Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  40S ribosomal protein S2  

UniProtKB / Swiss-Prot ID :  RS2_HUMAN

Gene Name (Synonyms) : 
RPS2, RPS4  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :   

Protein Sequence MADDAGAAGGPGGPGGPGMGNRGGFRGGFGSGIRGRGRGRGRGRGRGRGARGGKAEDKEWMPVTKLGRLV...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCEEHHHHHHHH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MADDAG
---CCCCCC
24.32UniProtKB
Link-
345-methylarginineGSGIRGRGR
CCCCCCCCC
32.08MeMo
Link-
365-methylarginineGIRGRGRGR
CCCCCCCCC
23.06MeMo
Link-
385-methylarginineRGRGRGRGR
CCCCCCCCC
30.21MeMo
Link-
405-methylarginineRGRGRGRGR
CCCCCCCCC
30.21MeMo
Link-
425-methylarginineRGRGRGRGR
CCCCCCCCC
30.21MeMo
Link-
445-methylarginineRGRGRGRGR
CCCCCCCCC
30.21MeMo
Link-
465-methylarginineRGRGRGRGA
CCCCCCCCC
30.21MeMo
Link-
485-methylarginineRGRGRGARG
CCCCCCCCC
33.95MeMo
Link-
58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KAEDKEWMP
CCCCCCCEE
44.79Phosphositeplus
Link
65Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)MPVTKLGRL
EEHHHHHHH
49.53Phosphositeplus
Link
76Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DMKIKSLEE
CCCCCCHHH
43.39Phosphositeplus
Link
77PhosphoserineMKIKSLEEI
CCCCCHHHH
44.48Phosphositeplus
Link
108Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DEVLKIMPV
EEEEEEECE
41.98Phosphositeplus
Link
114Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)MPVQKQTRA
ECEEEEECC
54.60Phosphositeplus
Link
133PhosphotyrosineAIGDYNGHV
EEECCCCEE
20.17HPRD
Link
133PhosphotyrosineAIGDYNGHV
EEECCCCEE
20.17Phosphositeplus
Link
133Phosphotyrosine.AIGDYNGHV
EEECCCCEE
20.17UniProtKB
Link
206PhosphoserineTGIVSAPVP
CEEEECCHH
25.57Phosphositeplus
Link
229S-nitrosocysteineSARGCTATL
EECCCCCCH
1.63dbSNO
Link
246Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DAISKTYSY
HHHHHCCCC
45.42Phosphositeplus
Link
248PhosphotyrosineISKTYSYLT
HHHCCCCCC
10.08Phosphositeplus
Link
257Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PDLWKETVF
HHHHHHCCC
51.29Phosphositeplus
Link
262PhosphothreonineETVFTKSPY
HCCCCCCHH
26.69HPRD
Link
263Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TVFTKSPYQ
CCCCCCHHH
37.66Phosphositeplus
Link
263N6-acetyllysineTVFTKSPYQ
CCCCCCHHH
37.66HPRD
Link
263N6-acetyllysineTVFTKSPYQ
CCCCCCHHH
37.66Phosphositeplus
Link
263N6-acetyllysine.TVFTKSPYQ
CCCCCCHHH
37.66UniProtKB
Link
264PhosphoserineVFTKSPYQE
CCCCCHHHH
26.28HPRD
Link
264PhosphoserineVFTKSPYQE
CCCCCHHHH
26.28PhosphoELM
Link
264PhosphoserineVFTKSPYQE
CCCCCHHHH
26.28Phosphositeplus
Link
264PhosphoserineVFTKSPYQE
CCCCCHHHH
26.28SysPTM
Link
264Phosphoserine.VFTKSPYQE
CCCCCHHHH
26.28UniProtKB
Link
266PhosphotyrosineTKSPYQEFT
CCCHHHHHH
27.97Phosphositeplus
Link
266PhosphotyrosineTKSPYQEFT
CCCHHHHHH
27.97SysPTM
Link
275Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DHLVKTHTR
HHHHHCCCC
40.73Phosphositeplus
Link
275N6-acetyllysineDHLVKTHTR
HHHHHCCCC
40.73HPRD
Link
275N6-acetyllysineDHLVKTHTR
HHHHHCCCC
40.73Phosphositeplus
Link
275N6-acetyllysine.DHLVKTHTR
HHHHHCCCC
40.73UniProtKB
Link
278PhosphothreonineVKTHTRVSV
HHCCCCEEE
37.69HPRD
Link-
278PhosphothreonineVKTHTRVSV
HHCCCCEEE
37.69PhosphoELM
Link-
278PhosphothreonineVKTHTRVSV
HHCCCCEEE
37.69Phosphositeplus
Link-
278Phosphothreonine.VKTHTRVSV
HHCCCCEEE
37.69UniProtKB
Link-
281PhosphoserineHTRVSVQRT
CCCEEEEEE
14.83HPRD
Link-
281PhosphoserineHTRVSVQRT
CCCEEEEEE
14.83Phosphositeplus
Link-
281Phosphoserine.HTRVSVQRT
CCCEEEEEE
14.83UniProtKB
Link-
293PhosphothreonineAVATT
CCCCC
27.20HPRD
Link
293PhosphothreonineAVATT
CCCCC
27.20PhosphoELM
Link
293PhosphothreonineAVATT
CCCCC
27.20Phosphositeplus
Link
293Phosphothreonine.AVATT
CCCCC
27.20UniProtKB
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
RS20_HUMANENSP00000341885STRING
RL18_HUMANENSP00000341885STRING
RS5_HUMANENSP00000341885STRING
RL6_HUMANENSP00000341885STRING
RS18_HUMANENSP00000341885STRING
EIF3D_HUMANENSP00000341885STRING
IF5_HUMANENSP00000341885STRING
EIF3E_HUMANENSP00000341885STRING
RS19_HUMANENSP00000341885STRING
RL18A_HUMANENSP00000341885STRING
RL19_HUMANENSP00000341885STRING
RS13_HUMANENSP00000341885STRING
RS12_HUMANENSP00000341885STRING
RS15_HUMANENSP00000341885STRING
RS25_HUMANENSP00000341885STRING
EIF3K_HUMANENSP00000341885STRING
RS4Y1_HUMANENSP00000341885STRING
RS16_HUMANENSP00000341885STRING
RL36_HUMANENSP00000341885STRING
IF2G_HUMANENSP00000341885STRING
EIF3G_HUMANENSP00000341885STRING
IF2A_HUMANENSP00000341885STRING
RL35_HUMANENSP00000341885STRING
EIF3J_HUMANENSP00000341885STRING
IF4B_HUMANENSP00000341885STRING
RL8_HUMANENSP00000341885STRING
RL31_HUMANENSP00000341885STRING
RL26L_HUMANENSP00000341885STRING
RL24_HUMANENSP00000341885STRING
IF4H_HUMANENSP00000341885STRING
RL3L_HUMANENSP00000341885STRING
RS11_HUMANENSP00000341885STRING
RL13A_HUMANENSP00000341885STRING
RS27A_HUMANENSP00000341885STRING
UBIQ_HUMANENSP00000341885STRING
RL37_HUMANENSP00000341885STRING
EIF3H_HUMANENSP00000341885STRING
RS3_HUMANENSP00000341885STRING
UBIM_HUMANENSP00000341885STRING
RS30_HUMANENSP00000341885STRING
IF4E_HUMANENSP00000341885STRING
RL30_HUMANENSP00000341885STRING
IF2P_HUMANENSP00000341885STRING
RL26_HUMANENSP00000341885STRING
RL29_HUMANENSP00000341885STRING
RS23_HUMANENSP00000341885STRING
RS9_HUMANENSP00000341885STRING
RL13_HUMANENSP00000341885STRING
EF2_HUMANENSP00000341885STRING
RL38_HUMANENSP00000341885STRING
EIF3F_HUMANENSP00000341885STRING
EIF3F_HUMANENSP00000341885STRING
RS14_HUMANENSP00000341885STRING
RL4_HUMANENSP00000341885STRING
PABP1_HUMANENSP00000341885STRING
RS15A_HUMANENSP00000341885STRING
RLA2_HUMANENSP00000341885STRING
IF4G1_HUMANENSP00000341885STRING
IF4A2_HUMANENSP00000341885STRING
RL35A_HUMANENSP00000341885STRING
RL35A_HUMANENSP00000341885STRING
EIF3C_HUMANENSP00000341885STRING
RLA0_HUMANENSP00000341885STRING
RL32_HUMANENSP00000341885STRING
RS7_HUMANENSP00000341885STRING
RL7_HUMANENSP00000341885STRING
RL10_HUMANENSP00000341885STRING
RL28_HUMANENSP00000341885STRING
RL3_HUMANENSP00000341885STRING
RL27A_HUMANENSP00000341885STRING
RLA1_HUMANENSP00000341885STRING
RL23_HUMANENSP00000341885STRING
RS17_HUMANENSP00000341885STRING
RS3A_HUMANENSP00000341885STRING
RSSA_HUMANENSP00000341885STRING
RL22_HUMANENSP00000341885STRING
RL15_HUMANENSP00000341885STRING
RL23A_HUMANENSP00000341885STRING
RS26_HUMANENSP00000341885STRING
RS28_HUMANENSP00000341885STRING
RL37A_HUMANENSP00000341885STRING
ERF1_HUMANENSP00000341885STRING
RL10A_HUMANENSP00000341885STRING
RL39_HUMANENSP00000341885STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-281, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-263 AND LYS-275, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-281, AND MASS SPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-133, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264 AND SER-281, ANDMASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-293, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-278, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-293, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures