STP1_YEAST - dbPTM
STP1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STP1_YEAST
UniProt AC Q00947
Protein Name Transcription factor STP1
Gene Name STP1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 519
Subcellular Localization Cell membrane
Peripheral membrane protein
Cytoplasmic side. Nucleus. Localizes to the cytoplasm in its unprocessed form and is targeted to the nucleus after proteolytic processing upon induction by amino acids. The SCF(MET30) ubiquitin ligase compl
Protein Description Transcription factor involved in the regulation of gene expression in response to extracellular amino acid levels. Synthesized as latent cytoplasmic precursor, which, upon a signal initiated by the plasma membrane SPS (SSY1-PTR3-SSY5) amino acid sensor system, becomes proteolytically activated and relocates to the nucleus, where it induces the expression of SPS-sensor-regulated genes, including the amino-acid permeases AGP1, BAP2, BAP3 and GNP1. Binding to promoters is facilitated by DAL81. Involved in the repression of genes subject to nitrogen catabolite repression and genes involved in stress response. Negatively regulated by inner nuclear membrane proteins ASI1, ASI2 and ASI3, which prevent unprocessed precursor forms that escape cytoplasmic anchoring from inducing SPS-sensor-regulated genes. May be involved in pre-tRNA splicing..
Protein Sequence MPSTTLLFPQKHIRAIPGKIYAFFRELVSGVIISKPDLSHHYSCENATKEEGKDAADEEKTTTSLFPESNNIDRSLNGGCSVIPCSMDVSDLNTPISITLSPENRIKSEVNAKSLLGSRPEQDTGAPIKMSTGVTSSPLSPSGSTPEHSTKVLNNGEEEFICHYCDATFRIRGYLTRHIKKHAIEKAYHCPFFNSATPPDLRCHNSGGFSRRDTYKTHLKARHVLYPKGVKPQDRNKSSGHCAQCGEYFSTIENFVENHIESGDCKALPQGYTKKNEKRSGKLRKIKTSNGHSRFISTSQSVVEPKVLFNKDAVEAMTIVANNSSGNDIISKYGNNKLMLNSENFKVDIPKRKRKYIKKKQQQVSGSTVTTPEVATQNNQEVAPDEISSATIFSPFDTHLLEPVPSSSSESSAEVMFHGKQMKNFLIDINSFTNQQQQAQDNPSFLPLDIEQSSYDLSEDAMSYPIISTQSNRDCTQYDNTKISQILQSQLNPEYLSENHMRETQQYLNFYNDNFGSQF
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
11UbiquitinationTTLLFPQKHIRAIPG
CEEECCHHHHHCCCH		41.0317644757
62PhosphorylationAADEEKTTTSLFPES
CCCCCHHHCCCCCCC		26.0028889911
75PhosphorylationESNNIDRSLNGGCSV
CCCCCCCHHCCCCEE		23.5729688323
81PhosphorylationRSLNGGCSVIPCSMD
CHHCCCCEEEEECCC		26.7629688323
86PhosphorylationGCSVIPCSMDVSDLN
CCEEEEECCCHHHCC		16.8029688323
90PhosphorylationIPCSMDVSDLNTPIS
EEECCCHHHCCCCEE		31.9229688323
94PhosphorylationMDVSDLNTPISITLS
CCHHHCCCCEEEEEC		29.3329688323
97PhosphorylationSDLNTPISITLSPEN
HHCCCCEEEEECCCC		15.6629688323
99PhosphorylationLNTPISITLSPENRI
CCCCEEEEECCCCCC		17.8829688323
101PhosphorylationTPISITLSPENRIKS
CCEEEEECCCCCCCC		22.8629688323
107UbiquitinationLSPENRIKSEVNAKS
ECCCCCCCCCCCHHH		37.0123749301
108PhosphorylationSPENRIKSEVNAKSL
CCCCCCCCCCCHHHH		44.3917563356
113UbiquitinationIKSEVNAKSLLGSRP
CCCCCCHHHHHCCCC		36.1123749301
118PhosphorylationNAKSLLGSRPEQDTG
CHHHHHCCCCCCCCC		44.6323749301
129UbiquitinationQDTGAPIKMSTGVTS
CCCCCCCEEECCCCC		26.2417644757
131PhosphorylationTGAPIKMSTGVTSSP
CCCCCEEECCCCCCC		19.6022369663
132PhosphorylationGAPIKMSTGVTSSPL
CCCCEEECCCCCCCC		31.9722369663
135PhosphorylationIKMSTGVTSSPLSPS
CEEECCCCCCCCCCC		25.4922369663
136PhosphorylationKMSTGVTSSPLSPSG
EEECCCCCCCCCCCC		27.7922369663
137PhosphorylationMSTGVTSSPLSPSGS
EECCCCCCCCCCCCC		22.0922369663
140PhosphorylationGVTSSPLSPSGSTPE
CCCCCCCCCCCCCCC		22.0222369663
142PhosphorylationTSSPLSPSGSTPEHS
CCCCCCCCCCCCCCE		41.8420377248
144PhosphorylationSPLSPSGSTPEHSTK
CCCCCCCCCCCCEEE		45.1620377248
145PhosphorylationPLSPSGSTPEHSTKV
CCCCCCCCCCCEEEE		35.9022369663
149PhosphorylationSGSTPEHSTKVLNNG
CCCCCCCEEEECCCC		28.4122369663
150PhosphorylationGSTPEHSTKVLNNGE
CCCCCCEEEECCCCC		27.3822369663
151UbiquitinationSTPEHSTKVLNNGEE
CCCCCEEEECCCCCE		47.9817644757
186UbiquitinationIKKHAIEKAYHCPFF
HHHHHHHHHHCCCCC		48.4017644757
237UbiquitinationVKPQDRNKSSGHCAQ
CCCCCCCCCCCCCCH		47.0617644757
266UbiquitinationHIESGDCKALPQGYT
HHHCCCCCCCCCCCC		58.6717644757
318PhosphorylationKDAVEAMTIVANNSS
CCHHHHEEEEEECCC		21.2429136822
324PhosphorylationMTIVANNSSGNDIIS
EEEEEECCCCCCHHH		39.1629136822
325PhosphorylationTIVANNSSGNDIISK
EEEEECCCCCCHHHH		43.6829136822
482UbiquitinationCTQYDNTKISQILQS
CCCCCHHHHHHHHHH		46.7617644757
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 STP1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STP1_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 STP1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
H2A2_YEASTHTA2physical
16554755
H3_YEASTHHT1physical
16554755
RPB1_YEASTRPO21physical
16554755
TOM1_YEASTTOM1physical
16554755
SSY5_YEASTSSY5physical
16778074
LSM3_YEASTLSM3genetic
19061648
SAC3_YEASTSAC3genetic
19061648
RU2A_YEASTLEA1genetic
19061648
STP2_YEASTSTP2genetic
19906648
DAL81_YEASTDAL81genetic
19906648
DAL81_YEASTDAL81genetic
15126393
STP2_YEASTSTP2genetic
20581295
STP2_YEASTSTP2genetic
21127045
STP2_YEASTSTP2genetic
26546823
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STP1_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-108, AND MASSSPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-140, ANDMASS SPECTROMETRY.

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