RS7B_YEAST - dbPTM
RS7B_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RS7B_YEAST
UniProt AC P48164
Protein Name 40S ribosomal protein S7-B {ECO:0000303|PubMed:9559554}
Gene Name RPS7B {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 MSSVQSKILSQAPSELELQVAKTFIDLESSSPELKADLRPLQIKSIREIDVTGGKKALVLFVPVPALSAYHKVQTKLTRELEKKFPDRHVIFLAERRILPKPSRTSRQVQKRPRSRTLTAVHDKVLEDMVFPTEIVGKRVRYLVGGNKIQKVLLDSKDVQQIDYKLESFQAVYNKLTGKQIVFEIPSQTN
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------MSSVQSKIL
------CCHHHHHHH		38.9410601260
2Phosphorylation------MSSVQSKIL
------CCHHHHHHH		38.9427717283
3Phosphorylation-----MSSVQSKILS
-----CCHHHHHHHH		23.9130377154
6Phosphorylation--MSSVQSKILSQAP
--CCHHHHHHHHCCC		21.3630377154
7Ubiquitination-MSSVQSKILSQAPS
-CCHHHHHHHHCCCC		30.4924961812
10PhosphorylationSVQSKILSQAPSELE
HHHHHHHHCCCCHHH		27.9822369663
14PhosphorylationKILSQAPSELELQVA
HHHHCCCCHHHHHHH		58.8022369663
22UbiquitinationELELQVAKTFIDLES
HHHHHHHHHHCCCCC		45.1523749301
23PhosphorylationLELQVAKTFIDLESS
HHHHHHHHHCCCCCC		18.9825521595
29PhosphorylationKTFIDLESSSPELKA
HHHCCCCCCCHHHCC		43.3322369663
30PhosphorylationTFIDLESSSPELKAD
HHCCCCCCCHHHCCC		40.3025521595
31PhosphorylationFIDLESSSPELKADL
HCCCCCCCHHHCCCC		31.5022369663
35AcetylationESSSPELKADLRPLQ
CCCCHHHCCCCCCCC		37.8924489116
35SuccinylationESSSPELKADLRPLQ
CCCCHHHCCCCCCCC		37.8923954790
35UbiquitinationESSSPELKADLRPLQ
CCCCHHHCCCCCCCC		37.8923749301
44AcetylationDLRPLQIKSIREIDV
CCCCCCCCEEEEEEC		27.2024489116
44UbiquitinationDLRPLQIKSIREIDV
CCCCCCCCEEEEEEC		27.2023749301
52PhosphorylationSIREIDVTGGKKALV
EEEEEECCCCCEEEE		36.1521440633
55SuccinylationEIDVTGGKKALVLFV
EEECCCCCEEEEEEE		35.9023954790
56UbiquitinationIDVTGGKKALVLFVP
EECCCCCEEEEEEEE		50.6723749301
68PhosphorylationFVPVPALSAYHKVQT
EEECCHHHHHHHHHH		28.9621440633
72UbiquitinationPALSAYHKVQTKLTR
CHHHHHHHHHHHHHH		24.3022817900
72AcetylationPALSAYHKVQTKLTR
CHHHHHHHHHHHHHH		24.3024489116
75PhosphorylationSAYHKVQTKLTRELE
HHHHHHHHHHHHHHH		30.8923749301
76UbiquitinationAYHKVQTKLTRELEK
HHHHHHHHHHHHHHH		30.6723749301
83UbiquitinationKLTRELEKKFPDRHV
HHHHHHHHHCCCCEE		72.7922817900
84UbiquitinationLTRELEKKFPDRHVI
HHHHHHHHCCCCEEE		53.4022817900
103PhosphorylationRRILPKPSRTSRQVQ
CCCCCCCCCCCHHHH		55.0830377154
106PhosphorylationLPKPSRTSRQVQKRP
CCCCCCCCHHHHHCC		21.4330377154
115PhosphorylationQVQKRPRSRTLTAVH
HHHHCCCCCCCHHHC		32.0922369663
117PhosphorylationQKRPRSRTLTAVHDK
HHCCCCCCCHHHCHH		29.7022369663
119PhosphorylationRPRSRTLTAVHDKVL
CCCCCCCHHHCHHHH		26.4822369663
124AcetylationTLTAVHDKVLEDMVF
CCHHHCHHHHHHCCC		33.5624489116
124UbiquitinationTLTAVHDKVLEDMVF
CCHHHCHHHHHHCCC		33.5617644757
138UbiquitinationFPTEIVGKRVRYLVG
CCHHHCCCEEEEEEC		36.5023749301
142PhosphorylationIVGKRVRYLVGGNKI
HCCCEEEEEECCCCC		11.6821440633
148UbiquitinationRYLVGGNKIQKVLLD
EEEECCCCCEEEECC		50.1923749301
151UbiquitinationVGGNKIQKVLLDSKD
ECCCCCEEEECCCCC		38.0223749301
156PhosphorylationIQKVLLDSKDVQQID
CEEEECCCCCHHHHH		30.6323749301
157UbiquitinationQKVLLDSKDVQQIDY
EEEECCCCCHHHHHH		62.6823749301
165UbiquitinationDVQQIDYKLESFQAV
CHHHHHHHHHHHHHH		41.8724961812
168PhosphorylationQIDYKLESFQAVYNK
HHHHHHHHHHHHHHH		32.8530377154
175UbiquitinationSFQAVYNKLTGKQIV
HHHHHHHHHCCCEEE		29.7323749301
179UbiquitinationVYNKLTGKQIVFEIP
HHHHHCCCEEEEECC		31.4523749301
187PhosphorylationQIVFEIPSQTN----
EEEEECCCCCC----		56.1328152593
189PhosphorylationVFEIPSQTN------
EEECCCCCC------		47.4330377154
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 RS7B_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RS7B_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 RS7B_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MPP10_YEASTMPP10physical
15590835
YCA2_YEASTYCL002Cgenetic
27708008
RPA14_YEASTRPA14genetic
27708008
CSN12_YEASTYJR084Wgenetic
27708008
ADY4_YEASTADY4genetic
27708008
CDC73_YEASTCDC73genetic
27708008
RAD14_YEASTRAD14genetic
27708008
IZH2_YEASTIZH2genetic
27708008
INO4_YEASTINO4genetic
27708008
CDC24_YEASTCDC24genetic
27708008
PRP6_YEASTPRP6genetic
27708008
TECR_YEASTTSC13genetic
27708008
RPN6_YEASTRPN6genetic
27708008
PSB3_YEASTPUP3genetic
27708008
CDC4_YEASTCDC4genetic
27708008
ACT_YEASTACT1genetic
27708008
TEL2_YEASTTEL2genetic
27708008
RPN1_YEASTRPN1genetic
27708008
MED6_YEASTMED6genetic
27708008
PRS7_YEASTRPT1genetic
27708008
PRP19_YEASTPRP19genetic
27708008
SEC22_YEASTSEC22genetic
27708008
YSY6_YEASTYSY6genetic
27708008
PAT1_YEASTPAT1genetic
27708008
S2538_YEASTYDL119Cgenetic
27708008
ATG9_YEASTATG9genetic
27708008
DHAS_YEASTHOM2genetic
27708008
LSM6_YEASTLSM6genetic
27708008
YFD4_YEASTYFL034Wgenetic
27708008
LIF1_YEASTLIF1genetic
27708008
ATG1_YEASTATG1genetic
27708008
YOR1_YEASTYOR1genetic
27708008
HTD2_YEASTHTD2genetic
27708008
COX23_YEASTCOX23genetic
27708008
POG1_YEASTPOG1genetic
27708008
SNX4_YEASTSNX4genetic
27708008
LSM1_YEASTLSM1genetic
27708008
HAL5_YEASTHAL5genetic
27708008
DENR_YEASTTMA22genetic
27708008
YJ24_YEASTKCH1genetic
27708008
CBF1_YEASTCBF1genetic
27708008
MDM35_YEASTMDM35genetic
27708008
HBS1_YEASTHBS1genetic
27708008
DNM1_YEASTDNM1genetic
27708008
RT109_YEASTRTT109genetic
27708008
ENT4_YEASTENT4genetic
27708008
RL8B_YEASTRPL8Bgenetic
27708008
RIC1_YEASTRIC1genetic
27708008
YL149_YEASTYLR149Cgenetic
27708008
VBA1_YEASTVBA1genetic
27708008
COX7_YEASTCOX7genetic
27708008
SCS7_YEASTSCS7genetic
27708008
PT127_YEASTPET127genetic
27708008
RTC6_YEASTRTC6genetic
27708008
GRE1_YEASTGRE1genetic
27708008
KAR3_YEASTKAR3genetic
27708008
RL36A_YEASTRPL36Agenetic
29158977
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RS7B_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.
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-14; SER-31;SER-115; THR-119 AND SER-156, 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-115 AND THR-117, ANDMASS SPECTROMETRY.
"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 SER-31, 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-31, AND MASSSPECTROMETRY.

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