P23396 · RS3_HUMAN
- ProteinSmall ribosomal subunit protein uS3
- GeneRPS3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids243 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of the small ribosomal subunit (PubMed:23636399, PubMed:8706699).
The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399, PubMed:8706699).
Has endonuclease activity and plays a role in repair of damaged DNA (PubMed:7775413).
Cleaves phosphodiester bonds of DNAs containing altered bases with broad specificity and cleaves supercoiled DNA more efficiently than relaxed DNA (PubMed:15707971).
Displays high binding affinity for 7,8-dihydro-8-oxoguanine (8-oxoG), a common DNA lesion caused by reactive oxygen species (ROS) (PubMed:14706345).
Has also been shown to bind with similar affinity to intact and damaged DNA (PubMed:18610840).
Stimulates the N-glycosylase activity of the base excision protein OGG1 (PubMed:15518571).
Enhances the uracil excision activity of UNG1 (PubMed:18973764).
Also stimulates the cleavage of the phosphodiester backbone by APEX1 (PubMed:18973764).
When located in the mitochondrion, reduces cellular ROS levels and mitochondrial DNA damage (PubMed:23911537).
Has also been shown to negatively regulate DNA repair in cells exposed to hydrogen peroxide (PubMed:17049931).
Plays a role in regulating transcription as part of the NF-kappa-B p65-p50 complex where it binds to the RELA/p65 subunit, enhances binding of the complex to DNA and promotes transcription of target genes (PubMed:18045535).
Represses its own translation by binding to its cognate mRNA (PubMed:20217897).
Binds to and protects TP53/p53 from MDM2-mediated ubiquitination (PubMed:19656744).
Involved in spindle formation and chromosome movement during mitosis by regulating microtubule polymerization (PubMed:23131551).
Involved in induction of apoptosis through its role in activation of CASP8 (PubMed:14988002).
Induces neuronal apoptosis by interacting with the E2F1 transcription factor and acting synergistically with it to up-regulate pro-apoptotic proteins BCL2L11/BIM and HRK/Dp5 (PubMed:20605787).
Interacts with TRADD following exposure to UV radiation and induces apoptosis by caspase-dependent JNK activation (PubMed:22510408).
The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399, PubMed:8706699).
Has endonuclease activity and plays a role in repair of damaged DNA (PubMed:7775413).
Cleaves phosphodiester bonds of DNAs containing altered bases with broad specificity and cleaves supercoiled DNA more efficiently than relaxed DNA (PubMed:15707971).
Displays high binding affinity for 7,8-dihydro-8-oxoguanine (8-oxoG), a common DNA lesion caused by reactive oxygen species (ROS) (PubMed:14706345).
Has also been shown to bind with similar affinity to intact and damaged DNA (PubMed:18610840).
Stimulates the N-glycosylase activity of the base excision protein OGG1 (PubMed:15518571).
Enhances the uracil excision activity of UNG1 (PubMed:18973764).
Also stimulates the cleavage of the phosphodiester backbone by APEX1 (PubMed:18973764).
When located in the mitochondrion, reduces cellular ROS levels and mitochondrial DNA damage (PubMed:23911537).
Has also been shown to negatively regulate DNA repair in cells exposed to hydrogen peroxide (PubMed:17049931).
Plays a role in regulating transcription as part of the NF-kappa-B p65-p50 complex where it binds to the RELA/p65 subunit, enhances binding of the complex to DNA and promotes transcription of target genes (PubMed:18045535).
Represses its own translation by binding to its cognate mRNA (PubMed:20217897).
Binds to and protects TP53/p53 from MDM2-mediated ubiquitination (PubMed:19656744).
Involved in spindle formation and chromosome movement during mitosis by regulating microtubule polymerization (PubMed:23131551).
Involved in induction of apoptosis through its role in activation of CASP8 (PubMed:14988002).
Induces neuronal apoptosis by interacting with the E2F1 transcription factor and acting synergistically with it to up-regulate pro-apoptotic proteins BCL2L11/BIM and HRK/Dp5 (PubMed:20605787).
Interacts with TRADD following exposure to UV radiation and induces apoptosis by caspase-dependent JNK activation (PubMed:22510408).
Catalytic activity
- 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + H+
Activity regulation
Endonuclease activity is inhibited by MgCl2 on apurinic/apyrimidinic DNA but not on UV-irradiated DNA.
pH Dependence
Optimum pH is between 8.0 and 9.0 with activity decreasing sharply below 8.0.
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameSmall ribosomal subunit protein uS3
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP23396
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Mitochondrion inner membrane ; Peripheral membrane protein
Note: In normal cells, located mainly in the cytoplasm with small amounts in the nucleus but translocates to the nucleus in cells undergoing apoptosis (By similarity).
Nuclear translocation is induced by DNA damaging agents such as hydrogen peroxide (PubMed:17560175).
Accumulates in the mitochondrion in response to increased ROS levels (PubMed:23911537).
Localizes to the spindle during mitosis (PubMed:23131551).
Localized in cytoplasmic mRNP granules containing untranslated mRNAs (PubMed:17289661).
Nuclear translocation is induced by DNA damaging agents such as hydrogen peroxide (PubMed:17560175).
Accumulates in the mitochondrion in response to increased ROS levels (PubMed:23911537).
Localizes to the spindle during mitosis (PubMed:23131551).
Localized in cytoplasmic mRNP granules containing untranslated mRNAs (PubMed:17289661).
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 6 | No effect on phosphorylation by CDK1. Greatly reduced phosphorylation by PRKCD. Abolishes phosphorylation by PRKCD; when associated with A-221. | ||||
Sequence: S → A | ||||||
Mutagenesis | 18 | No effect on sumoylation. Abolishes sumoylation; when associated with R-214 and R-230. | ||||
Sequence: K → R | ||||||
Mutagenesis | 35 | No effect on phosphorylation by PRKCD. | ||||
Sequence: S → A | ||||||
Mutagenesis | 42 | Abolishes phosphorylation by MAPK and translocation to the nucleus following exposure of cells to hydrogen peroxide. No effect on phosphorylation by CDK1 or PRKCD. | ||||
Sequence: T → A | ||||||
Mutagenesis | 42 | Phosphomimetic mutant which is detected exclusively in the nucleus. | ||||
Sequence: T → D | ||||||
Mutagenesis | 70 | No effect on phosphorylation by PRKCD. Abolishes phosphorylation by PKB. | ||||
Sequence: T → A | ||||||
Mutagenesis | 70 | Abolishes phosphorylation by PKB. | ||||
Sequence: T → D, E, or R | ||||||
Mutagenesis | 132 | Does not affect ability to cleave DNA but abolishes binding to 8-oxoG. | ||||
Sequence: K → A | ||||||
Mutagenesis | 139 | No effect on phosphorylation by PRKCD. | ||||
Sequence: S → A | ||||||
Mutagenesis | 149 | No effect on phosphorylation by PRKCD. | ||||
Sequence: S → A | ||||||
Mutagenesis | 195 | No effect on phosphorylation by PRKCD. | ||||
Sequence: T → A | ||||||
Mutagenesis | 209 | Reduced phosphorylation by IKKB. | ||||
Sequence: S → A | ||||||
Mutagenesis | 214 | No effect on sumoylation. Abolishes sumoylation; when associated with R-18 and R-230. Abolished ubiquitination by RNF10 in response to ribosome stalling and deubiquitination by USP10. | ||||
Sequence: K → R | ||||||
Mutagenesis | 221 | No effect on phosphorylation by MAPK. Significantly reduces phosphorylation by CDK1 and nuclear accumulation. Greatly reduced phosphorylation by PRKCD. Abolishes phosphorylation by PRKCD; when associated with A-6. | ||||
Sequence: T → A | ||||||
Mutagenesis | 227 | Does not affect ubiquitination in response to ribosome stalling. | ||||
Sequence: K → R | ||||||
Mutagenesis | 230 | No effect on sumoylation. Abolishes sumoylation; when associated with R-18 and R-214. Does not affect ubiquitination in response to ribosome stalling. | ||||
Sequence: K → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 187 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, cross-link, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000130320 | 2-243 | UniProt | Small ribosomal subunit protein uS3 | |||
Sequence: AVQISKKRKFVADGIFKAELNEFLTRELAEDGYSGVEVRVTPTRTEIIILATRTQNVLGEKGRRIRELTAVVQKRFGFPEGSVELYAEKVATRGLCAIAQAESLRYKLLGGLAVRRACYGVLRFIMESGAKGCEVVVSGKLRGQRAKSMKFVDGLMIHSGDPVNYYVDTAVRHVLLRQGVLGIKVKIMLPWDPTGKIGPKKPLPDHVSIVEPKDEILPTTPISEQKGGKPEPPAMPQPVPTA | |||||||
Modified residue | 6 | UniProt | Phosphoserine; by PKC/PRKCD | ||||
Sequence: S | |||||||
Modified residue | 35 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 42 | UniProt | Phosphothreonine; by MAPK | ||||
Sequence: T | |||||||
Modified residue | 62 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 64 | UniProt | Asymmetric dimethylarginine; by PRMT1 | ||||
Sequence: R | |||||||
Modified residue | 65 | UniProt | Asymmetric dimethylarginine; by PRMT1 | ||||
Sequence: R | |||||||
Modified residue | 67 | UniProt | Asymmetric dimethylarginine; by PRMT1 | ||||
Sequence: R | |||||||
Modified residue | 70 | UniProt | Phosphothreonine; by PKB | ||||
Sequence: T | |||||||
Cross-link | 90 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue | 104 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 104 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 107 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 120 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 132 | UniProt | N6-succinyllysine | ||||
Sequence: K | |||||||
Cross-link | 202 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue | 209 | UniProt | Phosphoserine; by IKKB | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 209 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 214 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | |||||||
Cross-link | 214 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate | ||||
Sequence: K | |||||||
Modified residue | 220 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 220 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 221 | UniProt | Phosphothreonine; by CDK1 and PKC/PRKCD | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 221 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 224 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 224 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 230 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 242 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 242 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Methylation by PRMT1 is required for import into the nucleolus and for ribosome assembly.
Sumoylation by SUMO1 enhances protein stability through increased resistance to proteolysis. Sumoylation occurs at one or more of the three consensus sites, Lys-18, Lys-214 and Lys-230.
Phosphorylation at Thr-221 by CDK1 occurs mainly in G2/M phase (PubMed:21871177).
Phosphorylation by PRKCD occurs on a non-ribosomal-associated form which results in translocation of RPS3 to the nucleus and enhances its endonuclease activity (PubMed:19059439).
Phosphorylated on Ser-209 by IKKB in response to activation of the NF-kappa-B p65-p50 complex which enhances the association of RPS3 with importin-alpha and mediates the nuclear translocation of RPS3 (PubMed:21399639).
Phosphorylation by MAPK is required for translocation to the nucleus following exposure of cells to DNA damaging agents such as hydrogen peroxide (PubMed:17560175).
Phosphorylation by PKB/AKT mediates RPS3 nuclear translocation, enhances RPS3 endonuclease activity and suppresses RPS3-induced neuronal apoptosis (PubMed:20605787).
Phosphorylation by PRKCD occurs on a non-ribosomal-associated form which results in translocation of RPS3 to the nucleus and enhances its endonuclease activity (PubMed:19059439).
Phosphorylated on Ser-209 by IKKB in response to activation of the NF-kappa-B p65-p50 complex which enhances the association of RPS3 with importin-alpha and mediates the nuclear translocation of RPS3 (PubMed:21399639).
Phosphorylation by MAPK is required for translocation to the nucleus following exposure of cells to DNA damaging agents such as hydrogen peroxide (PubMed:17560175).
Phosphorylation by PKB/AKT mediates RPS3 nuclear translocation, enhances RPS3 endonuclease activity and suppresses RPS3-induced neuronal apoptosis (PubMed:20605787).
Ubiquitinated; ubiquitination is prevented by interaction with HSP90 which stabilizes the protein (PubMed:16314389).
Monoubiquitinated at Lys-214 by RNF10 and ZNF598 when a ribosome has stalled during translation of poly(A) sequences, leading to preclude synthesis of a long poly-lysine tail and initiate the ribosome quality control (RQC) pathway to degrade the potentially detrimental aberrant nascent polypeptide (PubMed:28065601, PubMed:28132843, PubMed:32011234, PubMed:34348161, PubMed:34469731).
Deubiquitinated at Lys-214 by USP10, preventing degradation by the proteasome and promoting 40S ribosome subunit recycling following ribosome dissociation (PubMed:31981475, PubMed:34469731).
Monoubiquitinated at Lys-214 by RNF10 and ZNF598 when a ribosome has stalled during translation of poly(A) sequences, leading to preclude synthesis of a long poly-lysine tail and initiate the ribosome quality control (RQC) pathway to degrade the potentially detrimental aberrant nascent polypeptide (PubMed:28065601, PubMed:28132843, PubMed:32011234, PubMed:34348161, PubMed:34469731).
Deubiquitinated at Lys-214 by USP10, preventing degradation by the proteasome and promoting 40S ribosome subunit recycling following ribosome dissociation (PubMed:31981475, PubMed:34469731).
Ufmylated by UFL1.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Component of the 40S small ribosomal subunit (PubMed:23636399, PubMed:8706699).
Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (PubMed:17289661).
Interacts with HNRPD (PubMed:24423872).
Interacts with PRMT1; the interaction methylates RPS3 (PubMed:19460357).
Interacts with SUMO1; the interaction sumoylates RPS3 (PubMed:21968017).
Interacts with UBC9 (PubMed:21968017).
Interacts with CDK1; the interaction phosphorylates RPS3 (PubMed:21871177).
Interacts with PRKCD; the interaction phosphorylates RPS3 (PubMed:19059439).
Interacts with PKB/AKT; the interaction phosphorylates RPS3 (PubMed:20605787).
Interacts with E2F1; the interaction occurs in the absence of nerve growth factor and increases transcription of pro-apoptotic proteins BCL2L11/BIM and HRK/Dp5 (PubMed:20605787).
Interacts with the base excision repair proteins APEX1 and OGG1; interaction with OGG1 increases OGG1 N-glycosylase activity (PubMed:15518571).
Interacts with UNG; the interaction increases the uracil excision activity of UNG1 (PubMed:18973764).
Interacts with HSP90; the interaction prevents the ubiquitination and proteasome-dependent degradation of RPS3 and is suppressed by increased ROS levels (PubMed:16314389).
Interacts with TOM70; the interaction promotes translocation of RPS3 to the mitochondrion (PubMed:23911537).
Interacts (via N-terminus) with RELA (via N-terminus); the interaction enhances the DNA-binding activity of the NF-kappa-B p65-p50 complex (PubMed:18045535).
Interacts with NFKBIA; the interaction is direct and may bridge the interaction between RPS3 and RELA (PubMed:24457201).
Interacts with IKKB; the interaction phosphorylates RPS3 and enhances its translocation to the nucleus (PubMed:21399639).
Interacts (via KH domain) with MDM2 and TP53 (PubMed:19656744).
Interacts with TRADD (PubMed:22510408).
Interacts (via N-terminus) with E.coli O157:H7 (strain EDL933) nleH1 and nleH2; the interaction with nleH1 inhibits phosphorylation by IKKB, reduces RPS3 nuclear abundance and inhibits transcriptional activation by the NF-kappa-B p65-p50 complex (PubMed:20041225, PubMed:21399639).
Interacts with ASCC3 (PubMed:28757607).
Identified in a HCV IRES-mediated translation complex, at least composed of EIF3C, IGF2BP1, RPS3 and HCV RNA-replicon (PubMed:19541769).
Interacts with CRY1 (By similarity).
Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (PubMed:17289661).
Interacts with HNRPD (PubMed:24423872).
Interacts with PRMT1; the interaction methylates RPS3 (PubMed:19460357).
Interacts with SUMO1; the interaction sumoylates RPS3 (PubMed:21968017).
Interacts with UBC9 (PubMed:21968017).
Interacts with CDK1; the interaction phosphorylates RPS3 (PubMed:21871177).
Interacts with PRKCD; the interaction phosphorylates RPS3 (PubMed:19059439).
Interacts with PKB/AKT; the interaction phosphorylates RPS3 (PubMed:20605787).
Interacts with E2F1; the interaction occurs in the absence of nerve growth factor and increases transcription of pro-apoptotic proteins BCL2L11/BIM and HRK/Dp5 (PubMed:20605787).
Interacts with the base excision repair proteins APEX1 and OGG1; interaction with OGG1 increases OGG1 N-glycosylase activity (PubMed:15518571).
Interacts with UNG; the interaction increases the uracil excision activity of UNG1 (PubMed:18973764).
Interacts with HSP90; the interaction prevents the ubiquitination and proteasome-dependent degradation of RPS3 and is suppressed by increased ROS levels (PubMed:16314389).
Interacts with TOM70; the interaction promotes translocation of RPS3 to the mitochondrion (PubMed:23911537).
Interacts (via N-terminus) with RELA (via N-terminus); the interaction enhances the DNA-binding activity of the NF-kappa-B p65-p50 complex (PubMed:18045535).
Interacts with NFKBIA; the interaction is direct and may bridge the interaction between RPS3 and RELA (PubMed:24457201).
Interacts with IKKB; the interaction phosphorylates RPS3 and enhances its translocation to the nucleus (PubMed:21399639).
Interacts (via KH domain) with MDM2 and TP53 (PubMed:19656744).
Interacts with TRADD (PubMed:22510408).
Interacts (via N-terminus) with E.coli O157:H7 (strain EDL933) nleH1 and nleH2; the interaction with nleH1 inhibits phosphorylation by IKKB, reduces RPS3 nuclear abundance and inhibits transcriptional activation by the NF-kappa-B p65-p50 complex (PubMed:20041225, PubMed:21399639).
Interacts with ASCC3 (PubMed:28757607).
Identified in a HCV IRES-mediated translation complex, at least composed of EIF3C, IGF2BP1, RPS3 and HCV RNA-replicon (PubMed:19541769).
Interacts with CRY1 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P23396 | CSNK2A1 P68400 | 2 | EBI-351193, EBI-347804 | |
BINARY | P23396 | HTT P42858 | 3 | EBI-351193, EBI-466029 | |
BINARY | P23396 | IKBKB O14920 | 4 | EBI-351193, EBI-81266 | |
BINARY | P23396 | LRRK2 Q5S007 | 4 | EBI-351193, EBI-5323863 | |
BINARY | P23396 | LTV1 Q96GA3 | 4 | EBI-351193, EBI-2558389 | |
BINARY | P23396 | MDM2 Q00987 | 8 | EBI-351193, EBI-389668 | |
BINARY | P23396 | NEDD8 Q15843 | 3 | EBI-351193, EBI-716247 | |
BINARY | P23396 | NFKB1 P19838 | 4 | EBI-351193, EBI-300010 | |
BINARY | P23396 | NFKBIA P25963 | 6 | EBI-351193, EBI-307386 | |
BINARY | P23396 | PPID Q08752 | 4 | EBI-351193, EBI-716596 | |
BINARY | P23396 | RELA Q04206 | 8 | EBI-351193, EBI-73886 | |
BINARY | P23396 | RPS10 P46783 | 3 | EBI-351193, EBI-354442 | |
BINARY | P23396 | TP53 P04637 | 4 | EBI-351193, EBI-366083 | |
BINARY | P23396 | YWHAZ P63104 | 2 | EBI-351193, EBI-347088 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 21-92 | KH type-2 | ||||
Sequence: LNEFLTRELAEDGYSGVEVRVTPTRTEIIILATRTQNVLGEKGRRIRELTAVVQKRFGFPEGSVELYAEKVA | ||||||
Region | 214-243 | Disordered | ||||
Sequence: KDEILPTTPISEQKGGKPEPPAMPQPVPTA |
Sequence similarities
Belongs to the universal ribosomal protein uS3 family.
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
P23396-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length243
- Mass (Da)26,688
- Last updated1993-10-01 v2
- Checksum6ECBB34A8EE04AAF
P23396-2
- Name2
- Differences from canonical
- 85-85: E → ELKIMVMVTGYPLLPLK
Computationally mapped potential isoform sequences
There are 13 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H0YES8 | H0YES8_HUMAN | RPS3 | 33 | ||
H0YF32 | H0YF32_HUMAN | RPS3 | 123 | ||
H0YEU2 | H0YEU2_HUMAN | RPS3 | 171 | ||
H0YCJ7 | H0YCJ7_HUMAN | RPS3 | 135 | ||
E9PSF4 | E9PSF4_HUMAN | RPS3 | 103 | ||
E9PPU1 | E9PPU1_HUMAN | RPS3 | 158 | ||
E9PQ96 | E9PQ96_HUMAN | RPS3 | 91 | ||
E9PQX2 | E9PQX2_HUMAN | RPS3 | 44 | ||
E9PJN9 | E9PJN9_HUMAN | RPS3 | 36 | ||
E9PJH4 | E9PJH4_HUMAN | RPS3 | 115 | ||
E9PK82 | E9PK82_HUMAN | RPS3 | 128 | ||
E9PL09 | E9PL09_HUMAN | RPS3 | 231 | ||
F2Z2S8 | F2Z2S8_HUMAN | RPS3 | 117 |
Sequence caution
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 8 | in Ref. 2; AAB19349 | ||||
Sequence: K → R | ||||||
Alternative sequence | VSP_046667 | 85 | in isoform 2 | |||
Sequence: E → ELKIMVMVTGYPLLPLK | ||||||
Sequence conflict | 104 | in Ref. 1; CAA39248 | ||||
Sequence: S → C | ||||||
Sequence conflict | 233 | in Ref. 1; CAA39248 | ||||
Sequence: P → L |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U14990 EMBL· GenBank· DDBJ | AAB60336.1 EMBL· GenBank· DDBJ | mRNA | ||
U14991 EMBL· GenBank· DDBJ | AAB60337.1 EMBL· GenBank· DDBJ | mRNA | ||
U14992 EMBL· GenBank· DDBJ | AAB60338.1 EMBL· GenBank· DDBJ | mRNA | ||
X55715 EMBL· GenBank· DDBJ | CAA39248.1 EMBL· GenBank· DDBJ | mRNA | ||
S42658 EMBL· GenBank· DDBJ | AAB19349.2 EMBL· GenBank· DDBJ | mRNA | ||
AB061838 EMBL· GenBank· DDBJ | BAB79476.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY791291 EMBL· GenBank· DDBJ | AAV40835.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK313051 EMBL· GenBank· DDBJ | BAG35882.1 EMBL· GenBank· DDBJ | mRNA | ||
AP000744 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471076 EMBL· GenBank· DDBJ | EAW74963.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC003137 EMBL· GenBank· DDBJ | AAH03137.1 EMBL· GenBank· DDBJ | mRNA | ||
BC003577 EMBL· GenBank· DDBJ | AAH03577.1 EMBL· GenBank· DDBJ | mRNA | ||
BC013196 EMBL· GenBank· DDBJ | AAH13196.1 EMBL· GenBank· DDBJ | mRNA | ||
BC034149 EMBL· GenBank· DDBJ | AAH34149.1 EMBL· GenBank· DDBJ | mRNA | ||
BC071917 EMBL· GenBank· DDBJ | AAH71917.1 EMBL· GenBank· DDBJ | mRNA | ||
BC100284 EMBL· GenBank· DDBJ | AAI00285.1 EMBL· GenBank· DDBJ | mRNA | ||
L16016 EMBL· GenBank· DDBJ | AAA18095.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB062288 EMBL· GenBank· DDBJ | BAB93471.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |