YSC84_YEAST - dbPTM
YSC84_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YSC84_YEAST
UniProt AC P32793
Protein Name Protein YSC84
Gene Name YSC84
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 468
Subcellular Localization Cytoplasm, cytoskeleton, actin patch . Cortical actin patches.
Protein Description Essential for the organization of the actin cytoskeleton, fluid phase endocytosis and vesicle trafficking, together with LSB5..
Protein Sequence MGINNPIPRSLKSETKKAAKVLRSFVKPNQVFGADQVIPPYVLKRAKGLAIITVLKAGFLFSGRAGSGVIVARLKDGTWSAPSAIAMAGAGAGGMVGVELTDFVFILNSEEAVRSFSEFGTITLGGNVSVSAGPLGRSAEAAASASTGGVSAVFAYSKSKGLFAGVSVEGSAILERREANRKFYGDNCTSKMILSGRVKVPPAADPLLRILESRAFNFTRHDHDDNASGDDFYDDGQYSDNTSHYYDDIPDSFDSTDESSTRPNTRSSRRRGMSLGSRSRYDDDYDDDGYGRGRGYGDFDSEDEDYDYGRSPNRNSSRNRGPQIDRGTKPRANTRWEDDLYDRDTEYSRPNHSGRDYDNTRGNRRGYGRERGYSLGHGPTHPSNMSNVDDLSHKMSKTGLGNESTATNSATPTAVALYNFAGEQPGDLAFKKGDVITILKKSDSQNDWWTGRTNGKEGIFPANYVRVS
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
62PhosphorylationLKAGFLFSGRAGSGV
EECCEEECCCCCCCE		29.5328889911
182AcetylationERREANRKFYGDNCT
CHHHHHHCCCCCCCC		42.6225381059
190PhosphorylationFYGDNCTSKMILSGR
CCCCCCCCCEEEECC		23.5621440633
195PhosphorylationCTSKMILSGRVKVPP
CCCCEEEECCCCCCC		17.3921440633
199UbiquitinationMILSGRVKVPPAADP
EEEECCCCCCCCCCH		47.8923749301
274PhosphorylationSSRRRGMSLGSRSRY
HHHHCCCCCCCCCCC		32.1921082442
277PhosphorylationRRGMSLGSRSRYDDD
HCCCCCCCCCCCCCC		32.1629136822
279PhosphorylationGMSLGSRSRYDDDYD
CCCCCCCCCCCCCCC		36.5724930733
296PhosphorylationGYGRGRGYGDFDSED
CCCCCCCCCCCCCCC		16.5022890988
301PhosphorylationRGYGDFDSEDEDYDY
CCCCCCCCCCCCCCC		47.1122369663
306PhosphorylationFDSEDEDYDYGRSPN
CCCCCCCCCCCCCCC		14.7122890988
308PhosphorylationSEDEDYDYGRSPNRN
CCCCCCCCCCCCCCC		14.2822369663
311PhosphorylationEDYDYGRSPNRNSSR
CCCCCCCCCCCCCCC		23.3622369663
316PhosphorylationGRSPNRNSSRNRGPQ
CCCCCCCCCCCCCCC		27.6929136822
317PhosphorylationRSPNRNSSRNRGPQI
CCCCCCCCCCCCCCC		36.8029136822
373PhosphorylationGYGRERGYSLGHGPT
CCCCCCCCCCCCCCC		13.6217330950
374PhosphorylationYGRERGYSLGHGPTH
CCCCCCCCCCCCCCC		30.6017330950
380PhosphorylationYSLGHGPTHPSNMSN
CCCCCCCCCCCCCCC		51.5229136822
383PhosphorylationGHGPTHPSNMSNVDD
CCCCCCCCCCCCHHH		37.2429136822
386PhosphorylationPTHPSNMSNVDDLSH
CCCCCCCCCHHHHHH		37.6429136822
413PhosphorylationATNSATPTAVALYNF
CCCCCCCCEEHHHCC		29.4327214570
437PhosphorylationFKKGDVITILKKSDS
ECCCCEEEEEECCCC		21.8019795423
442PhosphorylationVITILKKSDSQNDWW
EEEEEECCCCCCCCC		40.6919779198
444PhosphorylationTILKKSDSQNDWWTG
EEEECCCCCCCCCCC		37.6627214570
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 YSC84_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YSC84_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 YSC84_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GFD1_YEASTGFD1physical
10688190
SLA1_YEASTSLA1physical
10688190
HUA1_YEASTHUA1physical
10688190
GPN3_YEASTGPN3physical
10688190
AIM3_YEASTAIM3physical
14737190
ERT1_YEASTERT1physical
14737190
BSP1_YEASTBSP1physical
14737190
ENG2_YEASTACF2physical
14737190
ACF4_YEASTACF4physical
14737190
LAS17_YEASTLAS17physical
14737190
GYL1_YEASTGYL1physical
14737190
ENG2_YEASTACF2physical
11743162
GYL1_YEASTGYL1physical
11743162
MMS4_YEASTMMS4physical
11743162
HUA1_YEASTHUA1physical
11743162
ACF4_YEASTACF4physical
11743162
PER33_YEASTPER33physical
11743162
APP1_YEASTAPP1physical
11743162
HUA2_YEASTHUA2physical
11743162
RBD2_YEASTRBD2physical
11743162
BSP1_YEASTBSP1physical
11743162
KTR3_YEASTKTR3physical
11743162
SNA3_YEASTSNA3physical
11743162
SYS1_YEASTSYS1physical
11743162
GMH1_YEASTGMH1physical
11743162
LAS17_YEASTLAS17physical
11743162
LAS17_YEASTLAS17physical
10512884
LSB5_YEASTLSB5genetic
12388763
YSC84_YEASTYSC84physical
18467557
LAS17_YEASTLAS17physical
18467557
CUE5_YEASTCUE5physical
18467557
LDB17_YEASTLDB17physical
19506040
ABP1_YEASTABP1physical
19841731
ENG2_YEASTACF2physical
19841731
ACF4_YEASTACF4physical
19841731
APP1_YEASTAPP1physical
19841731
BSP1_YEASTBSP1physical
19841731
ATU2_YEASTCCC2physical
19841731
CDC6_YEASTCDC6physical
19841731
XPO1_YEASTCRM1physical
19841731
CUE5_YEASTCUE5physical
19841731
ALG10_YEASTDIE2physical
19841731
ECM25_YEASTECM25physical
19841731
END3_YEASTEND3physical
19841731
ENT1_YEASTENT1physical
19841731
GYL1_YEASTGYL1physical
19841731
GYP5_YEASTGYP5physical
19841731
HAP4_YEASTHAP4physical
19841731
HUA2_YEASTHUA2physical
19841731
INP53_YEASTINP53physical
19841731
LAS17_YEASTLAS17physical
19841731
LDB17_YEASTLDB17physical
19841731
LSB5_YEASTLSB5physical
19841731
MYO3_YEASTMYO3physical
19841731
MYO5_YEASTMYO5physical
19841731
NHP6A_YEASTNHP6Aphysical
19841731
SEC8_YEASTSEC8physical
19841731
SLA1_YEASTSLA1physical
19841731
SPO75_YEASTSPO75physical
19841731
SRL1_YEASTSRL1physical
19841731
STP22_YEASTSTP22physical
19841731
TGL3_YEASTTGL3physical
19841731
UBP7_YEASTUBP7physical
19841731
YBP2_YEASTYBP2physical
19841731
AIM3_YEASTAIM3physical
19841731
ERT1_YEASTERT1physical
19841731
TDA5_YEASTTDA5physical
19841731
ACBP_YEASTACB1physical
19841731
ATG3_YEASTATG3physical
19841731
2ABA_YEASTCDC55physical
19841731
DIG2_YEASTDIG2physical
19841731
ENT2_YEASTENT2physical
19841731
EXG2_YEASTEXG2physical
19841731
SYG2_YEASTGRS2physical
19841731
GTS1_YEASTGTS1physical
19841731
HUA1_YEASTHUA1physical
19841731
MET31_YEASTMET31physical
19841731
SA155_YEASTSAP155physical
19841731
SYP1_YEASTSYP1physical
19841731
TVP15_YEASTTVP15physical
19841731
WWM1_YEASTWWM1physical
19841731
AP18B_YEASTYAP1802physical
19841731
LSB3_YEASTLSB3genetic
19158382
ACT_YEASTACT1physical
19158382
DCOR_YEASTSPE1genetic
20093466
RL22A_YEASTRPL22Agenetic
20093466
ADE_YEASTAAH1genetic
20093466
YSC84_YEASTYSC84physical
22615397
LAS17_YEASTLAS17physical
26312755
ODO2_YEASTKGD2genetic
27708008
MTHR2_YEASTMET13genetic
27708008
SUT1_YEASTSUT1genetic
27708008
DCOR_YEASTSPE1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YSC84_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-301; SER-311 ANDSER-374, 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-301 AND SER-374, 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 SER-301, AND MASSSPECTROMETRY.
"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-301, AND MASSSPECTROMETRY.

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