SFP1_YEAST - dbPTM
SFP1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SFP1_YEAST
UniProt AC P32432
Protein Name Transcription factor SFP1
Gene Name SFP1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 683
Subcellular Localization Cytoplasm. Nucleus. Nuclear under optimal growth conditions. Leaves the nucleus in response to stress or changes in nutrient availability. The [ISP+] aggregates appear to be nuclear.
Protein Description Transcription factor that regulates ribosomal protein (RP) and ribosome biogenesis (Ribi) gene expression in response to nutrients and stress. Promotes RP gene expression under optimal growth conditions. Leaves the nucleus upon environmental challenges, resulting in a down-regulation of RP gene transcription. The effect of the environmental cues on SFP1 localization is mediated through the TOR pathway. Also regulates the expression of genes involved in the G2/M transition during the mitotic cell cycle and the DNA-damage response. Required for carbon-source modulation of cell size..
Protein Sequence MDFTTMTMASNMATSTTTTATSAHASINSSSNFNIDIDSNQNTPSILINNNSDSSNGKNTDFNGVNNIHQKNIMNNTNNVHLYSPNIMDQTLLTPQDIAKLRRESIAHSQGMGGVSWGSISVGSWLRDEIISRRNSIVPASANGAASAAASATTTATNTLQIQQPTKRPSVSNPPYHRGYSISPQIAYTAYLPNLEKQYCKDYSCCGLSLPGLHDLLRHYEEAHISTSPNTTNMSQIPMNSAGNTSSSVRMTNNTSSANYNLQNNMAANTKNAGHKTNTMQAHSSNATNNTSINNMHANLQSNMDSNSTIRQSQHPHHQQNIIQQQLQSNSVNHTSGAVPTPSVMGSATASSTTANPNVISITGAPNSGLSMANHSQQLHLNGNLVDAVSTNDVFLRTSNSPSRHVPHNKQINSNNNSGININNNTSHNSNINMGSKNAMVNRPHTFNNYSLNKTSRNPIQHQSRKIDPHQTDLSPLVLVQDIDLSFMDDDILGPSNHNSMNSVVNPTTGSHNYNTFHSSVHAKSSQNMVEDQDIDDIDDDDDVDDDDDDDDDDDTENGSSSNGKSVHNNNYKMPQQAYIDDPARRLYVMDHEEQKPFKCPVIGCEKTYKNQNGLKYHRLHGHQNQKLHENPDGTFSVIDPDSTDSFGDGMGSAKDKPYRCEVCGKRYKNLNGLKYHRGHSTH
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
39PhosphorylationNFNIDIDSNQNTPSI
CEEEECCCCCCCCEE		40.4228889911
84PhosphorylationTNNVHLYSPNIMDQT
CCCEEECCCCCCCCC		20.1728889911
170PhosphorylationQQPTKRPSVSNPPYH
CCCCCCCCCCCCCCC		42.0625704821
172PhosphorylationPTKRPSVSNPPYHRG
CCCCCCCCCCCCCCC		48.2124961812
176PhosphorylationPSVSNPPYHRGYSIS
CCCCCCCCCCCCCCC		12.8524961812
180PhosphorylationNPPYHRGYSISPQIA
CCCCCCCCCCCHHHH		11.6422369663
181PhosphorylationPPYHRGYSISPQIAY
CCCCCCCCCCHHHHH		21.2922369663
183PhosphorylationYHRGYSISPQIAYTA
CCCCCCCCHHHHHEE		12.5722369663
188PhosphorylationSISPQIAYTAYLPNL
CCCHHHHHEEECCCH		8.1122369663
189PhosphorylationISPQIAYTAYLPNLE
CCHHHHHEEECCCHH		10.3722369663
191PhosphorylationPQIAYTAYLPNLEKQ
HHHHHEEECCCHHHH		18.1922369663
197UbiquitinationAYLPNLEKQYCKDYS
EECCCHHHHHCCCCC		50.1317644757
201UbiquitinationNLEKQYCKDYSCCGL
CHHHHHCCCCCCCCC		55.5617644757
209PhosphorylationDYSCCGLSLPGLHDL
CCCCCCCCCCCHHHH		20.1529650682
220PhosphorylationLHDLLRHYEEAHIST
HHHHHHHHHHHHCCC		14.7221082442
226PhosphorylationHYEEAHISTSPNTTN
HHHHHHCCCCCCCCC		16.9921440633
227PhosphorylationYEEAHISTSPNTTNM
HHHHHCCCCCCCCCC		47.8328889911
228PhosphorylationEEAHISTSPNTTNMS
HHHHCCCCCCCCCCC		14.9017330950
231PhosphorylationHISTSPNTTNMSQIP
HCCCCCCCCCCCCCC		23.9621440633
232PhosphorylationISTSPNTTNMSQIPM
CCCCCCCCCCCCCCC		35.2528889911
235PhosphorylationSPNTTNMSQIPMNSA
CCCCCCCCCCCCCCC		27.3328889911
401PhosphorylationVFLRTSNSPSRHVPH
EEEECCCCCCCCCCC		24.8227214570
414PhosphorylationPHNKQINSNNNSGIN
CCCCCCCCCCCCCCC		42.4322369663
418PhosphorylationQINSNNNSGININNN
CCCCCCCCCCCCCCC		43.0821440633
426PhosphorylationGININNNTSHNSNIN
CCCCCCCCCCCCCCC		33.2222369663
427PhosphorylationININNNTSHNSNINM
CCCCCCCCCCCCCCC		23.8522369663
430PhosphorylationNNNTSHNSNINMGSK
CCCCCCCCCCCCCCC		33.3922369663
436PhosphorylationNSNINMGSKNAMVNR
CCCCCCCCCCEECCC		16.3922369663
446PhosphorylationAMVNRPHTFNNYSLN
EECCCCCCCCCCCCC		30.6421440633
560PhosphorylationDDDTENGSSSNGKSV
CCCCCCCCCCCCCCC		42.0221551504
643PhosphorylationFSVIDPDSTDSFGDG
CEEECCCCCCCCCCC		39.2319779198
644PhosphorylationSVIDPDSTDSFGDGM
EEECCCCCCCCCCCC		42.9419779198
646PhosphorylationIDPDSTDSFGDGMGS
ECCCCCCCCCCCCCC		31.0827214570
655AcetylationGDGMGSAKDKPYRCE
CCCCCCCCCCCEEEE		68.9024489116
657AcetylationGMGSAKDKPYRCEVC
CCCCCCCCCEEEEEC		43.1524489116
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 SFP1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SFP1_YEAST !!
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 SFP1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LAS1_YEASTLAS1physical
11805837
RAEP_YEASTMRS6physical
11805837
RNQ1_YEASTRNQ1physical
11805837
RAS2_YEASTRAS2genetic
15466158
ASF1_YEASTASF1physical
16554755
RAEP_YEASTMRS6physical
18467557
SAC3_YEASTSAC3genetic
19547744
RAEP_YEASTMRS6physical
19328065
TOR1_YEASTTOR1physical
19328065
MOT1_YEASTMOT1physical
19328065
KOG1_YEASTKOG1physical
19328065
RS18A_YEASTRPS18Aphysical
19328065
RS18B_YEASTRPS18Aphysical
19328065
TRA1_YEASTTRA1physical
19328065
RPC3_YEASTRPC82physical
19328065
CSK21_YEASTCKA1physical
19328065
BMH1_YEASTBMH1physical
19328065
BMH2_YEASTBMH2physical
19328065
FBRL_YEASTNOP1physical
19328065
CSK22_YEASTCKA2physical
19328065
LST8_YEASTLST8physical
19328065
SCH9_YEASTSCH9genetic
19328065
TOR1_YEASTTOR1genetic
19073887
RAEP_YEASTMRS6physical
19684114
SAC3_YEASTSAC3genetic
20959818
IES1_YEASTIES1genetic
20959818
YPT6_YEASTYPT6genetic
20959818
SCH9_YEASTSCH9genetic
15466158
EDE1_YEASTEDE1physical
19776351
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SFP1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; SER-183 AND SER-228,AND MASS SPECTROMETRY.

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