IMP2_SCHPO - dbPTM
IMP2_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IMP2_SCHPO
UniProt AC Q10199
Protein Name Septation protein imp2
Gene Name imp2
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 670
Subcellular Localization Cytoplasm, cytoskeleton . Associates with the medial ring during septation.
Protein Description Required for normal septation. Involved in the disassembly of the medial ring during septation..
Protein Sequence MSQQLSFNASSAKPDKSFSNYFWGANDEGYHALLSRFSDVKHINEELRSFYHERANIEEDYAKRMAKLSRTTFSSLETGCLKESVQVMKAEVDNMAKSHLQISQLLQDDVENAFTRYAASLKDKKKMIVSGIEKVHKDKLSKHQALVKAQDKYHYLCKKVNYYVSQQNMLFGKELEKNNAKLNKTQNAITASSSDYQSAVAAVRDSYARWTNEWRSTCDKLQDIEEERRHFLKSVMWTFTLLISRSCFNDDQACERIRKNLEQCSVSQDVLEFIDAKSTGTGIPQPPKFYDYYKGEVPDDSVELVQANFQRAQTKIENDNMPLNRPYVLSATARNESSFENTLPNTPSAIQSLTTVSSNSSQNGRSSPKKSFLSKFKLTSRPSTPNVGNTAPDALSSPRNDSPLTSAADEQMKHLSLQEEPKQNPTPAAPGAFPNSNTLPPRYNELGSLPSPNSVSFTEDSRPNVNTPSRRQQIQEEFGSVLQMENRAVSPVYDSRKNGSRSSFTLRKSRSPKRPSSSLSQNASRLPRSLTPGNLEPNYDFGVRVDPASGTAPTDDEPYTDRDSSFVDDTINTKATGNTSNRLSLPAYPTDGGDTSIDNPTSTDGQRILGYVSALYDYDAAIPEEISFRKGDTIAVLKLYEDGWWEGFVVGEDDHNRGQFPSNFVREIEV
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------MSQQLSFNA
------CCCCCCCCC
27.0029996109
352PhosphorylationNTPSAIQSLTTVSSN
CCHHHHHHHEEECCC
22.9027738172
354PhosphorylationPSAIQSLTTVSSNSS
HHHHHHHEEECCCCC
30.3325720772
355PhosphorylationSAIQSLTTVSSNSSQ
HHHHHHEEECCCCCC
24.5525720772
361PhosphorylationTTVSSNSSQNGRSSP
EEECCCCCCCCCCCC
31.7325720772
366PhosphorylationNSSQNGRSSPKKSFL
CCCCCCCCCCCHHHH
53.0125720772
367PhosphorylationSSQNGRSSPKKSFLS
CCCCCCCCCCHHHHH
39.1025720772
379PhosphorylationFLSKFKLTSRPSTPN
HHHHCCCCCCCCCCC
24.2328889911
380PhosphorylationLSKFKLTSRPSTPNV
HHHCCCCCCCCCCCC
53.2628889911
383PhosphorylationFKLTSRPSTPNVGNT
CCCCCCCCCCCCCCC
56.2224763107
384PhosphorylationKLTSRPSTPNVGNTA
CCCCCCCCCCCCCCC
22.8928889911
390PhosphorylationSTPNVGNTAPDALSS
CCCCCCCCCCCHHCC
33.3725720772
396PhosphorylationNTAPDALSSPRNDSP
CCCCCHHCCCCCCCC
39.7625720772
397PhosphorylationTAPDALSSPRNDSPL
CCCCHHCCCCCCCCC
28.8228889911
402PhosphorylationLSSPRNDSPLTSAAD
HCCCCCCCCCCHHHH
25.9228889911
405PhosphorylationPRNDSPLTSAADEQM
CCCCCCCCHHHHHHH
21.5021712547
416PhosphorylationDEQMKHLSLQEEPKQ
HHHHHHCCCCCCCCC
27.9424763107
448PhosphorylationPRYNELGSLPSPNSV
CCCCCCCCCCCCCCC
50.1329996109
451PhosphorylationNELGSLPSPNSVSFT
CCCCCCCCCCCCCCC
41.8429996109
454PhosphorylationGSLPSPNSVSFTEDS
CCCCCCCCCCCCCCC
23.6329996109
456PhosphorylationLPSPNSVSFTEDSRP
CCCCCCCCCCCCCCC
26.6925720772
458PhosphorylationSPNSVSFTEDSRPNV
CCCCCCCCCCCCCCC
31.2325720772
461PhosphorylationSVSFTEDSRPNVNTP
CCCCCCCCCCCCCCH
43.3229996109
467PhosphorylationDSRPNVNTPSRRQQI
CCCCCCCCHHHHHHH
20.5429996109
469PhosphorylationRPNVNTPSRRQQIQE
CCCCCCHHHHHHHHH
37.7529996109
490PhosphorylationQMENRAVSPVYDSRK
HHHCCCCCCCCCCCC
13.9928889911
500PhosphorylationYDSRKNGSRSSFTLR
CCCCCCCCCCCEEEE
38.0824763107
502PhosphorylationSRKNGSRSSFTLRKS
CCCCCCCCCEEEECC
31.3421712547
503PhosphorylationRKNGSRSSFTLRKSR
CCCCCCCCEEEECCC
22.5728889911
505PhosphorylationNGSRSSFTLRKSRSP
CCCCCCEEEECCCCC
27.8324763107
509PhosphorylationSSFTLRKSRSPKRPS
CCEEEECCCCCCCCC
31.4025720772
511PhosphorylationFTLRKSRSPKRPSSS
EEEECCCCCCCCCCH
41.6925720772
516PhosphorylationSRSPKRPSSSLSQNA
CCCCCCCCCHHCCCH
36.2725720772
517PhosphorylationRSPKRPSSSLSQNAS
CCCCCCCCHHCCCHH
37.6728889911
518PhosphorylationSPKRPSSSLSQNASR
CCCCCCCHHCCCHHC
36.0629996109
520PhosphorylationKRPSSSLSQNASRLP
CCCCCHHCCCHHCCC
24.2829996109
524PhosphorylationSSLSQNASRLPRSLT
CHHCCCHHCCCCCCC
41.7325720772
529PhosphorylationNASRLPRSLTPGNLE
CHHCCCCCCCCCCCC
34.3629996109
531PhosphorylationSRLPRSLTPGNLEPN
HCCCCCCCCCCCCCC
30.3228889911
554PhosphorylationPASGTAPTDDEPYTD
CCCCCCCCCCCCCCC
54.3329996109
559PhosphorylationAPTDDEPYTDRDSSF
CCCCCCCCCCCCCCC
21.1625720772
560PhosphorylationPTDDEPYTDRDSSFV
CCCCCCCCCCCCCCC
34.9625720772
564PhosphorylationEPYTDRDSSFVDDTI
CCCCCCCCCCCCCCC
26.9429996109
565PhosphorylationPYTDRDSSFVDDTIN
CCCCCCCCCCCCCCC
33.3129996109
576PhosphorylationDTINTKATGNTSNRL
CCCCCCCCCCCCCCE
32.3029996109
579PhosphorylationNTKATGNTSNRLSLP
CCCCCCCCCCCEECC
28.8225720772
580PhosphorylationTKATGNTSNRLSLPA
CCCCCCCCCCEECCC
24.7727738172
584PhosphorylationGNTSNRLSLPAYPTD
CCCCCCEECCCCCCC
29.1225720772
588PhosphorylationNRLSLPAYPTDGGDT
CCEECCCCCCCCCCC
12.5329996109
595PhosphorylationYPTDGGDTSIDNPTS
CCCCCCCCCCCCCCC
30.7529996109
596PhosphorylationPTDGGDTSIDNPTST
CCCCCCCCCCCCCCC
32.4629996109

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 IMP2_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IMP2_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 IMP2_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CHS2_SCHPOchs2genetic
16772338
TPM_SCHPOcdc8genetic
9786952
CDC11_SCHPOcdc11genetic
9786952
CDC15_SCHPOcdc15genetic
9786952
MLR4_SCHPOcdc4genetic
9786952
INN1_SCHPOfic1physical
19139265
AIN1_SCHPOain1genetic
19139265
MYO2_SCHPOmyo2genetic
19139265
MYO3_SCHPOmyp2genetic
19139265
PP2B_SCHPOppb1genetic
19139265
RNG2_SCHPOrng2genetic
19139265
SID2_SCHPOsid2genetic
19139265
SID4_SCHPOsid4genetic
19139265
PROF_SCHPOcdc3genetic
19139265
MLR4_SCHPOcdc4genetic
19139265
FLP1_SCHPOclp1genetic
19139265
MLR1_SCHPOrlc1genetic
19139265
RGA7_SCHPOrga7genetic
25052092
RGA7_SCHPOrga7physical
25052092
IMP2_SCHPOimp2physical
26771498
PP2B_SCHPOppb1genetic
25580011

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IMP2_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-397; SER-503 ANDTHR-531, AND MASS SPECTROMETRY.

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