RS10B_YEAST - dbPTM
RS10B_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS10B_YEAST
UniProt AC P46784
Protein Name 40S ribosomal protein S10-B {ECO:0000303|PubMed:9559554}
Gene Name RPS10B {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 105
Subcellular Localization Cytoplasm .
Protein Description Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. [PubMed: 22096102 eS10 plays a role as a positive regulator of the GCN2 kinase activity by stimulating GCN1-mediated GCN2 activation]
Protein Sequence MLMPKQERNKIHQYLFQEGVVVAKKDFNQAKHEEIDTKNLYVIKALQSLTSKGYVKTQFSWQYYYYTLTEEGVEYLREYLNLPEHIVPGTYIQERNPSQRPQRRY
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
5Ubiquitination---MLMPKQERNKIH
---CCCCHHHHHHHH		51.3223749301
10UbiquitinationMPKQERNKIHQYLFQ
CCHHHHHHHHHHHHH		48.0323749301
10AcetylationMPKQERNKIHQYLFQ
CCHHHHHHHHHHHHH		48.0324489116
242-HydroxyisobutyrylationQEGVVVAKKDFNQAK
HCCCEEEECCHHHHH		41.06-
24UbiquitinationQEGVVVAKKDFNQAK
HCCCEEEECCHHHHH		41.0623749301
25UbiquitinationEGVVVAKKDFNQAKH
CCCEEEECCHHHHHH		58.7923749301
31SuccinylationKKDFNQAKHEEIDTK
ECCHHHHHHHHCCCC		41.6123954790
31AcetylationKKDFNQAKHEEIDTK
ECCHHHHHHHHCCCC		41.6124489116
31UbiquitinationKKDFNQAKHEEIDTK
ECCHHHHHHHHCCCC		41.6123749301
37PhosphorylationAKHEEIDTKNLYVIK
HHHHHCCCCHHHHHH		27.7428889911
38SuccinylationKHEEIDTKNLYVIKA
HHHHCCCCHHHHHHH		41.0023954790
38UbiquitinationKHEEIDTKNLYVIKA
HHHHCCCCHHHHHHH		41.0023749301
38AcetylationKHEEIDTKNLYVIKA
HHHHCCCCHHHHHHH		41.0024489116
382-HydroxyisobutyrylationKHEEIDTKNLYVIKA
HHHHCCCCHHHHHHH		41.00-
44UbiquitinationTKNLYVIKALQSLTS
CCHHHHHHHHHHHCC		32.7623749301
44AcetylationTKNLYVIKALQSLTS
CCHHHHHHHHHHHCC		32.7624489116
48PhosphorylationYVIKALQSLTSKGYV
HHHHHHHHHCCCCCE		34.1722369663
50PhosphorylationIKALQSLTSKGYVKT
HHHHHHHCCCCCEEE		33.3722369663
51PhosphorylationKALQSLTSKGYVKTQ
HHHHHHCCCCCEEEE		29.4022369663
52SuccinylationALQSLTSKGYVKTQF
HHHHHCCCCCEEEEE		49.3723954790
522-HydroxyisobutyrylationALQSLTSKGYVKTQF
HHHHHCCCCCEEEEE		49.37-
52AcetylationALQSLTSKGYVKTQF
HHHHHCCCCCEEEEE		49.3724489116
52UbiquitinationALQSLTSKGYVKTQF
HHHHHCCCCCEEEEE		49.3723749301
56UbiquitinationLTSKGYVKTQFSWQY
HCCCCCEEEEEEEEE		28.2922817900
98PhosphorylationYIQERNPSQRPQRRY
CCCCCCCCCCCCCCC		42.2324909858
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 RS10B_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS10B_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 RS10B_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EF3A_YEASTYEF3genetic
25437641
SDS3_YEASTSDS3genetic
27708008
RS30A_YEASTRPS30Agenetic
27708008
RS30B_YEASTRPS30Agenetic
27708008
CDC27_YEASTCDC27genetic
27708008
APC11_YEASTAPC11genetic
27708008
DAD1_YEASTDAD1genetic
27708008
RRP1_YEASTRRP1genetic
27708008
CDC1_YEASTCDC1genetic
27708008
CP51_YEASTERG11genetic
27708008
ATC7_YEASTNEO1genetic
27708008
SSL1_YEASTSSL1genetic
27708008
RU1C_YEASTYHC1genetic
27708008
DCP2_YEASTDCP2genetic
27708008
SGT1_YEASTSGT1genetic
27708008
NAB3_YEASTNAB3genetic
27708008
IPL1_YEASTIPL1genetic
27708008
DIB1_YEASTDIB1genetic
27708008
SHE1_YEASTSHE1genetic
27708008
QOR_YEASTZTA1genetic
27708008
PAT1_YEASTPAT1genetic
27708008
MCM21_YEASTMCM21genetic
27708008
LSM6_YEASTLSM6genetic
27708008
HSP31_YEASTHSP31genetic
27708008
FCY2_YEASTFCY2genetic
27708008
YEY6_YEASTYER156Cgenetic
27708008
RAD4_YEASTRAD4genetic
27708008
PUG1_YEASTPUG1genetic
27708008
UBP6_YEASTUBP6genetic
27708008
XRN1_YEASTXRN1genetic
27708008
ATG1_YEASTATG1genetic
27708008
SKI8_YEASTSKI8genetic
27708008
RS25A_YEASTRPS25Agenetic
27708008
PEF1_YEASTPEF1genetic
27708008
MAL12_YEASTMAL12genetic
27708008
NAM8_YEASTNAM8genetic
27708008
STB5_YEASTSTB5genetic
27708008
GPP1_YEASTGPP1genetic
27708008
YIF4_YEASTYIL054Wgenetic
27708008
HOC1_YEASTHOC1genetic
27708008
HBS1_YEASTHBS1genetic
27708008
RSSA2_YEASTRPS0Bgenetic
27708008
ERG6_YEASTERG6genetic
27708008
DOM34_YEASTDOM34genetic
27708008
RAS2_YEASTRAS2genetic
27708008
SUR1_YEASTSUR1genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
TGS1_YEASTTGS1genetic
27708008
DCAM_YEASTSPE2genetic
27453043
FNTA_YEASTRAM2genetic
27453043
ERG26_YEASTERG26genetic
27453043
YND1_YEASTYND1genetic
27453043
NMT_YEASTNMT1genetic
27453043
HIR1_YEASTHIR1genetic
27453043
RS19B_YEASTRPS19Bgenetic
27453043
MUP3_YEASTMUP3genetic
27453043
INP52_YEASTINP52genetic
27453043
MAP1_YEASTMAP1genetic
27453043
PVH1_YEASTYVH1genetic
27453043
SWC5_YEASTSWC5genetic
27453043
JHD2_YEASTJHD2genetic
27453043
PDK1_YEASTPKP1genetic
27453043
2A5D_YEASTRTS1genetic
27453043
FKBP_YEASTFPR1genetic
27453043
ADE_YEASTAAH1genetic
27453043
SYLM_YEASTNAM2genetic
27453043
TPM1_YEASTTPM1genetic
27453043
RPAC1_YEASTRPC40genetic
27453043
PTR2_YEASTPTR2genetic
27453043
PTPA2_YEASTRRD2genetic
27453043
MKK2_YEASTMKK2genetic
27453043
PNPH_YEASTPNP1genetic
27453043
CYPB_YEASTCPR2genetic
27453043
DOM34_YEASTDOM34genetic
27453043
PAN3_YEASTPAN3genetic
27453043
VPS75_YEASTVPS75genetic
27453043
MRC1_YEASTMRC1genetic
27453043
PYRD_YEASTURA1genetic
27453043
RTG1_YEASTRTG1genetic
27453043
AGP2_YEASTAGP2genetic
27453043
BRE1_YEASTBRE1genetic
27453043
AZF1_YEASTAZF1genetic
27453043
PLP1_YEASTPLP1genetic
27453043
SCH9_YEASTSCH9genetic
27453043
SSN8_YEASTSSN8genetic
27453043
EAF7_YEASTEAF7genetic
27453043
QCR2_YEASTQCR2genetic
27453043
LSM1_YEASTLSM1genetic
27453043
CDC42_YEASTCDC42genetic
27453043
SIN3_YEASTSIN3genetic
27453043
CTK3_YEASTCTK3genetic
27453043
BUB1_YEASTBUB1genetic
27453043
GAL4_YEASTGAL4genetic
27453043
PHO85_YEASTPHO85genetic
27453043
REV1_YEASTREV1genetic
27453043
IRA2_YEASTIRA2genetic
27453043
CYPC_YEASTCPR3genetic
27453043
RPB3_YEASTRPB3genetic
27453043
SHU1_YEASTSHU1genetic
27453043
AIM33_YEASTAIM33genetic
27453043
VPS53_YEASTVPS53genetic
27453043
DCOR_YEASTSPE1genetic
27453043
KAPA_YEASTTPK1genetic
27453043
UBA4_YEASTUBA4genetic
27453043
NM111_YEASTNMA111genetic
27453043
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RS10B_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-48, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND MASSSPECTROMETRY.

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