SAS10_YEAST - dbPTM
SAS10_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SAS10_YEAST
UniProt AC Q12136
Protein Name Something about silencing protein 10
Gene Name SAS10
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 610
Subcellular Localization Nucleus, nucleolus .
Protein Description Primarily required at the G2/M phase. Essential for viability: involved in nucleolar processing of pre-18S ribosomal RNA as part of the ribosomal small subunit (SSU) processome..
Protein Sequence MVRKGSNRTKTSEVGDEINPYGLNEVDDFASKREKVLLGQSTFGDSNKDDDHSLLEDEDEEEVLAMDEDDESIDEREDEEEEEEEELDGAAAYKKIFGRNLETDQLPEEDEENGMLDNENAWGSTKGEYYGADDLDDDEAAKEIEKEALRQQKKHLEELNMNDYLDEEEEEEWVKSAKEFDMGEFKNSTKQADTKTSITDILNMDDEARDNYLRTMFPEFAPLSKEFTELAPKFDELKKSEENEFNKLKLIALGSYLGTISCYYSILLHELHNNEDFTSMKGHPVMEKILTTKEIWRQASELPSSFDVNEGDGSESEETANIEAFNEKKLNELQNSEDSDAEDGGKQKQEIDEEERESDEEEEEEDVDIDDFEEYVAQSRLHSKPKTSSMPEADDFIESEIADVDAQDKKARRRTLRFYTSKIDQQENKKTDRFKGDDDIPYKERLFERQQRLLDEARKRGMHDNNGADLDDKDYGSEDEAVSRSINTQGENDYYQQVQRGKQDKKISRKEAHKNAVIAAREGKLAELAENVSGDGKRAINYQILKNKGLTPKRNKDNRNSRVKKRKKYQKAQKKLKSVRAVYSGGQSGVYEGEKTGIKKGLTRSVKFKN
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
9PhosphorylationVRKGSNRTKTSEVGD
CCCCCCCCCCCCCCC		42.8127017623
10AcetylationRKGSNRTKTSEVGDE
CCCCCCCCCCCCCCC		46.9823572591
11PhosphorylationKGSNRTKTSEVGDEI
CCCCCCCCCCCCCCC		29.5219779198
12PhosphorylationGSNRTKTSEVGDEIN
CCCCCCCCCCCCCCC		31.6617330950
32AcetylationEVDDFASKREKVLLG
CHHHHHHHHHHHEEC		62.2324489116
46PhosphorylationGQSTFGDSNKDDDHS
CCCCCCCCCCCCCCC		46.2728889911
53PhosphorylationSNKDDDHSLLEDEDE
CCCCCCCCCCCCCCH		41.4628889911
72PhosphorylationAMDEDDESIDEREDE
CCCCCCCCCCHHCHH		42.1928889911
125PhosphorylationNENAWGSTKGEYYGA
CCCCCCCCCCCCCCC		38.8521551504
146AcetylationEAAKEIEKEALRQQK
HHHHHHHHHHHHHHH		54.6824489116
178AcetylationEEWVKSAKEFDMGEF
HHHHHHHHHCCHHHH		67.0424489116
196PhosphorylationTKQADTKTSITDILN
CCCCCCCCCHHHHHC		27.7027017623
197PhosphorylationKQADTKTSITDILNM
CCCCCCCCHHHHHCC		25.6627017623
212PhosphorylationDDEARDNYLRTMFPE
CHHHHHHHHHHHCHH		11.2327017623
225UbiquitinationPEFAPLSKEFTELAP
HHHHHCCHHHHHHHH		65.6124961812
233AcetylationEFTELAPKFDELKKS
HHHHHHHHHHHHHHH		60.9024489116
238AcetylationAPKFDELKKSEENEF
HHHHHHHHHHHCCCC		52.8124489116
288AcetylationKGHPVMEKILTTKEI
CCCHHHHHHHHHHHH		25.5624489116
293AcetylationMEKILTTKEIWRQAS
HHHHHHHHHHHHHHH		41.8024489116
293UbiquitinationMEKILTTKEIWRQAS
HHHHHHHHHHHHHHH		41.8024961812
300PhosphorylationKEIWRQASELPSSFD
HHHHHHHHHCCCCCC		31.1822369663
304PhosphorylationRQASELPSSFDVNEG
HHHHHCCCCCCCCCC		57.1522369663
305PhosphorylationQASELPSSFDVNEGD
HHHHCCCCCCCCCCC		24.4322369663
314PhosphorylationDVNEGDGSESEETAN
CCCCCCCCCCHHHHC		42.5622369663
316PhosphorylationNEGDGSESEETANIE
CCCCCCCCHHHHCHH		42.2922369663
319PhosphorylationDGSESEETANIEAFN
CCCCCHHHHCHHHHC		22.4322369663
336PhosphorylationKLNELQNSEDSDAED
HHHHHHCCCCCCCCC		29.8022369663
339PhosphorylationELQNSEDSDAEDGGK
HHHCCCCCCCCCCCH		34.3722369663
358PhosphorylationIDEEERESDEEEEEE
CCHHHHHCCHHHHHH		57.4528132839
409AcetylationADVDAQDKKARRRTL
CCCCCCCHHHHHHHH		35.9324489116
421PhosphorylationRTLRFYTSKIDQQEN
HHHHHHHHCCCHHHC		19.0830377154
422AcetylationTLRFYTSKIDQQENK
HHHHHHHCCCHHHCC		42.3724489116
435AcetylationNKKTDRFKGDDDIPY
CCCCCCCCCCCCCCH		63.4225381059
475PhosphorylationADLDDKDYGSEDEAV
CCCCCCCCCCHHHHH		28.4325521595
477PhosphorylationLDDKDYGSEDEAVSR
CCCCCCCCHHHHHHH		35.3322369663
483PhosphorylationGSEDEAVSRSINTQG
CCHHHHHHHHHCCCC		27.6223749301
485PhosphorylationEDEAVSRSINTQGEN
HHHHHHHHHCCCCCC		16.8227214570
488PhosphorylationAVSRSINTQGENDYY
HHHHHHCCCCCCHHH		35.9619823750
494PhosphorylationNTQGENDYYQQVQRG
CCCCCCHHHHHHHCC		18.1119823750
495PhosphorylationTQGENDYYQQVQRGK
CCCCCHHHHHHHCCC		8.7119823750
510AcetylationQDKKISRKEAHKNAV
CCCCCCHHHHHHHHH		53.0825381059
514AcetylationISRKEAHKNAVIAAR
CCHHHHHHHHHHHHH		54.3625381059
524AcetylationVIAAREGKLAELAEN
HHHHHCCHHHHHHHH		39.5124489116
533PhosphorylationAELAENVSGDGKRAI
HHHHHHCCCCCHHHH		42.6320377248
537AcetylationENVSGDGKRAINYQI
HHCCCCCHHHHHHHH		43.3125381059
546AcetylationAINYQILKNKGLTPK
HHHHHHHHCCCCCCC		59.2422865919
571AcetylationKKRKKYQKAQKKLKS
HHHHHHHHHHHHHHH		50.0925381059
574AcetylationKKYQKAQKKLKSVRA
HHHHHHHHHHHHCHH		66.0025381059
578PhosphorylationKAQKKLKSVRAVYSG
HHHHHHHHCHHHHCC		27.5428889911
583PhosphorylationLKSVRAVYSGGQSGV
HHHCHHHHCCCCCCC		10.7028889911
584PhosphorylationKSVRAVYSGGQSGVY
HHCHHHHCCCCCCCC		29.8324603354
588PhosphorylationAVYSGGQSGVYEGEK
HHHCCCCCCCCCCCC		33.2428889911
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 SAS10_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SAS10_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 SAS10_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MPP10_YEASTMPP10physical
12068309
FAT1_YEASTFAT1physical
11283351
DUG2_YEASTDUG2physical
11283351
ERG24_YEASTERG24physical
11283351
TRM3_YEASTTRM3genetic
19061648
LRS4_YEASTLRS4genetic
19061648
UTP25_YEASTUTP25physical
20528918
MPP10_YEASTMPP10physical
20884785
SAS10_YEASTSAS10physical
20884785
UTP6_YEASTUTP6physical
20884785
UTP21_YEASTUTP21physical
20884785
UTP25_YEASTUTP25physical
20884785
SA185_YEASTSAP185physical
22875988
RNA1_YEASTRNA1physical
22875988
NOP2_YEASTNOP2physical
22875988
NUF2_YEASTNUF2physical
22875988
MOB2_YEASTMOB2genetic
27708008
ADH4_YEASTADH4genetic
27708008
MAL12_YEASTMAL12genetic
27708008
MED20_YEASTSRB2genetic
27708008
UBL1_YEASTYUH1genetic
27708008
LDS2_YEASTLDS2genetic
27708008
PMT3_YEASTPMT3genetic
27708008
SYIC_YEASTILS1genetic
27708008
KRR1_YEASTKRR1genetic
27708008
UTP6_YEASTUTP6genetic
27708008
ACT_YEASTACT1genetic
27708008
SWC4_YEASTSWC4genetic
27708008
SDA1_YEASTSDA1genetic
27708008
CYAA_YEASTCYR1genetic
27708008
ARP3_YEASTARP3genetic
27708008
SEC22_YEASTSEC22genetic
27708008
ERB1_YEASTERB1genetic
27708008
CBF3B_YEASTCEP3genetic
27708008
RIB2_YEASTRIB2genetic
27708008
CH10_YEASTHSP10genetic
27708008
OST2_YEASTOST2genetic
27708008
ESA1_YEASTESA1genetic
27708008
APC5_YEASTAPC5genetic
27708008
TBF1_YEASTTBF1genetic
27708008
YAJ9_YEASTYAR029Wgenetic
27708008
SWC5_YEASTSWC5genetic
27708008
CHK1_YEASTCHK1genetic
27708008
ATG15_YEASTATG15genetic
27708008
CSM1_YEASTCSM1genetic
27708008
RAD4_YEASTRAD4genetic
27708008
ATC5_YEASTDNF1genetic
27708008
PAU5_YEASTPAU5genetic
27708008
LSB3_YEASTLSB3genetic
27708008
XRN1_YEASTXRN1genetic
27708008
VAM7_YEASTVAM7genetic
27708008
YG1X_YEASTYGR050Cgenetic
27708008
TBP7_YEASTYTA7genetic
27708008
YJY1_YEASTYJR011Cgenetic
27708008
BFA1_YEASTBFA1genetic
27708008
CSN12_YEASTYJR084Wgenetic
27708008
YJ66_YEASTYJR096Wgenetic
27708008
YJ90_YEASTYJR120Wgenetic
27708008
HIR3_YEASTHIR3genetic
27708008
CTK1_YEASTCTK1genetic
27708008
SAC1_YEASTSAC1genetic
27708008
CSF1_YEASTCSF1genetic
27708008
APTH1_YEASTYLR118Cgenetic
27708008
YL287_YEASTYLR287Cgenetic
27708008
CSI1_YEASTCSI1genetic
27708008
TRI1_YEASTTRI1genetic
27708008
TDA1_YEASTTDA1genetic
27708008
PET8_YEASTPET8genetic
27708008
RNH2A_YEASTRNH201genetic
27708008
YNN4_YEASTYNL134Cgenetic
27708008
NOP12_YEASTNOP12genetic
27708008
INO4_YEASTINO4genetic
27708008
WHI5_YEASTWHI5genetic
27708008
SFL1_YEASTSFL1genetic
27708008
HAP5_YEASTHAP5genetic
27708008
VTS1_YEASTVTS1genetic
27708008
RAD1_YEASTRAD1genetic
27708008
NCBP2_YEASTCBC2genetic
27708008
NEW1_YEASTNEW1genetic
27708008
FUMH_YEASTFUM1genetic
27708008
YP022_YEASTYPR022Cgenetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SAS10_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-314; SER-316; SER-336;SER-339; SER-477 AND SER-483, 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-314; SER-336; SER-339AND SER-477, 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-336 AND SER-339, 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-477, AND MASSSPECTROMETRY.

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