HPH1_YEAST - dbPTM
HPH1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HPH1_YEAST
UniProt AC Q99332
Protein Name Protein HPH1
Gene Name FRT1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 602
Subcellular Localization Endoplasmic reticulum membrane
Single-pass membrane protein . Punctate foci at the endoplasmic reticulum membrane. The distribution of FRT1 on the endoplasmic reticulum membrane depends on CaCl2 and calcineurin activity.
Protein Description Calcineurin-dependent protein required for growth under high NaCl, alkaline pH and cell wall stress..
Protein Sequence MNLLIDRMENPGSRNCTLLPPSFPRGFCKGRRASSGDAVKIKESGLQPQPQPEPLQAKTNVAHFSKSSSRLPVIAVNDNPVVPRPSTEVNLGSLLQKEREKEKEEQPALHDRRHLYVTKNRAHGVRQRSLEMTSLPVLGSTKTGKFSDFLFEDDIDNRVGRHSRSYSGASSLDDPFRVSPKTDFNSNRARLSCLSKGRRGSMSVFQSCHTGLAFNQIQGSSSSQRRSSAGSFDYERKRLVNQFLQPSLGNSDPFDTLRESVVFEPSSTAGGIKLGNMHSQSQISVNSSPSTSLFYHDLDGSAVNDSSSFLYSRSNVPAFLSSSAFSSTSSTSSDSEDVDRRSLNGVYPSLGYLTNQRKPRNSSGSSTAPGTDTLGFKYLLNRQKSADSSTRFKSVLKVNNNNGSAATPDSSSNSISKSNSNLNDNIDELNYYQNHISTLLVKIENEMRRNLNDTIIKNENNVQKTIQKYDLLSGELTLLLDEMTTLRTTVINQFLVKLKSDFDEDDNKAFINELKISVEESVAQLQGLERRMEVCQERLNKQKSSLREMDSLIELKNVLNKSKNNTKSIYLYRYFIIDIIAFLLMGGFIVYVKNLLTRFFTR
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
34PhosphorylationFCKGRRASSGDAVKI
CCCCCCCCCCCCEEE		32.8028889911
35PhosphorylationCKGRRASSGDAVKIK
CCCCCCCCCCCEEEC		39.4428889911
59PhosphorylationPEPLQAKTNVAHFSK
CCCCCCCCCEEECCC		37.6323749301
65PhosphorylationKTNVAHFSKSSSRLP
CCCEEECCCCCCCCC		23.0423749301
67PhosphorylationNVAHFSKSSSRLPVI
CEEECCCCCCCCCEE		32.1422369663
68PhosphorylationVAHFSKSSSRLPVIA
EEECCCCCCCCCEEE		24.1821440633
69PhosphorylationAHFSKSSSRLPVIAV
EECCCCCCCCCEEEE		44.9520377248
86PhosphorylationNPVVPRPSTEVNLGS
CCCCCCCCCCCCHHH		38.1820377248
87PhosphorylationPVVPRPSTEVNLGSL
CCCCCCCCCCCHHHH		46.7820377248
93PhosphorylationSTEVNLGSLLQKERE
CCCCCHHHHHHHHHH		29.1322369663
165PhosphorylationRVGRHSRSYSGASSL
CCCCCCCCCCCCCCC		27.0228889911
166PhosphorylationVGRHSRSYSGASSLD
CCCCCCCCCCCCCCC		15.2628889911
167PhosphorylationGRHSRSYSGASSLDD
CCCCCCCCCCCCCCC		29.1823749301
170PhosphorylationSRSYSGASSLDDPFR
CCCCCCCCCCCCCCC		34.6523749301
171PhosphorylationRSYSGASSLDDPFRV
CCCCCCCCCCCCCCC		34.9721440633
179PhosphorylationLDDPFRVSPKTDFNS
CCCCCCCCCCCCCCC		19.2023749301
192PhosphorylationNSNRARLSCLSKGRR
CCCHHHHHHHHCCCC		13.8821440633
201PhosphorylationLSKGRRGSMSVFQSC
HHCCCCCCCHHHHHC		13.1819779198
207PhosphorylationGSMSVFQSCHTGLAF
CCCHHHHHCCCCCHH		9.0819779198
228PhosphorylationSSSQRRSSAGSFDYE
CCCCCHHCCCCCHHH		34.5317563356
231PhosphorylationQRRSSAGSFDYERKR
CCHHCCCCCHHHHHH		18.0517563356
247PhosphorylationVNQFLQPSLGNSDPF
HHHHHCHHHCCCCCC		35.6327738172
256PhosphorylationGNSDPFDTLRESVVF
CCCCCCCCHHHEEEE		28.2627738172
342PhosphorylationSEDVDRRSLNGVYPS
CHHCHHHHHCCCCCH		27.3825752575
347PhosphorylationRRSLNGVYPSLGYLT
HHHHCCCCCHHHHHC		6.6228889911
362PhosphorylationNQRKPRNSSGSSTAP
CCCCCCCCCCCCCCC		37.0423749301
363PhosphorylationQRKPRNSSGSSTAPG
CCCCCCCCCCCCCCC		46.3625752575
365PhosphorylationKPRNSSGSSTAPGTD
CCCCCCCCCCCCCCC		26.8521551504
366PhosphorylationPRNSSGSSTAPGTDT
CCCCCCCCCCCCCCC		31.9223749301
367PhosphorylationRNSSGSSTAPGTDTL
CCCCCCCCCCCCCCC		38.2728889911
385PhosphorylationYLLNRQKSADSSTRF
HHHHCCCCCCCCCHH		29.0427717283
388PhosphorylationNRQKSADSSTRFKSV
HCCCCCCCCCHHEEE		33.0721440633
389PhosphorylationRQKSADSSTRFKSVL
CCCCCCCCCHHEEEE		24.9327717283
390PhosphorylationQKSADSSTRFKSVLK
CCCCCCCCHHEEEEE		44.0427717283
394PhosphorylationDSSTRFKSVLKVNNN
CCCCHHEEEEEEECC		29.9421440633
407PhosphorylationNNNGSAATPDSSSNS
CCCCCCCCCCCCCCC		27.6122369663
410PhosphorylationGSAATPDSSSNSISK
CCCCCCCCCCCCCCC		36.5520377248
411PhosphorylationSAATPDSSSNSISKS
CCCCCCCCCCCCCCC		40.7022369663
412PhosphorylationAATPDSSSNSISKSN
CCCCCCCCCCCCCCC		38.2522369663
414PhosphorylationTPDSSSNSISKSNSN
CCCCCCCCCCCCCCC		30.1323749301
416PhosphorylationDSSSNSISKSNSNLN
CCCCCCCCCCCCCCC		29.8320377248
418PhosphorylationSSNSISKSNSNLNDN
CCCCCCCCCCCCCCC		38.4121440633
420PhosphorylationNSISKSNSNLNDNID
CCCCCCCCCCCCCHH		50.1922369663
465PhosphorylationNENNVQKTIQKYDLL
CCCHHHHHHHHHCCH		16.1421551504
566PhosphorylationLNKSKNNTKSIYLYR
HHHCCCCCCHHHHHH		35.2521440633
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 HPH1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HPH1_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 HPH1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PP2B1_YEASTCNA1physical
15189990
PP2B2_YEASTCMP2physical
15189990
HPH2_YEASTFRT2genetic
15189990
HIS7_YEASTHIS3genetic
19595784
YCA2_YEASTYCL002Cgenetic
20093466
DPO4_YEASTPOL4genetic
20093466
SPT3_YEASTSPT3genetic
20093466
LSB3_YEASTLSB3genetic
20093466
ATG32_YEASTATG32genetic
20093466
YIW2_YEASTYIR042Cgenetic
20093466
DCOR_YEASTSPE1genetic
20093466
YL413_YEASTINA1genetic
20093466
HXT2_YEASTHXT2genetic
20093466
PHO23_YEASTPHO23genetic
20093466
PP2B2_YEASTCMP2physical
21097665
HPH2_YEASTFRT2physical
21097665
HPH1_YEASTFRT1physical
21097665
SEC66_YEASTSEC66physical
21097665
SEC72_YEASTSEC72physical
21097665
SEC62_YEASTSEC62physical
21097665
SEC63_YEASTSEC63physical
21097665
SC61A_YEASTSEC61physical
21097665
HPH2_YEASTFRT2genetic
21097665
PKR1_YEASTPKR1genetic
21097665
CSG2_YEASTCSG2genetic
21987634
SSD1_YEASTSSD1genetic
21987634
ERG2_YEASTERG2genetic
21987634
KIN3_YEASTKIN3physical
22875988
HDA2_YEASTHDA2physical
22875988
SPC25_YEASTSPC25physical
22875988
FMP32_YEASTFMP32physical
22875988
MAD1_YEASTMAD1physical
22875988
VAM7_YEASTVAM7physical
22875988
NNF1_YEASTNNF1physical
22875988
SPC42_YEASTSPC42physical
22875988
BLI1_YEASTBLI1physical
22875988
MRP8_YEASTMRP8physical
22875988
MIC60_YEASTMIC60physical
22875988
RCF1_YEASTRCF1physical
22875988
STV1_YEASTSTV1physical
22875988
SPC24_YEASTSPC24physical
22875988
END3_YEASTEND3physical
22875988
AF9_YEASTYAF9physical
22875988
PFD4_YEASTGIM3physical
22875988
YEF3_YEASTYEL043Wphysical
22875988
LAM4_YEASTYHR080Cphysical
22875988
STB6_YEASTSTB6physical
22875988
YKT6_YEASTYKT6physical
22875988
STB2_YEASTSTB2physical
22875988
YP216_YEASTYPL216Wphysical
22875988
YIW2_YEASTYIR042Cgenetic
27708008
MTC2_YEASTMTC2genetic
27708008
YCA2_YEASTYCL002Cgenetic
27708008
DPO4_YEASTPOL4genetic
27708008
RL13A_YEASTRPL13Agenetic
27708008
UFD2_YEASTUFD2genetic
27708008
RIM15_YEASTRIM15genetic
27708008
ASK10_YEASTASK10genetic
27708008
SNF6_YEASTSNF6genetic
27708008
ATG32_YEASTATG32genetic
27708008
VPS53_YEASTVPS53genetic
27708008
DCOR_YEASTSPE1genetic
27708008
HXT2_YEASTHXT2genetic
27708008
RIM11_YEASTRIM11genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HPH1_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 TYR-166; SER-171; SER-228;SER-342; SER-362 AND SER-363, 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-228 AND SER-231, ANDMASS SPECTROMETRY.

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