RL7A_YEAST - dbPTM
RL7A_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL7A_YEAST
UniProt AC P05737
Protein Name 60S ribosomal protein L7-A {ECO:0000303|PubMed:9559554}
Gene Name RPL7A {ECO:0000303|PubMed:9559554}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 244
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..
Protein Sequence MAAEKILTPESQLKKSKAQQKTAEQVAAERAARKAANKEKRAIILERNAAYQKEYETAERNIIQAKRDAKAAGSYYVEAQHKLVFVVRIKGINKIPPKPRKVLQLLRLTRINSGTFVKVTKATLELLKLIEPYVAYGYPSYSTIRQLVYKRGFGKINKQRVPLSDNAIIEANLGKYGILSIDDLIHEIITVGPHFKQANNFLWPFKLSNPSGGWGVPRKFKHFIQGGSFGNREEFINKLVKSMN
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
8PhosphorylationMAAEKILTPESQLKK
CCCCCCCCHHHHHHH		28.6025521595
11PhosphorylationEKILTPESQLKKSKA
CCCCCHHHHHHHHHH		41.8525521595
14SuccinylationLTPESQLKKSKAQQK
CCHHHHHHHHHHHHH		47.5723954790
14UbiquitinationLTPESQLKKSKAQQK
CCHHHHHHHHHHHHH		47.5723749301
14AcetylationLTPESQLKKSKAQQK
CCHHHHHHHHHHHHH		47.5724489116
142-HydroxyisobutyrylationLTPESQLKKSKAQQK
CCHHHHHHHHHHHHH		47.57-
15UbiquitinationTPESQLKKSKAQQKT
CHHHHHHHHHHHHHH		66.8224961812
16PhosphorylationPESQLKKSKAQQKTA
HHHHHHHHHHHHHHH		31.4721440633
17UbiquitinationESQLKKSKAQQKTAE
HHHHHHHHHHHHHHH		60.1222817900
21UbiquitinationKKSKAQQKTAEQVAA
HHHHHHHHHHHHHHH		37.3123749301
22PhosphorylationKSKAQQKTAEQVAAE
HHHHHHHHHHHHHHH		30.9623749301
51PhosphorylationILERNAAYQKEYETA
HHHHHHHHHHHHHHH		20.0828889911
532-HydroxyisobutyrylationERNAAYQKEYETAER
HHHHHHHHHHHHHHH		49.98-
53SuccinylationERNAAYQKEYETAER
HHHHHHHHHHHHHHH		49.9823954790
53UbiquitinationERNAAYQKEYETAER
HHHHHHHHHHHHHHH		49.9823749301
53AcetylationERNAAYQKEYETAER
HHHHHHHHHHHHHHH		49.9824489116
55PhosphorylationNAAYQKEYETAERNI
HHHHHHHHHHHHHHH		26.1421082442
66SuccinylationERNIIQAKRDAKAAG
HHHHHHHHHHHHHHC		34.1423954790
662-HydroxyisobutyrylationERNIIQAKRDAKAAG
HHHHHHHHHHHHHHC		34.14-
66AcetylationERNIIQAKRDAKAAG
HHHHHHHHHHHHHHC		34.1425381059
66UbiquitinationERNIIQAKRDAKAAG
HHHHHHHHHHHHHHC		34.1423749301
70UbiquitinationIQAKRDAKAAGSYYV
HHHHHHHHHHCCEEE		42.9622106047
70SuccinylationIQAKRDAKAAGSYYV
HHHHHHHHHHCCEEE		42.9623954790
70AcetylationIQAKRDAKAAGSYYV
HHHHHHHHHHCCEEE		42.9624489116
74PhosphorylationRDAKAAGSYYVEAQH
HHHHHHCCEEEEECC		14.4721440633
75PhosphorylationDAKAAGSYYVEAQHK
HHHHHCCEEEEECCE		15.6024961812
982-HydroxyisobutyrylationGINKIPPKPRKVLQL
CCCCCCCCCHHHHHH		52.69-
113PhosphorylationLRLTRINSGTFVKVT
HHHEEECCCCEEEEE		36.5222369663
118AcetylationINSGTFVKVTKATLE
ECCCCEEEEEHHHHH		39.7424489116
118SuccinylationINSGTFVKVTKATLE
ECCCCEEEEEHHHHH		39.7423954790
1182-HydroxyisobutyrylationINSGTFVKVTKATLE
ECCCCEEEEEHHHHH		39.74-
118UbiquitinationINSGTFVKVTKATLE
ECCCCEEEEEHHHHH		39.7423749301
121AcetylationGTFVKVTKATLELLK
CCEEEEEHHHHHHHH		42.2224489116
121SuccinylationGTFVKVTKATLELLK
CCEEEEEHHHHHHHH		42.2223954790
1212-HydroxyisobutyrylationGTFVKVTKATLELLK
CCEEEEEHHHHHHHH		42.22-
121UbiquitinationGTFVKVTKATLELLK
CCEEEEEHHHHHHHH		42.2223749301
128UbiquitinationKATLELLKLIEPYVA
HHHHHHHHHHHHHHH		61.1023749301
140PhosphorylationYVAYGYPSYSTIRQL
HHHCCCCCHHHHHHH		24.1927214570
164PhosphorylationNKQRVPLSDNAIIEA
CCCCCCCCCCEEEEE		23.8121440633
180PhosphorylationLGKYGILSIDDLIHE
CCCCCCCCHHHHHHH		23.2717287358
206AcetylationNNFLWPFKLSNPSGG
CCEEECEECCCCCCC		47.1024489116
208PhosphorylationFLWPFKLSNPSGGWG
EEECEECCCCCCCCC		47.4928889911
211PhosphorylationPFKLSNPSGGWGVPR
CEECCCCCCCCCCCC		54.9421440633
221AcetylationWGVPRKFKHFIQGGS
CCCCCCCHHHHCCCC		40.4124489116
228PhosphorylationKHFIQGGSFGNREEF
HHHHCCCCCCCHHHH		36.4822369663
2382-HydroxyisobutyrylationNREEFINKLVKSMN-
CHHHHHHHHHHHCC-		50.25-
238AcetylationNREEFINKLVKSMN-
CHHHHHHHHHHHCC-		50.2524489116
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 RL7A_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL7A_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 RL7A_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RL7B_YEASTRPL7Bgenetic
8536309
SSB1_YEASTSSB1physical
19536198
SIR2_YEASTSIR2genetic
21902802
RL7B_YEASTRPL7Bgenetic
22377630
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RL7A_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 THR-8 AND SER-11, AND MASSSPECTROMETRY.
"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 THR-8 AND SER-11, AND MASSSPECTROMETRY.
"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 THR-8 AND SER-11, 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 THR-8 AND SER-11, AND MASSSPECTROMETRY.
"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 THR-8, 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 THR-8, AND MASSSPECTROMETRY.

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