FTH1_YEAST - dbPTM
FTH1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FTH1_YEAST
UniProt AC P38310
Protein Name Iron transporter FTH1
Gene Name FTH1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 465
Subcellular Localization Vacuole membrane
Multi-pass membrane protein .
Protein Description High affinity iron transporter probably involved in transport of intravacuolar stores of iron..
Protein Sequence MAFEDYFSFQIFFIFLRESLEIVVIVSILLTIVKQGLSVEDDSPFEGSSSSAGLPSPNTNTNADSTTAFLQAGPSDGNAIGTSATAANNKSRPLNVEEEEEIYEYSNELRDQDRESDEHTADNVKLYQKLKIQILAGGAFGLLLCMLIGGAFVSIFYHIGTDLWTLSEHYYEGVLSLVASVIISVMGLFFLRMGKLREKFRVKLASIIYSKDNNLLGNKTQKGVKFSEKYSFFILPFITTLREGLEAVVFIGGIGIDQPLSSIPLSMVLATAISTVFGIFFFRYSSSLSLKICLVVATCFLYLIAAGLFSKGVWQLELQDYVNKCNGQDMSEVGNGPGSYDISRSVWHVNCCNGEKDGGWMIFTAIFGWTNSATVGSVISYNAYWLVLICALKLLMIEEKYGYIPYLPISWQKKRIMKRLSIAKASLDLKHHTSELNSSTSEPDSQRRSKDSSVPLIIDSSGSAN
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
6Phosphorylation--MAFEDYFSFQIFF
--CCHHHCHHHHHHH		8.2330377154
8PhosphorylationMAFEDYFSFQIFFIF
CCHHHCHHHHHHHHH		15.2630377154
116PhosphorylationLRDQDRESDEHTADN
HHCCCCCCCCCCHHH		49.5525005228
120PhosphorylationDRESDEHTADNVKLY
CCCCCCCCHHHHHHH		33.3930377154
211UbiquitinationLASIIYSKDNNLLGN
HHHHHCCCCCCCCCC		47.7223749301
219UbiquitinationDNNLLGNKTQKGVKF
CCCCCCCCCCCCCCC		51.0023749301
222UbiquitinationLLGNKTQKGVKFSEK
CCCCCCCCCCCCCHH		71.5422817900
225UbiquitinationNKTQKGVKFSEKYSF
CCCCCCCCCCHHHCE		52.4122817900
285PhosphorylationGIFFFRYSSSLSLKI
HHHHHHHCCCCHHHH		14.8117563356
287PhosphorylationFFFRYSSSLSLKICL
HHHHHCCCCHHHHHH		18.9417563356
433PhosphorylationSLDLKHHTSELNSST
HHHHHHHHHHCCCCC		24.5024961812
434PhosphorylationLDLKHHTSELNSSTS
HHHHHHHHHCCCCCC		35.4119823750
438PhosphorylationHHTSELNSSTSEPDS
HHHHHCCCCCCCCCH		47.8419823750
439PhosphorylationHTSELNSSTSEPDSQ
HHHHCCCCCCCCCHH		34.5719823750
440PhosphorylationTSELNSSTSEPDSQR
HHHCCCCCCCCCHHH		36.6119779198
441PhosphorylationSELNSSTSEPDSQRR
HHCCCCCCCCCHHHC		49.4329136822
445PhosphorylationSSTSEPDSQRRSKDS
CCCCCCCHHHCCCCC		35.9821551504
449PhosphorylationEPDSQRRSKDSSVPL
CCCHHHCCCCCCCCE		42.9022369663
450UbiquitinationPDSQRRSKDSSVPLI
CCHHHCCCCCCCCEE		60.8723749301
452PhosphorylationSQRRSKDSSVPLIID
HHHCCCCCCCCEEEC		36.6522369663
453PhosphorylationQRRSKDSSVPLIIDS
HHCCCCCCCCEEECC		37.5822369663
460PhosphorylationSVPLIIDSSGSAN--
CCCEEECCCCCCC--		26.6229688323
461PhosphorylationVPLIIDSSGSAN---
CCEEECCCCCCC---		32.7829688323
463PhosphorylationLIIDSSGSAN-----
EEECCCCCCC-----		26.9623749301
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 FTH1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FTH1_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 FTH1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ADH1_YEASTADH1physical
11805826
FET5_YEASTFET5physical
11805826
FKS1_YEASTFKS1physical
11805826
GEA2_YEASTGEA2physical
11805826
IMB4_YEASTKAP123physical
11805826
RPN3_YEASTRPN3physical
11805826
KEX2_YEASTKEX2physical
18467557
COT1_YEASTCOT1physical
18467557
ATG27_YEASTATG27physical
18467557
VATF_YEASTVMA7physical
18467557
VAC8_YEASTVAC8physical
18467557
MRL1_YEASTMRL1physical
18467557
EMP47_YEASTEMP47physical
18467557
FET5_YEASTFET5physical
18467557
FTH1_YEASTFTH1physical
18467557
ATC2_YEASTPMC1physical
18467557
YPQ2_YEASTYPQ2physical
18467557
VPS35_YEASTVPS35physical
18467557
YD199_YEASTYDL199Cphysical
18467557
ATC5_YEASTDNF1physical
18467557
YBT1_YEASTYBT1physical
18467557
YMB8_YEASTYML018Cphysical
18467557
HXT1_YEASTHXT1physical
18467557
VATD_YEASTVMA8physical
18467557
MEH1_YEASTMEH1physical
18467557
GTR2_YEASTGTR2physical
18467557
SNA4_YEASTSNA4physical
18467557
KEX1_YEASTKEX1physical
18467557
DPP1_YEASTDPP1physical
18467557
VATH_YEASTVMA13physical
18467557
SYG1_YEASTSYG1physical
18467557
TVP15_YEASTTVP15physical
18467557
CTR2_YEASTCTR2physical
18467557
VPH1_YEASTVPH1physical
18467557
DOP1_YEASTDOP1physical
18467557
VPS64_YEASTVPS64genetic
20526336
SLT2_YEASTSLT2genetic
20526336
RV161_YEASTRVS161genetic
20526336
VPS33_YEASTVPS33genetic
20526336
RTG3_YEASTRTG3genetic
20526336
YPT7_YEASTYPT7genetic
20526336
SRN2_YEASTSRN2genetic
20526336
VPS13_YEASTVPS13genetic
20526336
SST2_YEASTSST2genetic
20526336
KEX2_YEASTKEX2physical
22615397
RHO3_YEASTRHO3genetic
23891562
SGF29_YEASTSGF29genetic
27708008
GPR1_YEASTGPR1genetic
27708008
PFD3_YEASTPAC10genetic
27708008
VMA21_YEASTVMA21genetic
27708008
ELM1_YEASTELM1genetic
27708008
ERG3_YEASTERG3genetic
27708008
PKR1_YEASTPKR1genetic
27708008
2A5D_YEASTRTS1genetic
27708008
STI1_YEASTSTI1genetic
27708008
NEW1_YEASTNEW1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FTH1_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-449 AND SER-453, ANDMASS 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-285 AND SER-287, ANDMASS SPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-449, AND MASSSPECTROMETRY.

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