RS7A_YEAST - dbPTM
RS7A_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS7A_YEAST
UniProt AC P26786
Protein Name 40S ribosomal protein S7-A {ECO:0000303|PubMed:9559554}
Gene Name RPS7A {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 190
Subcellular Localization Cytoplasm . Nucleus, nucleolus .
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 eS7 is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly]
Protein Sequence MSAPQAKILSQAPTELELQVAQAFVELENSSPELKAELRPLQFKSIREIDVAGGKKALAIFVPVPSLAGFHKVQTKLTRELEKKFQDRHVIFLAERRILPKPSRTSRQVQKRPRSRTLTAVHDKILEDLVFPTEIVGKRVRYLVGGNKIQKVLLDSKDVQQIDYKLESFQAVYNKLTGKQIVFEIPSETH
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
2Acetylation------MSAPQAKIL
------CCCCHHHHH		48.9710601260
7Ubiquitination-MSAPQAKILSQAPT
-CCCCHHHHHHCCCC		38.6417644757
10PhosphorylationAPQAKILSQAPTELE
CCHHHHHHCCCCHHH		27.98-
31PhosphorylationFVELENSSPELKAEL
HHHHHCCCHHHHHHH		33.6921440633
35UbiquitinationENSSPELKAELRPLQ
HCCCHHHHHHHCCCC		37.8517644757
44UbiquitinationELRPLQFKSIREIDV
HHCCCCCCCEEEEEE		31.8223749301
44SuccinylationELRPLQFKSIREIDV
HHCCCCCCCEEEEEE		31.8223954790
44AcetylationELRPLQFKSIREIDV
HHCCCCCCCEEEEEE		31.8224489116
45PhosphorylationLRPLQFKSIREIDVA
HCCCCCCCEEEEEEC		28.3221440633
55UbiquitinationEIDVAGGKKALAIFV
EEEECCCCEEEEEEE		33.6723749301
55SuccinylationEIDVAGGKKALAIFV
EEEECCCCEEEEEEE		33.6723954790
552-HydroxyisobutyrylationEIDVAGGKKALAIFV
EEEECCCCEEEEEEE		33.67-
56UbiquitinationIDVAGGKKALAIFVP
EEECCCCEEEEEEEE		52.4823749301
56AcetylationIDVAGGKKALAIFVP
EEECCCCEEEEEEEE		52.4824489116
66PhosphorylationAIFVPVPSLAGFHKV
EEEEECCCCCCHHHH		30.9621440633
72AcetylationPSLAGFHKVQTKLTR
CCCCCHHHHHHHHHH		33.5024489116
72UbiquitinationPSLAGFHKVQTKLTR
CCCCCHHHHHHHHHH		33.5023749301
75PhosphorylationAGFHKVQTKLTRELE
CCHHHHHHHHHHHHH		30.8923749301
762-HydroxyisobutyrylationGFHKVQTKLTRELEK
CHHHHHHHHHHHHHH		30.67-
76UbiquitinationGFHKVQTKLTRELEK
CHHHHHHHHHHHHHH		30.6723749301
76AcetylationGFHKVQTKLTRELEK
CHHHHHHHHHHHHHH		30.6724489116
83UbiquitinationKLTRELEKKFQDRHV
HHHHHHHHHHCCCCE		72.0822817900
842-HydroxyisobutyrylationLTRELEKKFQDRHVI
HHHHHHHHHCCCCEE		38.59-
84UbiquitinationLTRELEKKFQDRHVI
HHHHHHHHHCCCCEE		38.5922817900
103PhosphorylationRRILPKPSRTSRQVQ
CCCCCCCCCCCHHHH		55.0830377154
106PhosphorylationLPKPSRTSRQVQKRP
CCCCCCCCHHHHHCC		21.4330377154
115PhosphorylationQVQKRPRSRTLTAVH
HHHHCCCCCCCHHHH		32.0922369663
117PhosphorylationQKRPRSRTLTAVHDK
HHCCCCCCCHHHHHH		29.7022369663
119PhosphorylationRPRSRTLTAVHDKIL
CCCCCCCHHHHHHHH		26.4822369663
124AcetylationTLTAVHDKILEDLVF
CCHHHHHHHHHHCCC		34.0224489116
124UbiquitinationTLTAVHDKILEDLVF
CCHHHHHHHHHHCCC		34.0222106047
138SuccinylationFPTEIVGKRVRYLVG
CCHHHCCCEEEEEEC		36.5023954790
138AcetylationFPTEIVGKRVRYLVG
CCHHHCCCEEEEEEC		36.5024489116
138UbiquitinationFPTEIVGKRVRYLVG
CCHHHCCCEEEEEEC		36.5023749301
142PhosphorylationIVGKRVRYLVGGNKI
HCCCEEEEEECCCCC		11.6821440633
148AcetylationRYLVGGNKIQKVLLD
EEEECCCCCEEEECC		50.1922865919
148UbiquitinationRYLVGGNKIQKVLLD
EEEECCCCCEEEECC		50.1923749301
151AcetylationVGGNKIQKVLLDSKD
ECCCCCEEEECCCCC		38.0224489116
151UbiquitinationVGGNKIQKVLLDSKD
ECCCCCEEEECCCCC		38.0223749301
1512-HydroxyisobutyrylationVGGNKIQKVLLDSKD
ECCCCCEEEECCCCC		38.02-
156PhosphorylationIQKVLLDSKDVQQID
CEEEECCCCCHHHHH		30.6323749301
157AcetylationQKVLLDSKDVQQIDY
EEEECCCCCHHHHHH		62.6824489116
157SuccinylationQKVLLDSKDVQQIDY
EEEECCCCCHHHHHH		62.6823954790
1572-HydroxyisobutyrylationQKVLLDSKDVQQIDY
EEEECCCCCHHHHHH		62.68-
157UbiquitinationQKVLLDSKDVQQIDY
EEEECCCCCHHHHHH		62.6823749301
165AcetylationDVQQIDYKLESFQAV
CHHHHHHHHHHHHHH		41.8724489116
165SuccinylationDVQQIDYKLESFQAV
CHHHHHHHHHHHHHH		41.8723954790
165UbiquitinationDVQQIDYKLESFQAV
CHHHHHHHHHHHHHH		41.8724961812
168PhosphorylationQIDYKLESFQAVYNK
HHHHHHHHHHHHHHH		32.8530377154
175AcetylationSFQAVYNKLTGKQIV
HHHHHHHHCCCCEEE		29.7324489116
175UbiquitinationSFQAVYNKLTGKQIV
HHHHHHHHCCCCEEE		29.7323749301
179UbiquitinationVYNKLTGKQIVFEIP
HHHHCCCCEEEEECC		31.4523749301
179SuccinylationVYNKLTGKQIVFEIP
HHHHCCCCEEEEECC		31.4523954790
179AcetylationVYNKLTGKQIVFEIP
HHHHCCCCEEEEECC		31.4524489116
187PhosphorylationQIVFEIPSETH----
EEEEECCCCCC----		61.8725521595
189PhosphorylationVFEIPSETH------
EEECCCCCC------		36.9025521595
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 RS7A_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS7A_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 RS7A_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MPP10_YEASTMPP10physical
15590835
RS7B_YEASTRPS7Bgenetic
1737755
RS7B_YEASTRPS7Bphysical
22243599
NOT4_YEASTMOT2physical
22243599
NOT5_YEASTNOT5physical
22243599
RS7B_YEASTRPS7Bgenetic
22377630
ERD2_YEASTERD2genetic
27708008
TF2B_YEASTSUA7genetic
27708008
RS6A_YEASTRPS6Bgenetic
27708008
RS6B_YEASTRPS6Bgenetic
27708008
RMD9L_YEASTYBR238Cgenetic
27708008
PP2C1_YEASTPTC1genetic
27708008
DAS1_YEASTDAS1genetic
27708008
APC11_YEASTAPC11genetic
27708008
NOP14_YEASTNOP14genetic
27708008
SLY1_YEASTSLY1genetic
27708008
SMT3_YEASTSMT3genetic
27708008
CDC12_YEASTCDC12genetic
27708008
DNA2_YEASTDNA2genetic
27708008
MCM10_YEASTMCM10genetic
27708008
ESS1_YEASTESS1genetic
27708008
RRN3_YEASTRRN3genetic
27708008
BET3_YEASTBET3genetic
27708008
ORC1_YEASTORC1genetic
27708008
MED11_YEASTMED11genetic
27708008
RNA1_YEASTRNA1genetic
27708008
TRM6_YEASTGCD10genetic
27708008
DPOA_YEASTPOL1genetic
27708008
MYO2_YEASTMYO2genetic
27708008
RPA1_YEASTRPA190genetic
27708008
TBF1_YEASTTBF1genetic
27708008
SEC23_YEASTSEC23genetic
27708008
NU170_YEASTNUP170genetic
27708008
BIK1_YEASTBIK1genetic
27708008
GCN20_YEASTGCN20genetic
27708008
UBP6_YEASTUBP6genetic
27708008
RTG2_YEASTRTG2genetic
27708008
MOG1_YEASTMOG1genetic
27708008
HOC1_YEASTHOC1genetic
27708008
VPS24_YEASTVPS24genetic
27708008
DCOR_YEASTSPE1genetic
27708008
DPH2_YEASTDPH2genetic
27708008
DBP7_YEASTDBP7genetic
27708008
NU188_YEASTNUP188genetic
27708008
MSC1_YEASTMSC1genetic
27708008
MAC1_YEASTMAC1genetic
27708008
COX7_YEASTCOX7genetic
27708008
AEP2_YEASTAEP2genetic
27708008
RS7B_YEASTRPS7Bgenetic
27708008
SUR1_YEASTSUR1genetic
27708008
COX10_YEASTCOX10genetic
27708008
QCR2_YEASTQCR2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RS7A_YEAST

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"The action of N-terminal acetyltransferases on yeast ribosomalproteins.";
Arnold R.J., Polevoda B., Reilly J.P., Sherman F.;
J. Biol. Chem. 274:37035-37040(1999).
Cited for: CLEAVAGE OF INITIATOR METHIONINE, AND ACETYLATION AT SER-2 BY NATA.
"NH2-terminal acetylation of ribosomal proteins of Saccharomycescerevisiae.";
Takakura H., Tsunasawa S., Miyagi M., Warner J.R.;
J. Biol. Chem. 267:5442-5445(1992).
Cited for: PROTEIN SEQUENCE OF 2-26, AND ACETYLATION AT SER-2 BY NATA.
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-31, AND MASSSPECTROMETRY.

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