G1SJB4 · RACK1_RABIT
- ProteinSmall ribosomal subunit protein RACK1
- GeneRACK1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids317 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Scaffolding protein involved in the recruitment, assembly and/or regulation of a variety of signaling molecules (By similarity).
Interacts with a wide variety of proteins and plays a role in many cellular processes (By similarity).
Component of the 40S ribosomal subunit involved in translational repression (PubMed:23873042, PubMed:25601755, PubMed:27863242, PubMed:30517857).
Involved in the initiation of the ribosome quality control (RQC), a pathway that takes place when a ribosome has stalled during translation, by promoting ubiquitination of a subset of 40S ribosomal subunits (By similarity).
Binds to and stabilizes activated protein kinase C (PKC), increasing PKC-mediated phosphorylation (By similarity).
May recruit activated PKC to the ribosome, leading to phosphorylation of EIF6 (By similarity).
Inhibits the activity of SRC kinases including SRC, LCK and YES1 (By similarity).
Inhibits cell growth by prolonging the G0/G1 phase of the cell cycle (By similarity).
Enhances phosphorylation of BMAL1 by PRKCA and inhibits transcriptional activity of the BMAL1-CLOCK heterodimer (By similarity).
Facilitates ligand-independent nuclear translocation of AR following PKC activation, represses AR transactivation activity and is required for phosphorylation of AR by SRC (By similarity).
Modulates IGF1R-dependent integrin signaling and promotes cell spreading and contact with the extracellular matrix (By similarity).
Involved in PKC-dependent translocation of ADAM12 to the cell membrane (By similarity).
Promotes the ubiquitination and proteasome-mediated degradation of proteins such as CLEC1B and HIF1A (By similarity).
Required for VANGL2 membrane localization, inhibits Wnt signaling, and regulates cellular polarization and oriented cell division during gastrulation (By similarity).
Required for PTK2/FAK1 phosphorylation and dephosphorylation (By similarity).
Regulates internalization of the muscarinic receptor CHRM2 (By similarity).
Promotes apoptosis by increasing oligomerization of BAX and disrupting the interaction of BAX with the anti-apoptotic factor BCL2L (By similarity).
Inhibits TRPM6 channel activity (By similarity).
Regulates cell surface expression of some GPCRs such as TBXA2R (By similarity).
Plays a role in regulation of FLT1-mediated cell migration (By similarity).
Involved in the transport of ABCB4 from the Golgi to the apical bile canalicular membrane (By similarity).
Promotes migration of breast carcinoma cells by binding to and activating RHOA (By similarity).
Acts as an adapter for the dephosphorylation and inactivation of AKT1 by promoting recruitment of PP2A phosphatase to AKT1 (By similarity).
Interacts with a wide variety of proteins and plays a role in many cellular processes (By similarity).
Component of the 40S ribosomal subunit involved in translational repression (PubMed:23873042, PubMed:25601755, PubMed:27863242, PubMed:30517857).
Involved in the initiation of the ribosome quality control (RQC), a pathway that takes place when a ribosome has stalled during translation, by promoting ubiquitination of a subset of 40S ribosomal subunits (By similarity).
Binds to and stabilizes activated protein kinase C (PKC), increasing PKC-mediated phosphorylation (By similarity).
May recruit activated PKC to the ribosome, leading to phosphorylation of EIF6 (By similarity).
Inhibits the activity of SRC kinases including SRC, LCK and YES1 (By similarity).
Inhibits cell growth by prolonging the G0/G1 phase of the cell cycle (By similarity).
Enhances phosphorylation of BMAL1 by PRKCA and inhibits transcriptional activity of the BMAL1-CLOCK heterodimer (By similarity).
Facilitates ligand-independent nuclear translocation of AR following PKC activation, represses AR transactivation activity and is required for phosphorylation of AR by SRC (By similarity).
Modulates IGF1R-dependent integrin signaling and promotes cell spreading and contact with the extracellular matrix (By similarity).
Involved in PKC-dependent translocation of ADAM12 to the cell membrane (By similarity).
Promotes the ubiquitination and proteasome-mediated degradation of proteins such as CLEC1B and HIF1A (By similarity).
Required for VANGL2 membrane localization, inhibits Wnt signaling, and regulates cellular polarization and oriented cell division during gastrulation (By similarity).
Required for PTK2/FAK1 phosphorylation and dephosphorylation (By similarity).
Regulates internalization of the muscarinic receptor CHRM2 (By similarity).
Promotes apoptosis by increasing oligomerization of BAX and disrupting the interaction of BAX with the anti-apoptotic factor BCL2L (By similarity).
Inhibits TRPM6 channel activity (By similarity).
Regulates cell surface expression of some GPCRs such as TBXA2R (By similarity).
Plays a role in regulation of FLT1-mediated cell migration (By similarity).
Involved in the transport of ABCB4 from the Golgi to the apical bile canalicular membrane (By similarity).
Promotes migration of breast carcinoma cells by binding to and activating RHOA (By similarity).
Acts as an adapter for the dephosphorylation and inactivation of AKT1 by promoting recruitment of PP2A phosphatase to AKT1 (By similarity).
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | dendrite | |
Cellular Component | nucleus | |
Cellular Component | perikaryon | |
Cellular Component | perinuclear region of cytoplasm | |
Cellular Component | phagocytic cup | |
Cellular Component | ribonucleoprotein complex | |
Cellular Component | ribosome | |
Molecular Function | protein kinase C binding | |
Molecular Function | ribosome binding | |
Molecular Function | translation regulator activity | |
Biological Process | apoptotic process | |
Biological Process | gastrulation | |
Biological Process | positive regulation of protein phosphorylation | |
Biological Process | rescue of stalled ribosome | |
Biological Process | rhythmic process |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameSmall ribosomal subunit protein RACK1
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Lagomorpha > Leporidae > Oryctolagus
Accessions
- Primary accessionG1SJB4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Note: Recruited to the plasma membrane through interaction with KRT1 which binds to membrane-bound ITGB1. Also associated with the membrane in oncogene-transformed cells. PKC activation induces translocation from the perinuclear region to the cell periphery (By similarity).
In the brain, detected mainly in cell bodies and dendrites with little expression in axonal fibers or nuclei (By similarity).
Localized to phagocytic cups following infection by Y.pestis (By similarity).
In the brain, detected mainly in cell bodies and dendrites with little expression in axonal fibers or nuclei (By similarity).
Localized to phagocytic cups following infection by Y.pestis (By similarity).
Keywords
- Cellular component
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000460072 | 1-317 | Small ribosomal subunit protein RACK1 | |||
Sequence: MTEQMTLRGTLKGHNGWVTQIATTPQFPDMILSASRDKTIIMWKLTRDETNYGIPQRALRGHSHFVSDVVISSDGQFALSGSWDGTLRLWDLTTGTTTRRFVGHTKDVLSVAFSSDNRQIVSGSRDKTIKLWNTLGVCKYTVQDESHSEWVSCVRFSPNSSNPIIVSCGWDKLVKVWNLANCKLKTNHIGHTGYLNTVTVSPDGSLCASGGKDGQAMLWDLNEGKHLYTLDGGDIINALCFSPNRYWLCAATGPSIKIWDLEGKIIVDELKQEVISTSSKAEPPQCTSLAWSADGQTLFAGYTDNLVRVWQVTIGTR | ||||||
Modified residue | 6 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 10 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 52 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 96 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 130 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 183 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 228 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 276 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 277 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 278 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 279 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 316 | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Phosphorylated on Tyr-228 and/or Tyr-246 by SRC. This is required for binding to SRC.
Keywords
- PTM
Proteomic databases
Expression
Gene expression databases
Interaction
Subunit
Monomer; also forms homod (By similarity)imers and homooligomers (By similarity).
Interacts with CPNE3 (By similarity).
May interact with ABCB4 (By similarity).
Component of the small (40S) ribosomal subunit (By similarity).
Interacts with the 80S ribosome (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242, PubMed:29856316, PubMed:30293783, PubMed:30355441, PubMed:30517857, PubMed:31246176, PubMed:31609474, PubMed:31768042, PubMed:32286223, PubMed:33296660, PubMed:35679869, PubMed:35822879, PubMed:36653451).
Binds NHERF1 (By similarity).
Forms a ternary complex with TRIM63 and PRKCE (By similarity).
Interacts with HABP4, KRT1 and OTUB1 (By similarity).
Interacts with SRC (via SH2 domain); the interaction is enhanced by tyrosine phosphorylation of RACK1 (By similarity).
Recruited in a circadian manner into a nuclear complex which also includes BMAL1 and PRKCA (By similarity).
Interacts with AR (By similarity).
Interacts with IGF1R but not with INSR (By similarity).
Interacts with ADAM12 (By similarity).
Interacts with CLEC1B (via N-terminal region) and with HIF1A; the interaction promotes their degradation (By similarity).
Interacts with RHOA; this enhances RHOA activation and promotes cell migration (By similarity)3 Interacts with CHRM2; the interaction regulates CHRM2 internalization (By similarity).
Interacts with TRPM6 (via kinase domain) (By similarity).
Interacts with PTK2/FAK1; required for PTK2/FAK1 phosphorylation and dephosphorylation (By similarity).
Interacts with FLT1 (By similarity).
Interacts with TBXA2R isoform 2 (By similarity).
Interacts with HRAS (By similarity).
Interacts with LARP4B (By similarity).
Interacts with LARP4 (By similarity).
Interacts with PKD2L1 (By similarity).
Interacts with isoform 2 of SLC4A7 (By similarity).
Interacts with SLC9A5; this interaction regulates SLC9A5 cell-surface targeting and SLC9A5 activity (By similarity).
Interacts with SLC9A6; this interaction regulates the distribution of SLC9A6 between endosomes and the plasma membrane (By similarity).
Interacts with CPNE3 (By similarity).
May interact with ABCB4 (By similarity).
Component of the small (40S) ribosomal subunit (By similarity).
Interacts with the 80S ribosome (PubMed:23873042, PubMed:25601755, PubMed:26245381, PubMed:27863242, PubMed:29856316, PubMed:30293783, PubMed:30355441, PubMed:30517857, PubMed:31246176, PubMed:31609474, PubMed:31768042, PubMed:32286223, PubMed:33296660, PubMed:35679869, PubMed:35822879, PubMed:36653451).
Binds NHERF1 (By similarity).
Forms a ternary complex with TRIM63 and PRKCE (By similarity).
Interacts with HABP4, KRT1 and OTUB1 (By similarity).
Interacts with SRC (via SH2 domain); the interaction is enhanced by tyrosine phosphorylation of RACK1 (By similarity).
Recruited in a circadian manner into a nuclear complex which also includes BMAL1 and PRKCA (By similarity).
Interacts with AR (By similarity).
Interacts with IGF1R but not with INSR (By similarity).
Interacts with ADAM12 (By similarity).
Interacts with CLEC1B (via N-terminal region) and with HIF1A; the interaction promotes their degradation (By similarity).
Interacts with RHOA; this enhances RHOA activation and promotes cell migration (By similarity)3 Interacts with CHRM2; the interaction regulates CHRM2 internalization (By similarity).
Interacts with TRPM6 (via kinase domain) (By similarity).
Interacts with PTK2/FAK1; required for PTK2/FAK1 phosphorylation and dephosphorylation (By similarity).
Interacts with FLT1 (By similarity).
Interacts with TBXA2R isoform 2 (By similarity).
Interacts with HRAS (By similarity).
Interacts with LARP4B (By similarity).
Interacts with LARP4 (By similarity).
Interacts with PKD2L1 (By similarity).
Interacts with isoform 2 of SLC4A7 (By similarity).
Interacts with SLC9A5; this interaction regulates SLC9A5 cell-surface targeting and SLC9A5 activity (By similarity).
Interacts with SLC9A6; this interaction regulates the distribution of SLC9A6 between endosomes and the plasma membrane (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 13-44 | WD 1 | ||||
Sequence: GHNGWVTQIATTPQFPDMILSASRDKTIIMWK | ||||||
Repeat | 61-91 | WD 2 | ||||
Sequence: GHSHFVSDVVISSDGQFALSGSWDGTLRLWD | ||||||
Repeat | 103-133 | WD 3 | ||||
Sequence: GHTKDVLSVAFSSDNRQIVSGSRDKTIKLWN | ||||||
Repeat | 146-178 | WD 4 | ||||
Sequence: SHSEWVSCVRFSPNSSNPIIVSCGWDKLVKVWN | ||||||
Repeat | 190-220 | WD 5 | ||||
Sequence: GHTGYLNTVTVSPDGSLCASGGKDGQAMLWD | ||||||
Repeat | 231-260 | WD 6 | ||||
Sequence: DGGDIINALCFSPNRYWLCAATGPSIKIWD | ||||||
Repeat | 281-311 | WD 7 | ||||
Sequence: AEPPQCTSLAWSADGQTLFAGYTDNLVRVWQ |
Domain
The 7 WD repeats mediate protein-protein interactions with binding partners.
Sequence similarities
Belongs to the WD repeat G protein beta family. Ribosomal protein RACK1 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length317
- Mass (Da)35,077
- Last updated2024-03-27 v3
- Checksum257F91E369ED2044
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AAGW02043964 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |