MOD5P_SCHPO - dbPTM
MOD5P_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MOD5P_SCHPO
UniProt AC O59740
Protein Name Cell polarity protein mod5
Gene Name mod5
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 522
Subcellular Localization Cell membrane
Peripheral membrane protein
Cytoplasmic side . localizes to the cell tips.
Protein Description With tea1, acts in a positive-feedback loop in the microtubule-mediated regulation of cell polarity. Involved in the anchoring of tea1 at the cortex as well as the correct localization of tea3..
Protein Sequence MSALSESPAIPSFWRPETSEISKKPRPNTTVGFQFDNRNVGTSAPSTPAIRRNNTDSFERGLSLPLPSSKQDTGSSVLDPDGDAYVNRYARPVTAGSIYIPSNYHKSFSPNTFSGFNVKRSASKSPKRSANGSTSEDISIEGSPSETAKGARSSFNSNFRTFDIGSERRRRILEASQDSSRPGRYSYRTKSASPALIDTSTLDSRLNFTMGRLERSIAQLSKNTMRAVSHLENPPKDITLPKLNVKNSAWPLQPYSPPANETPASSSSSAKARPVSVPDMSSPVPASSVEYESLKAAVTYSPSQNPKKVAETDSESRKSSFQSSYNDADRPFQVGAQTQSTPNRISRSDSPIVYDVDTHSEDNASTASSEAISQSMRSFQPQPNTGSPFPRFTSTNTEDEQESDIPQSDANDSTVNLNQPNYANLTPTPQVSPKRPTYSRSSPLPSASVPALGDGSPDPPAAPSIQNSLSVHESEMPPHVTRDYTQPAASATPVPKEKPSEKSEKPPKKKGSKLEKFCCILM
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
2Phosphorylation------MSALSESPA
------CCCCCCCCC		37.6129996109
5Phosphorylation---MSALSESPAIPS
---CCCCCCCCCCCC		35.4329996109
7Phosphorylation-MSALSESPAIPSFW
-CCCCCCCCCCCCCC		19.0929996109
29PhosphorylationSKKPRPNTTVGFQFD
CCCCCCCCEEEEEEC		26.0725720772
30PhosphorylationKKPRPNTTVGFQFDN
CCCCCCCEEEEEECC		25.8529996109
42PhosphorylationFDNRNVGTSAPSTPA
ECCCCCCCCCCCCHH		19.8929996109
43PhosphorylationDNRNVGTSAPSTPAI
CCCCCCCCCCCCHHH		32.0528889911
46PhosphorylationNVGTSAPSTPAIRRN
CCCCCCCCCHHHHCC		46.9029996109
47PhosphorylationVGTSAPSTPAIRRNN
CCCCCCCCHHHHCCC		18.7129996109
55PhosphorylationPAIRRNNTDSFERGL
HHHHCCCCCCCCCCC		36.2529996109
57PhosphorylationIRRNNTDSFERGLSL
HHCCCCCCCCCCCCC		27.2825720772
63PhosphorylationDSFERGLSLPLPSSK
CCCCCCCCCCCCCCC		30.6629996109
73PhosphorylationLPSSKQDTGSSVLDP
CCCCCCCCCCCCCCC		36.1521712547
76PhosphorylationSKQDTGSSVLDPDGD
CCCCCCCCCCCCCCC		28.2225720772
89PhosphorylationGDAYVNRYARPVTAG
CCCEECCCCCEECCC		11.1925720772
94PhosphorylationNRYARPVTAGSIYIP
CCCCCEECCCEEECC		28.1625720772
97PhosphorylationARPVTAGSIYIPSNY
CCEECCCEEECCCCC		15.1125720772
99PhosphorylationPVTAGSIYIPSNYHK
EECCCEEECCCCCCC		14.4229996109
107PhosphorylationIPSNYHKSFSPNTFS
CCCCCCCCCCCCCCC		20.0421712547
109PhosphorylationSNYHKSFSPNTFSGF
CCCCCCCCCCCCCCC		25.0824763107
112PhosphorylationHKSFSPNTFSGFNVK
CCCCCCCCCCCCEEC		23.6721712547
114PhosphorylationSFSPNTFSGFNVKRS
CCCCCCCCCCEECCC		40.2025720772
139PhosphorylationGSTSEDISIEGSPSE
CCCCCCCEECCCHHH		27.2321712547
143PhosphorylationEDISIEGSPSETAKG
CCCEECCCHHHCCCC		16.6821712547
153PhosphorylationETAKGARSSFNSNFR
HCCCCCHHHCCCCCC		38.4529996109
154PhosphorylationTAKGARSSFNSNFRT
CCCCCHHHCCCCCCE		23.9325720772
157PhosphorylationGARSSFNSNFRTFDI
CCHHHCCCCCCEEEC		35.0225720772
189PhosphorylationPGRYSYRTKSASPAL
CCCCCCCCCCCCCCE		22.5529996109
191PhosphorylationRYSYRTKSASPALID
CCCCCCCCCCCCEEC		33.1129996109
193PhosphorylationSYRTKSASPALIDTS
CCCCCCCCCCEECCC		20.1429996109
224PhosphorylationIAQLSKNTMRAVSHL
HHHHCHHHHHHHHCC		16.2721712547
229PhosphorylationKNTMRAVSHLENPPK
HHHHHHHHCCCCCCC		22.7521712547
265PhosphorylationPANETPASSSSSAKA
CCCCCCCCCCCCCCC		31.7724763107
266PhosphorylationANETPASSSSSAKAR
CCCCCCCCCCCCCCC		36.0224763107
267PhosphorylationNETPASSSSSAKARP
CCCCCCCCCCCCCCC		26.3024763107
268PhosphorylationETPASSSSSAKARPV
CCCCCCCCCCCCCCC		35.9421712547
276PhosphorylationSAKARPVSVPDMSSP
CCCCCCCCCCCCCCC		30.5225720772
281PhosphorylationPVSVPDMSSPVPASS
CCCCCCCCCCCCHHH		38.5821712547
282PhosphorylationVSVPDMSSPVPASSV
CCCCCCCCCCCHHHH		24.2324763107
287PhosphorylationMSSPVPASSVEYESL
CCCCCCHHHHCHHHH		28.9321712547
288PhosphorylationSSPVPASSVEYESLK
CCCCCHHHHCHHHHH		22.5225720772
291PhosphorylationVPASSVEYESLKAAV
CCHHHHCHHHHHHHE		14.5221712547
293PhosphorylationASSVEYESLKAAVTY
HHHHCHHHHHHHEEE		33.9821712547
299PhosphorylationESLKAAVTYSPSQNP
HHHHHHEEECCCCCC		17.3524763107
300PhosphorylationSLKAAVTYSPSQNPK
HHHHHEEECCCCCCC		16.4021712547
301PhosphorylationLKAAVTYSPSQNPKK
HHHHEEECCCCCCCC		14.5428889911
303PhosphorylationAAVTYSPSQNPKKVA
HHEEECCCCCCCCEE		36.3328889911
350PhosphorylationNRISRSDSPIVYDVD
CCCCCCCCCCEEECC		20.1312789340
378PhosphorylationAISQSMRSFQPQPNT
HHHHHHHHCCCCCCC		21.4225720772
385PhosphorylationSFQPQPNTGSPFPRF
HCCCCCCCCCCCCCC		45.8029996109
387PhosphorylationQPQPNTGSPFPRFTS
CCCCCCCCCCCCCCC		22.7129996109
470PhosphorylationPSIQNSLSVHESEMP
CCHHHCCCCCHHCCC		22.6527738172
481PhosphorylationSEMPPHVTRDYTQPA
HCCCCCCCCCCCCCC		18.1327738172
490PhosphorylationDYTQPAASATPVPKE
CCCCCCCCCCCCCCC		34.4825720772
492PhosphorylationTQPAASATPVPKEKP
CCCCCCCCCCCCCCC		23.4829996109
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 MOD5P_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MOD5P_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 MOD5P_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TEA1_SCHPOtea1physical
16222337
TEA3_SCHPOtea3physical
16222337
TBG_SCHPOgtb1physical
20850323
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MOD5P_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-43; SER-303 AND SER-350,AND MASS SPECTROMETRY.

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