FFT2_SCHPO - dbPTM
FFT2_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FFT2_SCHPO
UniProt AC O74842
Protein Name ATP-dependent helicase fft2
Gene Name fft2
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 1284
Subcellular Localization Cytoplasm . Nucleus .
Protein Description DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is required for heterochromatin organization..
Protein Sequence MLPYNSNYLSDNGKRKFSDENPQSEVYGSSQTGLPSSYGNPQSYGTPPVQQSSAMYGVNNSMGGGMYNTSENTQFMNTDYSQTSSYASTPMSNAYSRDAPAAINNNFGYSYVGQSSQPVPSYNPLPSYNTASLPNAGIPAAMPGMPSGYPGTVPIPQGGYNAHYSSPYNNGYPIGAVNPTSAIPAQPPAQPVNNVLPSYVRSNSRSSARSTARSAPRSTQRSRSSSANPVTTPPVNNTLLTPPAPPVELPPVTTTSPNAIIRSVQWIRSFVPQAPIHQVINTLAQTKWDETAALSILSQKYLSCDLGIPIQEHKRFKQSPVASNMPTYGSSNRTVQSQKRSIRDKYIQMPNDSTQASLMPSYTRKTSNASKKLTTEEDEFYDSEEEPEAIVHRDTSALERTVLNFINSSTAKELSDTASCPLSHSKLLLEHRPFQTLAEACIIKHPDDVPSKPGRRGRRREKNPMGQKIVNACMETMEGYYAIDNLIAKCEFLGNRISKGMASWGIKLEMSNGELNIVDMESVPTEAADNSDFPKFVTEQPKTLASDVQLKSYQLVGVNWLHLLYQQKLSGILADEMGLGKTCQVVAFFALLLEQGHHGPHLVVVPSSTLENWLRELARFCPSLRVEPYYGSQQERANIREAIEENEIKYDILVTTYQLATNNKEDRSFLKHQNFDVCVYDEGHYLKNRMSERYKHLMNLNANFRLLLTGTPLQNNLKELVSLLAFILPNMFDSDMDDLDVIFKAKPTADADIEQALLSKQRISRAKTMMTPFVLRRRKNQVLNDLPKKTQIIEHCKLSENQLEIYNRYAALQKNQQLRRDDKRNKRSKNDEESDGKSLSAGHVLMQLRKAANHALLFRKFYDDEKLKQMAKDIMQEEQYKNANEQYIYEDMEVMSDFELHRLCRSFPTLQSYTLKDDPWMDSGKIRVLKELLPKMKEEGSRILLFSQFTQMLDILEQVLDTLKISYVRLDGSTQVEVRQDIIDQFHKEEDVTVFLLSTKAGGFGINLACANVVILYDCSYNPFDDLQAEDRAHRVGQVREVTVIRLITDNTIEEYIQKLANTKLALDMSLSSDGKDREEIGERLVQDMLDEENNGNNTKPEITGNESDGEFKVSSSNNSKQTDAEETNTGVPLEGSQPNSVEKTDLADGDEKANIKTEMKSETVEGDNKELRETMKGENVQTDSNAAVPSSKSSTEEPNESVLSGHLDLDTEASPVVSTIEKTTKGDVSVTEEQQSANIDGQLEKPEIEESKKPDVLNQVSLSIEEEKPKNKESEVDNNAAKD
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
238PhosphorylationTTPPVNNTLLTPPAP
CCCCCCCCCCCCCCC		20.2427738172
253PhosphorylationPVELPPVTTTSPNAI
CCCCCCCCCCCCCHH		30.0827738172
256PhosphorylationLPPVTTTSPNAIIRS
CCCCCCCCCCHHHHH		17.6727738172
319PhosphorylationEHKRFKQSPVASNMP
HCHHHCCCCCHHCCC		23.1824763107
323PhosphorylationFKQSPVASNMPTYGS
HCCCCCHHCCCCCCC		33.6228889911
381PhosphorylationTTEEDEFYDSEEEPE
CCCCCCCCCCCCCCC		19.2625720772
383PhosphorylationEEDEFYDSEEEPEAI
CCCCCCCCCCCCCCE		35.2128889911
1104PhosphorylationNNTKPEITGNESDGE
CCCCCCCCCCCCCCC		32.0924763107
1108PhosphorylationPEITGNESDGEFKVS
CCCCCCCCCCCEEEC		55.7229996109
1137PhosphorylationTGVPLEGSQPNSVEK
CCCCCCCCCCCCCCC		32.8427738172
1191PhosphorylationDSNAAVPSSKSSTEE
CCCCCCCCCCCCCCC		43.7429996109
1192PhosphorylationSNAAVPSSKSSTEEP
CCCCCCCCCCCCCCC		30.4129996109
1202PhosphorylationSTEEPNESVLSGHLD
CCCCCCCCHHCCCCC		34.6929996109
1205PhosphorylationEPNESVLSGHLDLDT
CCCCCHHCCCCCCCC		23.2429996109
1212PhosphorylationSGHLDLDTEASPVVS
CCCCCCCCCCCCCEE		40.5229996109
1215PhosphorylationLDLDTEASPVVSTIE
CCCCCCCCCCEEEEE		16.4029996109
1230PhosphorylationKTTKGDVSVTEEQQS
ECCCCCCCCCHHHHH		28.2324763107
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 FFT2_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FFT2_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 FFT2_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PEF1_SCHPOpef1genetic
18818364
PDX1_SCHPOsnz1genetic
22681890
CCQ1_SCHPOccq1genetic
22681890
DAD1_SCHPOdad1genetic
22681890
AATC_SCHPOSPAC10F6.13cgenetic
22681890
PAB2_SCHPOpab2genetic
22681890
SCS7_SCHPOscs7genetic
22681890
COQ10_SCHPOcoq10genetic
22681890
RM39_SCHPOmrpl39genetic
22681890
FFT3_SCHPOfft3genetic
22681890
DAD2_SCHPOdad2genetic
22681890
MU123_SCHPOmug123genetic
22681890
SDE2_SCHPOsde2genetic
22681890
GEF1_SCHPOgef1genetic
22681890
RL21B_SCHPOrpl2102genetic
22681890
YGK5_SCHPOSPBC725.05cgenetic
22681890
MAD1_SCHPOmad1genetic
22681890
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FFT2_SCHPO

loading...

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-323 AND SER-383, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory