TSR4_YEAST - dbPTM
TSR4_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TSR4_YEAST
UniProt AC P25040
Protein Name 20S rRNA accumulation protein 4
Gene Name TSR4
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 408
Subcellular Localization Cytoplasm .
Protein Description Required for processing of the 20S pre-rRNA at site D to generate mature 18S rRNA..
Protein Sequence MSKIEELPPSDTDDHSYSSKPGDVFLAFVDAPVKETDDILVEDSFIGGEPKWLHPDSEPPAELLKCGACKSADNMKLLLQAFSPLDDEQMSAIQQRLGINNMSYINPQDDRVLYVFLCTECQRKGNSVRCIRGVKKNKNVDSLSEKMASTSLEKDFQINPFDLSNNSDSKCNAFSSNPFGGANANPFGADSINSNISQSKDEGKKKESATVSAKTARKLHDLQKDKEYDGNKCFKSCLLYVEEETFKNKKPAHLQLPKNLKIDKEALDLTGDEDLEKDPIKLDPRTEKLSKFLDDDTFQKFQEVVGYNPLQVLRYDLGGKPLLYAETKVDILSTVPRPGYNPSSQRIFEMQLMPKMIFDLEEVVSVDNGMEWGTILVFTDVENYMPEFDEHGVGYVEECVKVQWESRT
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------MSKIEELPP
------CCCCCCCCC		42.2022369663
10PhosphorylationKIEELPPSDTDDHSY
CCCCCCCCCCCCCCC		51.7222369663
12PhosphorylationEELPPSDTDDHSYSS
CCCCCCCCCCCCCCC		47.8920377248
16PhosphorylationPSDTDDHSYSSKPGD
CCCCCCCCCCCCCCC		33.4322369663
17PhosphorylationSDTDDHSYSSKPGDV
CCCCCCCCCCCCCCE		17.3422369663
18PhosphorylationDTDDHSYSSKPGDVF
CCCCCCCCCCCCCEE		34.5921440633
19PhosphorylationTDDHSYSSKPGDVFL
CCCCCCCCCCCCEEE		34.3422369663
142PhosphorylationKKNKNVDSLSEKMAS
CCCCCHHHHHHHHHH		29.5225521595
144PhosphorylationNKNVDSLSEKMASTS
CCCHHHHHHHHHHCC		38.8425521595
149PhosphorylationSLSEKMASTSLEKDF
HHHHHHHHCCHHHCC		18.2822369663
150PhosphorylationLSEKMASTSLEKDFQ
HHHHHHHCCHHHCCC		28.0022369663
151PhosphorylationSEKMASTSLEKDFQI
HHHHHHCCHHHCCCC		31.8422369663
154AcetylationMASTSLEKDFQINPF
HHHCCHHHCCCCCCC		69.9624489116
164PhosphorylationQINPFDLSNNSDSKC
CCCCCCCCCCCCCCC		35.4930377154
167PhosphorylationPFDLSNNSDSKCNAF
CCCCCCCCCCCCCCC		47.7322369663
169PhosphorylationDLSNNSDSKCNAFSS
CCCCCCCCCCCCCCC		38.6422369663
208PhosphorylationDEGKKKESATVSAKT
CCCCCHHHCCCCHHH		37.8117287358
264AcetylationPKNLKIDKEALDLTG
CCCCCCCHHHHCCCC		48.6524489116
270PhosphorylationDKEALDLTGDEDLEK
CHHHHCCCCCCCHHH		42.1022369663
288UbiquitinationKLDPRTEKLSKFLDD
CCCCCHHHHHHHCCH		58.4022817900
291UbiquitinationPRTEKLSKFLDDDTF
CCHHHHHHHCCHHHH		61.4523749301
291AcetylationPRTEKLSKFLDDDTF
CCHHHHHHHCCHHHH		61.4524489116
320AcetylationLRYDLGGKPLLYAET
EEEECCCCEEEEEEE		30.6024489116
328UbiquitinationPLLYAETKVDILSTV
EEEEEEEEEEEECCC		29.4323749301
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 TSR4_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TSR4_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 TSR4_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SMD1_YEASTSMD1genetic
27708008
THRC_YEASTTHR4genetic
27708008
FAD1_YEASTFAD1genetic
27708008
RPC10_YEASTRPC11genetic
27708008
CDC1_YEASTCDC1genetic
27708008
MOB2_YEASTMOB2genetic
27708008
ACT_YEASTACT1genetic
27708008
KTHY_YEASTCDC8genetic
27708008
TAD3_YEASTTAD3genetic
27708008
RSC9_YEASTRSC9genetic
27708008
MCM1_YEASTMCM1genetic
27708008
RNA1_YEASTRNA1genetic
27708008
GPI12_YEASTGPI12genetic
27708008
NOP2_YEASTNOP2genetic
27708008
RPC6_YEASTRPC34genetic
27708008
SEC62_YEASTSEC62genetic
27708008
NAB3_YEASTNAB3genetic
27708008
SEC23_YEASTSEC23genetic
27708008
RS8A_YEASTRPS8Agenetic
27708008
RS8B_YEASTRPS8Agenetic
27708008
CHK1_YEASTCHK1genetic
27708008
ATG15_YEASTATG15genetic
27708008
SLX5_YEASTSLX5genetic
27708008
MTU1_YEASTSLM3genetic
27708008
MAF1_YEASTMAF1genetic
27708008
IPT1_YEASTIPT1genetic
27708008
VPS41_YEASTVPS41genetic
27708008
ARO1_YEASTARO1genetic
27708008
SAC3_YEASTSAC3genetic
27708008
CP56_YEASTDIT2genetic
27708008
CAJ1_YEASTCAJ1genetic
27708008
ERJ5_YEASTERJ5genetic
27708008
CGR1_YEASTCGR1genetic
27708008
XRN1_YEASTXRN1genetic
27708008
KEL2_YEASTKEL2genetic
27708008
OCA5_YEASTOCA5genetic
27708008
MUP3_YEASTMUP3genetic
27708008
KEL1_YEASTKEL1genetic
27708008
SWE1_YEASTSWE1genetic
27708008
YJ85_YEASTYJR115Wgenetic
27708008
MET5_YEASTMET5genetic
27708008
APE2_YEASTAPE2genetic
27708008
YRA2_YEASTYRA2genetic
27708008
ALAM_YEASTALT1genetic
27708008
RL37A_YEASTRPL37Agenetic
27708008
ATG33_YEASTATG33genetic
27708008
SRR1L_YEASTBER1genetic
27708008
RAD10_YEASTRAD10genetic
27708008
IMP2_YEASTIMP2genetic
27708008
RAD14_YEASTRAD14genetic
27708008
PEX27_YEASTPEX27genetic
27708008
UBA3_YEASTUBA3genetic
27708008
MED1_YEASTMED1genetic
27708008
AXL1_YEASTAXL1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TSR4_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-10; SER-142 AND SER-151,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-208, AND MASSSPECTROMETRY.

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