PLO1_SCHPO - dbPTM
PLO1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PLO1_SCHPO
UniProt AC P50528
Protein Name Serine/threonine-protein kinase plo1
Gene Name plo1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 683
Subcellular Localization Chromosome, centromere, kinetochore . Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body .
Protein Description Required to form a bipolar spindle, the actin ring and septum. Functions upstream of the whole septum formation pathway, including actin ring formation (regulated by late septation genes) and septal material deposition (regulated by early septation genes). Behaves as a "septum-promoting factor", and could also be involved in inducing other late events of cell division. [PubMed: 12615979]
Protein Sequence MASVAIKEPKTAITPKKKSKASRLCFTPPTNLHNNKKNIFYTRYDCIGEGGFARCFRVKDNYGNIYAAKVIAKRSLQNDKTKLKLFGEIKVHQSMSHPNIVGFIDCFEDSTNIYLILELCEHKSLMELLRKRKQLTEPEVRYLMMQILGALKYMHKKRVIHRDLKLGNIMLDESNNVKIGDFGLAALLMDDEERKMTICGTPNYIAPEILFNSKEGHSFEVDLWSAGVVMYALLIGKPPFQDKEVKTIYRKIKANSYSFPSNVDISAEAKDLISSLLTHDPSIRPSIDDIVDHEFFHTGYMASTLPDEILHSMPIWPSSQSKSSFQRNLDFVASASGVGFGNSAGVEKNKPYALRTDEVDNDRILPSVLSPRDRVNPVMKIGPETKPVPSKLSTALHAARKSTDGSLGSRVKVLREESQSFVPTKSAVTEQVEPIQLIRSLSANTVSRLSKVGNMKSDIWISVKKTALKIGMALEAHTHALTSEDADSEPVLFITKWVDYSNKYGLGYQLSDESVGVHFNDDTSLLFSADEEVVEYALHPKDTEIKPYIYPASKVPESIRSKLQLLKHFKSYMGQNLSKAVQDESFEKPKNSTSNTMLFMQHYLRTRQAIMFRLSNGIFQFNFLDHRKVVISSTARKIIVLDKERERVELPLQEASAFSEDLRSRLKYIRETLESWASKMEVS
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
3Phosphorylation-----MASVAIKEPK
-----CCCCCCCCCC
15.6929996109
14PhosphorylationKEPKTAITPKKKSKA
CCCCCCCCCCCCCCC
26.9628889911
22PhosphorylationPKKKSKASRLCFTPP
CCCCCCCHHHCCCCC
29.5321712547
27PhosphorylationKASRLCFTPPTNLHN
CCHHHCCCCCCCCCC
27.6229996109
197PhosphorylationDDEERKMTICGTPNY
CHHHHCEEECCCCCC
19.0229996109
370PhosphorylationRILPSVLSPRDRVNP
CCCHHCCCHHHCCCC
18.7429996109
402PhosphorylationALHAARKSTDGSLGS
HHHHHHHCCCCCCHH
26.6124763107
403PhosphorylationLHAARKSTDGSLGSR
HHHHHHCCCCCCHHH
47.6327738172
406PhosphorylationARKSTDGSLGSRVKV
HHHCCCCCCHHHEEH
32.1624763107
409PhosphorylationSTDGSLGSRVKVLRE
CCCCCCHHHEEHHHH
38.9121712547
418PhosphorylationVKVLREESQSFVPTK
EEHHHHHHHCCCCCC
26.7724763107
420PhosphorylationVLREESQSFVPTKSA
HHHHHHHCCCCCCCC
37.1721712547
424PhosphorylationESQSFVPTKSAVTEQ
HHHCCCCCCCCCCCC
32.1221712547
429PhosphorylationVPTKSAVTEQVEPIQ
CCCCCCCCCCCCHHH
22.0321712547
440PhosphorylationEPIQLIRSLSANTVS
CHHHHHHHCCHHHHH
21.4921712547
442PhosphorylationIQLIRSLSANTVSRL
HHHHHHCCHHHHHHH
22.2528889911
445PhosphorylationIRSLSANTVSRLSKV
HHHCCHHHHHHHHHC
21.4121712547
447PhosphorylationSLSANTVSRLSKVGN
HCCHHHHHHHHHCCC
26.0129996109
585PhosphorylationSKAVQDESFEKPKNS
HHHHHCCCCCCCCCC
47.1728889911

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 PLO1_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PLO1_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 PLO1_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
POM1_SCHPOpom1genetic
9852154
APC8_SCHPOcut23genetic
11777938
APC8_SCHPOcut23physical
12615979
SUM2_SCHPOsum2physical
12615979
SCK1_SCHPOsck1physical
12615979
ABP2_SCHPOabp2physical
12615979
YLP3_SCHPOred1physical
12615979
MU185_SCHPOmug185physical
12615979
YEG5_SCHPOmga2physical
12615979
CUT12_SCHPOcut12physical
12815070
SID4_SCHPOsid4physical
15062098
MBX1_SCHPOmbx1physical
18057023
SCK1_SCHPOsck1physical
18057023
MID1_SCHPOmid1genetic
10930468
MBX1_SCHPOmbx1genetic
21098641
FLP1_SCHPOclp1genetic
21098641
BYR4_SCHPObyr4physical
21131906
MID1_SCHPOmid1physical
21376600
CDR2_SCHPOcdr2genetic
22298427
MID1_SCHPOmid1genetic
22298427
PP11_SCHPOdis2genetic
22375062
DAM1_SCHPOdam1physical
22375062
MBX1_SCHPOmbx1physical
22451489
PCP1_SCHPOpcp1physical
22438582
CUT12_SCHPOcut12physical
22438582
PTPA2_SCHPOypa2genetic
22267499
PP2A2_SCHPOppa2genetic
22267499
CDC16_SCHPOcdc16genetic
11250892
YKZ2_SCHPOSPAC15E1.02cgenetic
22681890
YD22_SCHPOSPAC56F8.02genetic
22681890
DAD2_SCHPOdad2genetic
22681890
NPY1_SCHPOSPBC1778.03cgenetic
22681890
YKEE_SCHPOSPAC1805.14genetic
22681890
YDEA_SCHPOnod1genetic
23349808
GEF2_SCHPOgef2genetic
23349808
MID1_SCHPOmid1physical
9852154
ALP7_SCHPOalp7physical
23770679
CDR2_SCHPOcdr2genetic
24424027

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PLO1_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-442 AND SER-585, ANDMASS SPECTROMETRY.

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