimary (citable) accession number: P87074
    Secondary accession number(s): Q09754
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2002
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 99 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3