PHO87_YEAST - dbPTM
PHO87_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHO87_YEAST
UniProt AC P25360
Protein Name Inorganic phosphate transporter PHO87
Gene Name PHO87
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 923
Subcellular Localization Membrane
Multi-pass membrane protein.
Protein Description Involved in the uptake of inorganic phosphate..
Protein Sequence MRFSHFLKYNAVPEWQNHYLDYNELKNLIYTLQTDELKQETPTGDLNDDADSQTPGPIADIESNIAAGEPSSSKRRFTHKLKRKLFGSKTPSGSKRGDSDEKAIDGNNINEETIELDELSPQGKTTSFNKNFIRKKFFESRSSSVSSEGKTLFSSYDTFVTNLSDEKLKVDDFYKRMEAKFYERFDHLINDLEKEGIVTRLNETFNPEIQALPPLREIISGTSETHSSNNPFEIHSSNIDSELRNRFDYSEEEMDEDDDVDVFADTTDNTALLNYSQFNIKSQKKSLLKQTIINLYIDLCQLKSFIELNRMGFSKITKKSDKVLHMNTRQELIESEEFFKDTYIFQHETLSSLNSKIAQLIEFYAVLMGQPGNVDSCKQELKSYLHDHIVWERSNTWKDMLGLSSQNNDIITIEDEAEKLMQEKLQIEYFKYPLPKPINLKFTKIENLAVPKLFFGKRAMKIGFIIIVTGVLLGVKTFNDPVEHRCMALVECCAFLWASEAIPLHITGLLVPLLTVLFRVLKDDDGKVMGAAAASTEILGTMWSSTIMILLAGFTLGEALSQYNVAKVLASWLLALAGTKPRNVLLMAMSVVFFLSMWISNVASPVLTYSLLTPLLDPLDYTSPFAKALVMGVALSADIGGMASPISSPQNIISMQYLKPYGIGWGQFFAVALPTGILSMLCSWALMILTFKIGKTKLEKFKPIRTRFTIKQYFIIIVTIATILLWCVESQIESAFGSSGEIAVIPIVLFFGTGLLSTKDFNTFPWSIVVLAMGGIALGKAVSSSGLLVTIARALQKKIQNDGVFAILCIFGILMLVVGTFVSHTVSAIIIIPLVQEVGDKLSDPKAAPILVFGCALLASCGMGLASSGFPNVTAISMTDKKGNRWLTVGAFISRGVPASLLAFVCVITLGYGISSSVLKGST
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
8UbiquitinationMRFSHFLKYNAVPEW
CCHHHHCCCCCCCHH		35.2017644757
26UbiquitinationYLDYNELKNLIYTLQ
CCCHHHHHHHHHHCC		43.4617644757
43PhosphorylationELKQETPTGDLNDDA
HHCCCCCCCCCCCCC		51.2321551504
52PhosphorylationDLNDDADSQTPGPIA
CCCCCCCCCCCCCHH		37.3620377248
54PhosphorylationNDDADSQTPGPIADI
CCCCCCCCCCCHHHH		33.8820377248
63PhosphorylationGPIADIESNIAAGEP
CCHHHHHCCCCCCCC		33.5921551504
89AcetylationKRKLFGSKTPSGSKR
HHHHHCCCCCCCCCC		65.9125381059
89UbiquitinationKRKLFGSKTPSGSKR
HHHHHCCCCCCCCCC		65.9123749301
102UbiquitinationKRGDSDEKAIDGNNI
CCCCCCCCCCCCCCC		56.4823749301
120PhosphorylationTIELDELSPQGKTTS
HEEHHHCCCCCCCCC		17.0929734811
124UbiquitinationDELSPQGKTTSFNKN
HHCCCCCCCCCCCHH		43.3023749301
127PhosphorylationSPQGKTTSFNKNFIR
CCCCCCCCCCHHHHH		31.8623749301
130UbiquitinationGKTTSFNKNFIRKKF
CCCCCCCHHHHHHHH		51.7523749301
135UbiquitinationFNKNFIRKKFFESRS
CCHHHHHHHHHCCCC		49.4722817900
140PhosphorylationIRKKFFESRSSSVSS
HHHHHHCCCCCCCCC		32.1021551504
142PhosphorylationKKFFESRSSSVSSEG
HHHHCCCCCCCCCCC		35.9221440633
143PhosphorylationKFFESRSSSVSSEGK
HHHCCCCCCCCCCCC		33.3820377248
144PhosphorylationFFESRSSSVSSEGKT
HHCCCCCCCCCCCCE		27.5420377248
146PhosphorylationESRSSSVSSEGKTLF
CCCCCCCCCCCCEEC		25.3121440633
147PhosphorylationSRSSSVSSEGKTLFS
CCCCCCCCCCCEECC		48.4920377248
154PhosphorylationSEGKTLFSSYDTFVT
CCCCEECCCCCEEEC		30.9721551504
162N-linked_GlycosylationSYDTFVTNLSDEKLK
CCCEEECCCCCCCCC		32.04-
202N-linked_GlycosylationEGIVTRLNETFNPEI
CCCCCHHHHCCCHHH		42.86-
220PhosphorylationPPLREIISGTSETHS
CCHHHHHCCCCCCCC		41.5028889911
222PhosphorylationLREIISGTSETHSSN
HHHHHCCCCCCCCCC		19.3219779198
223PhosphorylationREIISGTSETHSSNN
HHHHCCCCCCCCCCC		43.9825752575
225PhosphorylationIISGTSETHSSNNPF
HHCCCCCCCCCCCCE		27.1619779198
227PhosphorylationSGTSETHSSNNPFEI
CCCCCCCCCCCCEEE		42.0323749301
228PhosphorylationGTSETHSSNNPFEIH
CCCCCCCCCCCEEEE		32.7829688323
236PhosphorylationNNPFEIHSSNIDSEL
CCCEEEECCCCCHHH		30.6419779198
237PhosphorylationNPFEIHSSNIDSELR
CCEEEECCCCCHHHH		24.5219779198
241PhosphorylationIHSSNIDSELRNRFD
EECCCCCHHHHHCCC		34.4329688323
274N-linked_GlycosylationTDNTALLNYSQFNIK
CCCCHHCCHHHHCCH		34.95-
289UbiquitinationSQKKSLLKQTIINLY
HHHHHHHHHHHHHHH		51.1717644757
303UbiquitinationYIDLCQLKSFIELNR
HHHHHHHHHHHHHHH		19.9017644757
315UbiquitinationLNRMGFSKITKKSDK
HHHCCCCCCCCCCCC		52.7323749301
340UbiquitinationIESEEFFKDTYIFQH
HHCHHHHCCCHHHCH		55.2522106047
382UbiquitinationDSCKQELKSYLHDHI
HHHHHHHHHHHHHHH		35.9817644757
412PhosphorylationSQNNDIITIEDEAEK
CCCCCCEEEHHHHHH		20.7424961812
444UbiquitinationPINLKFTKIENLAVP
CCCCCEEEEECCCCC		51.6724961812
452UbiquitinationIENLAVPKLFFGKRA
EECCCCCCHHCCHHH		51.8624961812
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
-KUbiquitinationE3 ubiquitin ligaseRSP5P39940
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PHO87_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 PHO87_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PHO84_YEASTPHO84genetic
17804816
SPL2_YEASTSPL2physical
19590579
OST1_YEASTOST1physical
19590579
PHO88_YEASTPHO88physical
16093310
PHO84_YEASTPHO84genetic
8598055
PHO89_YEASTPHO89genetic
11779791
PHO90_YEASTPHO90genetic
11779791
PHO91_YEASTPHO91genetic
11779791
PHO4_YEASTPHO4genetic
21143198
PHO89_YEASTPHO89genetic
21143198
KTR3_YEASTKTR3genetic
21623372
SKN1_YEASTSKN1genetic
21623372
ELO3_YEASTELO3genetic
21623372
CISY1_YEASTCIT1genetic
21623372
CEM1_YEASTCEM1genetic
21623372
AATM_YEASTAAT1genetic
21623372
ARGJ_YEASTARG7genetic
21623372
SDHB_YEASTSDH2genetic
21623372
DPH5_YEASTDPH5genetic
21623372
POS5_YEASTPOS5genetic
21623372
SCS7_YEASTSCS7genetic
21623372
MET22_YEASTMET22genetic
21623372
SERC_YEASTSER1genetic
21623372
ACH1_YEASTACH1genetic
21623372
IDH1_YEASTIDH1genetic
21623372
DDP1_YEASTDDP1genetic
21623372
TPS1_YEASTTPS1genetic
21623372
ALAM_YEASTALT1genetic
21623372
DS1P1_YEASTLCB3genetic
21623372
GPT1_YEASTSCT1genetic
21623372
IDH2_YEASTIDH2genetic
21623372
ODO2_YEASTKGD2genetic
21623372
GSH1_YEASTGSH1genetic
21623372
SERA_YEASTSER3genetic
21623372
SUR1_YEASTSUR1genetic
21623372
FABD_YEASTMCT1genetic
21623372
CATA_YEASTCTA1genetic
21623372
PHSG_YEASTGPH1genetic
21623372
ERG2_YEASTERG2genetic
21623372
GYS2_YEASTGSY2genetic
21623372
CHO2_YEASTCHO2genetic
21623372
CYS3_YEASTCYS3genetic
21623372
EF1G2_YEASTTEF4genetic
25887987
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PHO87_YEAST

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228, UBIQUITINATION ATLYS-102, AND MASS SPECTROMETRY.
Ubiquitylation
ReferencePubMed
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228, UBIQUITINATION ATLYS-102, AND MASS SPECTROMETRY.

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