G1SJB4 · RACK1_RABIT

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).

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentdendrite
Cellular Componentnucleus
Cellular Componentperikaryon
Cellular Componentperinuclear region of cytoplasm
Cellular Componentphagocytic cup
Cellular Componentribonucleoprotein complex
Cellular Componentribosome
Molecular Functionprotein kinase C binding
Molecular Functionribosome binding
Molecular Functiontranslation regulator activity
Biological Processapoptotic process
Biological Processgastrulation
Biological Processpositive regulation of protein phosphorylation
Biological Processrescue of stalled ribosome
Biological Processrhythmic process

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Small ribosomal subunit protein RACK1
  • Alternative names
    • Receptor of activated protein C kinase 1

Gene names

    • Name
      RACK1

Organism names

  • Taxonomic identifier
  • Strain
    • Thorbecke
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Lagomorpha > Leporidae > Oryctolagus

Accessions

  • Primary accession
    G1SJB4

Proteomes

Subcellular Location

Cell membrane
; Peripheral membrane protein
Cytoplasm
Nucleus
Perikaryon
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).

Keywords

PTM/Processing

Features

Showing features for modified residue, chain.

TypeIDPosition(s)Description
Modified residue1N-acetylmethionine
ChainPRO_00004600721-317Small ribosomal subunit protein RACK1
Modified residue6Phosphothreonine
Modified residue10Phosphothreonine
Modified residue52Phosphotyrosine
Modified residue96Phosphothreonine
Modified residue130N6-acetyllysine
Modified residue183N6-acetyllysine
Modified residue228Phosphotyrosine
Modified residue276Phosphoserine
Modified residue277Phosphothreonine
Modified residue278Phosphoserine
Modified residue279Phosphoserine
Modified residue316Phosphothreonine

Post-translational modification

Phosphorylated on Tyr-228 and/or Tyr-246 by SRC. This is required for binding to SRC.

Keywords

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).

Protein-protein interaction databases

Family & Domains

Features

Showing features for repeat.

TypeIDPosition(s)Description
Repeat13-44WD 1
Repeat61-91WD 2
Repeat103-133WD 3
Repeat146-178WD 4
Repeat190-220WD 5
Repeat231-260WD 6
Repeat281-311WD 7

Domain

The 7 WD repeats mediate protein-protein interactions with binding partners.

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    317
  • Mass (Da)
    35,077
  • Last updated
    2024-03-27 v3
  • Checksum
    257F91E369ED2044
MTEQMTLRGTLKGHNGWVTQIATTPQFPDMILSASRDKTIIMWKLTRDETNYGIPQRALRGHSHFVSDVVISSDGQFALSGSWDGTLRLWDLTTGTTTRRFVGHTKDVLSVAFSSDNRQIVSGSRDKTIKLWNTLGVCKYTVQDESHSEWVSCVRFSPNSSNPIIVSCGWDKLVKVWNLANCKLKTNHIGHTGYLNTVTVSPDGSLCASGGKDGQAMLWDLNEGKHLYTLDGGDIINALCFSPNRYWLCAATGPSIKIWDLEGKIIVDELKQEVISTSSKAEPPQCTSLAWSADGQTLFAGYTDNLVRVWQVTIGTR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAGW02043964
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

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