RL7B_YEAST - dbPTM
RL7B_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RL7B_YEAST
UniProt AC Q12213
Protein Name 60S ribosomal protein L7-B {ECO:0000303|PubMed:9559554}
Gene Name RPL7B {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 MSTEKILTPESQLKKTKAQQKTAEQIAAERAARKAANKEKRAIILERNAAYQKEYETAERNIIQAKRDAKAAGSYYVEAQHKLVFVVRIKGINKIPPKPRKVLQLLRLTRINSGTFVKVTKATLELLKLIEPYVAYGYPSYSTIRQLVYKRGFGKINKQRVPLSDNAIIEANLGKYGILSIDDLIHEIITVGPHFKQANNFLWPFKLSNPSGGWGVPRKFKHFIQGGSFGNREEFINKLVKAMN
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------MSTEKILTP
------CCCCCCCCH		45.3229136822
3Phosphorylation-----MSTEKILTPE
-----CCCCCCCCHH		39.7429136822
8PhosphorylationMSTEKILTPESQLKK
CCCCCCCCHHHHHHH		28.6022369663
11PhosphorylationEKILTPESQLKKTKA
CCCCCHHHHHHHHHH		41.8522369663
14AcetylationLTPESQLKKTKAQQK
CCHHHHHHHHHHHHH		51.2425381059
14UbiquitinationLTPESQLKKTKAQQK
CCHHHHHHHHHHHHH		51.2423749301
15UbiquitinationTPESQLKKTKAQQKT
CHHHHHHHHHHHHHH		64.9424961812
51PhosphorylationILERNAAYQKEYETA
HHHHHHHHHHHHHHH		20.0828889911
53UbiquitinationERNAAYQKEYETAER
HHHHHHHHHHHHHHH		49.9823749301
55PhosphorylationNAAYQKEYETAERNI
HHHHHHHHHHHHHHH		26.1421082442
66UbiquitinationERNIIQAKRDAKAAG
HHHHHHHHHHHHHHC		34.1423749301
70UbiquitinationIQAKRDAKAAGSYYV
HHHHHHHHHHCCEEE		42.9622106047
74PhosphorylationRDAKAAGSYYVEAQH
HHHHHHCCEEEEECC		14.4721440633
75PhosphorylationDAKAAGSYYVEAQHK
HHHHHCCEEEEECCE		15.6024961812
113PhosphorylationLRLTRINSGTFVKVT
HHHEEECCCCEEEEE		36.5222369663
118UbiquitinationINSGTFVKVTKATLE
ECCCCEEEEEHHHHH		39.7423749301
121UbiquitinationGTFVKVTKATLELLK
CCEEEEEHHHHHHHH		42.2223749301
128UbiquitinationKATLELLKLIEPYVA
HHHHHHHHHHHHHHH		61.1023749301
140PhosphorylationYVAYGYPSYSTIRQL
HHHCCCCCHHHHHHH		24.1927214570
164PhosphorylationNKQRVPLSDNAIIEA
CCCCCCCCCCEEEEE		23.8121440633
180PhosphorylationLGKYGILSIDDLIHE
CCCCCCCCHHHHHHH		23.2717287358
208PhosphorylationFLWPFKLSNPSGGWG
EEECEECCCCCCCCC		47.4928889911
211PhosphorylationPFKLSNPSGGWGVPR
CEECCCCCCCCCCCC		54.9421440633
228PhosphorylationKHFIQGGSFGNREEF
HHHHCCCCCCCHHHH		36.4822369663
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 RL7B_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RL7B_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 RL7B_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SSB1_YEASTSSB1physical
19536198
RLP7_YEASTRLP7physical
23945946
HAS1_YEASTHAS1physical
23945946
FBRL_YEASTNOP1physical
23945946
RL1A_YEASTRPL1Bphysical
23945946
RL1B_YEASTRPL1Bphysical
23945946
RL35A_YEASTRPL35Aphysical
23945946
RL35B_YEASTRPL35Aphysical
23945946
MOB2_YEASTMOB2genetic
27708008
CALM_YEASTCMD1genetic
27708008
TECR_YEASTTSC13genetic
27708008
FAL1_YEASTFAL1genetic
27708008
TAF12_YEASTTAF12genetic
27708008
CDC1_YEASTCDC1genetic
27708008
GPI19_YEASTGPI19genetic
27708008
TBP_YEASTSPT15genetic
27708008
ACT_YEASTACT1genetic
27708008
SWC4_YEASTSWC4genetic
27708008
PRP18_YEASTPRP18genetic
27708008
BIG1_YEASTBIG1genetic
27708008
CDC12_YEASTCDC12genetic
27708008
SEC22_YEASTSEC22genetic
27708008
VTI1_YEASTVTI1genetic
27708008
MED7_YEASTMED7genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RL7B_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-180 AND SER-228, ANDMASS SPECTROMETRY.
"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.
"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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