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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

GO - Biological processi

  • mitotic DNA replication checkpoint Source: PomBase
  • mitotic G2 DNA damage checkpoint Source: PomBase
  • negative regulation of DNA replication Source: UniProtKB-KW
  • negative regulation of protein kinase activity Source: PomBase
  • positive regulation of DNA repair Source: PomBase
  • positive regulation of transcription from RNA polymerase II promoter Source: GO_Central
  • regulation of double-strand break repair via homologous recombination Source: PomBase
  • signal transduction involved in mitotic DNA damage checkpoint Source: PomBase
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
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

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

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi73T → A in crb2-2AQ; abrogates DSB-focus formation by chk1, but not crb2; when associated with A-80. 1 Publication1
Mutagenesisi80S → A in crb2-2AQ; abrogates DSB-focus formation by chk1, but not crb2; when associated with A-73. 1 Publication1
Mutagenesisi184V → A: Abolishes formation of radiation-induced crb2 foci at DSB sites. Severely impairs checkpoint response after DNA damage. 1 Publication1
Mutagenesisi187T → A: Abolishes formation of radiation-induced crb2 foci at DSB sites. Severely impairs checkpoint response after DNA damage. 1 Publication1
Mutagenesisi188V → 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 Publication1
Mutagenesisi215T → 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 Publications1
Mutagenesisi235T → A: Abolishes formation of radiation-induced crb2 foci at DSB sites. Impairs checkpoint response after DNA damage. 2 Publications1
Mutagenesisi616R → E: Disrupts gamma-H2A binding, but has no effect on dimer formation. 1 Publication1
Mutagenesisi617K → E: Disrupts gamma-H2A binding, but has no effect on dimer formation. 1 Publication1
Mutagenesisi619K → E: Disrupts gamma-H2A binding, but has no effect on dimer formation. 1 Publication1
Mutagenesisi663C → R: Disrupts dimer formation, but not gamma-H2A binding. 1 Publication1
Mutagenesisi666S → R: Disrupts dimer formation, but not gamma-H2A binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000973281 – 778DNA repair protein crb2Add BLAST778

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei73Phosphothreonine; by ATM1 Publication1
Modified residuei80Phosphoserine; by ATM1 Publication1
Modified residuei187Phosphothreonine1 Publication1
Modified residuei215Phosphothreonine; by cdc23 Publications1
Modified residuei235Phosphothreonine1 Publication1

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

Proteomic databases

PRIDEiP87074.

PTM databases

iPTMnetiP87074.

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi277508. 117 interactors.
IntActiP87074. 5 interactors.
MINTiMINT-1179460.

Structurei

Secondary structure

1778
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi182 – 184Combined sources3
Helixi237 – 239Combined sources3
Helixi362 – 364Combined sources3
Beta strandi365 – 369Combined sources5
Beta strandi372 – 374Combined sources3
Beta strandi377 – 386Combined sources10
Beta strandi395 – 400Combined sources6
Beta strandi405 – 409Combined sources5
Beta strandi412 – 416Combined sources5
Beta strandi423 – 426Combined sources4
Beta strandi434 – 440Combined sources7
Helixi449 – 451Combined sources3
Beta strandi459 – 464Combined sources6
Beta strandi467 – 472Combined sources6
Helixi473 – 475Combined sources3
Beta strandi476 – 478Combined sources3
Helixi480 – 483Combined sources4
Turni539 – 542Combined sources4
Beta strandi543 – 547Combined sources5
Helixi558 – 567Combined sources10
Helixi578 – 580Combined sources3
Turni584 – 587Combined sources4
Helixi599 – 603Combined sources5
Beta strandi605 – 610Combined sources6
Helixi618 – 626Combined sources9
Helixi634 – 642Combined sources9
Helixi649 – 651Combined sources3
Beta strandi652 – 658Combined sources7
Turni659 – 662Combined sources4
Beta strandi663 – 666Combined sources4
Helixi678 – 684Combined sources7
Turni688 – 691Combined sources4
Beta strandi693 – 696Combined sources4
Helixi714 – 726Combined sources13
Beta strandi730 – 732Combined sources3
Beta strandi743 – 746Combined sources4
Beta strandi748 – 750Combined sources3
Helixi763 – 772Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP87074.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini535 – 653BRCTPROSITE-ProRule annotationAdd BLAST119

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni141 – 245Interaction with rad41 PublicationAdd BLAST105
Regioni358 – 493Tudor-like1 PublicationAdd BLAST136
Regioni370 – 404Interaction with dimethylated histone H41 PublicationAdd BLAST35

Domaini

The Tudor-like region mediates binding to H4K20me2.1 Publication

Sequence similaritiesi

Contains 1 BRCT domain.PROSITE-ProRule annotation

Phylogenomic databases

InParanoidiP87074.
OrthoDBiEOG092C2JST.
PhylomeDBiP87074.

Family and domain databases

CDDicd00027. BRCT. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti76F → C in BAA13093 (PubMed:9407031).Curated1
Sequence conflicti84F → C in BAA13093 (PubMed:9407031).Curated1
Sequence conflicti162 – 163LK → YR in BAA13093 (PubMed:9407031).Curated2

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277508. 117 interactors.
IntActiP87074. 5 interactors.
MINTiMINT-1179460.

PTM databases

iPTMnetiP87074.

Proteomic databases

PRIDEiP87074.

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

InParanoidiP87074.
OrthoDBiEOG092C2JST.
PhylomeDBiP87074.

Miscellaneous databases

EvolutionaryTraceiP87074.
PROiP87074.

Family and domain databases

CDDicd00027. BRCT. 1 hit.
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...

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 30, 2016
This is version 120 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

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.