RAD5_SCHPO - dbPTM
RAD5_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAD5_SCHPO
UniProt AC P36607
Protein Name DNA repair protein rad8 {ECO:0000305|PubMed:8290359}
Gene Name rad8 {ECO:0000303|PubMed:8290359}
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 1133
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Probable helicase, member of the UBC2/RAD6 epistasis group. Functions with DNA repair protein rad18 in error-free postreplication DNA repair. Involved in the maintenance of wild-type rates of instability of simple repetitive sequences such as poly(GT) repeats (By similarity). Plays a role in surviving topoisomerase-mediated DNA damage. [PubMed: 14871939]
Protein Sequence MKRKVQKIIDEAPLEENSPPRFFDSDVEADSKPNDLTAANSIVDLKTNSQHENANAAGKEYGDSGVSESWVLDFLSVTGEKTISEFLAQKIWKTSNGDLNVAVDMYFDESFNIKNSNPDSESQKDTDASLTQMDQLSNTVSVKDLSINRNTNKKALNAVSPSLNLSSNSSVQDVSIDKEEMMKKQSRNALTPLDFIMKKNELMKYIGCFGVEAYSTASGTRTLQAGERIYLERQKLSIKSQSRNSRKKSKLLSINSSCYSNIVRFCNSDHHEIGKLPTEVASVISTLMEQGFWSFEAICIYSDNIIRFGSNVTLQVYCFINVNHPSLNRSPFTLATNSMQEEEEHLKASFAQNKRDHLLRLFTWIALEPDLEDCNTKESIHIDDILKTSSLPEARDESNSDLTPSSTEDEEDVVSDQLAILYDKVKTSGAELPSAPKPSTFALDLREYQKQALYWMCCKEEGVQSDGSAPKLHPLWSRFRFPKDSEFPEFFKCSSDDDNTHFYVNLYTGETTMLFPNSMPYHRGGILADEMGLGKTIEVLSLIHSRPCFSTDEIPEAFRHSKPSLPVASRTTLVVAPMSLLDQWHSEACKVSQGTKFRSMIYYGSEKPLDLKSCVIDTSTAPLIIITSYGVLLSEFSQQSHSSGLFSVHWFRVVLDEGHNIRNRESKTAKACHSISSQNRWVITGTPIVNKLDDLYSLIKFMRYEPWCNYTYWQTFVSLPYQSKDVLKALNVVQSILEFLVLRRTKETKDRNGNSIVTLPPKTVKIEYLDFSDSERKIYDSLYTKAKSTVNANIVAGTLFRNYTTILGLLLRLRQACCDPVLLSNMTINSETFDDFEFSVEQFNSLINQFVVTGKPIPSDILKIDTLKSFEALITECPICCNEPIQNPLLLNCKHACCGDCLSEHIQYQKRRNIIPPLCHTCRQPFNEQDVYKPFFVKNNGTQSTLLVGEEVKWKYWNRLQSVKLNGLLGQLRQLTHSSEPEKVVIFSQFTTFLDIIADVLESEKMGYARFDGTMSQQMRSTALETFRNDPDVNVLIISLKAGGVGLNLTCANHVFIMDPWWSWSVEAQAIDRIHRLGQEKPVFVTRYIVRDTVEERMLKIQERKNFITGTLGMSEGKQQVQSIEDIKMLFEY
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
18PhosphorylationEAPLEENSPPRFFDS
CCCCCCCCCCCCCCC		39.2928889911
25PhosphorylationSPPRFFDSDVEADSK
CCCCCCCCCCCCCCC		38.1025720772
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 RAD5_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAD5_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 RAD5_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAD13_SCHPOrad13genetic
8290359
RAD9_SCHPOrad9genetic
8290359
SMC6_SCHPOsmc6genetic
8290359
RAD21_SCHPOrad21genetic
8290359
RAD4_SCHPOrad4genetic
8290359
RAD55_SCHPOrad55genetic
19547744
MAG2_SCHPOmag2genetic
19547744
RAD57_SCHPOrad57genetic
18818364
ROK1_SCHPOrok1genetic
18818364
HRQ1_SCHPOhrq1genetic
18818364
PNK1_SCHPOpnk1genetic
18818364
EXO1_SCHPOexo1genetic
18818364
RAD14_SCHPOrhp14genetic
18818364
ARP42_SCHPOarp42genetic
18818364
MUB1_SCHPOSPBC31F10.10cgenetic
18818364
ASF1_SCHPOcia1genetic
18818364
MPH1L_SCHPOmph1genetic
22681890
RYH1_SCHPOryh1genetic
22681890
UBLH2_SCHPOuch2genetic
22681890
RAD55_SCHPOrad55genetic
22681890
PAM17_SCHPOpam17genetic
22681890
HRQ1_SCHPOhrq1genetic
22681890
SRR_SCHPOsry1genetic
22681890
SEL1_SCHPOsle1genetic
22681890
EXO1_SCHPOexo1genetic
22681890
YIT2_SCHPOSPAC105.02cgenetic
22681890
YCD2_SCHPOpxd1genetic
22681890
WIS4_SCHPOwis4genetic
22681890
RAD57_SCHPOrad57genetic
22681890
YHEH_SCHPOSPBPB2B2.17cgenetic
22681890
AROG_SCHPOSPAP8A3.07cgenetic
22681890
LTN1_SCHPOrkr1genetic
22681890
YQK8_SCHPOSPCC1494.08cgenetic
22681890
RHP26_SCHPOrhp26genetic
24875629
FBH1_SCHPOfbh1genetic
24875629
RAD54_SCHPOrad54genetic
24875629
RAD55_SCHPOrad55genetic
24875629
RAD57_SCHPOrad57genetic
24875629
PIF1_SCHPOpfh1genetic
24875629
DNA2_SCHPOdna2genetic
24875629
MPH1_SCHPOfml1genetic
24875629
MFH2_SCHPOfml2genetic
24875629
CHL1_SCHPOchl1genetic
24875629
SRS2_SCHPOsrs2genetic
24875629
MUS81_SCHPOmus81genetic
24875629
HUS2_SCHPOrqh1genetic
24875629
EXO1_SCHPOexo1genetic
24875629
RAD32_SCHPOmre11genetic
24875629
RFA1_SCHPOssb1genetic
24875629
CDS1_SCHPOcds1genetic
24875629
SWI1_SCHPOswi1genetic
24875629
SWI3_SCHPOswi3genetic
24875629
MRC1_SCHPOmrc1genetic
24875629
RLF2_SCHPOpcf1genetic
25313826
MMS2_SCHPOmms2physical
26771498
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RAD5_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-18, AND MASSSPECTROMETRY.

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