EKC1_SCHPO - dbPTM
EKC1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EKC1_SCHPO
UniProt AC O74511
Protein Name Extragenic suppressor of kinetochore protein 1
Gene Name ekc1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 838
Subcellular Localization Nucleus . Associated with chromatin.
Protein Description Has a role in chromosome segregation. May provide a dynamic connection between kinetochore microtubules and kinetochore chromatin..
Protein Sequence MFWRLGQGFGFQSSSAIEAILDKPEDEINLKELLEENGVLDECKSHNPKLLEYLCKPEVLSQLIDYILEVDETEIPSADGGYEEPEHTRLSYIASEILSSDVWSICEACVENKTLMVKLWSFLDSEGPLNPLQASYFAKVNEHFLDKKTEETVAFIQSIDNFVEKILRHAETSAIMDLLLKFISMDRCNTAIGIADWLYSQGLIQSLLRLLSPYVDPDVQFTVADVIKAIIAISANSNEPGVIGPNSLSRELVSRQTITTLTDYMTDSKAPHSATSLINGVSIVIELIRKNNSDYDVTPVLQMPLDTHPPTTRDPIYLGTMLRLFAEKIPVFQKILLKPSTESDLMPTSFGKIKPLGFERFRICELYAELLHCSNMSLLSDPNGEAMVMQRDHLRDYLFRHNSCARDLVMSDEDDDDSTFSDKNSKDFKETEDMNGAEDMHGRAPQITKDNLNLTTTDSPMSEAEPVSEEEYKDVMETAKALHHGDDDAASDTSYEPLPESVIEDAKKLPVIGDFLKIEFIQNNVIPTILDHFFDYPWNNFLHNVVYDVVQQVLNAPMDKDQNYALAVDMFKQGKITEKIVYGQELNDKKVAKPSGFRAGYMGHLTIIADEVVKFVEHYSSTFDQELLNLINDEKWQNFVNKTLVETRNRDNQLLGGLEPSMVGYLEDMDEGEMLDANNLPEMQFALEQELESNSSDDDVVEVHRELSHNSSSNDEDDGNDEDPLSREMSRRLSFESANDSDQDNRDHFAQYMSQQISDNNANQFSSSDEDDDDDDEVVEWVSRGNENKYPRSNFFINGSDREDFSDSEEEDGNDSSDDDRGFAEEEYSDGLVLNHGK
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
411PhosphorylationCARDLVMSDEDDDDS
CHHHHCCCCCCCCCC		30.3028889911
418PhosphorylationSDEDDDDSTFSDKNS
CCCCCCCCCCCCCCC		38.0428889911
419PhosphorylationDEDDDDSTFSDKNSK
CCCCCCCCCCCCCCC		33.8728889911
421PhosphorylationDDDDSTFSDKNSKDF
CCCCCCCCCCCCCCH		48.0028889911
425PhosphorylationSTFSDKNSKDFKETE
CCCCCCCCCCHHHCC		39.0728889911
455PhosphorylationTKDNLNLTTTDSPMS
CCCCCCCCCCCCCCC		26.9529996109
456PhosphorylationKDNLNLTTTDSPMSE
CCCCCCCCCCCCCCC		31.6028889911
457PhosphorylationDNLNLTTTDSPMSEA
CCCCCCCCCCCCCCC		29.2821712547
459PhosphorylationLNLTTTDSPMSEAEP
CCCCCCCCCCCCCCC		22.0228889911
462PhosphorylationTTTDSPMSEAEPVSE
CCCCCCCCCCCCCCH		36.7225720772
468PhosphorylationMSEAEPVSEEEYKDV
CCCCCCCCHHHHHHH		50.4328889911
472PhosphorylationEPVSEEEYKDVMETA
CCCCHHHHHHHHHHH		18.7729996109
478PhosphorylationEYKDVMETAKALHHG
HHHHHHHHHHHHHCC		18.5025720772
491PhosphorylationHGDDDAASDTSYEPL
CCCCCCCCCCCCCCC		43.0428889911
493PhosphorylationDDDAASDTSYEPLPE
CCCCCCCCCCCCCCH		30.6128889911
494PhosphorylationDDAASDTSYEPLPES
CCCCCCCCCCCCCHH		32.2728889911
495PhosphorylationDAASDTSYEPLPESV
CCCCCCCCCCCCHHH		24.5328889911
501PhosphorylationSYEPLPESVIEDAKK
CCCCCCHHHHHHHHH		26.8429996109
708PhosphorylationVEVHRELSHNSSSND
HHHHHHHHCCCCCCC		18.8325720772
711PhosphorylationHRELSHNSSSNDEDD
HHHHHCCCCCCCCCC		29.7128889911
712PhosphorylationRELSHNSSSNDEDDG
HHHHCCCCCCCCCCC		38.1829996109
713PhosphorylationELSHNSSSNDEDDGN
HHHCCCCCCCCCCCC		48.3928889911
726PhosphorylationGNDEDPLSREMSRRL
CCCCCHHHHHHHHHH		31.4225720772
734PhosphorylationREMSRRLSFESANDS
HHHHHHHCCCCCCCC		25.7528889911
737PhosphorylationSRRLSFESANDSDQD
HHHHCCCCCCCCCCC		30.2928889911
741PhosphorylationSFESANDSDQDNRDH
CCCCCCCCCCCCHHH		36.6625720772
800PhosphorylationSNFFINGSDREDFSD
CCCEECCCCCCCCCC		29.0728889911
829PhosphorylationGFAEEEYSDGLVLNH
CCCHHHHCCCCEECC		28.6028889911
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 EKC1_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EKC1_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 EKC1_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PPE1_SCHPOppe1physical
12773390
MIS12_SCHPOmis12physical
12773390
CENPA_SCHPOcnp1physical
12773390
YEX1_SCHPOSPAC1A6.01cgenetic
22681890
ELP3_SCHPOelp3genetic
22681890
BCS1_SCHPOSPAC644.07genetic
22681890
RL27A_SCHPOrpl2701genetic
22681890
YHZ3_SCHPOath1genetic
22681890
SHF1_SCHPOshf1genetic
22681890
ELP3_SCHPOelp3physical
19371376
ELP5_SCHPOelp5physical
19371376
CSE1_SCHPOkap109physical
19371376
ELP1_SCHPOelp1physical
19371376
ELP6_SCHPOelp6physical
19371376
SDS23_SCHPOsds23physical
19371376
ELP4_SCHPOelp4physical
19371376
PPE1_SCHPOppe1physical
19371376
TIP41_SCHPOtip41physical
19371376
ELP2_SCHPOelp2physical
19371376
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EKC1_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-411; SER-418; THR-419;SER-425; SER-459; SER-468; SER-491; THR-493; SER-494; SER-711 ANDSER-713, AND MASS SPECTROMETRY.

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