FKH2_SCHPO - dbPTM
FKH2_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FKH2_SCHPO
UniProt AC O60129
Protein Name Fork head protein homolog 2
Gene Name fkh2
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 642
Subcellular Localization Nucleus .
Protein Description Required for promoter sequence element PCB-driven, M-phase-specific transcription. Acts as a transcriptional activator with a role in the regulation of mitosis. Binds, cooperatively with mcm1, the CLB cluster regulatory elements throughout the cell cycle. Regulates the periodic transcription of cdc15 and spo12. Required for the correct timing, positioning and contraction of the division septum..
Protein Sequence MTVRRLESKSEHISDDEERKEQLDYKKQMDVDTDRNIVLNGRLESQIAKLSVPPHEMRVVDDYSNSKNAERHSGEIQAYAKFAGSTWTYYVKKIRIILGREPANPSPKGKNEDLEVIDMNFGPSKVVSRKHAVVEYDLDDQTWNCSVYGRNGIKVDGKLFKNGETVKLTSGSILEVAGLQMMFVLPNAAEQKQTDESTIKEDAIKSEISAAVNDAAEYGDNKKPPYSYSVMIAQAILSSSECMMTLSNIYSWISTHYPYYRTTKSGWQNSIRHNLSLNKAFRKVPRKSGEQGKGMKWSIVPEFREEFIAKTRKTPRKRSPSSPVPLLAKKREGSPSLPIPILPKMKDTSIPAAEPASSTTSARDQTPSTPKDVGSPSTAETSAEEKQMETYKTPTHAALSDIISTHDYALDANSASQTKKAAFGSPIGSSTYPTSSPAPFWKYVAVPNPHDWPQVGSYDTISPYRNPVNSHLIYSQIQQSSPKKIDEQLHDLQGVDLVNGFEGISSWRESMVNKLRSSVSDSPTMNLANSNSKSSPVAVQRVSTLPQASANKQAKEMESKMSNSPTQKSKTEENNQAVRAILDASATMEKQYDLHRLPTPTSQTESASVPQIANPPNSQNLVKEKSPQQYIQVPQSNVKSSA
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
10PhosphorylationVRRLESKSEHISDDE
CCCCCCCCCCCCCHH		43.6221712547
14PhosphorylationESKSEHISDDEERKE
CCCCCCCCCHHHHHH		40.7021712547
73PhosphorylationSKNAERHSGEIQAYA
CCCCCHHCCCHHHHH		44.3225720772
106PhosphorylationGREPANPSPKGKNED
CCCCCCCCCCCCCCC		38.7721712547
206PhosphorylationIKEDAIKSEISAAVN
HHHHHHHHHHHHHHH		33.7721712547
218PhosphorylationAVNDAAEYGDNKKPP
HHHHHHHHCCCCCCC		25.6721712547
314PhosphorylationFIAKTRKTPRKRSPS
HHHHCCCCCCCCCCC		25.6521712547
319PhosphorylationRKTPRKRSPSSPVPL
CCCCCCCCCCCCCCC		31.9728889911
321PhosphorylationTPRKRSPSSPVPLLA
CCCCCCCCCCCCCCC		48.8228889911
322PhosphorylationPRKRSPSSPVPLLAK
CCCCCCCCCCCCCCC		33.0428889911
334PhosphorylationLAKKREGSPSLPIPI
CCCCCCCCCCCCCCC		13.4328889911
336PhosphorylationKKREGSPSLPIPILP
CCCCCCCCCCCCCCC		48.7728889911
357PhosphorylationIPAAEPASSTTSARD
CCCCCCCCCCCCCCC		38.6421712547
358PhosphorylationPAAEPASSTTSARDQ
CCCCCCCCCCCCCCC		37.5021712547
359PhosphorylationAAEPASSTTSARDQT
CCCCCCCCCCCCCCC		23.4421712547
366PhosphorylationTTSARDQTPSTPKDV
CCCCCCCCCCCCCCC		24.4021712547
368PhosphorylationSARDQTPSTPKDVGS
CCCCCCCCCCCCCCC		61.8129996109
369PhosphorylationARDQTPSTPKDVGSP
CCCCCCCCCCCCCCC		35.2421712547
375PhosphorylationSTPKDVGSPSTAETS
CCCCCCCCCCCCCCC		18.6128889911
377PhosphorylationPKDVGSPSTAETSAE
CCCCCCCCCCCCCHH		41.7825720772
390PhosphorylationAEEKQMETYKTPTHA
HHHHHHHHHCCCCHH		25.6021712547
391PhosphorylationEEKQMETYKTPTHAA
HHHHHHHHCCCCHHH		10.2724763107
393PhosphorylationKQMETYKTPTHAALS
HHHHHHCCCCHHHHH		24.0121712547
395PhosphorylationMETYKTPTHAALSDI
HHHHCCCCHHHHHHH		29.4029996109
400PhosphorylationTPTHAALSDIISTHD
CCCHHHHHHHHHHCC		23.2621712547
405PhosphorylationALSDIISTHDYALDA
HHHHHHHHCCCCCCC		14.3621712547
416PhosphorylationALDANSASQTKKAAF
CCCCCCCCCCHHHHC		37.9021712547
418PhosphorylationDANSASQTKKAAFGS
CCCCCCCCHHHHCCC		31.8324763107
425PhosphorylationTKKAAFGSPIGSSTY
CHHHHCCCCCCCCCC		13.5924763107
430PhosphorylationFGSPIGSSTYPTSSP
CCCCCCCCCCCCCCC		27.0921712547
431PhosphorylationGSPIGSSTYPTSSPA
CCCCCCCCCCCCCCC		34.9129996109
432PhosphorylationSPIGSSTYPTSSPAP
CCCCCCCCCCCCCCC		13.3727738172
434PhosphorylationIGSSTYPTSSPAPFW
CCCCCCCCCCCCCCC		31.2724763107
435PhosphorylationGSSTYPTSSPAPFWK
CCCCCCCCCCCCCCE		29.8024763107
436PhosphorylationSSTYPTSSPAPFWKY
CCCCCCCCCCCCCEE		27.7921712547
460PhosphorylationPQVGSYDTISPYRNP
CCCCCCCCCCCCCCC		18.3427738172
480PhosphorylationIYSQIQQSSPKKIDE
HHHHHHHCCCHHHHH		32.0329996109
481PhosphorylationYSQIQQSSPKKIDEQ
HHHHHHCCCHHHHHH		36.0825720772
520PhosphorylationNKLRSSVSDSPTMNL
HHHHHHCCCCCCCCC		34.0324763107
522PhosphorylationLRSSVSDSPTMNLAN
HHHHCCCCCCCCCCC		18.1129996109
524PhosphorylationSSVSDSPTMNLANSN
HHCCCCCCCCCCCCC		23.7325720772
530PhosphorylationPTMNLANSNSKSSPV
CCCCCCCCCCCCCCC		36.5529996109
532PhosphorylationMNLANSNSKSSPVAV
CCCCCCCCCCCCCHH		33.4627738172
534PhosphorylationLANSNSKSSPVAVQR
CCCCCCCCCCCHHHH		39.4324763107
535PhosphorylationANSNSKSSPVAVQRV
CCCCCCCCCCHHHHH		27.4228889911
562PhosphorylationKEMESKMSNSPTQKS
HHHHHHHCCCCCHHC		37.5828889911
564PhosphorylationMESKMSNSPTQKSKT
HHHHHCCCCCHHCCH		23.2427738172
566PhosphorylationSKMSNSPTQKSKTEE
HHHCCCCCHHCCHHH		48.7428889911
599PhosphorylationYDLHRLPTPTSQTES
CCCCCCCCCCCCCCC		43.7328889911
606PhosphorylationTPTSQTESASVPQIA
CCCCCCCCCCCCCCC		29.2727738172
626PhosphorylationQNLVKEKSPQQYIQV
CCCCCCCCHHHEEEC		29.0928889911
630PhosphorylationKEKSPQQYIQVPQSN
CCCCHHHEEECCHHH		6.5121712547
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 FKH2_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FKH2_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 FKH2_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MBX1_SCHPOmbx1genetic
15509866
FHL1_SCHPOfhl1genetic
18059475
MEI4_SCHPOmei4genetic
18059475
SEP1_SCHPOsep1genetic
15509866
CLR6_SCHPOclr6physical
25002536
SDS3_SCHPOsds3physical
25002536
YJNJ_SCHPOnts1physical
25002536
MBX1_SCHPOmbx1genetic
26237280
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FKH2_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-319; SER-321; SER-322;SER-334; SER-336; SER-375; SER-535 AND SER-626, AND MASS SPECTROMETRY.

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