RHP9_SCHPO - dbPTM
RHP9_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RHP9_SCHPO
UniProt AC P87074
Protein Name DNA repair protein crb2 {ECO:0000305|PubMed:9407031}
Gene Name crb2 {ECO:0000303|PubMed:9407031}
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 778
Subcellular Localization Nucleus . Recruited to sites of DNA damage, such as double stand breaks.
Protein Description 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]
Protein Sequence MEVNDTSLHKGFGLDINSQRVFGAQAAISRNNYSKVNASINPSPPRSNDNSNKEFSYSKDVNNNGAVEELSLTQLFEVPSQAAFAKQSSQDISDDELIQHDSRKVISSPYSPKQTHTVLKRLYDRQSVISDHEKLLTPQNVSNSSQILSPFTSLLPSTLSTLKDTPLSVSQNEKNLETVGEVLVPETVAQHRTKFYDYTLDEMENETESGQVETTPTRLATSLGSPVLYGRVESTPPAFLPETSEKQYKRKFSFTEPSSEKVDNTETKFSKKTKNINDENFPNPFNVISSYETSASPSTVIDQSSQVSSIFVNKRLRKSVNNQAISRSDSLSLDTPKIDSLFTRASIKPLKPSQSPNSRRSFKNRVLAFFKGYPSFYYPATLVAPVHSAVTSSIMYKVQFDDATMSTVNSNQIKRFFLKKGDVVQSTRLGKIKHTVVKTFRSTNEQLSLIAVDALNNDMVILAHGEIEVTVPISTIYVAPVNIRRFQGRDLSFSTLKDMKFEETSFLPSHDSQRNRSSLKERDSSFVKKNLDSESNQLIFDDCVFAFSGPVHEDAYDRSALETVVQDHGGLVLDTGLRPLFNDPFKSKQKKLRHLKPQKRSKSWNQAFVVSDTFSRKVKYLEALAFNIPCVHPQFIKQCLKMNRVVDFSPYLLASGYSHRLDCTLSQRIEPFDTTDSLYDRLLARKGPLFGKKILFIIPEAKSWQKKIENTEQGQKALAHVYHALALGADVEIRPNVAHLECDLILTMDGNIVDETNCPVVDPEWIVECLISQSDIST
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
43PhosphorylationVNASINPSPPRSNDN
CCEECCCCCCCCCCC		42.9421712547
47PhosphorylationINPSPPRSNDNSNKE
CCCCCCCCCCCCCCC		55.0721712547
73PhosphorylationAVEELSLTQLFEVPS
CEEEEEEHHEECCCC		21.6122792081
80PhosphorylationTQLFEVPSQAAFAKQ
HHEECCCCHHHHHHH		37.3122792081
88PhosphorylationQAAFAKQSSQDISDD
HHHHHHHCCCCCCHH		29.2921712547
89PhosphorylationAAFAKQSSQDISDDE
HHHHHHCCCCCCHHH		29.4024763107
93PhosphorylationKQSSQDISDDELIQH
HHCCCCCCHHHHHHC		47.5024763107
108PhosphorylationDSRKVISSPYSPKQT
HHHCHHCCCCCHHHH		19.4124763107
111PhosphorylationKVISSPYSPKQTHTV
CHHCCCCCHHHHHHH		29.0725720772
187PhosphorylationGEVLVPETVAQHRTK
EEEECHHHHHHHCCC		18.3128889911
215PhosphorylationESGQVETTPTRLATS
CCCCCCCCCCHHHHH		14.7928889911
221PhosphorylationTTPTRLATSLGSPVL
CCCCHHHHHCCCCEE		29.1329996109
222PhosphorylationTPTRLATSLGSPVLY
CCCHHHHHCCCCEEE		25.7329996109
225PhosphorylationRLATSLGSPVLYGRV
HHHHHCCCCEEECCC		19.6828889911
235PhosphorylationLYGRVESTPPAFLPE
EECCCCCCCCCCCCC		21.5618676809
253PhosphorylationKQYKRKFSFTEPSSE
HHHHHCCCCCCCCCC		34.0029996109
330PhosphorylationQAISRSDSLSLDTPK
CCCCCCCCCCCCCCC		22.5429996109
675PhosphorylationRIEPFDTTDSLYDRL
CCCCCCCCHHHHHHH		25.9925720772
677PhosphorylationEPFDTTDSLYDRLLA
CCCCCCHHHHHHHHH		27.0825720772
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
73TPhosphorylationKinaseATMO74630
Uniprot
80SPhosphorylationKinaseATMO74630
Uniprot
215TPhosphorylationKinaseCDC2P04551
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RHP9_SCHPO !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of RHP9_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TOP3_SCHPOtop3genetic
12023299
HUS2_SCHPOrqh1genetic
12023299
KU70_SCHPOpku70genetic
12196391
TAZ1_SCHPOtaz1genetic
12196391
DPOD3_SCHPOcdc27genetic
9928931
DPOA_SCHPOpol1genetic
9928931
DPOE_SCHPOcdc20genetic
9928931
CDC18_SCHPOcdc18genetic
9928931
DNLI1_SCHPOcdc17genetic
9928931
CDC24_SCHPOcdc24genetic
9928931
CDC10_SCHPOcdc10genetic
9928931
CHK1_SCHPOchk1genetic
9407031
SET1_SCHPOset1genetic
12589755
SET9_SCHPOset9genetic
15550243
H2A1_SCHPOhta1genetic
16314498
H2A2_SCHPOhta2genetic
16314498
RAD4_SCHPOrad4physical
16778077
RAD22_SCHPOrad52physical
12917337
RHP9_SCHPOcrb2physical
15229228
RHP9_SCHPOcrb2physical
18676809
EXO1_SCHPOexo1genetic
18931302
RAD57_SCHPOrad57genetic
18931302
DDB1_SCHPOddb1genetic
18931302
RHP41_SCHPOrhp41genetic
18931302
FEN1_SCHPOrad2genetic
18931302
MRC1_SCHPOmrc1genetic
18931302
TLG2_SCHPOtlg2genetic
18931302
SRS2_SCHPOsrs2genetic
18931302
SWI3_SCHPOswi3genetic
18931302
RAD13_SCHPOrad13genetic
9153313
FEN1_SCHPOrad2genetic
9153313
CUT1_SCHPOcut1genetic
9153313
H2A1_SCHPOhta1genetic
20679485
H2A2_SCHPOhta2genetic
20679485
RSC1_SCHPOrsc1genetic
18818364
RAD14_SCHPOrhp14genetic
18818364
RAD7_SCHPOrhp7genetic
18818364
PPK31_SCHPOppk31genetic
18818364
YK82_SCHPObdf2genetic
22095079
BDF1_SCHPObdf1genetic
22095079
H2A1_SCHPOhta1genetic
16778077
H2A2_SCHPOhta2genetic
16778077
RAD4_SCHPOrad4genetic
16778077
CHK1_SCHPOchk1physical
22792081
DDB1_SCHPOddb1genetic
22681890
VAM7_SCHPOSPCC594.06cgenetic
22681890
RAD55_SCHPOrad55genetic
22681890
YPS1_SCHPOyps1genetic
22681890
AYR1_SCHPOayr1genetic
22681890
HRQ1_SCHPOhrq1genetic
22681890
YDE9_SCHPOpet801genetic
22681890
SPO15_SCHPOspo15genetic
22681890
YDA4_SCHPOSPAC1F12.04cgenetic
22681890
EXO1_SCHPOexo1genetic
22681890
DCTD_SCHPOdcd1genetic
22681890
YM04_SCHPOSPAC212.04cgenetic
22681890
YBPC_SCHPOSPBC16H5.12cgenetic
22681890
GLRX3_SCHPOgrx3genetic
22681890
MFH2_SCHPOfml2genetic
22681890
RAD57_SCHPOrad57genetic
22681890
SDU1_SCHPOsdu1genetic
22681890
VPS38_SCHPOvps38genetic
22681890
SSN3_SCHPOsrb10genetic
22681890
YGK4_SCHPOSPBC725.04genetic
22681890
YJM5_SCHPOSPCC1020.05genetic
22681890
YIDH_SCHPOSPAC227.17cgenetic
22681890
PDC3_SCHPOSPAC186.09genetic
22681890
CTK3_SCHPOlsg1genetic
22681890
ERD11_SCHPOerd1genetic
22681890
ASK1_SCHPOask1genetic
22681890
TOM70_SCHPOtom70genetic
22681890
DGK1_SCHPOptp4genetic
22681890
YA4C_SCHPOSPAC31A2.12genetic
22681890
SUM2_SCHPOsum2genetic
22681890
YNV5_SCHPOSPBC3H7.05cgenetic
22681890
STM1_SCHPOstm1genetic
22681890
SLX1_SCHPOslx1genetic
22681890
EMC1_SCHPOemc1genetic
22681890
PRZ1_SCHPOprz1genetic
22681890
PSMD9_SCHPOSPAC2H10.02cgenetic
22681890
RHP23_SCHPOrhp23genetic
22681890
YI43_SCHPOSPBC1348.03genetic
22681890
RS4A_SCHPOrps401genetic
22681890
PCNA_SCHPOpcn1genetic
9928931
DPOD_SCHPOcdc6genetic
12589755
PRI1_SCHPOspp1genetic
12589755
SWD2_SCHPOswd2genetic
12589755
HUS2_SCHPOrqh1genetic
12589755
MUS81_SCHPOmus81genetic
12589755
CHK1_SCHPOchk1genetic
15229228
CHK1_SCHPOchk1physical
23422000
PP2C1_SCHPOptc1physical
23695164
CG23_SCHPOcdc13physical
23695164
RAD4_SCHPOrad4physical
24074952
RAD4_SCHPOrad4physical
24663817
RAD9_SCHPOrad9physical
24663817
MDB1_SCHPOmdb1genetic
24806815
H2A1_SCHPOhta1genetic
24806815
H2A2_SCHPOhta2genetic
24806815
CG23_SCHPOcdc13physical
26771498
PP2C1_SCHPOptc1physical
26771498
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RHP9_SCHPO

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Cooperative control of Crb2 by ATM family and Cdc2 kinases isessential 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).
Cited for: PHOSPHORYLATION AT THR-215, AND MUTAGENESIS OF THR-215.

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