SRW1_SCHPO - dbPTM
SRW1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SRW1_SCHPO
UniProt AC O13286
Protein Name WD repeat-containing protein srw1
Gene Name srw1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 556
Subcellular Localization Nucleus .
Protein Description Has a role in cell differentiation and cell cycling by negatively regulating cig2 and cdc12-associated cdc2. Down-regulates the level of cdc13, particularly in a nitrogen deprived environment. Regulator of cell cycle G1 phase progression. Prevents onset of mitosis during the pre-Start G1 period. Required for degradation of cdc13 mitotic cyclin B during G1 arrest but not during mitotic exit..
Protein Sequence MDEFDGFTRPTSSNSSANRNSNNSMNRVENNNSNSDSANTVDSRGDAHTRMRQGFEKSFPSSPNKKRPRTNEGDRFIPSRDASTELWTGFTKVEGPLTPVKKKQSVADRNFTTLLRSELFGSNDETFNNSPIATPNTTIGVSTPRTDSGIDDIELTQRTPPSSSHTSSSILQNTPVTPSRKIFHYLSPRDRNKSSYGKKAQYQDNPNRTIYSLSPVRSITKDLISASRLEGRELPSIPYRVLDAPGLAGDFYLNLLDWGQCNMLAVALASRVYLWSGISSEVTVMHNFYPTDTVTSLRWVQRGTHLAVGTHNGSVEIWDAATCKKTRTMSGHTERVGALSWNDHVLSSGGRDNHILHRDVRAPEHYFRVLTAHRQEVCGLEWNSNENLLASGGNDNALMVWDKFEEKPLYSFHNHIAAVKAITWSPHQRGILASGGGTADRTIKLWNTQRGSMLHNIDTGSQVCNLLWSKQTNEFISTHGFMENEVALWNYPSVSRVGTLKGHTDRVLYLAMSPNGENIVTGAADETLRFWKLFDSKSKHSASTMSSPFDPTMKIR
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
62PhosphorylationFEKSFPSSPNKKRPR
HHHHCCCCCCCCCCC
32.5010921878
98PhosphorylationTKVEGPLTPVKKKQS
CEEECCCCCCCCCCC
29.2110921878
177PhosphorylationILQNTPVTPSRKIFH
HHCCCCCCCCHHHEE
19.4210921878
185PhosphorylationPSRKIFHYLSPRDRN
CCHHHEEECCCCCCC
9.7225720772
187PhosphorylationRKIFHYLSPRDRNKS
HHHEEECCCCCCCCC
15.6628889911
212PhosphorylationNPNRTIYSLSPVRSI
CCCCEEEECCCCHHH
20.6525720772
214PhosphorylationNRTIYSLSPVRSITK
CCEEEECCCCHHHHH
18.5310921878
218PhosphorylationYSLSPVRSITKDLIS
EECCCCHHHHHHHHH
34.5424763107
220PhosphorylationLSPVRSITKDLISAS
CCCCHHHHHHHHHHH
21.5425720772

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 SRW1_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SRW1_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 SRW1_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WEE1_SCHPOwee1genetic
9571240
RUM1_SCHPOrum1genetic
9571240
CDK1_SCHPOcdc2genetic
14985109
CG23_SCHPOcdc13genetic
14985109
WEE1_SCHPOwee1genetic
9398669
CDK1_SCHPOcdc2genetic
9398669
CG23_SCHPOcdc13genetic
9398669
AMS2_SCHPOams2physical
23195958
CG22_SCHPOcig2genetic
9571240
CDC10_SCHPOcdc10genetic
9571240
CG22_SCHPOcig2genetic
9398669
SECU_SCHPOcut2physical
21389117
CG23_SCHPOcdc13physical
21389117
MES1_SCHPOmes1physical
21389117
SRW1_SCHPOsrw1physical
26771498
CG23_SCHPOcdc13physical
26771498

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SRW1_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-187, AND MASSSPECTROMETRY.
"Fission yeast Fizzy-related protein srw1p is a G(1)-specific promoterof mitotic cyclin B degradation.";
Yamaguchi S., Okayama H., Nurse P.;
EMBO J. 19:3968-3977(2000).
Cited for: FUNCTION, PHOSPHORYLATION AT SER-62; THR-98; THR-177 AND SER-214, ANDMUTAGENESIS OF SER-62; THR-98; THR-177 AND SER-214.

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