FRA1_YEAST - dbPTM
FRA1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FRA1_YEAST
UniProt AC Q07825
Protein Name Putative Xaa-Pro aminopeptidase FRA1
Gene Name FRA1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 749
Subcellular Localization Cytoplasm .
Protein Description Involved in the regulation of the iron regulon in responss to decreased mitochondrial iron-sulfur cluster synthesis..
Protein Sequence MTSKPSTSDGRAHSISHVPGTHMRGTSASHSPRPFRPCADCTCSPGLLSRQGRRASLFLRQLENSRRSSSMLLNELKGAGGGSSAGNGSVYSCDSLCAVNREVNTTDRLLKLRQEMKKHDLCCYIVPSCDEHQSEYVSLRDQRRAFISGFSGSAGVACITRDLLNFNDDHPDGKSILSTDGRYFNQARQELDYNWTLLRQNEDPITWQEWCVREALEMAKGLGNKEGMVLKIGIDPKLITFNDYVSFRKMIDTKYDAKGKVELVPVEENLVDSIWPDFETLPERPCNDLLLLKYEFHGEEFKDKKEKLLKKLNDKASSATTGRNTFIVVALDEICWLLNLRGSDIDYNPVFFSYVAINEDETILFTNNPFNDDISEYFKINGIEVRPYEQIWEHLTKITSQASSAEHEFLIPDSASWQMVRCLNTSTNANGAIAKKMTAQNFAIIHSPIDVLKSIKNDIEIKNAHKAQVKDAVCLVQYFAWLEQQLVGREALIDEYRAAEKLTEIRKTQRNFMGNSFETISSTGSNAAIIHYSPPVENSSMIDPTKIYLCDSGSQFLEGTTDITRTIHLTKPTKEEMDNYTLVLKGGLALERLIFPENTPGFNIDAIARQFLWSRGLDYKHGTGHGIGSFLNVHEGPMGVGFRPHLMNFPLRAGNIISNEPGYYKDGEYGIRIESDMLIKKATEKGNFLKFENMTVVPYCRKLINTKLLNEEEKTQINEYHARVWRTIVHFLQPQSISYKWLKRETSPL
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
14PhosphorylationTSDGRAHSISHVPGT
CCCCCCCCCCCCCCC		25.4622890988
16PhosphorylationDGRAHSISHVPGTHM
CCCCCCCCCCCCCCC		22.8022890988
26PhosphorylationPGTHMRGTSASHSPR
CCCCCCCCCCCCCCC		15.6828889911
27PhosphorylationGTHMRGTSASHSPRP
CCCCCCCCCCCCCCC		30.5130377154
29PhosphorylationHMRGTSASHSPRPFR
CCCCCCCCCCCCCCC		25.0229136822
31PhosphorylationRGTSASHSPRPFRPC
CCCCCCCCCCCCCCC		21.8028889911
42PhosphorylationFRPCADCTCSPGLLS
CCCCCCCCCCCCHHH		19.3019779198
56PhosphorylationSRQGRRASLFLRQLE
HCCCHHHHHHHHHHH		20.1725533186
65PhosphorylationFLRQLENSRRSSSML
HHHHHHHCCHHHHHH		21.5022369663
68PhosphorylationQLENSRRSSSMLLNE
HHHHCCHHHHHHHHH		26.1722369663
69PhosphorylationLENSRRSSSMLLNEL
HHHCCHHHHHHHHHH		20.2522369663
70PhosphorylationENSRRSSSMLLNELK
HHCCHHHHHHHHHHC		18.0722369663
83PhosphorylationLKGAGGGSSAGNGSV
HCCCCCCCCCCCCCE		21.9322369663
84PhosphorylationKGAGGGSSAGNGSVY
CCCCCCCCCCCCCEE		43.3922369663
89PhosphorylationGSSAGNGSVYSCDSL
CCCCCCCCEECCCCC		23.1420377248
91PhosphorylationSAGNGSVYSCDSLCA
CCCCCCEECCCCCEE		12.7920377248
92PhosphorylationAGNGSVYSCDSLCAV
CCCCCEECCCCCEEC		14.8620377248
95PhosphorylationGSVYSCDSLCAVNRE
CCEECCCCCEECCCC		29.6722369663
105PhosphorylationAVNREVNTTDRLLKL
ECCCCCCCHHHHHHH		34.9420377248
106PhosphorylationVNREVNTTDRLLKLR
CCCCCCCHHHHHHHH		17.5821440633
566PhosphorylationGTTDITRTIHLTKPT
CCCCCEEEEEECCCC		12.2322369663
570PhosphorylationITRTIHLTKPTKEEM
CEEEEEECCCCHHHH		22.3322369663
573PhosphorylationTIHLTKPTKEEMDNY
EEEECCCCHHHHCCE		53.2822369663
580PhosphorylationTKEEMDNYTLVLKGG
CHHHHCCEEEEEECC		9.3722369663
581PhosphorylationKEEMDNYTLVLKGGL
HHHHCCEEEEEECCE		19.3522369663
685UbiquitinationLIKKATEKGNFLKFE
EEEEHHHCCCEEEEC		55.5923749301
740AcetylationQPQSISYKWLKRETS
CCCCCCHHHHHCCCC		38.9824489116
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 FRA1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FRA1_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 FRA1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSP72_YEASTSSA2physical
19536198
CG13_YEASTCLN3genetic
20093466
YBY9_YEASTYBR139Wgenetic
20093466
SMY2_YEASTSMY2genetic
20093466
RMD9L_YEASTYBR238Cgenetic
20093466
BSD2_YEASTBSD2genetic
20093466
STE50_YEASTSTE50genetic
20093466
YD176_YEASTYDL176Wgenetic
20093466
KAR_YEASTYDL124Wgenetic
20093466
VAM6_YEASTVAM6genetic
20093466
VPS41_YEASTVPS41genetic
20093466
UBC13_YEASTUBC13genetic
20093466
PPB_YEASTPHO8genetic
20093466
EMI1_YEASTEMI1genetic
20093466
RTF1_YEASTRTF1genetic
20093466
VAM7_YEASTVAM7genetic
20093466
PALF_YEASTRIM8genetic
20093466
YG34_YEASTYGR122Wgenetic
20093466
IMPX_YEASTIMP2genetic
20093466
PTPA1_YEASTRRD1genetic
20093466
SAC1_YEASTSAC1genetic
20093466
DCOR_YEASTSPE1genetic
20093466
IXR1_YEASTIXR1genetic
20093466
RL1D1_YEASTUTP30genetic
20093466
ELO3_YEASTELO3genetic
20093466
MUB1_YEASTMUB1genetic
20093466
RIM13_YEASTRIM13genetic
20093466
SSO2_YEASTSSO2genetic
20093466
YNL5_YEASTYNL115Cgenetic
20093466
MKS1_YEASTMKS1genetic
20093466
IRA2_YEASTIRA2genetic
20093466
DFG16_YEASTDFG16genetic
20093466
SWT1_YEASTSWT1genetic
20093466
GAL4_YEASTGAL4genetic
20093466
ELP3_YEASTELP3genetic
20093466
CCC1_YEASTCCC1genetic
24798331
APC11_YEASTAPC11genetic
27708008
ARPC2_YEASTARC35genetic
27708008
TCPD_YEASTCCT4genetic
27708008
DBF4_YEASTDBF4genetic
27708008
MOB2_YEASTMOB2genetic
27708008
SAD1_YEASTSAD1genetic
27708008
SEC65_YEASTSEC65genetic
27708008
DCP2_YEASTDCP2genetic
27708008
HRP1_YEASTHRP1genetic
27708008
MED10_YEASTNUT2genetic
27708008
RL19A_YEASTRPL19Bgenetic
27708008
RL19B_YEASTRPL19Bgenetic
27708008
BSD2_YEASTBSD2genetic
27708008
STE50_YEASTSTE50genetic
27708008
INO2_YEASTINO2genetic
27708008
SAC3_YEASTSAC3genetic
27708008
UME6_YEASTUME6genetic
27708008
CTU1_YEASTNCS6genetic
27708008
ASK10_YEASTASK10genetic
27708008
CHO2_YEASTCHO2genetic
27708008
PTPA1_YEASTRRD1genetic
27708008
IMPX_YEASTIMP2genetic
27708008
PHO86_YEASTPHO86genetic
27708008
RL14A_YEASTRPL14Agenetic
27708008
IXR1_YEASTIXR1genetic
27708008
DCOR_YEASTSPE1genetic
27708008
MRS4_YEASTMRS4genetic
27708008
POC1_YEASTPBA1genetic
27708008
MUB1_YEASTMUB1genetic
27708008
GID8_YEASTGID8genetic
27708008
MKS1_YEASTMKS1genetic
27708008
YNL5_YEASTYNL115Cgenetic
27708008
YPQ1_YEASTYPQ1genetic
27708008
VPS17_YEASTVPS17genetic
27708008
RKM1_YEASTRKM1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FRA1_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-68; SER-69 AND SER-95,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-56 AND SER-69, AND MASSSPECTROMETRY.

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