PHO81_YEAST - dbPTM
PHO81_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHO81_YEAST
UniProt AC P17442
Protein Name Phosphate system positive regulatory protein PHO81
Gene Name PHO81
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1178
Subcellular Localization Cytoplasm. Nucleus. Localizes predominantly to the nucleus in both high- and low-phosphate conditions.
Protein Description Inhibits the kinase activity of the cyclin-CDKs PHO80-PHO85 and PCL7-PHO85 under low-phosphate conditions..
Protein Sequence MKFGKYLEARQLELAEYNSHFIDYKALKKLIKQLAIPTLKASSDLDLHLTLDDIDEKIIHQRLQENKAAFFFKLERELEKVNGYYLARESDLRIKFNILHSKYKDYKINGKLNSNQATSFKNLYAAFKKFQKDLRNLEQYVELNKTGFSKALKKWDKRSQSHDKDFYLATVVSIQPIFTRDGPLKLNDETLHILLELNDIDNNNRRADIQSSTFTNDDDDDNNTSNNNKHNNNNNNNNNNNNNNNNNNILHNNYELTTSKISENQLEHLFQASSSSLDMEMEIENWYKEILNIATVKDVQRKHALLRNFRETKIFTYLLQNSSESFHKNVFSLLKECLTTLFLLLVASPLDDNSLHIFYKSNQDHIDLSYCDEDDQVFSRKNVFHEAASCPEKSRLFILDEALTTSKLSKETVQKLLNAQDIHSRVPLHYAAELGKLEFVHSLLITNLLEDVDPIDSDSKTPLVLAITNNHIDVVRDLLTIGGANASPIEKPILDYSKNVISSTKVQFDPLNVACKFNNHDAAKLLLEIRSKQNADNAKNKSSQHLCQPLFKKNSTGLCTLHIVAKIGGDPQLIQLLIRYGADPNEIDGFNKWTPIFYAVRSGHSEVITELLKHNARLDIEDDNGHSPLFYALWESHVDVLNALLQRPLNLPSAPLNEINSQSSTQRLNTIDLTPNDDKFDLDIQDSIPDFALPPPIIPLRKYGHNFLEKKIFIKLKLRPGLESIKLTQDNGIIMSSSPGRITLSSNLPEIIPRNVILPVRSGEINNFCKDISETNDEEDDDEISEDHDDGEIIFQVDSIDDFSMDFEIFPSFGTRIIAKTTAMPFLFKKVAINSIATMNLPLFDTRLNNIGSLTLDYQIIFPYPGNPLKIINYEPYWKSTGSDLMTSSKDGNFVTSSSLNGSFISVLVCALNDETIVAAPKPYVEFKGTKILLNDLTKEQLEKVVDYDFGKIDGSFDEVTLKQYLSSRVVPLRSLLEVIPGSAQLVIRVYFPTDKEIDTIPIKISPFININQFIDKLLLIIFEHERFLRHSGSGSMRQIVFSSCNWEACSILNWKQPNFPVLLQMKNLLRDSTTGKFVGDTPNCLKELAVNPQKMSYLNTELINIHTMVQFAMNNNLLGVTLPYEVLKICPSLARIIKQNGLLLIASVGENDQIPADGGYSGIYYACELLFENNIDM
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
42PhosphorylationAIPTLKASSDLDLHL
HCCCCCCCCCCEEEE		23.8522369663
43PhosphorylationIPTLKASSDLDLHLT
CCCCCCCCCCEEEEE		47.2322369663
118PhosphorylationKLNSNQATSFKNLYA
CCCCCCCCCHHHHHH		25.5727214570
211PhosphorylationNRRADIQSSTFTNDD
CCEECCEECCCCCCC		31.5122369663
212PhosphorylationRRADIQSSTFTNDDD
CEECCEECCCCCCCC		15.9123749301
213PhosphorylationRADIQSSTFTNDDDD
EECCEECCCCCCCCC		39.4622369663
215PhosphorylationDIQSSTFTNDDDDDN
CCEECCCCCCCCCCC		37.5122369663
224PhosphorylationDDDDDNNTSNNNKHN
CCCCCCCCCCCCCCC		38.8022369663
225PhosphorylationDDDDNNTSNNNKHNN
CCCCCCCCCCCCCCC		39.4222369663
348PhosphorylationLFLLLVASPLDDNSL
HHHHHHHCCCCCCCE		20.6528889911
461PhosphorylationPIDSDSKTPLVLAIT
CCCCCCCCCEEEEEE		26.3028889911
487PhosphorylationTIGGANASPIEKPIL
HCCCCCCCCCCCCCC		26.6417563356
502PhosphorylationDYSKNVISSTKVQFD
CCCCCCCCCCEEEEC		27.8930377154
516AcetylationDPLNVACKFNNHDAA
CCCCEEEEECCHHHH		41.1924489116
542PhosphorylationADNAKNKSSQHLCQP
HHHCCCCCCHHHHHH		44.6222369663
543PhosphorylationDNAKNKSSQHLCQPL
HHCCCCCCHHHHHHH		24.1922369663
627PhosphorylationIEDDNGHSPLFYALW
CCCCCCCCHHHHHHH		25.3828889911
661PhosphorylationAPLNEINSQSSTQRL
CCHHHCCCCCCCEEC		36.7828889911
664PhosphorylationNEINSQSSTQRLNTI
HHCCCCCCCEECCCC		22.4128889911
665PhosphorylationEINSQSSTQRLNTID
HCCCCCCCEECCCCC		23.9728889911
670PhosphorylationSSTQRLNTIDLTPND
CCCEECCCCCCCCCC		22.0628889911
674PhosphorylationRLNTIDLTPNDDKFD
ECCCCCCCCCCCCCC		19.1229136822
687PhosphorylationFDLDIQDSIPDFALP
CCCCCCCCCCCCCCC		21.4621440633
737PhosphorylationDNGIIMSSSPGRITL
CCCEEEECCCCCEEE		24.1528889911
738PhosphorylationNGIIMSSSPGRITLS
CCEEEECCCCCEEEC		24.8628889911
883PhosphorylationPYWKSTGSDLMTSSK
CCCCCCCCCCCCCCC		27.8830377154
938PhosphorylationKILLNDLTKEQLEKV
EEEECCCCHHHHHHH		35.0830377154
956PhosphorylationDFGKIDGSFDEVTLK
CCCCCCCCCCHHHHH		26.2720190278
1082PhosphorylationTGKFVGDTPNCLKEL
CCCCCCCCCCHHHHH		15.5227214570
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 PHO81_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHO81_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 PHO81_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PHO80_YEASTPHO80physical
7957107
PCL7_YEASTPCL7physical
11069666
PHO80_YEASTPHO80physical
11069666
PHO85_YEASTPHO85physical
7823964
PHO80_YEASTPHO80physical
11533256
PHO85_YEASTPHO85physical
11533256
PHO80_YEASTPHO80physical
7939631
PHO85_YEASTPHO85physical
7939631
PHO4_YEASTPHO4physical
7957107
PLC1_YEASTPLC1genetic
9475719
PHO80_YEASTPHO80genetic
9832515
PHO80_YEASTPHO80genetic
15926040
PHO85_YEASTPHO85genetic
15926040
PHO80_YEASTPHO80physical
16554755
PHO85_YEASTPHO85physical
16554755
CYAA_YEASTCYR1physical
16429126
PHO80_YEASTPHO80physical
16429126
PHO85_YEASTPHO85physical
16429126
CAP_YEASTSRV2physical
16429126
PCL5_YEASTPCL5physical
16611745
PCL7_YEASTPCL7physical
16611745
DDI1_YEASTDDI1physical
18035052
PHO80_YEASTPHO80physical
18059263
PHO85_YEASTPHO85physical
18059263
PHO80_YEASTPHO80genetic
8493108
PHO86_YEASTPHO86genetic
8709965
PHO84_YEASTPHO84genetic
8709965
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PHO81_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-42; SER-43; SER-487;SER-542; SER-543; SER-627; SER-661; SER-664; THR-665; SER-738 ANDSER-956, AND MASS SPECTROMETRY.
"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-487, AND MASSSPECTROMETRY.

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