RAD22_SCHPO - dbPTM
RAD22_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAD22_SCHPO
UniProt AC P36592
Protein Name DNA repair and recombination protein rad22
Gene Name rad22
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 469
Subcellular Localization Nucleus .
Protein Description Active in the repair of DNA damage and in mating-type switching. Probably involved in the repair of DNA double-strands breaks. Has a role in promoting S phase completion..
Protein Sequence MSFEQKQHVASEDQGHFNTAYSHEEFNFLQSSLTRKLGPEYVSRRSGPGGFSVSYIESWKAIELANEIFGFNGWSSSIRSINVDFMDENKENGRISLGLSVIVRVTIKDGAYHEDIGYGSIDNCRGKASAFEKCKKEGTTDALKRALRNFGNSLGNCMYDKYYLREVGKMKPPTYHFDSGDLFRKTDPAARESFIKKQKTLNSTRTVNNQPLVNKGEQLAPRRAAELNDEQTREIEMYADEELDNIFVEDDIIAHLAVAEDTAHPAANNHHSEKAGTQINNKDKGSHNSAKPVQRSHTYPVAVPQNTSDSVGNAVTDTSPKTLFDPLKPNTGTPSPKFISARAAAAAEGVVSAPFTNNFNPRLDSPSIRKTSIIDHSKSLPVQRASVLPIIKQSSQTSPVSNNSMIRDSESIINERKENIGLIGVKRSLHDSTTSHNKSDLMRTNSDPQSAMRSRENYDATVDKKAKKG
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
296PhosphorylationSAKPVQRSHTYPVAV
CCCCCCCCCCCCEEC		11.7728889911
318PhosphorylationVGNAVTDTSPKTLFD
CCCCCCCCCCCCCCC		37.2524763107
319PhosphorylationGNAVTDTSPKTLFDP
CCCCCCCCCCCCCCC		27.4928889911
331PhosphorylationFDPLKPNTGTPSPKF
CCCCCCCCCCCCHHH		51.4621712547
333PhosphorylationPLKPNTGTPSPKFIS
CCCCCCCCCCHHHHH		20.6825720772
335PhosphorylationKPNTGTPSPKFISAR
CCCCCCCCHHHHHHH		40.3328889911
365PhosphorylationNFNPRLDSPSIRKTS
CCCCCCCCCCCCCCC		25.7429996109
394PhosphorylationVLPIIKQSSQTSPVS
HHHHHCCCCCCCCCC		21.2925720772
395PhosphorylationLPIIKQSSQTSPVSN
HHHHCCCCCCCCCCC		34.6829996109
397PhosphorylationIIKQSSQTSPVSNNS
HHCCCCCCCCCCCCH		36.6321712547
398PhosphorylationIKQSSQTSPVSNNSM
HCCCCCCCCCCCCHH		18.7025720772
446PhosphorylationSDLMRTNSDPQSAMR
HHHHHCCCCHHHHHH		50.4828889911
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

Oops, there are no upstream regulatory protein records of RAD22_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAD22_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 RAD22_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HUS2_SCHPOrqh1genetic
11452021
RTI1_SCHPOrti1genetic
10512870
RFA1_SCHPOssb1genetic
10512870
SWI10_SCHPOswi10genetic
11057444
FBH1_SCHPOfbh1genetic
16135800
RAD22_SCHPOrad52physical
11884628
RAD55_SCHPOrad55physical
11560889
RTI1_SCHPOrti1physical
11560889
RAD22_SCHPOrad52physical
11560889
RAD22_SCHPOrad52physical
12050150
ESA1_SCHPOmst1physical
18505873
SLX1_SCHPOslx1genetic
16467377
SLX4_SCHPOslx4genetic
16467377
H2A2_SCHPOhta2genetic
15226425
H2A1_SCHPOhta1genetic
15226425
HUS2_SCHPOrqh1genetic
20705238
FBH1_SCHPOfbh1genetic
21149262
RTI1_SCHPOrti1genetic
21149262
RAD22_SCHPOrad52physical
23695164
RAD55_SCHPOrad55physical
23695164
RAD3_SCHPOrad3physical
23779158
MSH6_SCHPOmsh6physical
23779158
DNA2_SCHPOdna2physical
23779158
MSH2_SCHPOmsh2physical
23779158
HSP71_SCHPOssa1physical
23779158
HSP72_SCHPOssa2physical
23779158
RFA1_SCHPOssb1physical
23779158
ABP2_SCHPOabp2physical
23779158
RUVB2_SCHPOrvb2physical
23779158
RUVB1_SCHPOrvb1physical
23779158
RTI1_SCHPOrti1physical
23779158
RFA2_SCHPOssb2physical
23779158
SAP1_SCHPOsap1physical
23779158
BAG1A_SCHPObag101physical
23779158
RIM1_SCHPOrim1physical
23779158
MUS81_SCHPOmus81genetic
24748152
RAD22_SCHPOrad52physical
26771498
RAD55_SCHPOrad55physical
26771498
EXO1_SCHPOexo1genetic
28475874
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RAD22_SCHPO

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296 AND SER-319, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory