FAR1_YEAST - dbPTM
FAR1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FAR1_YEAST
UniProt AC P21268
Protein Name Cyclin-dependent kinase inhibitor FAR1
Gene Name FAR1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 830
Subcellular Localization
Protein Description Inhibitor of the cyclin-dependent kinase CDC28. Necessary for cell cycle arrest. Involved in pheromone response. Contributes to mating efficiency. Required for oriented polarization of yeast cells in response to mating pheromones..
Protein Sequence MKTPTRVSFEKKIHTPPSGDRDAERSPPKKFLRGLSGKVFRKTPEFKKQQMPTFGYIEESQFTPNLGLMMSKRGNIPKPLNLSKPISPPPSLKKTAGSVASGFSKTGQLSALQSPVNITSSNKYNIKATNLTTSLLRESISDSTTMCDTLSDINLTVMDEDYRIDGDSYYEEDSPTFMISLERNIKKCNSQFSPKRYIGEKCLICEESISSTFTGEKVVESTCSHTSHYNCYLMLFETLYFQGKFPECKICGEVSKPKDKDIVPEMVSKLLTGAGAHDDGPSSNMQQQWIDLKTARSFTGEFPQFTPQEQLIRTADISCDGFRTPRLSNSNQFEAVSYLDSPFLNSPFVNKMATTDPFDLSDDEKLDCDDEIDESAAEVWFSKTGGEHVMVSVKFQEMRTSDDLGVLQDVNHVDHEELEEREKEWKKKIDQYIETNVDKDSEFGSLILFDKLMYSDDGEQWVDNNLVILFSKFLVLFDFEEMKILGKIPRDQFYQVIKFNEDVLLCSLKSTNIPEIYLRFNENCEKWLLPKWKYCLENSSLETLPLSEIVSTVKELSHVNIIGALGAPPDVISAQSHDSRLPWKRLHSDTPLKLIVCLNLSHADGELYRKRVLKSVHQILDGLNTDDLLGIVVVGRDGSGVVGPFGTFIGMINKNWDGWTTFLDNLEVVNPNVFRDEKQQYKVTLQTCERLASTSAYVDTDDHIATGYAKQILVLNGSDVVDIEHDQKLKKAFDQLSYHWRYEISQRRMTPLNASIKQFLEELHTKRYLDVTLRLPQATFEQVYLGDMAAGEQKTRLIMDEHPHSSLIEIEYFDLVKQQRIHQTLEVPNL
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
3Phosphorylation-----MKTPTRVSFE
-----CCCCCEEEEE		28.7020377248
5Phosphorylation---MKTPTRVSFEKK
---CCCCCEEEEEEC		49.2721440633
8PhosphorylationMKTPTRVSFEKKIHT
CCCCCEEEEEECCCC		25.1320377248
15PhosphorylationSFEKKIHTPPSGDRD
EEEECCCCCCCCCCC		40.1320377248
18PhosphorylationKKIHTPPSGDRDAER
ECCCCCCCCCCCCHH		55.3020377248
26PhosphorylationGDRDAERSPPKKFLR
CCCCCHHCCCHHHHH		36.7420377248
43PhosphorylationSGKVFRKTPEFKKQQ
CCCHHHCCHHHHHHC		24.6421440633
83PhosphorylationIPKPLNLSKPISPPP
CCCCCCCCCCCCCCC		35.0021440633
87PhosphorylationLNLSKPISPPPSLKK
CCCCCCCCCCCCHHC		39.6220377248
91PhosphorylationKPISPPPSLKKTAGS
CCCCCCCCHHCCCCC		59.6021440633
98PhosphorylationSLKKTAGSVASGFSK
CHHCCCCCHHCCCCC		16.4317330950
101PhosphorylationKTAGSVASGFSKTGQ
CCCCCHHCCCCCCCC		37.9129734811
104PhosphorylationGSVASGFSKTGQLSA
CCHHCCCCCCCCCEE		32.6029734811
105UbiquitinationSVASGFSKTGQLSAL
CHHCCCCCCCCCEEC		55.1817644757
106PhosphorylationVASGFSKTGQLSALQ
HHCCCCCCCCCEECC		29.0319684113
110PhosphorylationFSKTGQLSALQSPVN
CCCCCCCEECCCCCC		21.0317330950
114PhosphorylationGQLSALQSPVNITSS
CCCEECCCCCCCCCC		31.5017330950
119PhosphorylationLQSPVNITSSNKYNI
CCCCCCCCCCCCCEE		22.3924961812
120PhosphorylationQSPVNITSSNKYNIK
CCCCCCCCCCCCEEE		28.2824961812
123UbiquitinationVNITSSNKYNIKATN
CCCCCCCCCEEEEEE		41.4417644757
174PhosphorylationDSYYEEDSPTFMISL
CCCCCCCCCCEEEEE		29.1728889911
193PhosphorylationKKCNSQFSPKRYIGE
HHHCCCCCCCCCCCC		23.1325704821
227PhosphorylationESTCSHTSHYNCYLM
EECCCCCCHHHHHHH		20.6727017623
238PhosphorylationCYLMLFETLYFQGKF
HHHHHHHHHHHCCCC		21.3027017623
297PhosphorylationIDLKTARSFTGEFPQ
EEHHHHHHHCCCCCC		25.3717330950
299PhosphorylationLKTARSFTGEFPQFT
HHHHHHHCCCCCCCC		36.7317330950
306PhosphorylationTGEFPQFTPQEQLIR
CCCCCCCCCHHHHHH		20.8617330950
318PhosphorylationLIRTADISCDGFRTP
HHHHCCCCCCCCCCC		13.5028889911
341PhosphorylationEAVSYLDSPFLNSPF
EEEEECCCCCCCCCC		18.2428889911
346PhosphorylationLDSPFLNSPFVNKMA
CCCCCCCCCCCCCCC		23.1229650682
354PhosphorylationPFVNKMATTDPFDLS
CCCCCCCCCCCCCCC		28.3821126336
361PhosphorylationTTDPFDLSDDEKLDC
CCCCCCCCCCCCCCC		44.8822890988
543PhosphorylationLENSSLETLPLSEIV
HHCCCCCCCCHHHHH		38.6821551504
614UbiquitinationLYRKRVLKSVHQILD
HHHHHHHHHHHHHHC		47.8017644757
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
87SPhosphorylationKinaseCDC28P00546
Uniprot
-KUbiquitinationE3 ubiquitin ligaseCDC4P07834
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FAR1_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 FAR1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
COPA_YEASTCOP1physical
11805837
IMA1_YEASTSRP1physical
11805837
PRS6B_YEASTRPT3physical
11805837
CLU_YEASTCLU1physical
11805837
SSK2_YEASTSSK2physical
11805837
UBP15_YEASTUBP15physical
11805837
CDK1_YEASTCDC28physical
9632750
GBB_YEASTSTE4physical
10087263
BEM1_YEASTBEM1physical
9822386
BEM1_YEASTBEM1physical
11927541
MSN5_YEASTMSN5physical
10485850
CDC24_YEASTCDC24physical
9822386
CDC42_YEASTCDC42physical
9822386
GBB_YEASTSTE4physical
9822386
CGS5_YEASTCLB5physical
15200949
CG12_YEASTCLN2physical
15200949
CG12_YEASTCLN2physical
9632750
CG12_YEASTCLN2physical
8395009
MCM1_YEASTMCM1genetic
10049917
CG12_YEASTCLN2genetic
10049917
PEA2_YEASTPEA2genetic
9822386
CG12_YEASTCLN2genetic
2142620
CDC24_YEASTCDC24genetic
10725324
CG12_YEASTCLN2genetic
2147873
FUS3_YEASTFUS3physical
16364919
STE5_YEASTSTE5genetic
8246877
KCS1_YEASTKCS1genetic
19269370
IME2_YEASTIME2genetic
19269370
ADK_YEASTADO1genetic
19269370
SSB1_YEASTSSB1physical
19536198
CDC24_YEASTCDC24physical
20489023
MPM1_YEASTMPM1physical
20489023
STE5_YEASTSTE5genetic
10049917
STE11_YEASTSTE11genetic
10049917
GBB_YEASTSTE4genetic
10049917
STE7_YEASTSTE7genetic
10049917
STE12_YEASTSTE12genetic
10049917
GPA1_YEASTGPA1genetic
10049917
SST2_YEASTSST2genetic
10049917
STE50_YEASTSTE50genetic
10049917
FUS3_YEASTFUS3genetic
10049917
KSS1_YEASTKSS1genetic
10049917
CGS5_YEASTCLB5genetic
10049917
CG13_YEASTCLN3genetic
10049917
CDC24_YEASTCDC24physical
22117027
STE12_YEASTSTE12genetic
22114773
SFP1_YEASTSFP1genetic
21964263
CDC48_YEASTCDC48physical
14557244
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FAR1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-98, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-114 ANDTHR-306, AND MASS SPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASSSPECTROMETRY.

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