SWI1_SCHPO - dbPTM
SWI1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SWI1_SCHPO
UniProt AC Q9UUM2
Protein Name Mating-type switching protein swi1
Gene Name swi1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 971
Subcellular Localization Nucleus . Associated with chromatin during S phase. Nuclear accumulation requires swi3.
Protein Description Forms a fork protection complex (FPC) with swi3. FPC coordinates leading and lagging strand synthesis and moves with the replication fork. It is required for programmed fork-pausing which is necessary for mating-type switching. FPC stabilizes replication forks in a configuration that is recognized by replication checkpoint sensors. It is involved in termination at the mat1-proximal polar-terminator of replication (RTS1) and also required for activation of the Rad53-like checkpoint kinase cds1..
Protein Sequence MELDEVIQGIVSAIGGFDYSDDEKVYVLGDEALACLKDLKRYLQVVDEKYKVWQIRSLLSSLQLVTNDICPILSDWDKDITNYRNWRIALACVELLVPLTWPLETEHETFRENVDVLYNLRQAQSNYKNSILSYKKGSVLSAILAVLLKPLSTPAESRTLRDKGIIRIVLLLFRNILQIDELKTKNETIISFAKAHILDLIVTLVSNLDEFEHFDVYILEIVYNLIRGCKPSALFSDASLTNSQTELNSLLLKESTQNRYLKRNAHTRHNRFGTMLSVQTEDRRFTIASQNIKTDGLDELDSHKRFRKRGTRRKHFDDINKSFFINTEAGTALRNFAVEFLEAGFNPLFQSLLKDLEREDPRVLPIHKMQLLYVQSFFLEFMRFSSKPKKTEEIYSNDYSFGLAASVFDQRALIMHNRLMVESFEMKQWSTFQASMLSMTQLLFTLRSMTLCSSEIYQRIADNLLSNIFYQEEILLLVYSALKHFKTQSFGYLDAITELTIVLLKELEKFSSAKQYLYVKKRRRNQKSVDSNVLESDEDEESSLINANAAVEDRLFDFGRYESRYCDNGCIDSFVLFLQCYQDLDSKQIHRAISFFYRIFVKQKCHVYLYRLDFLRVLDKMFNDHVYFSTTNSARQDFEQFFVYYMRKLSDALKDVPALFIELPFPKLTDTFYYLEYGKSPLFSIHGSRKGPLYETVPGLSHLEKVAAVVACLINENKSDLLDELKVQLNCLISERKLITLADENKYINEGGNDGERMGKNLKGDTDSFNTALLKDGKFRLLLELCGFEESDNNIDVQALWKLPNSVIIDELVEHAMLLRRFTDDPPTFEGTKPEDLLVRKQRGNVRLPSSSEGETSDEEIEFEADDPITFANRREALNKITDRKRKKMKTNETIIDHTTRKKKENHLRSAKYIVDSDDDSETDIAFFQSEAALREKNAQKASALFKRIDDLEMEGKLQEIEQLSENSSSD
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
528PhosphorylationKRRRNQKSVDSNVLE
HHCCCCCCCCCCCCC		22.7628889911
531PhosphorylationRNQKSVDSNVLESDE
CCCCCCCCCCCCCCC		27.0429996109
536PhosphorylationVDSNVLESDEDEESS
CCCCCCCCCCCHHHH		41.9828889911
542PhosphorylationESDEDEESSLINANA
CCCCCHHHHCCCCCH		28.5325720772
913PhosphorylationNHLRSAKYIVDSDDD
HCCCCCEEEECCCCC		13.0921712547
917PhosphorylationSAKYIVDSDDDSETD
CCEEEECCCCCCHHH		31.8521712547
921PhosphorylationIVDSDDDSETDIAFF
EECCCCCCHHHHHHH		49.7621712547
923PhosphorylationDSDDDSETDIAFFQS
CCCCCCHHHHHHHHH		36.3425720772
965PhosphorylationLQEIEQLSENSSSD-
HHHHHHHHHCCCCC-		34.1324763107
968PhosphorylationIEQLSENSSSD----
HHHHHHCCCCC----		27.4524763107
969PhosphorylationEQLSENSSSD-----
HHHHHCCCCC-----		50.5421712547
970PhosphorylationQLSENSSSD------
HHHHCCCCC------		47.3528889911
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 SWI1_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SWI1_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 SWI1_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDS1_SCHPOcds1genetic
15767681
CHK1_SCHPOchk1genetic
15767681
CDS1_SCHPOcds1genetic
15367656
MUS81_SCHPOmus81genetic
15367656
DPOD_SCHPOcdc6genetic
15367656
HSK1_SCHPOhsk1genetic
16263721
SWI3_SCHPOswi3physical
15509785
SWI3_SCHPOswi3physical
15367656
HSK1_SCHPOhsk1physical
16263721
HIM1_SCHPOdfp1physical
16263721
CTF18_SCHPOctf18genetic
18045993
RAD21_SCHPOrad21genetic
18045993
RHP9_SCHPOcrb2genetic
14560029
CHK1_SCHPOchk1genetic
14560029
PLI1_SCHPOpli1genetic
17209013
HUS2_SCHPOrqh1genetic
18045993
SAP1_SCHPOsap1genetic
17151242
MCM2_SCHPOmcm2genetic
20176980
PSF2_SCHPOpsf2genetic
20176980
HUS2_SCHPOrqh1genetic
20176980
RAD21_SCHPOrad21genetic
20176980
SWI6_SCHPOswi6genetic
20176980
HSK1_SCHPOhsk1genetic
20176980
RAD18_SCHPOrhp18genetic
20176980
RAD26_SCHPOrad26genetic
20967229
SWI3_SCHPOswi3physical
20924116
BDF1_SCHPObdf1genetic
22095079
YK82_SCHPObdf2genetic
22095079
ESA1_SCHPOmst1genetic
22095079
EAF_SCHPOvid21genetic
22095079
SWI3_SCHPOswi3physical
22952839
TEL2_SCHPOtel2genetic
17189249
SWI3_SCHPOswi3physical
26771498
POF3_SCHPOpof3genetic
23349636
RIF1_SCHPOrif1genetic
27473316
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SWI1_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-528; SER-536 ANDSER-970, AND MASS SPECTROMETRY.

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