YHP7_YEAST - dbPTM
YHP7_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YHP7_YEAST
UniProt AC P38809
Protein Name Uncharacterized protein YHR097C
Gene Name YHR097C
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 366
Subcellular Localization Cytoplasm . Nucleus .
Protein Description
Protein Sequence MNQTGRTIGGPQNGVNTVINPFRVSPSEDRVSSRDETPRNYNNPFLNEDDTRRAHNSSVSNSRQERLPSYEEAAGTPKQQAPYPKEKKRSSGSNSHQHNHHHHRRTSHGHRDKDKQKSKSRTKVKPPKNVDTIDKMDVTGLFGGSFHHDGPFDACTPQRNKNNKVAPVLAFPADGPNNTVGGRTSKKSTLDEVFGRETVDDDSETLNQLQDRAYLFNKANSSTTTLDAIKPNSKNITQFDSKMKTELVHGPITMGLGSTTFLDGAPASSAAIEQDVINHAQESRRKNSIARKKSLPSRRHLQVNNNNLKLVKTHSGHLEQKDVDDNRTSVPVTATQGSGHEDVVKKENTGNKLLRRVKSLKTSKKH
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
7Phosphorylation-MNQTGRTIGGPQNG
-CCCCCCCCCCCCCC		25.8929136822
17PhosphorylationGPQNGVNTVINPFRV
CCCCCCCCEECCCCC		21.9829136822
25PhosphorylationVINPFRVSPSEDRVS
EECCCCCCCCCCCCC		20.6022369663
27PhosphorylationNPFRVSPSEDRVSSR
CCCCCCCCCCCCCCC		44.6222369663
32PhosphorylationSPSEDRVSSRDETPR
CCCCCCCCCCCCCCC		22.1329136822
33PhosphorylationPSEDRVSSRDETPRN
CCCCCCCCCCCCCCC		40.6828889911
57PhosphorylationDTRRAHNSSVSNSRQ
HHHHHHHHCCCCHHH		23.4228889911
58PhosphorylationTRRAHNSSVSNSRQE
HHHHHHHCCCCHHHH		34.5823749301
60PhosphorylationRAHNSSVSNSRQERL
HHHHHCCCCHHHHCC		30.9128889911
62PhosphorylationHNSSVSNSRQERLPS
HHHCCCCHHHHCCCC		28.0323749301
69PhosphorylationSRQERLPSYEEAAGT
HHHHCCCCHHHHCCC		50.1722369663
70PhosphorylationRQERLPSYEEAAGTP
HHHCCCCHHHHCCCC		18.8223749301
76PhosphorylationSYEEAAGTPKQQAPY
CHHHHCCCCCCCCCC		23.6819795423
78UbiquitinationEEAAGTPKQQAPYPK
HHHCCCCCCCCCCCC		55.6823749301
85UbiquitinationKQQAPYPKEKKRSSG
CCCCCCCCCCCCCCC		76.0723749301
87UbiquitinationQAPYPKEKKRSSGSN
CCCCCCCCCCCCCCC		60.6622817900
88UbiquitinationAPYPKEKKRSSGSNS
CCCCCCCCCCCCCCC		59.6122817900
119UbiquitinationDKDKQKSKSRTKVKP
CCCHHCCCCCCCCCC		51.5022817900
123UbiquitinationQKSKSRTKVKPPKNV
HCCCCCCCCCCCCCC		47.3422817900
125UbiquitinationSKSRTKVKPPKNVDT
CCCCCCCCCCCCCCC		58.1022817900
128UbiquitinationRTKVKPPKNVDTIDK
CCCCCCCCCCCCCCC		77.4722817900
135UbiquitinationKNVDTIDKMDVTGLF
CCCCCCCCCCCCEEC		32.9017644757
145PhosphorylationVTGLFGGSFHHDGPF
CCEECCCCCCCCCCC		23.0623749301
156PhosphorylationDGPFDACTPQRNKNN
CCCCCCCCCCCCCCC		24.9523749301
161UbiquitinationACTPQRNKNNKVAPV
CCCCCCCCCCCCCEE		65.1817644757
164UbiquitinationPQRNKNNKVAPVLAF
CCCCCCCCCCEEEEE		49.5217644757
179PhosphorylationPADGPNNTVGGRTSK
ECCCCCCCCCCCCCC		27.4522369663
184PhosphorylationNNTVGGRTSKKSTLD
CCCCCCCCCCCCCHH		48.4422369663
185PhosphorylationNTVGGRTSKKSTLDE
CCCCCCCCCCCCHHH		36.4022369663
186UbiquitinationTVGGRTSKKSTLDEV
CCCCCCCCCCCHHHH		50.5622817900
187UbiquitinationVGGRTSKKSTLDEVF
CCCCCCCCCCHHHHH		48.7323749301
188PhosphorylationGGRTSKKSTLDEVFG
CCCCCCCCCHHHHHC		37.6322369663
189PhosphorylationGRTSKKSTLDEVFGR
CCCCCCCCHHHHHCC		47.2922369663
198PhosphorylationDEVFGRETVDDDSET
HHHHCCCCCCCCHHH		28.0722890988
203PhosphorylationRETVDDDSETLNQLQ
CCCCCCCHHHHHHHH		39.2022890988
205PhosphorylationTVDDDSETLNQLQDR
CCCCCHHHHHHHHHH		34.6521551504
214PhosphorylationNQLQDRAYLFNKANS
HHHHHHHHHHHCCCC		16.8421440633
218UbiquitinationDRAYLFNKANSSTTT
HHHHHHHCCCCCCCC		41.4323749301
221PhosphorylationYLFNKANSSTTTLDA
HHHHCCCCCCCCHHH		33.6422369663
222PhosphorylationLFNKANSSTTTLDAI
HHHCCCCCCCCHHHC		29.5822369663
223PhosphorylationFNKANSSTTTLDAIK
HHCCCCCCCCHHHCC		24.5025521595
224PhosphorylationNKANSSTTTLDAIKP
HCCCCCCCCHHHCCC		27.5825521595
225PhosphorylationKANSSTTTLDAIKPN
CCCCCCCCHHHCCCC		23.8022369663
230UbiquitinationTTTLDAIKPNSKNIT
CCCHHHCCCCCCCCC		39.6123749301
233PhosphorylationLDAIKPNSKNITQFD
HHHCCCCCCCCCCCC		35.2922369663
234UbiquitinationDAIKPNSKNITQFDS
HHCCCCCCCCCCCCH		60.0423749301
242UbiquitinationNITQFDSKMKTELVH
CCCCCCHHHHHEEEC		46.3823749301
244UbiquitinationTQFDSKMKTELVHGP
CCCCHHHHHEEECCC		42.4522817900
245PhosphorylationQFDSKMKTELVHGPI
CCCHHHHHEEECCCE		30.9323749301
258PhosphorylationPITMGLGSTTFLDGA
CEECCCCCCEECCCC		29.3523749301
260PhosphorylationTMGLGSTTFLDGAPA
ECCCCCCEECCCCCC		24.7323749301
288PhosphorylationQESRRKNSIARKKSL
HHHHHHHHHHHHHCC		22.2117287358
294PhosphorylationNSIARKKSLPSRRHL
HHHHHHHCCCCCCEE		48.8520377248
297PhosphorylationARKKSLPSRRHLQVN
HHHHCCCCCCEEEEC		47.4424909858
309UbiquitinationQVNNNNLKLVKTHSG
EECCCCEEEEEECCC		54.0523749301
312UbiquitinationNNNLKLVKTHSGHLE
CCCEEEEEECCCCCC		51.4623749301
313PhosphorylationNNLKLVKTHSGHLEQ
CCEEEEEECCCCCCC		17.5019823750
315PhosphorylationLKLVKTHSGHLEQKD
EEEEEECCCCCCCCC		32.8919823750
321UbiquitinationHSGHLEQKDVDDNRT
CCCCCCCCCCCCCCC		50.7917644757
321AcetylationHSGHLEQKDVDDNRT
CCCCCCCCCCCCCCC		50.7924489116
328PhosphorylationKDVDDNRTSVPVTAT
CCCCCCCCCCCEEEE		40.0922369663
329PhosphorylationDVDDNRTSVPVTATQ
CCCCCCCCCCEEEEC		22.6122369663
333PhosphorylationNRTSVPVTATQGSGH
CCCCCCEEEECCCCC		20.2321440633
335PhosphorylationTSVPVTATQGSGHED
CCCCEEEECCCCCHH		24.8922369663
338PhosphorylationPVTATQGSGHEDVVK
CEEEECCCCCHHHCC		27.4522369663
345UbiquitinationSGHEDVVKKENTGNK
CCCHHHCCCCCHHHH		54.9717644757
346UbiquitinationGHEDVVKKENTGNKL
CCHHHCCCCCHHHHH		44.5817644757
349PhosphorylationDVVKKENTGNKLLRR
HHCCCCCHHHHHHHH		43.1321440633
352UbiquitinationKKENTGNKLLRRVKS
CCCCHHHHHHHHHHH		50.6817644757
359PhosphorylationKLLRRVKSLKTSKKH
HHHHHHHHHHCCCCC		32.0417287358
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 YHP7_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YHP7_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 YHP7_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CYPD_YEASTCPR5physical
16554755
SSB1_YEASTSSB1physical
19536198
KPC1_YEASTPKC1genetic
27708008
PRP6_YEASTPRP6genetic
27708008
APC11_YEASTAPC11genetic
27708008
CDC37_YEASTCDC37genetic
27708008
ACT_YEASTACT1genetic
27708008
PAN1_YEASTPAN1genetic
27708008
KRE9_YEASTKRE9genetic
27708008
SEC23_YEASTSEC23genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YHP7_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-69; THR-189; SER-222;THR-223; THR-313 AND SER-315, 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-25; SER-69; THR-189;SER-221; SER-222 AND THR-223, 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-288; SER-294; SER-297;SER-315 AND SER-359, AND MASS SPECTROMETRY.
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-7; THR-76; THR-205;SER-221 AND THR-223, UBIQUITINATION AT LYS-78; LYS-187 AND LYS-242,AND MASS SPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222 AND THR-224, ANDMASS SPECTROMETRY.
"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 THR-189, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-7; THR-76; THR-205;SER-221 AND THR-223, UBIQUITINATION AT LYS-78; LYS-187 AND LYS-242,AND MASS SPECTROMETRY.

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