PIC1_SCHPO - dbPTM
PIC1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PIC1_SCHPO
UniProt AC Q1MTN3
Protein Name Inner centromere protein-related protein pic1
Gene Name pic1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 1018
Subcellular Localization Nucleus. Cytoplasm, cytoskeleton, spindle. Associates with the elongating spindle during anaphase.
Protein Description Required for chromosome segregation and cytokinesis. Has a role in sister chromatid cohesion and condensation..
Protein Sequence MGSNGSELWFNKELEYSQQLTNGKMKEFFFLVSETMDWLNEHMLEVSKLQLESDIYELVRTPTKIKEKYSTPRLSPVHRCALPTPRMRLTSIQHQLEEAAVEGYKSGESNTVKEPKELHTATNTETQFDDDRDSTKLSSEYVKDDIVNKSTKGGVSPIKETRLPTNLPAFSPTSVERRFTEWNVPLRETSPSPSETADSPNKLPKQKHPAYSFVTLPKREEILKRPASLHSRVESTNSFINQLNRRRTKDNLTNNPEISLDEPIKALPSTTSDAPSSLLNTNVSSSPSKFRKFLSSVIPAKTDLSAKESLTSSTRLSTSYKTRKRSSGVAFSSETVTSSSKERKRSVENEMLKPHPTIFESPPEITSFDKSNAVEAEALTAKLKSNEERLPVSSQPGSDAKSQEFDFFEAKIPDSIAKLNELTASNENHYELKTYDRAERLRQKIQEVSSNKRLIPSTPPTKKPINAVLDAAKNSAAKDLHLAKMKLNNKNDESSLSPAKSHAVITQAPKIPLISTFTRLSTRKSSNDFNSSNSRPSSNALKSDANENTDSSLPPSKKEFIEKSLHKLSEPLHDDSRQNSDHNFAPHSRPIAIRVATASQRELEQTEKRKAKNGAANASNMESRSSENETHRFKKFYGKERELSNNEFPSRQTKTVTSANSSNIRDMEHTISDKPRSEPDAIPSSKSMHSNKPFEEKSEKPTTKRLVTNPSNVNASWHSNMLKRQEDLRKKKPLTDNGATSRHMLKSGLTRVTSKPTQRFANELAEDMSLAFHSTIPKKMEPDSVTSVTQPSVGSLRNNFDIGTTNSQNEDRKKKIAAQKNKNPVHGNVGLTNQHGFKTMHHNVNPFTKQNGIMKGKLPSSSTSQSNKPFIEKASMHAPAKGRNSSMQEPSSKSPLLKTPKSNYFPGYGSLSPNTSVELPEINSDYSDDSDDEGNKKKVNLPSWAESPELREQLKRQQKWDPDKIFGMIKPLQMDEYFRSKDRSKIRFRPRSSSADWSSQDRLTQAEIDNYKKNMGFL
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
53PhosphorylationVSKLQLESDIYELVR
HHCHHHHCCHHHHHC		37.5929996109
56PhosphorylationLQLESDIYELVRTPT
HHHHCCHHHHHCCCC		14.2727738172
61PhosphorylationDIYELVRTPTKIKEK
CHHHHHCCCCCHHHH		28.0324763107
69PhosphorylationPTKIKEKYSTPRLSP
CCCHHHHCCCCCCCC		20.9029996109
70PhosphorylationTKIKEKYSTPRLSPV
CCHHHHCCCCCCCCC		42.9029996109
71PhosphorylationKIKEKYSTPRLSPVH
CHHHHCCCCCCCCCC		14.8825720772
75PhosphorylationKYSTPRLSPVHRCAL
HCCCCCCCCCCCCCC		26.5925720772
134PhosphorylationQFDDDRDSTKLSSEY
CCCCCCCCCCCCHHH		28.4721712547
135PhosphorylationFDDDRDSTKLSSEYV
CCCCCCCCCCCHHHH		40.0529996109
156PhosphorylationKSTKGGVSPIKETRL
CCCCCCCCCCCCCCC		24.9629996109
165PhosphorylationIKETRLPTNLPAFSP
CCCCCCCCCCCCCCC		54.7129996109
171PhosphorylationPTNLPAFSPTSVERR
CCCCCCCCCCCHHHH		29.4028889911
173PhosphorylationNLPAFSPTSVERRFT
CCCCCCCCCHHHHHH		44.1829996109
174PhosphorylationLPAFSPTSVERRFTE
CCCCCCCCHHHHHHC		25.9325720772
189PhosphorylationWNVPLRETSPSPSET
CCCCCCCCCCCCCCC		39.2329996109
190PhosphorylationNVPLRETSPSPSETA
CCCCCCCCCCCCCCC		20.7325720772
192PhosphorylationPLRETSPSPSETADS
CCCCCCCCCCCCCCC		40.6029996109
194PhosphorylationRETSPSPSETADSPN
CCCCCCCCCCCCCCC		52.4927738172
196PhosphorylationTSPSPSETADSPNKL
CCCCCCCCCCCCCCC		39.8525720772
199PhosphorylationSPSETADSPNKLPKQ
CCCCCCCCCCCCCCC		28.1029996109
284PhosphorylationSLLNTNVSSSPSKFR
HHHCCCCCCCHHHHH		27.4529996109
285PhosphorylationLLNTNVSSSPSKFRK
HHCCCCCCCHHHHHH		41.8229996109
286PhosphorylationLNTNVSSSPSKFRKF
HCCCCCCCHHHHHHH		26.2029996109
288PhosphorylationTNVSSSPSKFRKFLS
CCCCCCHHHHHHHHH		46.5029996109
295PhosphorylationSKFRKFLSSVIPAKT
HHHHHHHHHCCCCCC		26.2021712547
296PhosphorylationKFRKFLSSVIPAKTD
HHHHHHHHCCCCCCC		26.6421712547
302PhosphorylationSSVIPAKTDLSAKES
HHCCCCCCCCCHHHH		44.2521712547
305PhosphorylationIPAKTDLSAKESLTS
CCCCCCCCHHHHCCC		39.8521712547
326PhosphorylationSYKTRKRSSGVAFSS
CCCCCCCCCCCCCCC		34.1825720772
327PhosphorylationYKTRKRSSGVAFSSE
CCCCCCCCCCCCCCC		41.1224763107
357PhosphorylationEMLKPHPTIFESPPE
HCCCCCCCCCCCCCC		34.9521712547
361PhosphorylationPHPTIFESPPEITSF
CCCCCCCCCCCCCCC		34.7024763107
366PhosphorylationFESPPEITSFDKSNA
CCCCCCCCCCCCCCC		22.9821712547
367PhosphorylationESPPEITSFDKSNAV
CCCCCCCCCCCCCCH		36.7921712547
475PhosphorylationVLDAAKNSAAKDLHL
HHHHHHCHHHHHHHH		28.9721712547
497PhosphorylationKNDESSLSPAKSHAV
CCCCCCCCHHHHCCE		25.4329996109
525PhosphorylationTRLSTRKSSNDFNSS
CHHHCCCCCCCCCCC		30.9624763107
526PhosphorylationRLSTRKSSNDFNSSN
HHHCCCCCCCCCCCC		43.3725720772
569PhosphorylationEKSLHKLSEPLHDDS
HHHHHHHCCCCCCCC		41.8129996109
626PhosphorylationSNMESRSSENETHRF
CCCCCCCCCCHHHHH		43.2421712547
644PhosphorylationYGKERELSNNEFPSR
HCCHHCCCCCCCCCC		32.6221712547
885PhosphorylationAPAKGRNSSMQEPSS
CCCCCCCCCCCCCCC		26.3121712547
894PhosphorylationMQEPSSKSPLLKTPK
CCCCCCCCCCCCCCC		23.8029996109
943PhosphorylationKKKVNLPSWAESPEL
CCCCCCCHHHCCHHH		41.9324763107
947PhosphorylationNLPSWAESPELREQL
CCCHHHCCHHHHHHH		18.8724763107
994PhosphorylationRFRPRSSSADWSSQD
CCCCCCCCCCCCHHH		31.3425720772
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 PIC1_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PIC1_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 PIC1_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARK1_SCHPOark1physical
17301288
BIR1_SCHPObir1physical
17301288
ARK1_SCHPOark1genetic
11950927
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PIC1_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-171, AND MASSSPECTROMETRY.

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