ATC5_YEAST - dbPTM
ATC5_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATC5_YEAST
UniProt AC P32660
Protein Name Phospholipid-transporting ATPase DNF1
Gene Name DNF1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1571
Subcellular Localization Cell membrane
Multi-pass membrane protein . Endosome membrane
Multi-pass membrane protein . Golgi apparatus, trans-Golgi network membrane
Multi-pass membrane protein .
Protein Description This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of phospholipids..
Protein Sequence MSGTFHGDGHAPMSPFEDTFQFEDNSSNEDTHIAPTHFDDGATSNKYSRPQVSFNDETPKNKREDAEEFTFNDDTEYDNHSFQPTPKLNNGSGTFDDVELDNDSGEPHTNYDGMKRFRMGTKRNKKGNPIMGRSKTLKWARKNIPNPFEDFTKDDIDPGAINRAQELRTVYYNMPLPKDMIDEEGNPIMQYPRNKIRTTKYTPLTFLPKNILFQFHNFANVYFLVLIILGAFQIFGVTNPGLSAVPLVVIVIITAIKDAIEDSRRTVLDLEVNNTKTHILEGVENENVSTDNISLWRRFKKANSRLLFKFIQYCKEHLTEEGKKKRMQRKRHELRVQKTVGTSGPRSSLDSIDSYRVSADYGRPSLDYDNLEQGAGEANIVDRSLPPRTDCKFAKNYWKGVKVGDIVRIHNNDEIPADIILLSTSDTDGACYVETKNLDGETNLKVRQSLKCTNTIRTSKDIARTKFWIESEGPHSNLYTYQGNMKWRNLADGEIRNEPITINNVLLRGCTLRNTKWAMGVVMFTGGDTKIMLNSGITPTKKSRISRELNFSVVINFVLLFILCFVSGIANGVYYDKKGRSRFSYEFGTIAGSAATNGFVSFWVAVILYQSLVPISLYISVEIIKTAQAAFIYGDVLLYNAKLDYPCTPKSWNISDDLGQVEYIFSDKTGTLTQNVMEFKKCTINGVSYGRAYTEALAGLRKRQGIDVETEGRREKAEIAKDRDTMIDELRALSGNSQFYPEEVTFVSKEFVRDLKGASGEVQQRCCEHFMLALALCHSVLVEANPDNPKKLDLKAQSPDEAALVATARDVGFSFVGKTKKGLIIEMQGIQKEFEILNILEFNSSRKRMSCIVKIPGLNPGDEPRALLICKGADSIIYSRLSRQSGSNSEAILEKTALHLEQYATEGLRTLCIAQRELSWSEYEKWNEKYDIAAASLANREDELEVVADSIERELILLGGTAIEDRLQDGVPDCIELLAEAGIKLWVLTGDKVETAINIGFSCNLLNNEMELLVIKTTGDDVKEFGSEPSEIVDALLSKYLKEYFNLTGSEEEIFEAKKDHEFPKGNYAIVIDGDALKLALYGEDIRRKFLLLCKNCRAVLCCRVSPSQKAAVVKLVKDSLDVMTLAIGDGSNDVAMIQSADVGIGIAGEEGRQAVMCSDYAIGQFRYLARLVLVHGRWSYKRLAEMIPEFFYKNMIFALALFWYGIYNDFDGSYLYEYTYMMFYNLAFTSLPVIFLGILDQDVNDTISLVVPQLYRVGILRKEWNQRKFLWYMLDGLYQSIICFFFPYLVYHKNMIVTSNGLGLDHRYFVGVYVTTIAVISCNTYVLLHQYRWDWFSGLFIALSCLVVFAWTGIWSSAIASREFFKAAARIYGAPSFWAVFFVAVLFCLLPRFTYDSFQKFFYPTDVEIVREMWQHGHFDHYPPGYDPTDPNRPKVTKAGQHGEKIIEGIALSDNLGGSNYSRDSVVTEEIPMTFMHGEDGSPSGYQKQETWMTSPKETQDLLQSPQFQQAQTFGRGPSTNVRSSLDRTREQMIATNQLDNRYSVERARTSLDLPGVTNAASLIGTQQNN
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
2Phosphorylation------MSGTFHGDG
------CCCCCCCCC		58.8219823750
4Phosphorylation----MSGTFHGDGHA
----CCCCCCCCCCC		23.0419823750
14PhosphorylationGDGHAPMSPFEDTFQ
CCCCCCCCCCCCCEE		25.9419823750
19PhosphorylationPMSPFEDTFQFEDNS
CCCCCCCCEECCCCC		16.4919823750
26PhosphorylationTFQFEDNSSNEDTHI
CEECCCCCCCCCCEE		47.0319823750
27PhosphorylationFQFEDNSSNEDTHIA
EECCCCCCCCCCEEC		50.9619823750
31PhosphorylationDNSSNEDTHIAPTHF
CCCCCCCCEECCCCC		14.7019823750
36PhosphorylationEDTHIAPTHFDDGAT
CCCEECCCCCCCCCC		26.5919823750
43PhosphorylationTHFDDGATSNKYSRP
CCCCCCCCCCCCCCC		38.0619823750
44PhosphorylationHFDDGATSNKYSRPQ
CCCCCCCCCCCCCCC		30.6919823750
47PhosphorylationDGATSNKYSRPQVSF
CCCCCCCCCCCCCCC		17.7327717283
48PhosphorylationGATSNKYSRPQVSFN
CCCCCCCCCCCCCCC		38.8127717283
53PhosphorylationKYSRPQVSFNDETPK
CCCCCCCCCCCCCCC		17.0622369663
58PhosphorylationQVSFNDETPKNKRED
CCCCCCCCCCCHHHC		42.2922369663
62UbiquitinationNDETPKNKREDAEEF
CCCCCCCHHHCCHHC		64.3924961812
70PhosphorylationREDAEEFTFNDDTEY
HHCCHHCCCCCCCCC		25.4728889911
75PhosphorylationEFTFNDDTEYDNHSF
HCCCCCCCCCCCCCC		39.0328889911
77PhosphorylationTFNDDTEYDNHSFQP
CCCCCCCCCCCCCCC		24.9219823750
81PhosphorylationDTEYDNHSFQPTPKL
CCCCCCCCCCCCCCC		31.6517330950
85PhosphorylationDNHSFQPTPKLNNGS
CCCCCCCCCCCCCCC		23.4417330950
92PhosphorylationTPKLNNGSGTFDDVE
CCCCCCCCCCCCCEE		36.4622369663
94PhosphorylationKLNNGSGTFDDVELD
CCCCCCCCCCCEEEC		26.1122369663
104PhosphorylationDVELDNDSGEPHTNY
CEEECCCCCCCCCCC		51.8422369663
109PhosphorylationNDSGEPHTNYDGMKR
CCCCCCCCCCCCCHH		46.3020377248
111PhosphorylationSGEPHTNYDGMKRFR
CCCCCCCCCCCHHHC		18.2820377248
338UbiquitinationRHELRVQKTVGTSGP
HHHHHHHHCCCCCCC		42.1723749301
347PhosphorylationVGTSGPRSSLDSIDS
CCCCCCCHHCCCHHE		38.0828889911
348PhosphorylationGTSGPRSSLDSIDSY
CCCCCCHHCCCHHEE		37.1619779198
351PhosphorylationGPRSSLDSIDSYRVS
CCCHHCCCHHEEECC		33.3228889911
354PhosphorylationSSLDSIDSYRVSADY
HHCCCHHEEECCCCC		17.1119779198
355PhosphorylationSLDSIDSYRVSADYG
HCCCHHEEECCCCCC		15.9919779198
358PhosphorylationSIDSYRVSADYGRPS
CHHEEECCCCCCCCC		13.3628889911
361PhosphorylationSYRVSADYGRPSLDY
EEECCCCCCCCCCCC		18.1022369663
365PhosphorylationSADYGRPSLDYDNLE
CCCCCCCCCCCCCCC		32.2922369663
368PhosphorylationYGRPSLDYDNLEQGA
CCCCCCCCCCCCCCC		16.4222369663
541MethylationNSGITPTKKSRISRE
CCCCCCCCCHHHCHH		50.3720137074
681UbiquitinationQNVMEFKKCTINGVS
HHHCCCCCCEECCEE		41.7623749301
734PhosphorylationIDELRALSGNSQFYP
HHHHHHHHCCCCCCH		34.6422369663
737PhosphorylationLRALSGNSQFYPEEV
HHHHHCCCCCCHHHE		25.7822369663
740PhosphorylationLSGNSQFYPEEVTFV
HHCCCCCCHHHEEEE		11.3322369663
756UbiquitinationKEFVRDLKGASGEVQ
HHHHHHHCCCCHHHH		57.6423749301
871UbiquitinationPRALLICKGADSIIY
CCEEEEECCCCHHHH		50.5723749301
1023UbiquitinationKTTGDDVKEFGSEPS
EECCCHHHHHCCCHH		55.0824961812
1027PhosphorylationDDVKEFGSEPSEIVD
CHHHHHCCCHHHHHH		52.2120377248
1030PhosphorylationKEFGSEPSEIVDALL
HHHCCCHHHHHHHHH		35.5820377248
1038PhosphorylationEIVDALLSKYLKEYF
HHHHHHHHHHHHHHH		21.8020377248
1120PhosphorylationVVKLVKDSLDVMTLA
HHHHHHHCCCEEEEE		22.2827017623
1125PhosphorylationKDSLDVMTLAIGDGS
HHCCCEEEEEECCCC		16.9427017623
1132PhosphorylationTLAIGDGSNDVAMIQ
EEEECCCCCCEEEEE		34.3027017623
1454PhosphorylationIIEGIALSDNLGGSN
EEEEEEECCCCCCCC		18.5421440633
1460PhosphorylationLSDNLGGSNYSRDSV
ECCCCCCCCCCCCCC		30.6921440633
1462PhosphorylationDNLGGSNYSRDSVVT
CCCCCCCCCCCCCCC		13.5419779198
1463PhosphorylationNLGGSNYSRDSVVTE
CCCCCCCCCCCCCCE		33.5820377248
1466PhosphorylationGSNYSRDSVVTEEIP
CCCCCCCCCCCEECC		19.8521551504
1469PhosphorylationYSRDSVVTEEIPMTF
CCCCCCCCEECCCEE		26.2420377248
1475PhosphorylationVTEEIPMTFMHGEDG
CCEECCCEEEECCCC		16.6821440633
1483PhosphorylationFMHGEDGSPSGYQKQ
EEECCCCCCCCCCCC		28.3720377248
1485PhosphorylationHGEDGSPSGYQKQET
ECCCCCCCCCCCCCC		52.4022369663
1487PhosphorylationEDGSPSGYQKQETWM
CCCCCCCCCCCCCCC		19.5122369663
1492PhosphorylationSGYQKQETWMTSPKE
CCCCCCCCCCCCCHH		20.3119779198
1495PhosphorylationQKQETWMTSPKETQD
CCCCCCCCCCHHHHH		33.1828889911
1496PhosphorylationKQETWMTSPKETQDL
CCCCCCCCCHHHHHH		20.1925521595
1498UbiquitinationETWMTSPKETQDLLQ
CCCCCCCHHHHHHHH		73.4923749301
1500PhosphorylationWMTSPKETQDLLQSP
CCCCCHHHHHHHHCH		33.2428132839
1506PhosphorylationETQDLLQSPQFQQAQ
HHHHHHHCHHHHHHH		22.1917330950
1520PhosphorylationQTFGRGPSTNVRSSL
HHHCCCCCCCHHHHC		35.1223749301
1521PhosphorylationTFGRGPSTNVRSSLD
HHCCCCCCCHHHHCH		40.6522369663
1525PhosphorylationGPSTNVRSSLDRTRE
CCCCCHHHHCHHHHH		30.8522369663
1526PhosphorylationPSTNVRSSLDRTREQ
CCCCHHHHCHHHHHH		24.5922369663
1537PhosphorylationTREQMIATNQLDNRY
HHHHHHHHHCCCCCC		16.7522369663
1544PhosphorylationTNQLDNRYSVERART
HHCCCCCCCHHHHHH		24.2722369663
1545PhosphorylationNQLDNRYSVERARTS
HCCCCCCCHHHHHHC		17.7922369663
1551PhosphorylationYSVERARTSLDLPGV
CCHHHHHHCCCCCCC		32.4322369663
1552PhosphorylationSVERARTSLDLPGVT
CHHHHHHCCCCCCCC		17.8422369663
1559PhosphorylationSLDLPGVTNAASLIG
CCCCCCCCCHHHHHC		25.6722369663
1563PhosphorylationPGVTNAASLIGTQQN
CCCCCHHHHHCCCCC		20.3622369663
1567PhosphorylationNAASLIGTQQNN---
CHHHHHCCCCCC---		21.7122369663
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 ATC5_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATC5_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 ATC5_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATC4_YEASTDNF2genetic
12631737
LEM3_YEASTLEM3physical
16600184
SEC6_YEASTSEC6physical
18467557
PIN2_YEASTPIN2physical
18467557
AP18B_YEASTYAP1802physical
18467557
CHS5_YEASTCHS5physical
18467557
LSB3_YEASTLSB3physical
18467557
SMI1_YEASTSMI1physical
18467557
ATC5_YEASTDNF1physical
18467557
LEM3_YEASTLEM3physical
18467557
KEX1_YEASTKEX1physical
18467557
ATC4_YEASTDNF2genetic
18931395
ATC4_YEASTDNF2genetic
19452121
PDR10_YEASTPDR10genetic
19452121
KES1_YEASTKES1genetic
19403696
TCB3_YEASTTCB3physical
19968326
ATC4_YEASTDNF2genetic
16600184
EMP24_YEASTEMP24physical
16093310
RV161_YEASTRVS161genetic
20526336
ATC4_YEASTDNF2genetic
22344035
LEM3_YEASTLEM3physical
15090616
ATC4_YEASTDNF2genetic
23250744
LEM3_YEASTLEM3physical
22791719
SRO7_YEASTSRO7genetic
23891562
SEC1_YEASTSEC1genetic
23891562
BPH1_YEASTBPH1genetic
23891562
PSS_YEASTCHO1genetic
24390140
PSD2_YEASTPSD2genetic
24390140
ATC3_YEASTDRS2genetic
25378585
ATC8_YEASTDNF3genetic
25378585
ATC4_YEASTDNF2genetic
25378585
CG11_YEASTCLN1genetic
25378585
CG13_YEASTCLN3genetic
25378585
APC11_YEASTAPC11genetic
27708008
MAK21_YEASTMAK21genetic
27708008
PRP28_YEASTPRP28genetic
27708008
MOB2_YEASTMOB2genetic
27708008
UTP9_YEASTUTP9genetic
27708008
NU192_YEASTNUP192genetic
27708008
PRP21_YEASTPRP21genetic
27708008
GRC3_YEASTGRC3genetic
27708008
PRP19_YEASTPRP19genetic
27708008
CDC42_YEASTCDC42genetic
27708008
SEC65_YEASTSEC65genetic
27708008
GPI12_YEASTGPI12genetic
27708008
NOP2_YEASTNOP2genetic
27708008
SEC62_YEASTSEC62genetic
27708008
PSB5_YEASTPRE2genetic
27708008
ART5_YEASTART5genetic
25781026
ITR1_YEASTITR1genetic
25781026
ITR2_YEASTITR2genetic
25781026
PSS_YEASTCHO1genetic
25781026
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ATC5_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-53; THR-58; TYR-77;SER-81; THR-94; SER-347; SER-351; SER-365; SER-1460; SER-1483;SER-1506; SER-1545; THR-1551 AND SER-1552, 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-53; SER-92 AND SER-365,AND MASS 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-53, 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-81; THR-85 AND SER-1506,AND MASS SPECTROMETRY.

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