PCK2_SCHPO - dbPTM
PCK2_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PCK2_SCHPO
UniProt AC P36583
Protein Name Protein kinase C-like 2
Gene Name pck2
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 1016
Subcellular Localization
Protein Description Involved in the control of the cell shape. Target of the inhibitor staurosporine..
Protein Sequence MDMIDEAITEVVRKIERERSVIHGALSMKRLTQNQTVHQQLHSNIEESKKSIIYLEERLEKLKLRKNGVRKSNSEKPSVGIEKNPSFSTTKSAKSFSSTSSNIDSNLDLLNYDTPLTISKISFLLQQLEFKLSVEEQYRKGIEKMAKLYEREHDRRSIAEAEKKYVESAQKITLLKQALKRYHDLHIEIDEEDVPSTESRGNLNARRPQSGLLKITVGSLRNVTHSAGISKQTEMIVAIRAEDLERARTRPSRTDRFNETFEIDLEKTNEVEIVVYEKKNEKLLLPVGLLWIRLSDLVEKQRRKKVEQEVSDKGWVSADKMINQRLSIFLPSALNNISKPESTDRPNTASGNQSVSAWFSLEPMGQINLTMNFTKHNTRKRPMDAGLGRQGAIRQRKESVHEVYGHKFLQHQFYQIMRCALCGEFLKNAAGMQCIDCHYTCHKKCYPKVVTKCISKSSDSASSEYEKINHRIPHHFESHTNIGANWCCHCGYILPLGRKTARKCTECGITAHAQCVHLVPDFCGMSMEMANRVISEIRTTKIYKAQQHKQKSSHHKHHHHKKSKSSSSKHKENDKASVSITTTTTPSITPADPVPTSPKPLAIEPVKRKPVHAGNLEVTSVSDNKLGATVQVVEQKVDDKADALTKPPSLDAVKEPIPVPSVETSVVAQDLTHKAKRIGLEDFTFLSVLGKGNFGKVMLAELKSEKQLYAIKVLKKEFILENDEVESTKSEKRVFLVANRERHPFLVNLHSCFQTETRIYFVMDFVSGGDLMLHIQQEQFSRRRAQFYAAEVCLALKYFHDNGIIYRDLKLDNILLSPDGHVKVADYGLCKEDMWHDNTTATFCGTPEFMAPEILLEQQYTRSVDWWAFGVLIYQMLLGQSPFRGEDEEEIFDAILSDEPLYPIHMPRDSVSILQQLLTRDPKKRLGSGPNDAEDVMTHPFFSNINWDDIYHKRTQPPYIPSLNSPTDTKYFDEEFTRELPVLTPVNSILTKEMQQHFEGFSYSCEDDKPSTTDNA
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
20PhosphorylationRKIERERSVIHGALS
HHHHHHHHHHHHHHH		22.2224763107
27PhosphorylationSVIHGALSMKRLTQN
HHHHHHHHHHHHCCC		23.0224763107
72PhosphorylationRKNGVRKSNSEKPSV
HHCCCCCCCCCCCCC		34.7221712547
74PhosphorylationNGVRKSNSEKPSVGI
CCCCCCCCCCCCCCC		54.8327738172
86PhosphorylationVGIEKNPSFSTTKSA
CCCCCCCCCCCCCCC		41.0224763107
88PhosphorylationIEKNPSFSTTKSAKS
CCCCCCCCCCCCCCC		39.2325720772
92PhosphorylationPSFSTTKSAKSFSST
CCCCCCCCCCCCCCC		38.5525720772
95PhosphorylationSTTKSAKSFSSTSSN
CCCCCCCCCCCCCCC		30.0325720772
97PhosphorylationTKSAKSFSSTSSNID
CCCCCCCCCCCCCCC		39.5427738172
101PhosphorylationKSFSSTSSNIDSNLD
CCCCCCCCCCCCCCC		37.5821712547
105PhosphorylationSTSSNIDSNLDLLNY
CCCCCCCCCCCCCCC		35.1821712547
112PhosphorylationSNLDLLNYDTPLTIS
CCCCCCCCCCCCHHH		22.5921712547
114PhosphorylationLDLLNYDTPLTISKI
CCCCCCCCCCHHHHH		15.1621712547
399PhosphorylationAIRQRKESVHEVYGH
HHHHHHHCHHHHHCH		31.6328889911
596PhosphorylationTPADPVPTSPKPLAI
CCCCCCCCCCCCCEE		58.8729996109
597PhosphorylationPADPVPTSPKPLAIE
CCCCCCCCCCCCEEE		25.5129996109
645PhosphorylationDDKADALTKPPSLDA
CCCHHHCCCCCCCCC		43.1321712547
649PhosphorylationDALTKPPSLDAVKEP
HHCCCCCCCCCCCCC		47.6228889911
661PhosphorylationKEPIPVPSVETSVVA
CCCCCCCCCCCCHHH		32.5929996109
846PhosphorylationTTATFCGTPEFMAPE
CCCEECCCCCHHCHH		22.3329996109
910PhosphorylationPIHMPRDSVSILQQL
CCCCCCCHHHHHHHH		21.0225720772
912PhosphorylationHMPRDSVSILQQLLT
CCCCCHHHHHHHHHH		22.8725720772
962PhosphorylationTQPPYIPSLNSPTDT
CCCCCCCCCCCCCCC		30.5328889911
965PhosphorylationPYIPSLNSPTDTKYF
CCCCCCCCCCCCCCC		34.1728889911
969PhosphorylationSLNSPTDTKYFDEEF
CCCCCCCCCCCCHHH		30.0728889911
984PhosphorylationTRELPVLTPVNSILT
HHHCCCCCCHHHHCH		25.9828889911
988PhosphorylationPVLTPVNSILTKEMQ
CCCCCHHHHCHHHHH		21.1424763107
991PhosphorylationTPVNSILTKEMQQHF
CCHHHHCHHHHHHHH		24.2421712547
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 PCK2_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PCK2_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 PCK2_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RHO2_SCHPOrho2genetic
11102532
PCK1_SCHPOpck1genetic
15923187
SPM1_SCHPOpmk1genetic
17005909
SKH1_SCHPOpek1genetic
17005909
MKH1_SCHPOmkh1genetic
17005909
GBLP_SCHPOcpc2physical
11263963
RHO1_SCHPOrho1physical
10651902
RHO1_SCHPOrho1physical
10504305
RHO2_SCHPOrho2physical
10504305
CDC42_SCHPOcdc42physical
10504305
PMP1_SCHPOpmp1genetic
17881729
PP2C1_SCHPOptc1genetic
17881729
PP2C3_SCHPOptc3genetic
17881729
KSG1_SCHPOksg1genetic
14625898
BGS1_SCHPObgs1genetic
10504305
GLU2A_SCHPOgls2genetic
10504305
SPM1_SCHPOpmk1genetic
9199286
WIS1_SCHPOwis1genetic
9199286
HOG1_SCHPOsty1genetic
9199286
MKH1_SCHPOmkh1genetic
9199286
EHS1_SCHPOyam8genetic
11016847
AP1_SCHPOpap1genetic
1899230
SPK1_SCHPOspk1genetic
1899230
RHO2_SCHPOrho2genetic
24498240
RHO1_SCHPOrho1genetic
24498240
RHO4_SCHPOrho4physical
25651781
RHO5_SCHPOrho5physical
25651781
RHO1_SCHPOrho1physical
25651781
PMP1_SCHPOpmp1genetic
27451356
SKB5_SCHPOskb5genetic
27451356
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PCK2_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 THR-984, AND MASSSPECTROMETRY.

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