MDB1_SCHPO - dbPTM
MDB1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MDB1_SCHPO
UniProt AC O14079
Protein Name DNA damage response protein Mdb1 {ECO:0000305}
Gene Name mdb1 {ECO:0000303|PubMed:24806815}
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 624
Subcellular Localization Nucleus . Chromosome . Cytoplasm, cytoskeleton, spindle . Associated with chromatin. Relocalizes to discrete nuclear foci at DNA double strand breaks (DSBs) following DNA damage by the HO endonuclease and ionizing radiation (IR). Focus formation requ
Protein Description Involved in DNA damage response (DDR) mediated through its interaction with phosphorylated H2A proteins hta1 and hta2 which mark the discrete foci of DNA damage..
Protein Sequence MEIQFGNQRCRMVNSGGFLATDGSHLKEMETDDVLVEFLNIEHQLFIRNIRAIVKIADTTVLPSASDKKLLYYVFDETRVRINDTPVIFSKLEEDNANVNEGSKMGVMTVPNTPQKPNLQQQKFEAINANEDQIDYSSNLEQNYNSLIRQGSDQVIPLSRFASEKSALELEKELFSERIPESQSAAEPVLKVENSENDLDEKLVLDGQHVEGDHSSDTEEEVVSEDQKQLNKTDDESTFIESHQIYIQGETKSPSSVSQSLSGDPSLKPAEVFDRKQSAEINSPIEKDVNPQQNISDSSIKNNSIHSDEVNPEVRPDLTPSNENEESKRSAPEIALKEKESTSQDESNREAEEAPISTNYSFPSSSLEDQPDKNVQSSAVENKNKHTNLVTSSFNLTKPMKSFIRRNGLRVQESVTDETDFVILGSPPLRRTHKFLLATSLGIPLVSSQYLTDCIKSGKVLDFRSYKYKDEEAEAKWGFRLDDIHRRTCFNGKRLYITKAIRDSMVGDSIHGLYSILETSGAEIVGDIKRAQEKDTIILAQPDNDQEGRNMSATGLNVYKIELVALSILRDRIDFDEFLIDYDADSPTKVIGKRNVSKASRTGQGRKRSSRSSWNKPSAKEQRT
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
103PhosphorylationNANVNEGSKMGVMTV
CCCCCCCCEEEEEEC		17.1929996109
109PhosphorylationGSKMGVMTVPNTPQK
CCEEEEEECCCCCCC		30.3321712547
113PhosphorylationGVMTVPNTPQKPNLQ
EEEECCCCCCCCCCC		22.4928889911
152PhosphorylationNSLIRQGSDQVIPLS
HHHHHCCCCCEEEHH		19.2828889911
163PhosphorylationIPLSRFASEKSALEL
EEHHHHCCHHHHHHH		42.7325720772
166PhosphorylationSRFASEKSALELEKE
HHHCCHHHHHHHHHH		33.7521712547
182PhosphorylationFSERIPESQSAAEPV
HHCCCCCCCCCCCCE		24.8724763107
184PhosphorylationERIPESQSAAEPVLK
CCCCCCCCCCCCEEE		38.4329996109
195PhosphorylationPVLKVENSENDLDEK
CEEEEECCCCCCCCC		25.0324763107
215PhosphorylationQHVEGDHSSDTEEEV
CCCCCCCCCCCHHHH		34.3524763107
216PhosphorylationHVEGDHSSDTEEEVV
CCCCCCCCCCHHHHC		45.1728889911
218PhosphorylationEGDHSSDTEEEVVSE
CCCCCCCCHHHHCCH		47.4424763107
224PhosphorylationDTEEEVVSEDQKQLN
CCHHHHCCHHHHHHC		40.4021712547
233PhosphorylationDQKQLNKTDDESTFI
HHHHHCCCCCCCHHC		47.8421712547
237PhosphorylationLNKTDDESTFIESHQ
HCCCCCCCHHCEEEE		35.3024763107
238PhosphorylationNKTDDESTFIESHQI
CCCCCCCHHCEEEEE		26.9524763107
242PhosphorylationDESTFIESHQIYIQG
CCCHHCEEEEEEEEC		18.8421712547
253PhosphorylationYIQGETKSPSSVSQS
EEECCCCCCCCCCHH		37.1228889911
255PhosphorylationQGETKSPSSVSQSLS
ECCCCCCCCCCHHHC		50.9228889911
256PhosphorylationGETKSPSSVSQSLSG
CCCCCCCCCCHHHCC		29.2221712547
258PhosphorylationTKSPSSVSQSLSGDP
CCCCCCCCHHHCCCC		18.9221712547
260PhosphorylationSPSSVSQSLSGDPSL
CCCCCCHHHCCCCCC		19.5924763107
278PhosphorylationEVFDRKQSAEINSPI
HHCCCCHHCCCCCCC		30.7928889911
283PhosphorylationKQSAEINSPIEKDVN
CHHCCCCCCCCCCCC		32.6828889911
296PhosphorylationVNPQQNISDSSIKNN
CCCCCCCCHHHHHCC		38.7024763107
298PhosphorylationPQQNISDSSIKNNSI
CCCCCCHHHHHCCCC		27.4621712547
299PhosphorylationQQNISDSSIKNNSIH
CCCCCHHHHHCCCCC		42.4421712547
304PhosphorylationDSSIKNNSIHSDEVN
HHHHHCCCCCCCCCC		30.9528889911
307PhosphorylationIKNNSIHSDEVNPEV
HHCCCCCCCCCCCCC		33.5224763107
319PhosphorylationPEVRPDLTPSNENEE
CCCCCCCCCCCCCHH		31.8621712547
321PhosphorylationVRPDLTPSNENEESK
CCCCCCCCCCCHHHH		52.0921712547
327PhosphorylationPSNENEESKRSAPEI
CCCCCHHHHHCCCCH		27.4721712547
347PhosphorylationESTSQDESNREAEEA
CCCCCCCHHHHHHHC		49.8621712547
378PhosphorylationPDKNVQSSAVENKNK
CCCCCCCHHHCCCCC		21.1729996109
609PhosphorylationTGQGRKRSSRSSWNK
CCCCCCCCCCCCCCC		32.8921712547
610PhosphorylationGQGRKRSSRSSWNKP
CCCCCCCCCCCCCCC		39.9721712547
612PhosphorylationGRKRSSRSSWNKPSA
CCCCCCCCCCCCCCH		41.4724763107
613PhosphorylationRKRSSRSSWNKPSAK
CCCCCCCCCCCCCHH		33.2924763107
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 MDB1_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MDB1_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 MDB1_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
H2A1_SCHPOhta1physical
24806815
SET9_SCHPOset9genetic
24806815
RHP9_SCHPOcrb2genetic
24806815
H2A1_SCHPOhta1genetic
24806815
H2A2_SCHPOhta2genetic
24806815
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MDB1_SCHPO

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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-253 AND SER-283, ANDMASS SPECTROMETRY.

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