SDS23_SCHPO - dbPTM
SDS23_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SDS23_SCHPO
UniProt AC Q09826
Protein Name Protein sds23/moc1
Gene Name sds23
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 408
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Required for normal DNA replication and for proper mitosis. Induces sexual development and ascus formation..
Protein Sequence MPLSTQSSDSLSSAGRQSFGVNSVSDFLAQFPIPTNLPSNKWQDIPVTFLHDNEIALIDPETSMEEASSILIDRDLSALPIVAAKGSNEIATTFDYADLNSFLLMVVGFDDFNDGRFKKVAEDIRAGKVITAYEVAKLGKNKDDFITIPHTTSLGRLAEILSSGIRRVAVTNEQGELSFMASQRSIIRFLWNNIRAFPDLEPLMSRTIHSLDIGSTDITCISGDQKVAAALRQMNQTGIGSLAVVDAQFRLLGNISLVDVKYVTRSSSVYLLNKSCAHFLSVIKSEQGIRAGKDSAPAFNIYESSTFAFTLAKLVATQCHRLWLVQSPSCPPSPKNNAHLSPGSMGGVKVNQLLGVVSLTDIISVLYAHMKGTLPPAPHSAPSLRHGRRGSTSSHRSHSKASVDTQRR
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
4Phosphorylation----MPLSTQSSDSL
----CCCCCCCCCCC		20.6629996109
5Phosphorylation---MPLSTQSSDSLS
---CCCCCCCCCCCH		39.9029996109
7Phosphorylation-MPLSTQSSDSLSSA
-CCCCCCCCCCCHHH		35.8829996109
8PhosphorylationMPLSTQSSDSLSSAG
CCCCCCCCCCCHHHH		22.7729996109
10PhosphorylationLSTQSSDSLSSAGRQ
CCCCCCCCCHHHHHH		31.9029996109
77PhosphorylationILIDRDLSALPIVAA
HHHCCCHHCCCEEEE		31.8628889911
266PhosphorylationDVKYVTRSSSVYLLN
EEEEEECCCEEEEEC		20.0128889911
327PhosphorylationHRLWLVQSPSCPPSP
CEEEEECCCCCCCCC		15.9929996109
329PhosphorylationLWLVQSPSCPPSPKN
EEEECCCCCCCCCCC		44.4928889911
333PhosphorylationQSPSCPPSPKNNAHL
CCCCCCCCCCCCCCC		33.3828889911
341PhosphorylationPKNNAHLSPGSMGGV
CCCCCCCCCCCCCCC		19.8328889911
344PhosphorylationNAHLSPGSMGGVKVN
CCCCCCCCCCCCHHH		20.0328889911
383PhosphorylationPAPHSAPSLRHGRRG
CCCCCCCCCCCCCCC		37.4428889911
397PhosphorylationGSTSSHRSHSKASVD
CCCCCCCCCCCCCCC		27.0429996109
399PhosphorylationTSSHRSHSKASVDTQ
CCCCCCCCCCCCCCC		31.0329996109
402PhosphorylationHRSHSKASVDTQRR-
CCCCCCCCCCCCCC-		25.0229996109
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
333SPhosphorylationKinaseCDK1P04551
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SDS23_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 SDS23_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KAPR_SCHPOcgs1physical
16819157
PDE1_SCHPOcgs2physical
16819157
CYAA_SCHPOcyr1physical
16819157
PP12_SCHPOsds21genetic
8978689
CUT9_SCHPOcut9genetic
8978689
APC3_SCHPOnuc2genetic
8978689
EKC1_SCHPOekc1physical
19371376
PPE1_SCHPOppe1physical
19371376
2AAA_SCHPOpaa1physical
19371376
PP2A1_SCHPOppa1physical
19371376
MYO52_SCHPOmyo52physical
19371376
GCN1_SCHPOSPAC18G6.05cphysical
19371376
NOP58_SCHPOSPAC23G3.06physical
19371376
UCP7_SCHPOucp7physical
19371376
BRL1_SCHPObrl1physical
19371376
HSP78_SCHPOSPBC4F6.17cphysical
19371376
CEK1_SCHPOcek1physical
19371376
PP2A2_SCHPOppa2physical
19371376
2ABA_SCHPOpab1physical
19371376
SSP1_SCHPOssp1genetic
19371376
UFD2_SCHPOufd2physical
23640764
TPX1_SCHPOtpx1physical
19682301
ALG9_SCHPOalg9physical
19682301
SRP54_SCHPOsrp54physical
19682301
RL38A_SCHPOrpl3801physical
19682301
RS3A2_SCHPOrps102physical
19682301
RS20_SCHPOrps20physical
19682301
RPB3_SCHPOrpb3physical
19682301
P25_SCHPOobr1physical
19682301
SFH1_SCHPOsfh1physical
19682301
UFD2_SCHPOufd2physical
19682301
G3P1_SCHPOtdh1physical
19682301
RL29_SCHPOrpl29physical
19682301
RL32A_SCHPOrpl3202physical
19682301
ENO11_SCHPOeno101physical
19682301
PSA5_SCHPOpup2physical
19682301
SODC_SCHPOsod1physical
19682301
SYEM_SCHPOmse1physical
19682301
GBLP_SCHPOcpc2physical
19682301
PSU1_SCHPOpsu1physical
19682301
ALF_SCHPOfba1physical
19682301
IPI3_SCHPOcrb3physical
19682301
CPSFX_SCHPOppn1physical
19682301
RLA4_SCHPOrpp202physical
19682301
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SDS23_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-77; SER-329; SER-333 ANDSER-341, AND MASS SPECTROMETRY.
"A novel protein, Psp1, essential for cell cycle progression ofSchizosaccharomyces pombe is phosphorylated by Cdc2-Cdc13 upon entryinto G0-like stationary phase of cell growth.";
Jang Y.-J., Won M., Chung K.-S., Kim D.-U., Hoe K.-L., Park C.,Yoo H.-S.;
J. Biol. Chem. 272:19993-20002(1997).
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,PHOSPHORYLATION AT SER-333, AND MUTAGENESIS OF SER-333.

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