RPS3 | ENSG00000149273 | NCBI 6188

Details for: RPS3

Gene ID: 6188

Gene Type: Protein-coding - A gene that serves as a template for producing a messenger RNA (mRNA) molecule, which is then translated into a functional protein.

Symbol: RPS3

Ensembl ID: ENSG00000149273

Description: ribosomal protein S3

Cell Significance Landscape

Display Count:

Associated with

Activation of the mrna upon binding of the cap-binding complex and eifs, and subsequent binding to 43s
(R-HSA-72662)
Axon guidance
(R-HSA-422475)
Cap-dependent translation initiation
(R-HSA-72737)
Cellular responses to stimuli
(R-HSA-8953897)
Cellular responses to stress
(R-HSA-2262752)
Cellular response to starvation
(R-HSA-9711097)
Developmental biology
(R-HSA-1266738)
Disease
(R-HSA-1643685)
Eukaryotic translation elongation
(R-HSA-156842)
Eukaryotic translation initiation
(R-HSA-72613)
Eukaryotic translation termination
(R-HSA-72764)
Formation of a pool of free 40s subunits
(R-HSA-72689)
Formation of the ternary complex, and subsequently, the 43s complex
(R-HSA-72695)
Gtp hydrolysis and joining of the 60s ribosomal subunit
(R-HSA-72706)
Infectious disease
(R-HSA-5663205)
Influenza infection
(R-HSA-168255)
Influenza viral rna transcription and replication
(R-HSA-168273)
L13a-mediated translational silencing of ceruloplasmin expression
(R-HSA-156827)
Major pathway of rrna processing in the nucleolus and cytosol
(R-HSA-6791226)
Metabolism
(R-HSA-1430728)
Metabolism of amino acids and derivatives
(R-HSA-71291)
Metabolism of proteins
(R-HSA-392499)
Metabolism of rna
(R-HSA-8953854)
Nervous system development
(R-HSA-9675108)
Nonsense-mediated decay (nmd)
(R-HSA-927802)
Nonsense mediated decay (nmd) enhanced by the exon junction complex (ejc)
(R-HSA-975957)
Nonsense mediated decay (nmd) independent of the exon junction complex (ejc)
(R-HSA-975956)
Peptide chain elongation
(R-HSA-156902)
Regulation of expression of slits and robos
(R-HSA-9010553)
Response of eif2ak4 (gcn2) to amino acid deficiency
(R-HSA-9633012)
Ribosomal scanning and start codon recognition
(R-HSA-72702)
Rrna processing
(R-HSA-72312)
Rrna processing in the nucleus and cytosol
(R-HSA-8868773)
Sars-cov-1 infection
(R-HSA-9678108)
Sars-cov-1 modulates host translation machinery
(R-HSA-9735869)
Sars-cov-1-host interactions
(R-HSA-9692914)
Sars-cov-2 infection
(R-HSA-9694516)
Sars-cov-2 modulates host translation machinery
(R-HSA-9754678)
Sars-cov-2-host interactions
(R-HSA-9705683)
Sars-cov infections
(R-HSA-9679506)
Selenoamino acid metabolism
(R-HSA-2408522)
Selenocysteine synthesis
(R-HSA-2408557)
Signaling by robo receptors
(R-HSA-376176)
Srp-dependent cotranslational protein targeting to membrane
(R-HSA-1799339)
Translation initiation complex formation
(R-HSA-72649)
Viral infection pathways
(R-HSA-9824446)
Viral mrna translation
(R-HSA-192823)
Apoptotic process
(GO:0006915)
Base-excision repair
(GO:0006284)
Cell division
(GO:0051301)
Cellular response to hydrogen peroxide
(GO:0070301)
Cellular response to reactive oxygen species
(GO:0034614)
Cellular response to tumor necrosis factor
(GO:0071356)
Chromosome segregation
(GO:0007059)
Class i dna-(apurinic or apyrimidinic site) endonuclease activity
(GO:0140078)
Cytoplasm
(GO:0005737)
Cytoplasmic translation
(GO:0002181)
Cytosol
(GO:0005829)
Cytosolic ribosome
(GO:0022626)
Cytosolic small ribosomal subunit
(GO:0022627)
Damaged dna binding
(GO:0003684)
Dna-(apurinic or apyrimidinic site) endonuclease activity
(GO:0003906)
Dna-binding transcription factor binding
(GO:0140297)
Dna binding
(GO:0003677)
Dna damage response
(GO:0006974)
Dna endonuclease activity
(GO:0004520)
Dna n-glycosylase activity
(GO:0019104)
Dna repair
(GO:0006281)
Endoplasmic reticulum
(GO:0005783)
Enzyme binding
(GO:0019899)
Extracellular exosome
(GO:0070062)
Focal adhesion
(GO:0005925)
Hsp70 protein binding
(GO:0030544)
Hsp90 protein binding
(GO:0051879)
Iron-sulfur cluster binding
(GO:0051536)
Kinase binding
(GO:0019900)
Membrane
(GO:0016020)
Microtubule binding
(GO:0008017)
Mitochondrial inner membrane
(GO:0005743)
Mitochondrial matrix
(GO:0005759)
Mitotic spindle
(GO:0072686)
Mrna binding
(GO:0003729)
Negative regulation of dna repair
(GO:0045738)
Negative regulation of protein ubiquitination
(GO:0031397)
Negative regulation of translation
(GO:0017148)
Nf-kappab complex
(GO:0071159)
Nucleolus
(GO:0005730)
Nucleoplasm
(GO:0005654)
Nucleus
(GO:0005634)
Oxidized purine dna binding
(GO:0032357)
Oxidized pyrimidine dna binding
(GO:0032358)
Plasma membrane
(GO:0005886)
Positive regulation of activated t cell proliferation
(GO:0042104)
Positive regulation of apoptotic signaling pathway
(GO:2001235)
Positive regulation of base-excision repair
(GO:1905053)
Positive regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis
(GO:2001272)
Positive regulation of dna repair
(GO:0045739)
Positive regulation of endodeoxyribonuclease activity
(GO:0032079)
Positive regulation of gene expression
(GO:0010628)
Positive regulation of interleukin-2 production
(GO:0032743)
Positive regulation of intrinsic apoptotic signaling pathway in response to dna damage
(GO:1902231)
Positive regulation of jun kinase activity
(GO:0043507)
Positive regulation of microtubule polymerization
(GO:0031116)
Positive regulation of nf-kappab transcription factor activity
(GO:0051092)
Positive regulation of non-canonical nf-kappab signal transduction
(GO:1901224)
Positive regulation of protein-containing complex assembly
(GO:0031334)
Positive regulation of t cell receptor signaling pathway
(GO:0050862)
Postsynaptic density
(GO:0014069)
Protein-containing complex binding
(GO:0044877)
Protein binding
(GO:0005515)
Protein kinase a binding
(GO:0051018)
Protein kinase binding
(GO:0019901)
Regulation of apoptotic process
(GO:0042981)
Response to tnf agonist
(GO:0061481)
Ribonucleoprotein complex
(GO:1990904)
Ribosome
(GO:0005840)
Rna binding
(GO:0003723)
Rna polymerase ii transcription regulatory region sequence-specific dna binding
(GO:0000977)
Ruffle membrane
(GO:0032587)
Small ribosomal subunit rrna binding
(GO:0070181)
Spindle assembly
(GO:0051225)
Structural constituent of ribosome
(GO:0003735)
Supercoiled dna binding
(GO:0097100)
Translation
(GO:0006412)
Translational initiation
(GO:0006413)
Tubulin binding
(GO:0015631)
Ubiquitin-like protein conjugating enzyme binding
(GO:0044390)

Significant Cells

Cell Significance Index (CSI) scores for the chosen context(s)

central memory CD4-positive, alpha-beta T cell CL0000904

CSI 163.81

rCSI 96.74%

PRS 2.52
hematopoietic stem cell CL0000037

CSI 149.55

rCSI 99.4%

PRS 2.15
CD16-positive, CD56-dim natural killer cell, human CL0000939

CSI 143.94

rCSI 95.93%

PRS 5.12
naive T cell CL0000898

CSI 143

rCSI 99.52%

PRS 2.63
naive thymus-derived CD8-positive, alpha-beta T cell CL0000900

CSI 142.72

rCSI 100%

PRS 5.52
central memory CD8-positive, alpha-beta T cell CL0000907

CSI 141.1

rCSI 95.06%

PRS 2.18
plasmacytoid dendritic cell, human CL0001058

CSI 138.75

rCSI 96.88%

PRS 1.9
double negative thymocyte CL0002489

CSI 137.76

rCSI 95.77%

PRS 2.11
CD4-positive, alpha-beta memory T cell CL0000897

CSI 136.22

rCSI 97.79%

PRS 2.46
CD16-negative, CD56-bright natural killer cell, human CL0000938

CSI 130.64

rCSI 97.97%

PRS 5.45
class switched memory B cell CL0000972

CSI 129.15

rCSI 96.42%

PRS 3.06
T follicular helper cell CL0002038

CSI 127.58

rCSI 95.48%

PRS 2.96
group 3 innate lymphoid cell CL0001071

CSI 127.32

rCSI 95.66%

PRS 1.86
neural crest cell CL0011012

CSI 125.01

rCSI 98.81%

PRS 1.25
effector CD8-positive, alpha-beta T cell CL0001050

CSI 124.82

rCSI 94.94%

PRS 2.4
epithelial cell of lower respiratory tract CL0002632

CSI 123.22

rCSI 95.52%

PRS 1.72
immature B cell CL0000816

CSI 122.89

rCSI 91.3%

PRS 2.69
mucosal invariant T cell CL0000940

CSI 122.54

rCSI 99.02%

PRS 4.74
pro-B cell CL0000826

CSI 122.53

rCSI 100%

PRS 1.8
CD4-positive, alpha-beta thymocyte CL0000810

CSI 122.19

rCSI 97.87%

PRS 3.39
common myeloid progenitor CL0000049

CSI 120.78

rCSI 97.66%

PRS 1.77
T-helper 17 cell CL0000899

CSI 118.99

rCSI 94.48%

PRS 3.21
mature T cell CL0002419

CSI 118.76

rCSI 92.37%

PRS 2.59
CD4-positive helper T cell CL0000492

CSI 118.23

rCSI 89.43%

PRS 2.53
keratinocyte CL0000312

CSI 117.3

rCSI 98.32%

PRS 2.17
bronchus fibroblast of lung CL2000093

CSI 116.46

rCSI 94.63%

PRS 1.88
granulocyte monocyte progenitor cell CL0000557

CSI 115.31

rCSI 99.84%

PRS 2.02
epithelial cell of lung CL0000082

CSI 113.89

rCSI 94.42%

PRS 1.68
mature B cell CL0000785

CSI 113.73

rCSI 98.87%

PRS 2.22
naive B cell CL0000788

CSI 113.71

rCSI 97.53%

PRS 5.87
early lymphoid progenitor CL0000936

CSI 113.65

rCSI 99.82%

PRS 2.02
effector memory CD8-positive, alpha-beta T cell CL0000913

CSI 112.05

rCSI 100%

PRS 2.82
CD14-low, CD16-positive monocyte CL0002396

CSI 110.92

rCSI 85.46%

PRS 1.63
unswitched memory B cell CL0000970

CSI 110.47

rCSI 92.94%

PRS 3.04
plasmablast CL0000980

CSI 108.77

rCSI 85.57%

PRS 2.14
activated CD4-positive, alpha-beta T cell CL0000896

CSI 108.17

rCSI 100%

PRS 3.31
megakaryocyte-erythroid progenitor cell CL0000050

CSI 107.65

rCSI 97.22%

PRS 1.59
precursor B cell CL0000817

CSI 107.58

rCSI 94.24%

PRS 2.44
skin fibroblast CL0002620

CSI 107.5

rCSI 92.67%

PRS 3.02
intestine goblet cell CL0019031

CSI 106.48

rCSI 94.52%

PRS 1.81
goblet cell CL0000160

CSI 100.65

rCSI 95.11%

PRS 1.89
CD4-positive, CD25-positive, alpha-beta regulatory T cell CL0000792

CSI 98.47

rCSI 96.71%

PRS 2.89
double-positive, alpha-beta thymocyte CL0000809

CSI 98.12

rCSI 100%

PRS 2.62
respiratory basal cell CL0002633

CSI 98.01

rCSI 100%

PRS 2.11
activated CD8-positive, alpha-beta T cell CL0000906

CSI 97.95

rCSI 96.28%

PRS 5.41
memory B cell CL0000787

CSI 97.57

rCSI 96.35%

PRS 8.01
hematopoietic precursor cell CL0008001

CSI 95.55

rCSI 98.3%

PRS 2.9
fibroblast of lung CL0002553

CSI 94.81

rCSI 88.23%

PRS 1.8
fallopian tube secretory epithelial cell CL4030006

CSI 94.71

rCSI 91.17%

PRS 1.88
pancreatic D cell CL0000173

CSI 94.58

rCSI 93.02%

PRS 2
CD8-positive, alpha-beta memory T cell CL0000909

CSI 93.04

rCSI 97.17%

PRS 5.83
small pre-B-II cell CL0000954

CSI 92.87

rCSI 89.31%

PRS 3.95
intestinal epithelial cell CL0002563

CSI 92.62

rCSI 96.81%

PRS 1.94
IgA plasma cell CL0000987

CSI 88.6

rCSI 90.7%

PRS 3.42
gamma-delta T cell CL0000798

CSI 87.35

rCSI 100%

PRS 18.38
activated type II NK T cell CL0000931

CSI 85.41

rCSI 96.12%

PRS 3.04
pancreatic A cell CL0000171

CSI 84.01

rCSI 88.01%

PRS 1.95
fraction A pre-pro B cell CL0002045

CSI 83.58

rCSI 95.67%

PRS 3.76
elicited macrophage CL0000861

CSI 81.97

rCSI 75.26%

PRS 2.06
alveolar type 1 fibroblast cell CL4028004

CSI 81.27

rCSI 89.01%

PRS 2.12
ciliated epithelial cell CL0000067

CSI 79.81

rCSI 70.19%

PRS 1.31
CD4-positive, alpha-beta T cell CL0000624

CSI 79.79

rCSI 100%

PRS 39.48
transit amplifying cell of colon CL0009011

CSI 79.72

rCSI 93.62%

PRS 2.21
naive thymus-derived CD4-positive, alpha-beta T cell CL0000895

CSI 79.04

rCSI 99.32%

PRS 9.96
neuroblast (sensu Nematoda and Protostomia) CL0000338

CSI 79.03

rCSI 91.27%

PRS 1.69
multi-ciliated epithelial cell CL0005012

CSI 78.95

rCSI 78.79%

PRS 1.52
common dendritic progenitor CL0001029

CSI 77.95

rCSI 97.83%

PRS 2.29
melanocyte CL0000148

CSI 76.88

rCSI 56.94%

PRS 1.72
mature NK T cell CL0000814

CSI 75.73

rCSI 96.87%

PRS 8.41
secretory cell CL0000151

CSI 74.97

rCSI 78.23%

PRS 1.85
CD1c-positive myeloid dendritic cell CL0002399

CSI 74.81

rCSI 90.36%

PRS 2.07
enteroendocrine cell CL0000164

CSI 74.72

rCSI 100%

PRS 2
respiratory suprabasal cell CL4033048

CSI 74.29

rCSI 95.28%

PRS 2.09
effector memory CD4-positive, alpha-beta T cell CL0000905

CSI 74.24

rCSI 100%

PRS 4.53
B cell CL0000236

CSI 73.97

rCSI 98.97%

PRS 11.11
M cell of gut CL0000682

CSI 73.89

rCSI 78.51%

PRS 3.27
CD4-positive, alpha-beta cytotoxic T cell CL0000934

CSI 72.79

rCSI 100%

PRS 3.88
extravillous trophoblast CL0008036

CSI 72.72

rCSI 89.96%

PRS 1.6
mesodermal cell CL0000222

CSI 72.3

rCSI 86.78%

PRS 1.81
conventional dendritic cell CL0000990

CSI 71.4

rCSI 59.61%

PRS 6.01
common lymphoid progenitor CL0000051

CSI 69.36

rCSI 92.69%

PRS 3.46
promyelocyte CL0000836

CSI 69.33

rCSI 100%

PRS 2.51
lung ciliated cell CL1000271

CSI 69.09

rCSI 79.89%

PRS 1.31
pulmonary ionocyte CL0017000

CSI 69.06

rCSI 84.07%

PRS 2.29
peripheral nervous system neuron CL2000032

CSI 69

rCSI 94.01%

PRS 1.65
neuroblast (sensu Vertebrata) CL0000031

CSI 68.28

rCSI 87.63%

PRS 1.82
pulmonary artery endothelial cell CL1001568

CSI 66.74

rCSI 90.81%

PRS 2.77
endothelial cell of artery CL1000413

CSI 66.33

rCSI 97.18%

PRS 11.16
mucous neck cell CL0000651

CSI 65.8

rCSI 94.83%

PRS 2.94
perivascular cell CL4033054

CSI 65.78

rCSI 89.92%

PRS 2.07
CD14-positive monocyte CL0001054

CSI 65.66

rCSI 81.78%

PRS 2.67
acinar cell CL0000622

CSI 65.45

rCSI 95.97%

PRS 2.39
enteric smooth muscle cell CL0002504

CSI 65.22

rCSI 93.08%

PRS 2.06
IgG plasma cell CL0000985

CSI 64.63

rCSI 77.42%

PRS 3.13
myofibroblast cell CL0000186

CSI 64.18

rCSI 88.89%

PRS 2.6
colon epithelial cell CL0011108

CSI 64.08

rCSI 67.12%

PRS 1.69
transit amplifying cell CL0009010

CSI 63.56

rCSI 97.22%

PRS 2.96
CD8-positive, alpha-beta cytotoxic T cell CL0000794

CSI 63.42

rCSI 75.72%

PRS 3.14
nasal mucosa goblet cell CL0002480

CSI 63.33

rCSI 73.45%

PRS 2.7
CD8-positive, alpha-beta thymocyte CL0000811

CSI 63.33

rCSI 98.75%

PRS 4.73

VIP GABAergic cortical interneuron CL4023016

CSI -53.6

rCSI -64.0%

PRS 1.2%
sst GABAergic cortical interneuron CL4023017

CSI -50.6

rCSI -65.2%

PRS 1.3%
pvalb GABAergic cortical interneuron CL4023018

CSI -48.2

rCSI -60.0%

PRS 1.1%
vascular leptomeningeal cell CL4023051

CSI -46.3

rCSI -81.2%

PRS 1.5%
inhibitory interneuron CL0000498

CSI -33.0

rCSI -76.2%

PRS 1.8%
astrocyte of the cerebral cortex CL0002605

CSI -26.3

rCSI -59.0%

PRS 1.2%
lamp5 GABAergic cortical interneuron CL4023011

CSI -26.2

rCSI -44.0%

PRS 1.2%
cardiac neuron CL0010022

CSI -25.5

rCSI -81.7%

PRS 1.3%
caudal ganglionic eminence derived cortical interneuron CL4023064

CSI -20.5

rCSI -36.1%

PRS 1.1%
kidney interstitial alternatively activated macrophage CL1000695

CSI -19.1

rCSI -49.7%

PRS 2.3%
sncg GABAergic cortical interneuron CL4023015

CSI -18.8

rCSI -30.3%

PRS 1.4%
L6b glutamatergic cortical neuron CL4023038

CSI -18.8

rCSI -58.7%

PRS 1.2%
mature astrocyte CL0002627

CSI -16.9

rCSI -71.9%

PRS 4.7%
L2/3-6 intratelencephalic projecting glutamatergic neuron CL4023040

CSI -16.3

rCSI -39.5%

PRS 1.2%
chandelier pvalb GABAergic cortical interneuron CL4023036

CSI -15.9

rCSI -49.7%

PRS 1.4%
L5 extratelencephalic projecting glutamatergic cortical neuron CL4023041

CSI -15.6

rCSI -56.2%

PRS 1.0%
adipocyte CL0000136

CSI -14.3

rCSI -18.4%

PRS 2.4%
near-projecting glutamatergic cortical neuron CL4023012

CSI -12.3

rCSI -46.6%

PRS 1.3%
GABAergic neuron CL0000617

CSI -12.0

rCSI -40.3%

PRS 2.0%
kidney proximal convoluted tubule epithelial cell CL1000838

CSI -10.7

rCSI -100.0%

PRS 28.7%
midzonal region hepatocyte CL0019028

CSI -10.0

rCSI -23.6%

PRS 3.3%
squamous epithelial cell CL0000076

CSI -9.9

rCSI -23.6%

PRS 2.4%
glutamatergic neuron CL0000679

CSI -8.0

rCSI -16.4%

PRS 2.2%
OFFx cell CL4033036

CSI -7.8

rCSI -36.9%

PRS 5.3%
periportal region hepatocyte CL0019026

CSI -7.8

rCSI -30.3%

PRS 3.2%
diffuse bipolar 6 cell CL4033032

CSI -7.7

rCSI -40.5%

PRS 5.6%
cerebral cortex neuron CL0010012

CSI -7.6

rCSI -30.9%

PRS 2.6%
retinal bipolar neuron CL0000748

CSI -7.1

rCSI -13.2%

PRS 1.5%
corticothalamic-projecting glutamatergic cortical neuron CL4023013

CSI -6.9

rCSI -40.9%

PRS 1.4%
cardiac endothelial cell CL0010008

CSI -6.9

rCSI -27.7%

PRS 2.2%
starburst amacrine cell CL0004232

CSI -6.9

rCSI -57.6%

PRS 5.0%
fast muscle cell CL0000190

CSI -6.1

rCSI -23.9%

PRS 11.3%
L4 intratelencephalic projecting glutamatergic neuron CL4030063

CSI -6.0

rCSI -14.5%

PRS 1.1%
neural cell CL0002319

CSI -5.7

rCSI -21.5%

PRS 4.3%
regular ventricular cardiac myocyte CL0002131

CSI -5.4

rCSI -33.9%

PRS 1.5%
diffuse bipolar 1 cell CL4033027

CSI -5.4

rCSI -40.7%

PRS 4.5%
kidney interstitial fibroblast CL1000692

CSI -5.4

rCSI -28.4%

PRS 13.8%
erythroid lineage cell CL0000764

CSI -5.1

rCSI -32.9%

PRS 5.2%
kidney granular cell CL0000648

CSI -4.9

rCSI -71.5%

PRS 23.4%
invaginating midget bipolar cell CL4033034

CSI -4.6

rCSI -27.3%

PRS 4.5%
renal interstitial pericyte CL1001318

CSI -4.3

rCSI -11.8%

PRS 2.1%
diffuse bipolar 4 cell CL4033031

CSI -4.0

rCSI -45.4%

PRS 5.8%
flat midget bipolar cell CL4033033

CSI -3.9

rCSI -27.9%

PRS 4.6%
cardiac blood vessel endothelial cell CL0010006

CSI -3.6

rCSI -25.4%

PRS 6.0%
epicardial adipocyte CL1000309

CSI -3.3

rCSI -10.6%

PRS 3.4%
cerebellar granule cell CL0001031

CSI -3.1

rCSI -4.6%

PRS 2.0%
rod bipolar cell CL0000751

CSI -2.8

rCSI -5.0%

PRS 1.6%
exhausted T cell CL0011025

CSI -2.4

rCSI -40.8%

PRS 10.4%
cell of skeletal muscle CL0000188

CSI -2.3

rCSI -25.1%

PRS 13.1%
ON midget ganglion cell CL4033046

CSI -1.9

rCSI -38.4%

PRS 2.3%
diffuse bipolar 2 cell CL4033028

CSI -1.8

rCSI -13.6%

PRS 5.1%
diffuse bipolar 3a cell CL4033029

CSI -1.6

rCSI -10.9%

PRS 4.5%
indirect pathway medium spiny neuron CL4023029

CSI -1.5

rCSI -35.2%

PRS 1.4%
OFF midget ganglion cell CL4033047

CSI -1.1

rCSI -21.8%

PRS 2.6%
Bergmann glial cell CL0000644

CSI -0.5

rCSI -0.7%

PRS 2.1%
cerebral cortex endothelial cell CL1001602

CSI -0.5

rCSI -0.8%

PRS 1.4%
kidney collecting duct principal cell CL1001431

CSI -0.4

rCSI -1.8%

PRS 12.8%
endocardial cell CL0002350

CSI 0.6

rCSI 3.0%

PRS 3.3%
glycinergic amacrine cell CL4030028

CSI 0.7

rCSI 1.7%

PRS 2.9%
differentiation-committed oligodendrocyte precursor CL4023059

CSI 0.7

rCSI 1.3%

PRS 2.1%
immature innate lymphoid cell CL0001082

CSI 0.9

rCSI 28.3%

PRS 33.4%
basal cell of epidermis CL0002187

CSI 1.0

rCSI 1.7%

PRS 2.6%
GABAergic amacrine cell CL4030027

CSI 1.0

rCSI 3.5%

PRS 2.7%
H2 horizontal cell CL0004218

CSI 1.1

rCSI 5.7%

PRS 3.7%
diffuse bipolar 3b cell CL4033030

CSI 1.4

rCSI 9.5%

PRS 4.8%
regular atrial cardiac myocyte CL0002129

CSI 1.4

rCSI 4.6%

PRS 2.3%
H1 horizontal cell CL0004217

CSI 1.5

rCSI 5.7%

PRS 5.3%
kidney resident macrophage CL1000698

CSI 1.5

rCSI 29.0%

PRS 47.0%
cardiac muscle cell CL0000746

CSI 2.0

rCSI 2.9%

PRS 1.6%
cholangiocyte CL1000488

CSI 2.1

rCSI 12.7%

PRS 4.3%
tracheobronchial goblet cell CL0019003

CSI 2.1

rCSI 34.3%

PRS 45.1%
group 3 innate lymphoid cell, human CL0001078

CSI 2.4

rCSI 49.7%

PRS 36.6%
macula densa epithelial cell CL1000850

CSI 2.4

rCSI 33.8%

PRS 28.5%
slow muscle cell CL0000189

CSI 2.7

rCSI 35.7%

PRS 25.1%
Purkinje cell CL0000121

CSI 2.7

rCSI 35.2%

PRS 18.8%
hepatic pit cell CL2000054

CSI 2.7

rCSI 37.0%

PRS 23.1%
B-1 B cell CL0000819

CSI 2.9

rCSI 74.5%

PRS 11.4%
cord blood hematopoietic stem cell CL2000095

CSI 3.0

rCSI 57.0%

PRS 16.0%
forebrain neuroblast CL1000042

CSI 3.0

rCSI 32.3%

PRS 27.7%
NKp44-negative group 3 innate lymphoid cell, human CL0001080

CSI 3.0

rCSI 93.4%

PRS 25.7%
pulmonary capillary endothelial cell CL4028001

CSI 3.1

rCSI 5.9%

PRS 2.9%
amacrine cell CL0000561

CSI 3.1

rCSI 9.1%

PRS 1.7%
helper T cell CL0000912

CSI 3.2

rCSI 4.5%

PRS 2.8%
renal intercalated cell CL0005010

CSI 3.2

rCSI 28.7%

PRS 18.0%
odontoblast CL0000060

CSI 3.2

rCSI 73.2%

PRS 11.0%
pluripotent stem cell CL0002248

CSI 3.3

rCSI 98.4%

PRS 4.7%
CD8-positive, alpha-beta memory T cell, CD45RO-positive CL0001203

CSI 3.6

rCSI 4.3%

PRS 2.8%
mesenchymal lymphangioblast CL0005021

CSI 3.7

rCSI 96.2%

PRS 10.6%
Merkel cell CL0000242

CSI 3.7

rCSI 86.3%

PRS 13.6%
kidney connecting tubule principal cell CL4030018

CSI 3.8

rCSI 27.3%

PRS 27.4%
osteoblast CL0000062

CSI 3.8

rCSI 95.0%

PRS 18.1%
platelet CL0000233

CSI 3.8

rCSI 15.9%

PRS 5.7%
lung microvascular endothelial cell CL2000016

CSI 3.8

rCSI 74.0%

PRS 6.7%
epithelial cell of urethra CL1000296

CSI 3.8

rCSI 96.6%

PRS 6.5%
eye photoreceptor cell CL0000287

CSI 4.0

rCSI 44.5%

PRS 7.8%
kidney collecting duct intercalated cell CL1001432

CSI 4.0

rCSI 28.6%

PRS 8.4%
prostate gland microvascular endothelial cell CL2000059

CSI 4.1

rCSI 96.8%

PRS 6.9%
cytotoxic T cell CL0000910

CSI 4.1

rCSI 23.4%

PRS 2.9%
hepatic stellate cell CL0000632

CSI 4.1

rCSI 15.4%

PRS 1.6%
serous secreting cell CL0000313

CSI 4.1

rCSI 20.8%

PRS 9.7%

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

Network Configuration

Explore relationships of the current gene. Select an Interaction Source: 'ONTOLOGY' for shared pathways (GO/Reactome) or 'STRING' for protein-protein interactions. Further refine by selecting context genes and comparing Cell Significance Index (CSI) scores between baseline and target cell types and their specific contexts.

Context Genes (max 20):

Interaction Source:

Pathway Categories (for ONTOLOGY source):

Baseline Cell Type:

Baseline Cell Context(s): Comma-separated if multiple.

Target Cell Type:

Target Cell Context(s): Comma-separated if multiple.

Legend:

Query Gene
Node Color (Target Cell CSI, relative to current network):
- Very High
- High
- Medium
- Low
- Very Low
- CSI N/A
Node Size: Proportional to Target Cell CSI magnitude
STRING PPI Edge
Shared Pathway Edge (ONTOLOGY)

Loading network (please wait)...

Other Information

This section provides additional information about the gene, including a description generated by an AI language model and details about associated proteins.

Description
Proteins

## Summary [RPS3](/details-gene/6188) (Ribosomal Protein S3) is a core component of the eukaryotic 40S ribosomal subunit, playing a fundamental role in protein synthesis as a [structural constituent of ribosome](/details-cell/GO:0003735). Beyond this canonical function, [RPS3](/details-gene/6188) exhibits critical extra-ribosomal activities, functioning as a DNA glycosylase/AP lyase involved in [base-excision repair](/details-cell/GO:0006284) and participating in the regulation of the [apoptotic process](/details-cell/GO:0006915) ([Link](https://doi.org/10.1074/jbc.270.23.13620), [Link](https://doi.org/10.1016/s0014-5793(04)00074-2)). Reflecting its central role in cellular metabolism and proliferation, **Overall**, its expression is most significant in highly active hematopoietic and immune cell populations, including [central memory CD4-positive, alpha-beta T cell](/details-cell/CL0000904) and [hematopoietic stem cell](/details-cell/CL0000037), while showing minimal expression in terminally differentiated neural cell types. ## Cellular Roles and Expression Landscape The expression profile of [RPS3](/details-gene/6188) underscores its importance in cells requiring high rates of protein synthesis for growth, proliferation, and effector function. **Overall**, it shows the highest significance in a broad range of immune lymphocytes. These include multiple T cell subsets such as [central memory CD4-positive, alpha-beta T cell](/details-cell/CL0000904), [naive T cell](/details-cell/CL0000898), and [naive thymus-derived CD8-positive, alpha-beta T cell](/details-cell/CL0000900), as well as cytotoxic lymphocytes like [CD16-positive, CD56-dim natural killer cell, human](/details-cell/CL0000939). Its high CSI in progenitor populations like [hematopoietic stem cell](/details-cell/CL0000037) is consistent with its foundational role in cell division and differentiation programs. In stark contrast, [RPS3](/details-gene/6188) exhibits very low significance in various subtypes of terminally differentiated neurons and glial cells. The list of anti-markers is dominated by cells of the central nervous system, including [VIP GABAergic cortical interneuron](/details-cell/CL4023016), [sst GABAergic cortical interneuron](/details-cell/CL4023017), and [astrocyte of the cerebral cortex](/details-cell/CL0002605). This suggests that while essential, its relative importance is diminished in quiescent cells with lower metabolic and proliferative demands compared to the highly dynamic cells of the hematopoietic system. ## Pathways and Molecular Function The functional annotations for [RPS3](/details-gene/6188) reveal a protein with a dual identity. Its primary and most well-understood role is within the ribosome, participating in nearly all stages of protein synthesis, from [Eukaryotic translation initiation](/details-cell/R-HSA-72613) to [Peptide chain elongation](/details-cell/R-HSA-156902) and [Eukaryotic translation termination](/details-cell/R-HSA-72764). This involvement in the [Translation](/details-cell/R-HSA-72766) machinery directly explains its high expression in rapidly dividing and functionally active immune cells. Indeed, GO terms such as [positive regulation of activated t cell proliferation](/details-cell/GO:0042104) and [positive regulation of interleukin-2 production](/details-cell/GO:0032743) explicitly link its function to the biology of its top-expressing cell types. Beyond the ribosome, [RPS3](/details-gene/6188) performs critical moonlighting functions in maintaining genomic integrity and regulating cell fate. It is an active enzyme in [DNA repair](/details-cell/GO:0006281), specifically possessing [DNA-(apurinic or apyrimidinic site) endonuclease activity](/details-cell/GO:0003906) crucial for the [base-excision repair](/details-cell/GO:0006284) pathway. Studies have shown it directly interacts with key DNA repair proteins like hAPE/Ref-1 and hOGG1, highlighting its direct role in resolving DNA damage ([Link](https://doi.org/10.1021/bi049234b)). Furthermore, [RPS3](/details-gene/6188) is implicated in the [apoptotic process](/details-cell/GO:0006915), capable of positively regulating caspase activity and the intrinsic apoptotic signaling pathway ([GO:1902231](/details-cell/GO:1902231)). This positions [RPS3](/details-gene/6188) at the nexus of protein synthesis, DNA damage response, and programmed cell death. ## Research Directions The dual functionality of [RPS3](/details-gene/6188) in both sustaining cellular life through translation and participating in its termination via apoptosis presents a fascinating regulatory challenge for the cell. This duality, combined with its high expression in lymphocytes, suggests it may play a key role in immune cell fate decisions. **Proposed Hypotheses:** 1. Given its roles in [positive regulation of activated t cell proliferation](/details-cell/GO:0042104) and [positive regulation of apoptotic signaling pathway](/details-cell/GO:2001235), post-translational modifications of [RPS3](/details-gene/6188), such as the previously reported phosphorylation by Erk ([Link](https://doi.org/10.1016/j.bbrc.2005.05.079)), may function as a molecular switch that determines T cell fate. Phosphorylation may favor its pro-proliferative ribosomal functions, while dephosphorylation could enhance its pro-apoptotic or DNA repair activities in response to cellular stress or activation-induced signals. 2. The high significance of [RPS3](/details-gene/6188) in [hematopoietic stem cell](/details-cell/CL0000037) suggests its DNA repair function is critical for maintaining genomic stability in this long-lived, multipotent population. A reduction in [RPS3](/details-gene/6188) expression or function could lead to an accumulation of DNA damage, potentially contributing to cellular senescence or malignant transformation in the hematopoietic lineage. **Experimental Approach:** To test the first hypothesis regarding T cell fate, one could utilize CRISPR-Cas9 to engineer primary human T cells or a T cell line (e.g., Jurkat) to express phosphorylation-deficient (e.g., Threonine-to-Alanine mutant) or phosphomimetic (e.g., Threonine-to-Glutamic acid mutant) versions of [RPS3](/details-gene/6188). After T cell receptor (TCR) stimulation, key outcomes could be assessed. Proliferation could be measured via CFSE dilution assays, while apoptosis could be quantified using Annexin V and propidium iodide staining followed by flow cytometry. This would directly test whether the phosphorylation status of [RPS3](/details-gene/6188) alters the balance between proliferation and apoptosis following T cell activation. **Therapeutic Potential:** As a ubiquitous and essential ribosomal protein, [RPS3](/details-gene/6188) is a challenging therapeutic target for systemic inhibition, which would likely cause unacceptable toxicity. However, its overexpression in certain malignancies, such as colorectal cancer ([Link](https://doi.org/10.1128/mcb.11.8.3842-3849.1991)), and its non-canonical roles present a potential therapeutic window. Instead of targeting its ribosomal function, developing small molecules that specifically disrupt the protein-protein interactions required for its DNA repair or anti-apoptotic functions could be a viable strategy. Such an approach would aim for inhibition, potentially sensitizing cancer cells to conventional DNA-damaging chemotherapies or radiotherapy while sparing normal tissues where these extra-ribosomal functions may be less critical for survival.

Disclaimer: This in-silico analysis is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

RS3_HUMAN

Genular Protein ID: 628908447

Symbol: RS3_HUMAN

Name: N/A

UniProtKB Accession Codes:

P23396 B2R7N5 J3KN86 Q498B5 Q8NI95

Database IDs:

Citations:

PubMed ID: 2129557

Title: Isolation of a cDNA encoding human 40S ribosomal protein s3.

PubMed ID: 2129557

DOI: 10.1093/nar/18.22.6689

PubMed ID: 1712897

Title: Ribosomal protein genes are overexpressed in colorectal cancer: isolation of a cDNA clone encoding the human S3 ribosomal protein.

PubMed ID: 1712897

DOI: 10.1128/mcb.11.8.3842-3849.1991

PubMed ID: 11875025

Title: The human ribosomal protein genes: sequencing and comparative analysis of 73 genes.

PubMed ID: 11875025

DOI: 10.1101/gr.214202

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 16554811

Title: Human chromosome 11 DNA sequence and analysis including novel gene identification.

PubMed ID: 16554811

DOI: 10.1038/nature04632

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 8319909

Title: A small nucleolar RNA is processed from an intron of the human gene encoding ribosomal protein S3.

PubMed ID: 8319909

DOI: 10.1101/gad.7.7a.1176

PubMed ID: 8706699

Title: Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry.

PubMed ID: 8706699

DOI: 10.1111/j.1432-1033.1996.0144u.x

PubMed ID: 7775413

Title: Implication of mammalian ribosomal protein S3 in the processing of DNA damage.

PubMed ID: 7775413

DOI: 10.1074/jbc.270.23.13620

PubMed ID: 14654843

Title: Proteomic characterization of the human centrosome by protein correlation profiling.

PubMed ID: 14654843

DOI: 10.1038/nature02166

PubMed ID: 15518571

Title: Human ribosomal protein S3 interacts with DNA base excision repair proteins hAPE/Ref-1 and hOGG1.

PubMed ID: 15518571

DOI: 10.1021/bi049234b

PubMed ID: 14706345

Title: Characterization of human ribosomal protein S3 binding to 7,8-dihydro-8-oxoguanine and abasic sites by surface plasmon resonance.

PubMed ID: 14706345

DOI: 10.1016/j.dnarep.2003.10.004

PubMed ID: 14988002

Title: RpS3, a DNA repair endonuclease and ribosomal protein, is involved in apoptosis.

PubMed ID: 14988002

DOI: 10.1016/s0014-5793(04)00074-2

PubMed ID: 15707971

Title: Characterization of a wide range base-damage-endonuclease activity of mammalian rpS3.

PubMed ID: 15707971

DOI: 10.1016/j.bbrc.2005.01.045

PubMed ID: 15950189

Title: Erk phosphorylates threonine 42 residue of ribosomal protein S3.

PubMed ID: 15950189

DOI: 10.1016/j.bbrc.2005.05.079

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16737853

Title: The high binding affinity of human ribosomal protein S3 to 7,8-dihydro-8-oxoguanine is abrogated by a single amino acid change.

PubMed ID: 16737853

DOI: 10.1016/j.dnarep.2006.04.001

PubMed ID: 16314389

Title: Interaction of Hsp90 with ribosomal proteins protects from ubiquitination and proteasome-dependent degradation.

PubMed ID: 16314389

DOI: 10.1091/mbc.e05-08-0713

PubMed ID: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

PubMed ID: 16807684

Title: Phosphoproteomic analysis of the human pituitary.

PubMed ID: 16807684

DOI: 10.1007/s11102-006-8916-x

PubMed ID: 18045535

Title: Ribosomal protein S3: a KH domain subunit in NF-kappaB complexes that mediates selective gene regulation.

PubMed ID: 18045535

DOI: 10.1016/j.cell.2007.10.009

PubMed ID: 17049931

Title: Knockdown of ribosomal protein S3 protects human cells from genotoxic stress.

PubMed ID: 17049931

DOI: 10.1016/j.dnarep.2006.09.004

PubMed ID: 17560175

Title: Translocation of human ribosomal protein S3 to sites of DNA damage is dependant on ERK-mediated phosphorylation following genotoxic stress.

PubMed ID: 17560175

DOI: 10.1016/j.dnarep.2007.04.009

PubMed ID: 17289661

Title: Molecular composition of IMP1 ribonucleoprotein granules.

PubMed ID: 17289661

DOI: 10.1074/mcp.m600346-mcp200

PubMed ID: 18610840

Title: Interactions of human ribosomal protein S3 with undamaged and damaged DNA.

PubMed ID: 18610840

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18973764

Title: Human ribosomal protein S3 (hRpS3) interacts with uracil-DNA glycosylase (hUNG) and stimulates its glycosylase activity.

PubMed ID: 18973764

DOI: 10.1016/j.mrfmmm.2008.09.013

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19460357

Title: Arginine methylation of ribosomal protein S3 affects ribosome assembly.

PubMed ID: 19460357

DOI: 10.1016/j.bbrc.2009.05.055

PubMed ID: 19059439

Title: PKCdelta-dependent functional switch of rpS3 between translation and DNA repair.

PubMed ID: 19059439

DOI: 10.1016/j.bbamcr.2008.10.017

PubMed ID: 19656744

Title: Ribosomal protein S3: A multi-functional protein that interacts with both p53 and MDM2 through its KH domain.

PubMed ID: 19656744

DOI: 10.1016/j.dnarep.2009.07.003

PubMed ID: 19369195

Title: Large-scale proteomics analysis of the human kinome.

PubMed ID: 19369195

DOI: 10.1074/mcp.m800588-mcp200

PubMed ID: 20041225

Title: Bacterial effector binding to ribosomal protein s3 subverts NF-kappaB function.

PubMed ID: 20041225

DOI: 10.1371/journal.ppat.1000708

PubMed ID: 19541769

Title: IGF2BP1 enhances HCV IRES-mediated translation initiation via the 3'UTR.

PubMed ID: 19541769

DOI: 10.1261/rna.1578409

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20605787

Title: Ribosomal protein S3, a new substrate of Akt, serves as a signal mediator between neuronal apoptosis and DNA repair.

PubMed ID: 20605787

DOI: 10.1074/jbc.m110.131367

PubMed ID: 20217897

Title: RpS3 translation is repressed by interaction with its own mRNA.

PubMed ID: 20217897

DOI: 10.1002/jcb.22537

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21968017

Title: Ribosomal protein S3 is stabilized by sumoylation.

PubMed ID: 21968017

DOI: 10.1016/j.bbrc.2011.09.099

PubMed ID: 21871177

Title: Ribosomal protein S3 is phosphorylated by Cdk1/cdc2 during G2/M phase.

PubMed ID: 21871177

DOI: 10.5483/bmbrep.2011.44.8.529

PubMed ID: 21399639

Title: IKKbeta phosphorylation regulates RPS3 nuclear translocation and NF-kappaB function during infection with Escherichia coli strain O157:H7.

PubMed ID: 21399639

DOI: 10.1038/ni.2007

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22510408

Title: Ribosomal protein S3 interacts with TRADD to induce apoptosis through caspase dependent JNK activation.

PubMed ID: 22510408

DOI: 10.1016/j.bbrc.2012.04.020

PubMed ID: 23131551

Title: Ribosomal protein S3 localizes on the mitotic spindle and functions as a microtubule associated protein in mitosis.

PubMed ID: 23131551

DOI: 10.1016/j.bbrc.2012.10.093

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23911537

Title: Cytoplasmic ribosomal protein S3 (rpS3) plays a pivotal role in mitochondrial DNA damage surveillance.

PubMed ID: 23911537

DOI: 10.1016/j.bbamcr.2013.07.015

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24524803

Title: A new system for naming ribosomal proteins.

PubMed ID: 24524803

DOI: 10.1016/j.sbi.2014.01.002

PubMed ID: 24457201

Title: Ribosomal protein S3 interacts with the NF-kappaB inhibitor IkappaBalpha.

PubMed ID: 24457201

DOI: 10.1016/j.febslet.2013.12.034

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 24423872

Title: AUF1 contributes to Cryptochrome1 mRNA degradation and rhythmic translation.

PubMed ID: 24423872

DOI: 10.1093/nar/gkt1379

PubMed ID: 25114211

Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.

PubMed ID: 25114211

DOI: 10.1073/pnas.1413825111

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 28065601

Title: Initiation of quality control during poly(A) translation requires site-specific ribosome ubiquitination.

PubMed ID: 28065601

DOI: 10.1016/j.molcel.2016.11.039

PubMed ID: 28132843

Title: ZNF598 and RACK1 regulate mammalian ribosome-associated quality control function by mediating regulatory 40S ribosomal ubiquitylation.

PubMed ID: 28132843

DOI: 10.1016/j.molcel.2016.12.026

PubMed ID: 28757607

Title: Ubiquitination of stalled ribosome triggers ribosome-associated quality control.

PubMed ID: 28757607

DOI: 10.1038/s41467-017-00188-1

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 32011234

Title: Distinct regulatory ribosomal ubiquitylation events are reversible and hierarchically organized.

PubMed ID: 32011234

DOI: 10.7554/elife.54023

PubMed ID: 31981475

Title: The G3BP1-family-USP10 deubiquitinase complex rescues ubiquitinated 40S subunits of ribosomes stalled in translation from lysosomal degradation.

PubMed ID: 31981475

DOI: 10.1016/j.molcel.2019.12.024

PubMed ID: 34348161

Title: The E3 ubiquitin ligase RNF10 modifies 40S ribosomal subunits of ribosomes compromised in translation.

PubMed ID: 34348161

DOI: 10.1016/j.celrep.2021.109468

PubMed ID: 34469731

Title: iRQC, a surveillance pathway for 40S ribosomal quality control during mRNA translation initiation.

PubMed ID: 34469731

DOI: 10.1016/j.celrep.2021.109642

PubMed ID: 23636399

Title: Structures of the human and Drosophila 80S ribosome.

PubMed ID: 23636399

DOI: 10.1038/nature12104

Sequence Information:

Length: 243
Mass: 26688
Checksum: 6ECBB34A8EE04AAF
Sequence:

MAVQISKKRK FVADGIFKAE LNEFLTRELA EDGYSGVEVR VTPTRTEIII LATRTQNVLG 
EKGRRIRELT AVVQKRFGFP EGSVELYAEK VATRGLCAIA QAESLRYKLL GGLAVRRACY 
GVLRFIMESG AKGCEVVVSG KLRGQRAKSM KFVDGLMIHS GDPVNYYVDT AVRHVLLRQG 
VLGIKVKIML PWDPTGKIGP KKPLPDHVSI VEPKDEILPT TPISEQKGGK PEPPAMPQPV 
PTA

Details for: RPS3

Cell Significance Landscape

Associated with

Significant Cells

Network Configuration

Legend:

Other Information

Isolation of a cDNA encoding human 40S ribosomal protein s3. PubMed ID: 2129557

Ribosomal protein genes are overexpressed in colorectal cancer: isolation of a cDNA clone encoding the human S3 ribosomal protein. PubMed ID: 1712897

The human ribosomal protein genes: sequencing and comparative analysis of 73 genes. PubMed ID: 11875025

Complete sequencing and characterization of 21,243 full-length human cDNAs. PubMed ID: 14702039

Human chromosome 11 DNA sequence and analysis including novel gene identification. PubMed ID: 16554811

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

A small nucleolar RNA is processed from an intron of the human gene encoding ribosomal protein S3. PubMed ID: 8319909

Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry. PubMed ID: 8706699

Implication of mammalian ribosomal protein S3 in the processing of DNA damage. PubMed ID: 7775413

Proteomic characterization of the human centrosome by protein correlation profiling. PubMed ID: 14654843

Human ribosomal protein S3 interacts with DNA base excision repair proteins hAPE/Ref-1 and hOGG1. PubMed ID: 15518571

Characterization of human ribosomal protein S3 binding to 7,8-dihydro-8-oxoguanine and abasic sites by surface plasmon resonance. PubMed ID: 14706345

RpS3, a DNA repair endonuclease and ribosomal protein, is involved in apoptosis. PubMed ID: 14988002

Characterization of a wide range base-damage-endonuclease activity of mammalian rpS3. PubMed ID: 15707971

Erk phosphorylates threonine 42 residue of ribosomal protein S3. PubMed ID: 15950189

Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PubMed ID: 17081983

The high binding affinity of human ribosomal protein S3 to 7,8-dihydro-8-oxoguanine is abrogated by a single amino acid change. PubMed ID: 16737853

Interaction of Hsp90 with ribosomal proteins protects from ubiquitination and proteasome-dependent degradation. PubMed ID: 16314389

A probability-based approach for high-throughput protein phosphorylation analysis and site localization. PubMed ID: 16964243

Phosphoproteomic analysis of the human pituitary. PubMed ID: 16807684

Ribosomal protein S3: a KH domain subunit in NF-kappaB complexes that mediates selective gene regulation. PubMed ID: 18045535

Knockdown of ribosomal protein S3 protects human cells from genotoxic stress. PubMed ID: 17049931

Translocation of human ribosomal protein S3 to sites of DNA damage is dependant on ERK-mediated phosphorylation following genotoxic stress. PubMed ID: 17560175

Molecular composition of IMP1 ribonucleoprotein granules. PubMed ID: 17289661

Interactions of human ribosomal protein S3 with undamaged and damaged DNA. PubMed ID: 18610840

Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. PubMed ID: 18691976

Human ribosomal protein S3 (hRpS3) interacts with uracil-DNA glycosylase (hUNG) and stimulates its glycosylase activity. PubMed ID: 18973764

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. PubMed ID: 19413330

Arginine methylation of ribosomal protein S3 affects ribosome assembly. PubMed ID: 19460357

PKCdelta-dependent functional switch of rpS3 between translation and DNA repair. PubMed ID: 19059439

Ribosomal protein S3: A multi-functional protein that interacts with both p53 and MDM2 through its KH domain. PubMed ID: 19656744

Large-scale proteomics analysis of the human kinome. PubMed ID: 19369195

Bacterial effector binding to ribosomal protein s3 subverts NF-kappaB function. PubMed ID: 20041225

IGF2BP1 enhances HCV IRES-mediated translation initiation via the 3'UTR. PubMed ID: 19541769

Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PubMed ID: 19690332

Lysine acetylation targets protein complexes and co-regulates major cellular functions. PubMed ID: 19608861

Ribosomal protein S3, a new substrate of Akt, serves as a signal mediator between neuronal apoptosis and DNA repair. PubMed ID: 20605787

RpS3 translation is repressed by interaction with its own mRNA. PubMed ID: 20217897

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Initial characterization of the human central proteome. PubMed ID: 21269460

Ribosomal protein S3 is stabilized by sumoylation. PubMed ID: 21968017

Ribosomal protein S3 is phosphorylated by Cdk1/cdc2 during G2/M phase. PubMed ID: 21871177

IKKbeta phosphorylation regulates RPS3 nuclear translocation and NF-kappaB function during infection with Escherichia coli strain O157:H7. PubMed ID: 21399639

System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. PubMed ID: 21406692

Ribosomal protein S3 interacts with TRADD to induce apoptosis through caspase dependent JNK activation. PubMed ID: 22510408

Ribosomal protein S3 localizes on the mitotic spindle and functions as a microtubule associated protein in mitosis. PubMed ID: 23131551

N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB. PubMed ID: 22814378

Cytoplasmic ribosomal protein S3 (rpS3) plays a pivotal role in mitochondrial DNA damage surveillance. PubMed ID: 23911537

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

A new system for naming ribosomal proteins. PubMed ID: 24524803

Ribosomal protein S3 interacts with the NF-kappaB inhibitor IkappaBalpha. PubMed ID: 24457201

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

AUF1 contributes to Cryptochrome1 mRNA degradation and rhythmic translation. PubMed ID: 24423872

Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli. PubMed ID: 25114211

N-terminome analysis of the human mitochondrial proteome. PubMed ID: 25944712

Initiation of quality control during poly(A) translation requires site-specific ribosome ubiquitination. PubMed ID: 28065601

ZNF598 and RACK1 regulate mammalian ribosome-associated quality control function by mediating regulatory 40S ribosomal ubiquitylation. PubMed ID: 28132843

Ubiquitination of stalled ribosome triggers ribosome-associated quality control. PubMed ID: 28757607

Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation. PubMed ID: 28112733

Distinct regulatory ribosomal ubiquitylation events are reversible and hierarchically organized. PubMed ID: 32011234

The G3BP1-family-USP10 deubiquitinase complex rescues ubiquitinated 40S subunits of ribosomes stalled in translation from lysosomal degradation. PubMed ID: 31981475

The E3 ubiquitin ligase RNF10 modifies 40S ribosomal subunits of ribosomes compromised in translation. PubMed ID: 34348161

iRQC, a surveillance pathway for 40S ribosomal quality control during mRNA translation initiation. PubMed ID: 34469731

Structures of the human and Drosophila 80S ribosome. PubMed ID: 23636399