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P87074

- RHP9_SCHPO

UniProt

P87074 - RHP9_SCHPO

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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

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

GO - Biological processi

  1. mitotic G2 DNA damage checkpoint Source: PomBase
  2. negative regulation of DNA replication Source: UniProtKB-KW
Complete GO annotation...

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
Complete GO annotation...

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. 117 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 – 1843Combined sources
Helixi237 – 2393Combined sources
Helixi362 – 3643Combined sources
Beta strandi365 – 3695Combined sources
Beta strandi372 – 3743Combined sources
Beta strandi377 – 38610Combined sources
Beta strandi395 – 4006Combined sources
Beta strandi405 – 4095Combined sources
Beta strandi412 – 4165Combined sources
Beta strandi423 – 4264Combined sources
Beta strandi434 – 4407Combined sources
Helixi449 – 4513Combined sources
Beta strandi459 – 4646Combined sources
Beta strandi467 – 4726Combined sources
Helixi473 – 4753Combined sources
Beta strandi476 – 4783Combined sources
Helixi480 – 4834Combined sources
Turni539 – 5424Combined sources
Beta strandi543 – 5475Combined sources
Helixi558 – 56710Combined sources
Helixi578 – 5803Combined sources
Turni584 – 5874Combined sources
Helixi599 – 6035Combined sources
Beta strandi605 – 6106Combined sources
Helixi618 – 6269Combined sources
Helixi634 – 6429Combined sources
Helixi649 – 6513Combined sources
Beta strandi652 – 6587Combined sources
Turni659 – 6624Combined sources
Beta strandi663 – 6664Combined sources
Helixi678 – 6847Combined sources
Turni688 – 6914Combined sources
Beta strandi693 – 6964Combined sources
Helixi714 – 72613Combined sources
Beta strandi730 – 7323Combined sources
Beta strandi743 – 7464Combined sources
Beta strandi748 – 7503Combined sources
Helixi763 – 77210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP87074.
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

        10         20         30         40         50
MEVNDTSLHK GFGLDINSQR VFGAQAAISR NNYSKVNASI NPSPPRSNDN
60 70 80 90 100
SNKEFSYSKD VNNNGAVEEL SLTQLFEVPS QAAFAKQSSQ DISDDELIQH
110 120 130 140 150
DSRKVISSPY SPKQTHTVLK RLYDRQSVIS DHEKLLTPQN VSNSSQILSP
160 170 180 190 200
FTSLLPSTLS TLKDTPLSVS QNEKNLETVG EVLVPETVAQ HRTKFYDYTL
210 220 230 240 250
DEMENETESG QVETTPTRLA TSLGSPVLYG RVESTPPAFL PETSEKQYKR
260 270 280 290 300
KFSFTEPSSE KVDNTETKFS KKTKNINDEN FPNPFNVISS YETSASPSTV
310 320 330 340 350
IDQSSQVSSI FVNKRLRKSV NNQAISRSDS LSLDTPKIDS LFTRASIKPL
360 370 380 390 400
KPSQSPNSRR SFKNRVLAFF KGYPSFYYPA TLVAPVHSAV TSSIMYKVQF
410 420 430 440 450
DDATMSTVNS NQIKRFFLKK GDVVQSTRLG KIKHTVVKTF RSTNEQLSLI
460 470 480 490 500
AVDALNNDMV ILAHGEIEVT VPISTIYVAP VNIRRFQGRD LSFSTLKDMK
510 520 530 540 550
FEETSFLPSH DSQRNRSSLK ERDSSFVKKN LDSESNQLIF DDCVFAFSGP
560 570 580 590 600
VHEDAYDRSA LETVVQDHGG LVLDTGLRPL FNDPFKSKQK KLRHLKPQKR
610 620 630 640 650
SKSWNQAFVV SDTFSRKVKY LEALAFNIPC VHPQFIKQCL KMNRVVDFSP
660 670 680 690 700
YLLASGYSHR LDCTLSQRIE PFDTTDSLYD RLLARKGPLF GKKILFIIPE
710 720 730 740 750
AKSWQKKIEN TEQGQKALAH VYHALALGAD VEIRPNVAHL ECDLILTMDG
760 770
NIVDETNCPV VDPEWIVECL ISQSDIST
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 117 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.
InParanoidi P87074.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 101 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