RACK1
entrez
10399
canonical
uniprot
P63244
canonical
ensembl
ENSG00000204628
resolver
ensp
ENSP00000426909
resolver
enst
ENST00000512805
resolver
genesymbol
RACK1
resolver
genesymbol_syn
GNB2L1
resolver
hgnc
HGNC:4399
resolver
uniprot
B3KTJ0
resolver
uniprot
D3DWS0
resolver
uniprot
E9KL35
resolver
uniprot
P25388
resolver
uniprot
P99049
resolver
uniprot
Q53HU2
resolver
uniprot
Q5J8M6
resolver
uniprot
Q5VLR4
resolver
uniprot
Q6FH47
resolver
uniprot_entry
E9KL35_HUMAN
resolver
uniprot_entry
RACK1_HUMAN
resolver
uniprot_sec
B3KTJ0
resolver
uniprot_sec
D3DWS0
resolver
uniprot_sec
P25388
resolver
uniprot_sec
P99049
resolver
uniprot_sec
Q53HU2
resolver
uniprot_sec
Q5J8M6
resolver
uniprot_sec
Q5VLR4
resolver
uniprot_sec
Q6FH47
resolver
amino_acid_sequence
MTEQMTLRGTLKGHNGWVTQIATTPQFPDMILSASRDKTIIMWKLTRDETNYGIPQRALRGHSHFVSDVVISSDGQFALSGSWDGTLRLWDLTTGTTTRRFVGHTKDVLSVAFSSDNRQIVSGSRDKTIKLWNTLGVCKYTVQDESHSEWVSCVRFSPNSSNPIIVSCGWDKLVKVWNLANCKLKTNHIGHTGYLNTVTVSPDGSLCASGGKDGQAMLWDLNEGKHLYTLDGGDIINALCFSPNRYWLCAATGPSIKIWDLEGKIIVDELKQEVISTSSKAEPPQCTSLAWSADGQTLFAGYTDNLVRVWQVTIGTR
uniprot
proteins
function
FUNCTION: Scaffolding protein involved in the recruitment, assembly and/or regulation of a variety of signaling molecules. Interacts with a wide variety of proteins and plays a role in many cellular processes. Component of the 40S ribosomal subunit involved in translational repression (PubMed:23636399). 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 (PubMed:28132843). Binds to and stabilizes activated protein kinase C (PKC), increasing PKC-mediated phosphorylation. May recruit activated PKC to the ribosome, leading to phosphorylation of EIF6. Inhibits the activity of SRC kinases including SRC, LCK and YES1. Inhibits cell growth by prolonging the G0/G1 phase of the cell cycle. Enhances phosphorylation of BMAL1 by PRKCA and inhibits transcriptional activity of the BMAL1-CLOCK heterodimer. Facilitates ligand-independent nuclear translocation of AR following PKC activation, represses AR transactivation activity and is required for phosphorylation of AR by SRC. Modulates IGF1R-dependent integrin signaling and promotes cell spreading and contact with the extracellular matrix. Involved in PKC-dependent translocation of ADAM12 to the cell membrane. Promotes the ubiquitination and proteasome-mediated degradation of proteins such as CLEC1B and HIF1A. Required for VANGL2 membrane localization, inhibits Wnt signaling, and regulates cellular polarization and oriented cell division during gastrulation. Required for PTK2/FAK1 phosphorylation and dephosphorylation. Regulates internalization of the muscarinic receptor CHRM2. Promotes apoptosis by increasing oligomerization of BAX and disrupting the interaction of BAX with the anti-apoptotic factor BCL2L. Inhibits TRPM6 channel activity. Regulates cell surface expression of some GPCRs such as TBXA2R. Plays a role in regulation of FLT1-mediated cell migration. Involved in the transport of ABCB4 from the Golgi to the apical bile canalicular membrane (PubMed:19674157). Promotes migration of breast carcinoma cells by binding to and activating RHOA (PubMed:20499158). Acts as an adapter for the dephosphorylation and inactivation of AKT1 by promoting recruitment of PP2A phosphatase to AKT1 (By similarity). {ECO:0000250|UniProtKB:P68040, ECO:0000269|PubMed:11884618, ECO:0000269|PubMed:12589061, ECO:0000269|PubMed:12958311, ECO:0000269|PubMed:17108144, ECO:0000269|PubMed:17244529, ECO:0000269|PubMed:17956333, ECO:0000269|PubMed:18088317, ECO:0000269|PubMed:18258429, ECO:0000269|PubMed:18621736, ECO:0000269|PubMed:19423701, ECO:0000269|PubMed:19674157, ECO:0000269|PubMed:19785988, ECO:0000269|PubMed:20499158, ECO:0000269|PubMed:20541605, ECO:0000269|PubMed:20573744, ECO:0000269|PubMed:20976005, ECO:0000269|PubMed:21212275, ECO:0000269|PubMed:21347310, ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:28132843, ECO:0000269|PubMed:9584165}.; FUNCTION: (Microbial infection) Binds to Y.pseudotuberculosis yopK which leads to inhibition of phagocytosis and survival of bacteria following infection of host cells. {ECO:0000269|PubMed:21347310}.; FUNCTION: (Microbial infection) Enhances phosphorylation of HIV-1 Nef by PKCs. {ECO:0000269|PubMed:11312657}.; FUNCTION: (Microbial infection) In case of poxvirus infection, remodels the ribosomes so that they become optimal for the viral mRNAs (containing poly-A leaders) translation but not for host mRNAs. {ECO:0000269|PubMed:28636603}.; FUNCTION: (Microbial infection) Contributes to the cap-independent internal ribosome entry site (IRES)-mediated translation by some RNA viruses. {ECO:0000269|PubMed:25416947}.
uniprot
proteins
mass_dalton
35077
uniprot
proteins
mutagenesis
MUTAGEN 36..38; /note="RDK->DDE: In DEmut; abolishes association with the ribosome and ability to initiate the ribosome quality control (RQC)."; /evidence="ECO:0000269|PubMed:28132843"; MUTAGEN 52; /note="Y->F: No effect on binding to SRC. Abolishes binding to PTK2/FAK1 and reduces cell adhesion and foci formation."; /evidence="ECO:0000269|PubMed:11279199, ECO:0000269|PubMed:12400005, ECO:0000269|PubMed:19423701"; MUTAGEN 57; /note="R->A: Decreased binding to PTK2/FAK1; when associated with A-60."; /evidence="ECO:0000269|PubMed:19423701"; MUTAGEN 60; /note="R->A: Decreased binding to PTK2/FAK1; when associated with A-57."; /evidence="ECO:0000269|PubMed:19423701"; MUTAGEN 127; /note="K->A: Decreased binding to PTK2/FAK1; when associated with A-130."; /evidence="ECO:0000269|PubMed:19423701"; MUTAGEN 130; /note="K->A: Decreased binding to PTK2/FAK1; when associated with A-127."; /evidence="ECO:0000269|PubMed:19423701"; MUTAGEN 140; /note="Y->F: No effect on binding to SRC."; /evidence="ECO:0000269|PubMed:11279199, ECO:0000269|PubMed:12400005"; MUTAGEN 194; /note="Y->F: No effect on binding to SRC."; /evidence="ECO:0000269|PubMed:11279199, ECO:0000269|PubMed:12400005"; MUTAGEN 228; /note="Y->F: No effect on binding to SRC. Does not abolish phosphorylation by SRC. Abolishes phosphorylation by SRC; when associated with F-246 and F-302."; /evidence="ECO:0000269|PubMed:11279199, ECO:0000269|PubMed:12400005"; MUTAGEN 246; /note="Y->F: Abolishes binding to SRC. Does not abolish phosphorylation by SRC. Abolishes phosphorylation by SRC; when associated with F-228 and F-302."; /evidence="ECO:0000269|PubMed:11279199, ECO:0000269|PubMed:12400005"; MUTAGEN 276..279; /note="STSS->EEEE: Enhanced translation of mRNAs containing poly-A leaders."; /evidence="ECO:0000269|PubMed:28636603"; MUTAGEN 278; /note="S->E: Enhanced translation of mRNAs containing poly-A leaders."; /evidence="ECO:0000269|PubMed:28636603"; MUTAGEN 302; /note="Y->F: No effect on binding to SRC. Abolishes phosphorylation by SRC; when associated with F-228 and F-246."; /evidence="ECO:0000269|PubMed:11279199, ECO:0000269|PubMed:12400005
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on Tyr-228 and/or Tyr-246 by SRC. This is required for binding to SRC. {ECO:0000269|PubMed:11279199, ECO:0000269|PubMed:12400005, ECO:0000269|PubMed:19423701}.; PTM: (Microbial infection) Phosphorylated by vaccinia virus B1 kinase on serine and threonine residues; this phosphorylation remodels the ribosome properties, favoring the viral mRNA translation. {ECO:0000269|PubMed:28636603}.
uniprot
proteins
protein_family
Ribosomal protein RACK1 subfamily
uniprot
proteins
protein_family
WD repeat G protein beta family
uniprot
proteins
pubmed
10849009
uniprot
proteins
pubmed
11279199
uniprot
proteins
pubmed
11312657
uniprot
proteins
pubmed
11884618
uniprot
proteins
pubmed
11956211
uniprot
proteins
pubmed
12400005
uniprot
proteins
pubmed
12589061
uniprot
proteins
pubmed
12958311
uniprot
proteins
pubmed
14500341
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
14699138
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15140893
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
15596539
uniprot
proteins
pubmed
17108144
uniprot
proteins
pubmed
17244529
uniprot
proteins
pubmed
17956333
uniprot
proteins
pubmed
18057008
uniprot
proteins
pubmed
18088317
uniprot
proteins
pubmed
18258429
uniprot
proteins
pubmed
18621736
uniprot
proteins
pubmed
18954305
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19423701
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19674157
uniprot
proteins
pubmed
19785988
uniprot
proteins
pubmed
20010870
uniprot
proteins
pubmed
20499158
uniprot
proteins
pubmed
20529362
uniprot
proteins
pubmed
20541605
uniprot
proteins
pubmed
20573744
uniprot
proteins
pubmed
20976005
uniprot
proteins
pubmed
21098120
uniprot
proteins
pubmed
21212275
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21347310
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22174419
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
22869111
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23636399
uniprot
proteins
pubmed
24006492
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24524803
uniprot
proteins
pubmed
2499885
uniprot
proteins
pubmed
25416947
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
28132843
uniprot
proteins
pubmed
28161490
uniprot
proteins
pubmed
28636603
uniprot
proteins
pubmed
29743600
uniprot
proteins
pubmed
33606008
uniprot
proteins
pubmed
37712706
uniprot
proteins
pubmed
37758692
uniprot
proteins
pubmed
38157925
uniprot
proteins
pubmed
9584165
uniprot
proteins
sequence_length
317
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11312657, ECO:0000269|PubMed:17956333}; Peripheral membrane protein. Cytoplasm {ECO:0000269|PubMed:10849009, ECO:0000269|PubMed:11279199, ECO:0000269|PubMed:12958311, ECO:0000269|PubMed:19785988, ECO:0000269|PubMed:20499158, ECO:0000269|PubMed:20573744, ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:29743600, ECO:0000269|PubMed:37712706}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:11279199, ECO:0000269|PubMed:12958311}. Nucleus {ECO:0000269|PubMed:10849009}. Perikaryon {ECO:0000250|UniProtKB:P68040}. Cell projection, dendrite {ECO:0000250|UniProtKB:P68040}. Cell projection, phagocytic cup {ECO:0000269|PubMed:21347310}. Note=Recruited to the plasma membrane through interaction with KRT1 which binds to membrane-bound ITGB1 (PubMed:17956333). Also associated with the membrane in oncogene-transformed cells (PubMed:11884618). PKC activation induces translocation from the perinuclear region to the cell periphery (PubMed:11279199). 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 (PubMed:21347310). {ECO:0000250|UniProtKB:P68040, ECO:0000269|PubMed:11279199, ECO:0000269|PubMed:11884618, ECO:0000269|PubMed:17956333, ECO:0000269|PubMed:21347310}.
uniprot
proteins