P39019 · RS19_HUMAN
- ProteinSmall ribosomal subunit protein eS19
- GeneRPS19
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids145 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of the small ribosomal subunit (PubMed:23636399).
The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399).
Required for pre-rRNA processing and maturation of 40S ribosomal subunits (PubMed:16990592).
Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797).
The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399).
Required for pre-rRNA processing and maturation of 40S ribosomal subunits (PubMed:16990592).
Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome (PubMed:34516797).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSmall ribosomal subunit protein eS19
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP39019
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Diamond-Blackfan anemia 1 (DBA1)
- Note
- DescriptionA form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of developing leukemia. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies.
- See alsoMIM:105650
Natural variants in DBA1
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_055436 | 9-14 | missing | in DBA1 | |
VAR_018438 | 15 | V>F | in DBA1; affects protein stability; does not localize to the nucleolus; dbSNP:rs104894717 | |
VAR_046145 | 17 | A>P | in DBA1; dbSNP:rs782329429 | |
VAR_018439 | 18 | L>P | in DBA1; affects protein stability; does not localize to the nucleolus; affects assembly into a functional ribosomal subunit | |
VAR_046146 | 18 | L>R | in DBA1 | |
VAR_055437 | 18-19 | LA>E | in DBA1 | |
VAR_055438 | 21 | F>S | in DBA1 | |
VAR_018440 | 47 | P>L | in DBA1; affects assembly into a functional ribosomal subunit | |
VAR_055439 | 52 | W>C | in DBA1 | |
VAR_018441 | 52 | W>R | in DBA1; affects assembly into a functional ribosomal subunit | |
VAR_018442 | 55 | T>M | in DBA1; dbSNP:rs147508369 | |
VAR_018437 | 56 | R>Q | in DBA1; affects assembly into a functional ribosomal subunit | |
VAR_055440 | 57 | A>P | in DBA1; affects protein stability; does not localize to the nucleolus; affects assembly into a functional ribosomal subunit | |
VAR_046147 | 58-60 | missing | in DBA1 | |
VAR_046148 | 59 | S>F | in DBA1 | |
VAR_018443 | 61 | A>E | in DBA1; does not localize to the nucleolus; affects assembly into a functional ribosomal subunit | |
VAR_018444 | 62 | R>Q | in DBA1; affects assembly into a functional ribosomal subunit; dbSNP:rs1555841301 | |
VAR_006924 | 62 | R>W | in DBA1; increased protein degradation; affects assembly into a functional ribosomal subunit; dbSNP:rs104894711 | |
VAR_055441 | 64 | L>P | in DBA1 | |
VAR_055442 | 76 | T>P | in DBA1 | |
VAR_055443 | 78-83 | IYGGRQ>R | in DBA1 | |
VAR_018445 | 101 | R>H | in DBA1; increased protein degradation; affects assembly into a functional ribosomal subunit | |
VAR_018446 | 120 | G>R | in DBA1 | |
VAR_055444 | 127 | G>E | in DBA1; affects protein stability; does not localize to the nucleolus; affects assembly into a functional ribosomal subunit; dbSNP:rs786200936 | |
VAR_018447 | 131 | L>P | in DBA1 | |
VAR_046149 | 131 | L>R | in DBA1 | |
VAR_055445 | 135 | A>T | in DBA1 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_055436 | 9-14 | in DBA1 | |||
Sequence: Missing | ||||||
Natural variant | VAR_018438 | 15 | in DBA1; affects protein stability; does not localize to the nucleolus; dbSNP:rs104894717 | |||
Sequence: V → F | ||||||
Natural variant | VAR_046145 | 17 | in DBA1; dbSNP:rs782329429 | |||
Sequence: A → P | ||||||
Natural variant | VAR_018439 | 18 | in DBA1; affects protein stability; does not localize to the nucleolus; affects assembly into a functional ribosomal subunit | |||
Sequence: L → P | ||||||
Natural variant | VAR_046146 | 18 | in DBA1 | |||
Sequence: L → R | ||||||
Natural variant | VAR_055437 | 18-19 | in DBA1 | |||
Sequence: LA → E | ||||||
Natural variant | VAR_055438 | 21 | in DBA1 | |||
Sequence: F → S | ||||||
Natural variant | VAR_018440 | 47 | in DBA1; affects assembly into a functional ribosomal subunit | |||
Sequence: P → L | ||||||
Natural variant | VAR_055439 | 52 | in DBA1 | |||
Sequence: W → C | ||||||
Natural variant | VAR_018441 | 52 | in DBA1; affects assembly into a functional ribosomal subunit | |||
Sequence: W → R | ||||||
Natural variant | VAR_018442 | 55 | in DBA1; dbSNP:rs147508369 | |||
Sequence: T → M | ||||||
Natural variant | VAR_018437 | 56 | in DBA1; affects assembly into a functional ribosomal subunit | |||
Sequence: R → Q | ||||||
Natural variant | VAR_055440 | 57 | in DBA1; affects protein stability; does not localize to the nucleolus; affects assembly into a functional ribosomal subunit | |||
Sequence: A → P | ||||||
Natural variant | VAR_046147 | 58-60 | in DBA1 | |||
Sequence: Missing | ||||||
Natural variant | VAR_046148 | 59 | in DBA1 | |||
Sequence: S → F | ||||||
Natural variant | VAR_018443 | 61 | in DBA1; does not localize to the nucleolus; affects assembly into a functional ribosomal subunit | |||
Sequence: A → E | ||||||
Natural variant | VAR_018444 | 62 | in DBA1; affects assembly into a functional ribosomal subunit; dbSNP:rs1555841301 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_006924 | 62 | in DBA1; increased protein degradation; affects assembly into a functional ribosomal subunit; dbSNP:rs104894711 | |||
Sequence: R → W | ||||||
Natural variant | VAR_055441 | 64 | in DBA1 | |||
Sequence: L → P | ||||||
Natural variant | VAR_055442 | 76 | in DBA1 | |||
Sequence: T → P | ||||||
Natural variant | VAR_055443 | 78-83 | in DBA1 | |||
Sequence: IYGGRQ → R | ||||||
Natural variant | VAR_018445 | 101 | in DBA1; increased protein degradation; affects assembly into a functional ribosomal subunit | |||
Sequence: R → H | ||||||
Natural variant | VAR_018446 | 120 | in DBA1 | |||
Sequence: G → R | ||||||
Natural variant | VAR_055444 | 127 | in DBA1; affects protein stability; does not localize to the nucleolus; affects assembly into a functional ribosomal subunit; dbSNP:rs786200936 | |||
Sequence: G → E | ||||||
Natural variant | VAR_018447 | 131 | in DBA1 | |||
Sequence: L → P | ||||||
Natural variant | VAR_046149 | 131 | in DBA1 | |||
Sequence: L → R | ||||||
Natural variant | VAR_055445 | 135 | in DBA1 | |||
Sequence: A → T |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 188 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Chain | PRO_0000153810 | 2-145 | UniProt | Small ribosomal subunit protein eS19 | |||
Sequence: PGVTVKDVNQQEFVRALAAFLKKSGKLKVPEWVDTVKLAKHKELAPYDENWFYTRAASTARHLYLRGGAGVGSMTKIYGGRQRNGVMPSHFSRGSKSVARRVLQALEGLKMVEKDQDGGRKLTPQGQRDLDRIAGQVAAANKKH | |||||||
Modified residue | 23 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 67 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 74 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 90 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 93 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 111 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 115 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 143 | UniProt | N6-succinyllysine | ||||
Sequence: K |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Higher level expression is seen in the colon carcinoma tissue than normal colon tissue.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Component of the small ribosomal subunit (PubMed:23636399).
Part of the small subunit (SSU) processome, composed of more than 70 proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3. Interacts with RPS19BP1; the interaction is direct and mediates the integration of RPS19 in state post-A1 (PubMed:34516797).
Interacts with RPS19BP1 (By similarity).
Part of the small subunit (SSU) processome, composed of more than 70 proteins and the RNA chaperone small nucleolar RNA (snoRNA) U3. Interacts with RPS19BP1; the interaction is direct and mediates the integration of RPS19 in state post-A1 (PubMed:34516797).
Interacts with RPS19BP1 (By similarity).
(Microbial infection) Interacts with Sin nombre virus nucleoprotein (via N-terminus); this interaction probably mediates the loading of the 40S ribosomal subunit on viral capped mRNA during N-mediated translation initiation.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P39019 | ATXN1 P54253 | 3 | EBI-354451, EBI-930964 | |
BINARY | P39019 | H1-5 P16401 | 2 | EBI-354451, EBI-5327611 | |
BINARY | P39019 | HTT P42858 | 3 | EBI-354451, EBI-466029 | |
BINARY | P39019 | PIM1 P11309 | 7 | EBI-354451, EBI-696621 | |
BINARY | P39019 | RPS16 P62249 | 4 | EBI-354451, EBI-352480 | |
BINARY | P39019 | SPG21 Q9NZD8 | 3 | EBI-354451, EBI-742688 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Length145
- Mass (Da)16,060
- Last updated2007-01-23 v2
- Checksum181F2DB898E56E41
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A075B6E2 | A0A075B6E2_HUMAN | RPS19 | 71 | ||
M0R140 | M0R140_HUMAN | RPS19 | 102 | ||
M0R2L9 | M0R2L9_HUMAN | RPS19 | 71 | ||
M0QYF7 | M0QYF7_HUMAN | RPS19 | 100 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M81757 EMBL· GenBank· DDBJ | AAA89070.1 EMBL· GenBank· DDBJ | mRNA | ||
AF092907 EMBL· GenBank· DDBJ | AAD13668.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF092906 EMBL· GenBank· DDBJ | AAD13668.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC000023 EMBL· GenBank· DDBJ | AAH00023.1 EMBL· GenBank· DDBJ | mRNA | ||
BC007615 EMBL· GenBank· DDBJ | AAH07615.1 EMBL· GenBank· DDBJ | mRNA | ||
BC018616 EMBL· GenBank· DDBJ | AAH18616.1 EMBL· GenBank· DDBJ | mRNA | ||
AB007155 EMBL· GenBank· DDBJ | BAA28593.1 EMBL· GenBank· DDBJ | Genomic DNA |