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P87074 (RHP9_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA repair protein rhp9
Alternative name(s):
RAD9 homolog
Gene names
Name:rhp9
Synonyms:crb2
ORF Names:SPBC342.05
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length778 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.5

Subunit structure

Interacts with sad1. Interacts with histone H4 that has been dimethylated at 'Lys-20'. Ref.4 Ref.7

Subcellular location

Nucleus. Note: Recruited to sites of DNA damage, such as double stand breaks. Ref.2 Ref.4 Ref.5

Sequence similarities

Contains 1 BRCT domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 778778DNA repair protein rhp9
PRO_0000097328

Regions

Domain535 – 653119BRCT
Region376 – 40328Interaction with dimethylated histone H4 By similarity

Amino acid modifications

Modified residue2151Phosphothreonine Ref.6

Experimental info

Mutagenesis2151T → A: Reduces hyper-phosphorylation in response to DNA damage. Impairs checkpoint response after DNA damage. Ref.6
Sequence conflict761F → C in BAA13093. Ref.2
Sequence conflict841F → C in BAA13093. Ref.2
Sequence conflict162 – 1632LK → YR in BAA13093. Ref.2

Secondary structure

...................................................................... 778
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P87074 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 5E35178828E6E42A

FASTA77887,462
        10         20         30         40         50         60 
MEVNDTSLHK GFGLDINSQR VFGAQAAISR NNYSKVNASI NPSPPRSNDN SNKEFSYSKD 

        70         80         90        100        110        120 
VNNNGAVEEL SLTQLFEVPS QAAFAKQSSQ DISDDELIQH DSRKVISSPY SPKQTHTVLK 

       130        140        150        160        170        180 
RLYDRQSVIS DHEKLLTPQN VSNSSQILSP FTSLLPSTLS TLKDTPLSVS QNEKNLETVG 

       190        200        210        220        230        240 
EVLVPETVAQ HRTKFYDYTL DEMENETESG QVETTPTRLA TSLGSPVLYG RVESTPPAFL 

       250        260        270        280        290        300 
PETSEKQYKR KFSFTEPSSE KVDNTETKFS KKTKNINDEN FPNPFNVISS YETSASPSTV 

       310        320        330        340        350        360 
IDQSSQVSSI FVNKRLRKSV NNQAISRSDS LSLDTPKIDS LFTRASIKPL KPSQSPNSRR 

       370        380        390        400        410        420 
SFKNRVLAFF KGYPSFYYPA TLVAPVHSAV TSSIMYKVQF DDATMSTVNS NQIKRFFLKK 

       430        440        450        460        470        480 
GDVVQSTRLG KIKHTVVKTF RSTNEQLSLI AVDALNNDMV ILAHGEIEVT VPISTIYVAP 

       490        500        510        520        530        540 
VNIRRFQGRD LSFSTLKDMK FEETSFLPSH DSQRNRSSLK ERDSSFVKKN LDSESNQLIF 

       550        560        570        580        590        600 
DDCVFAFSGP VHEDAYDRSA LETVVQDHGG LVLDTGLRPL FNDPFKSKQK KLRHLKPQKR 

       610        620        630        640        650        660 
SKSWNQAFVV SDTFSRKVKY LEALAFNIPC VHPQFIKQCL KMNRVVDFSP YLLASGYSHR 

       670        680        690        700        710        720 
LDCTLSQRIE PFDTTDSLYD RLLARKGPLF GKKILFIIPE AKSWQKKIEN TEQGQKALAH 

       730        740        750        760        770 
VYHALALGAD VEIRPNVAHL ECDLILTMDG NIVDETNCPV VDPEWIVECL ISQSDIST 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y09431 Genomic DNA. Translation: CAA70582.1.
D86478 Genomic DNA. Translation: BAA13093.1.
CU329671 Genomic DNA. Translation: CAB46775.1.
PIRT43223.
T45221.
RefSeqNP_596748.1. NM_001023768.2.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP87074.
SMRP87074. Positions 358-505, 538-778.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid277508. 115 interactions.
IntActP87074. 5 interactions.
MINTMINT-1179460.
STRING4896.SPBC342.05-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC342.05.1; SPBC342.05.1:pep; SPBC342.05.
GeneID2540992.
KEGGspo:SPBC342.05.

Organism-specific databases

PomBaseSPBC342.05.

Phylogenomic databases

eggNOGNOG323789.
OrthoDBEOG75J0WC.
PhylomeDBP87074.

Family and domain databases

Gene3D3.40.50.10190. 1 hit.
InterProIPR001357. BRCT_dom.
[Graphical view]
PfamPF00533. BRCT. 1 hit.
[Graphical view]
SMARTSM00292. BRCT. 1 hit.
[Graphical view]
SUPFAMSSF52113. SSF52113. 1 hit.
PROSITEPS50172. BRCT. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP87074.
NextBio20802107.
PROP87074.

Entry information

Entry nameRHP9_SCHPO
AccessionPrimary (citable) accession number: P87074
Secondary accession number(s): Q09754
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2002
Last sequence update: July 1, 1997
Last modified: April 16, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references