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Protein

DNA repair protein crb2

Gene

crb2

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

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 (PubMed:9153313, PubMed:9407031). Interaction with rad4 via its phosphorylation sites in the N-terminus couples the DNA checkpoint apparatus to chromatin via interaction of its C-terminal BRCT domains with epigenetic modifications on histones H4 and H2A, respectively, in the G1/S phase of the cell cycle, and facilitates recruitment of the checkpoint kinase chk1 (PubMed:15550243, PubMed:16778077, PubMed:18826944, PubMed:20679485, PubMed:22792081).7 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct

GO - Biological processi

  • mitotic G2 DNA damage checkpoint Source: PomBase
  • 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 crb21 Publication
Alternative name(s):
Checkpoint mediator protein crb21 Publication
Cut5-repeat binding protein 21 Publication
RAD9 protein homolog1 Publication
Gene namesi
Name:crb21 Publication
Synonyms:rhp91 Publication
ORF Names:SPBC342.05Imported
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC342.05.
PomBaseiSPBC342.05. crb2.

Subcellular locationi

GO - Cellular componenti

  • nuclear chromatin Source: PomBase
  • nucleus Source: PomBase
  • site of double-strand break Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi73 – 731T → A in crb2-2AQ; abrogates DSB-focus formation by chk1, but not crb2; when associated with A-80. 1 Publication
Mutagenesisi80 – 801S → A in crb2-2AQ; abrogates DSB-focus formation by chk1, but not crb2; when associated with A-73. 1 Publication
Mutagenesisi184 – 1841V → A: Abolishes formation of radiation-induced crb2 foci at DSB sites. Severely impairs checkpoint response after DNA damage. 1 Publication
Mutagenesisi187 – 1871T → A: Abolishes formation of radiation-induced crb2 foci at DSB sites. Severely impairs checkpoint response after DNA damage. 1 Publication
Mutagenesisi188 – 1881V → P: Transforms T-187 into a consensus CDK phosphorylation site and abolishes the dependence of T-187 phosphorylation on prior phosphorylation at T-215 and T-235. 1 Publication
Mutagenesisi215 – 2151T → A: Reduces hyper-phosphorylation in response to DNA damage. Abolishes formation of radiation-induced crb2 foci at DSB sites. Impairs checkpoint response after DNA damage. 2 Publications
Mutagenesisi235 – 2351T → A: Abolishes formation of radiation-induced crb2 foci at DSB sites. Impairs checkpoint response after DNA damage. 2 Publications
Mutagenesisi616 – 6161R → E: Disrupts gamma-H2A binding, but has no effect on dimer formation. 1 Publication
Mutagenesisi617 – 6171K → E: Disrupts gamma-H2A binding, but has no effect on dimer formation. 1 Publication
Mutagenesisi619 – 6191K → E: Disrupts gamma-H2A binding, but has no effect on dimer formation. 1 Publication
Mutagenesisi663 – 6631C → R: Disrupts dimer formation, but not gamma-H2A binding. 1 Publication
Mutagenesisi666 – 6661S → R: Disrupts dimer formation, but not gamma-H2A binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 778778DNA repair protein crb2PRO_0000097328Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei73 – 731Phosphothreonine; by ATM1 Publication
Modified residuei80 – 801Phosphoserine; by ATM1 Publication
Modified residuei187 – 1871Phosphothreonine1 Publication
Modified residuei215 – 2151Phosphothreonine; by cdc23 Publications
Modified residuei235 – 2351Phosphothreonine1 Publication

Post-translational modificationi

Phosphorylation of Thr-73 and Ser-80 by rad3/ATM promotes interaction with chk1 (PubMed:22792081). Phosphorylation at Thr-187 is dependent on phosphorylation at Thr-215 and Thr-235. Phosphorylation at Thr-215 and Thr-235 may prime the non-canonical Thr-187 site for cdc2/CDK phosphorylation (PubMed:24074952).2 Publications

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Homodimer. Dimerization is mediated via the BRCT domain (PubMed:16778077, PubMed:18676809). Interacts (via BRCT domain) with rad3 (PubMed:14739927). Interacts with rad4 (via BRCT1,2 domains) (PubMed:9407031, PubMed:14739927); a single rad4 molecule interacts simultaneously with both Thr-187 phosphorylation sites in a crb2 dimer (PubMed:24074952). Interacts (via Tudor domain) with histone H4K20me2 (PubMed:18826944, PubMed:17190600). Interacts (via BRCT dmain) with histone H2AS128ph (gamma-H2A) (PubMed:20679485, PubMed:18676809). Interacts with chk1 (PubMed:9407031, PubMed:14739927, PubMed:22792081). Interacts with sad1 (PubMed:14655046).1 Publication9 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
Regioni141 – 245105Interaction with rad41 PublicationAdd
BLAST
Regioni376 – 40328Tudor domain; interaction with dimethylated histone H41 PublicationAdd
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.
PIRiT43223.
T45221.
RefSeqiNP_596748.1. NM_001023768.2.

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...

Protein-protein interaction databases

BioGridi277508. 117 interactions.
IntActiP87074. 5 interactions.
MINTiMINT-1179460.
STRINGi4896.SPBC342.05.1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:SPBC342.05.
PomBaseiSPBC342.05. crb2.

Phylogenomic databases

eggNOGiNOG323789.
InParanoidiP87074.
OrthoDBiEOG75J0WC.
PhylomeDBiP87074.

Miscellaneous databases

EvolutionaryTraceiP87074.
NextBioi20802107.
PROiP87074.

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]
ProtoNetiSearch...

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, INTERACTION WITH RAD4 AND CHK1.
    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. "Cdc2 phosphorylation of Crb2 is required for reestablishing cell cycle progression after the damage checkpoint."
    Esashi F., Yanagida M.
    Mol. Cell 4:167-174(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-215 BY CDC2.
  5. "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.
  6. "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.
  7. "Regulation of checkpoint kinases through dynamic interaction with Crb2."
    Mochida S., Esashi F., Aono N., Tamai K., O'Connell M.J., Yanagida M.
    EMBO J. 23:418-428(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CHK1; RAD3 AND RAD4.
  8. "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.
  9. "Histone modification-dependent and -independent pathways for recruitment of checkpoint protein Crb2 to double-strand breaks."
    Du L.L., Nakamura T.M., Russell P.
    Genes Dev. 20:1583-1596(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF THR-235.
  10. "Di-methyl H4 lysine 20 targets the checkpoint protein Crb2 to sites of DNA damage."
    Greeson N.T., Sengupta R., Arida A.R., Jenuwein T., Sanders S.L.
    J. Biol. Chem. 283:33168-33174(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HISTONE H4.
  11. "BRCT domain interactions with phospho-histone H2A target Crb2 to chromatin at double-strand breaks and maintain the DNA damage checkpoint."
    Sofueva S., Du L.L., Limbo O., Williams J.S., Russell P.
    Mol. Cell. Biol. 30:4732-4743(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH HISTONE H2A.
  12. "Phosphorylation-dependent interactions between Crb2 and Chk1 are essential for DNA damage checkpoint."
    Qu M., Yang B., Tao L., Yates J.R., Russell P., Dong M.Q., Du L.L.
    PLoS Genet. 8:E1002817-E1002817(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CHK1, PHOSPHORYLATION AT THR-73 AND SER-80.
  13. "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.
  14. "Structural and functional analysis of the Crb2-BRCT2 domain reveals distinct roles in checkpoint signaling and DNA damage repair."
    Kilkenny M.L., Dore A.S., Roe S.M., Nestoras K., Ho J.C., Watts F.Z., Pearl L.H.
    Genes Dev. 22:2034-2047(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 537-778 IN COMPLEX WITH HISTONE H2A, SUBUNIT, MUTAGENESIS OF ARG-616; LYS-617; LYS-619; CYS-663 AND SER-666.
  15. "Phosphorylation-dependent assembly and coordination of the DNA damage checkpoint apparatus by Rad4(TopBP1)."
    Qu M., Rappas M., Wardlaw C.P., Garcia V., Ren J.Y., Day M., Carr A.M., Oliver A.W., Du L.L., Pearl L.H.
    Mol. Cell 51:723-736(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 180-193 AND OF 229-241, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-187; THR-215 AND THR-235, INTERACTION WITH RAD4, MUTAGENESIS OF VAL-184; THR-187; THR-215 AND THR-235.

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: June 24, 2015
This is version 106 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

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 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.