ID RACK1_MOUSE Reviewed; 317 AA. AC P68040; P25388; P99049; Q3THP0; Q3THY7; Q3TKQ0; Q3TW88; Q5NCC5; Q5NCC6; AC Q9CSQ0; Q9ERM6; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 04-NOV-2026, entry version 186. DE RecName: Full=Small ribosomal subunit protein RACK1 {ECO:0000305}; DE AltName: Full=12-3; DE AltName: Full=Guanine nucleotide-binding protein subunit beta-2-like 1; DE AltName: Full=Receptor for activated C kinase; DE AltName: Full=Receptor of activated protein C kinase 1; DE AltName: Full=Receptor of activated protein kinase C 1; DE AltName: Full=p205; DE Contains: DE RecName: Full=Small ribosomal subunit protein RACK1, N-terminally processed; DE AltName: Full=Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed; DE AltName: Full=Receptor of activated protein C kinase 1, N-terminally processed; GN Name=Rack1 {ECO:0000312|MGI:MGI:101849}; Synonyms=Gnb2-rs1, Gnb2l1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=7968370; DOI=10.1016/0169-328x(94)90144-9; RA Imai Y., Suzuki Y., Tohyama M., Wanaka A., Takagi T.; RT "Cloning and expression of a neural differentiation-associated gene, p205, RT in the embryonal carcinoma cell line P19 and in the developing mouse."; RL Brain Res. Mol. Brain Res. 24:313-319(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6J; TISSUE=Spleen; RA Raj N.B.K., Su Y., Au W.C., Pitha P.M.; RT "Primary sequence of the mouse guanine nucleotide binding protein related RT gene."; RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=BALB/cJ, C57BL/6J, and DBA/2J; RC TISSUE=Blastocyst, Embryo, Embryonic head, Embryonic spinal ganglion, RC Embryonic stem cell, Head, Kidney, Mammary gland, and Osteoclast; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-296. RC STRAIN=129/SvJ; RA Choi D., Messing R.O.; RT "Genomic structure and expression of mouse receptor for activated C kinase RT (RACK1)."; RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases. RN [8] RP PROTEIN SEQUENCE OF 2-11 AND 271-279, CLEAVAGE OF INITIATOR METHIONINE, RP ACETYLATION AT THR-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=C57BL/6J; TISSUE=Skeletal muscle; RA Kanor S., Quadroni M., Bienvenut W.V.; RL Submitted (MAR-2006) to UniProtKB. RN [9] RP PROTEIN SEQUENCE OF 226-317, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, and Hippocampus; RA Lubec G., Klug S., Yang J.W., Zigmond M.; RL Submitted (JUL-2007) to UniProtKB. RN [10] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=16414032; DOI=10.1016/j.brainres.2005.11.018; RA Ashique A.M., Kharazia V., Yaka R., Phamluong K., Peterson A.S., Ron D.; RT "Localization of the scaffolding protein RACK1 in the developing and adult RT mouse brain."; RL Brain Res. 1069:31-38(2006). RN [11] RP FUNCTION, AND INTERACTION WITH TRPM6. RX PubMed=18258429; DOI=10.1016/j.cub.2007.12.058; RA Cao G., Thebault S., van der Wijst J., van der Kemp A., Lasonder E., RA Bindels R.J., Hoenderop J.G.; RT "RACK1 inhibits TRPM6 activity via phosphorylation of the fused alpha- RT kinase domain."; RL Curr. Biol. 18:168-176(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-316, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [13] RP FUNCTION, INTERACTION WITH BMAL1 AND PRKCA, SUBCELLULAR LOCATION, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=20093473; DOI=10.1126/science.1180067; RA Robles M.S., Boyault C., Knutti D., Padmanabhan K., Weitz C.J.; RT "Identification of RACK1 and protein kinase Calpha as integral components RT of the mammalian circadian clock."; RL Science 327:463-466(2010). RN [14] RP FUNCTION. RX PubMed=21262816; DOI=10.1073/pnas.1013170108; RA Li S., Esterberg R., Lachance V., Ren D., Radde-Gallwitz K., Chi F., RA Parent J.L., Fritz A., Chen P.; RT "Rack1 is required for Vangl2 membrane localization and planar cell RT polarity signaling while attenuating canonical Wnt activity."; RL Proc. Natl. Acad. Sci. U.S.A. 108:2264-2269(2011). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-130 AND LYS-183, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [16] RP FUNCTION, AND INTERACTION WITH AIM2. RX PubMed=33505023; DOI=10.1038/s41586-021-03231-w; RA Chou W.C., Guo Z., Guo H., Chen L., Zhang G., Liang K., Xie L., Tan X., RA Gibson S.A., Rampanelli E., Wang Y., Montgomery S.A., Brickey W.J., RA Deng M., Freeman L., Zhang S., Su M.A., Chen X., Wan Y.Y., Ting J.P.; RT "AIM2 in regulatory T cells restrains autoimmune diseases."; RL Nature 591:300-305(2021). RN [17] {ECO:0007744|PDB:7CPU, ECO:0007744|PDB:7CPV} RP STRUCTURE BY ELECTRON MICROSCOPY OF RIBOSOME, FUNCTION, SUBUNIT, AND RP SUBCELLULAR LOCATION. RX PubMed=36517592; DOI=10.1038/s41586-022-05508-0; RA Li H., Huo Y., He X., Yao L., Zhang H., Cui Y., Xiao H., Xie W., Zhang D., RA Wang Y., Zhang S., Tu H., Cheng Y., Guo Y., Cao X., Zhu Y., Jiang T., RA Guo X., Qin Y., Sha J.; RT "A male germ-cell-specific ribosome controls male fertility."; RL Nature 0:0-0(2022). CC -!- FUNCTION: Scaffolding protein involved in the recruitment, assembly CC and/or regulation of a variety of signaling molecules (PubMed:18258429, CC PubMed:20093473, PubMed:21262816, PubMed:33505023, PubMed:36517592, CC PubMed:7968370). Interacts with a wide variety of proteins and plays a CC role in many cellular processes (PubMed:18258429, PubMed:20093473, CC PubMed:21262816, PubMed:36517592, PubMed:7968370). Component of the 40S CC ribosomal subunit involved in translational repression CC (PubMed:36517592). Involved in the initiation of the ribosome quality CC control (RQC), a pathway that takes place when a ribosome has stalled CC during translation, by promoting ubiquitination of a subset of 40S CC ribosomal subunits (By similarity). Binds to and stabilizes activated CC protein kinase C (PKC), increasing PKC-mediated phosphorylation (By CC similarity). May recruit activated PKC to the ribosome, leading to CC phosphorylation of EIF6 (By similarity). Inhibits the activity of SRC CC kinases including SRC, LCK and YES1 (By similarity). Inhibits cell CC growth by prolonging the G0/G1 phase of the cell cycle (By similarity). CC Enhances phosphorylation of BMAL1 by PRKCA and inhibits transcriptional CC activity of the BMAL1-CLOCK heterodimer (PubMed:20093473). Facilitates CC ligand-independent nuclear translocation of AR following PKC CC activation, represses AR transactivation activity and is required for CC phosphorylation of AR by SRC (By similarity). Modulates IGF1R-dependent CC integrin signaling and promotes cell spreading and contact with the CC extracellular matrix (By similarity). Involved in PKC-dependent CC translocation of ADAM12 to the cell membrane (By similarity). Promotes CC the ubiquitination and proteasome-mediated degradation of proteins such CC as CLEC1B and HIF1A (By similarity). Required for VANGL2 membrane CC localization, inhibits Wnt signaling, and regulates cellular CC polarization and oriented cell division during gastrulation CC (PubMed:21262816). Required for PTK2/FAK1 phosphorylation and CC dephosphorylation (By similarity). Regulates internalization of the CC muscarinic receptor CHRM2 (By similarity). Promotes apoptosis by CC increasing oligomerization of BAX and disrupting the interaction of BAX CC with the anti-apoptotic factor BCL2L (By similarity). Inhibits TRPM6 CC channel activity (PubMed:18258429). Regulates cell surface expression CC of some GPCRs such as TBXA2R (By similarity). Plays a role in CC regulation of FLT1-mediated cell migration (By similarity). Involved in CC the transport of ABCB4 from the Golgi to the apical bile canalicular CC membrane (By similarity). Acts as an adapter for the dephosphorylation CC and inactivation of AKT1 by promoting recruitment of PP2A phosphatase CC to AKT1 (PubMed:33505023). {ECO:0000250|UniProtKB:P63244, CC ECO:0000269|PubMed:18258429, ECO:0000269|PubMed:20093473, CC ECO:0000269|PubMed:21262816, ECO:0000269|PubMed:33505023, CC ECO:0000269|PubMed:36517592, ECO:0000269|PubMed:7968370}. CC -!- SUBUNIT: Monomer; also forms homodimers and homooligomers (By CC similarity). Interacts with CPNE3 (By similarity). May interact with CC ABCB4 (By similarity). Component of the small (40S) ribosomal subunit CC (PubMed:36517592). Interacts with LARP4B. Interacts with LARP4. CC Interacts with PKD2L1 (By similarity). Binds NHERF1 (By similarity). CC Forms a ternary complex with TRIM63 and PRKCE (By similarity). CC Interacts with HABP4, KRT1 and OTUB1 (By similarity). Interacts with CC SRC (via SH2 domain); the interaction is enhanced by tyrosine CC phosphorylation of RACK1 (By similarity). Recruited in a circadian CC manner into a nuclear complex which also includes BMAL1 and PRKCA CC (PubMed:20093473). Interacts with AR (By similarity). Interacts with CC IGF1R but not with INSR (By similarity). Interacts with ADAM12 (By CC similarity). Interacts with CLEC1B (via N-terminal region) and with CC HIF1A; the interaction promotes their degradation (By similarity). CC Interacts with RHOA; this enhances RHOA activation and promotes cell CC migration (By similarity). Interacts with CHRM2; the interaction CC regulates CHRM2 internalization (By similarity). Interacts with TRPM6 CC (via kinase domain) (PubMed:18258429). Interacts with PTK2/FAK1; CC required for PTK2/FAK1 phosphorylation and dephosphorylation (By CC similarity). Interacts with FLT1 (By similarity). Interacts with HRAS CC (By similarity). Interacts with SLC9A5; this interaction regulates CC SLC9A5 cell-surface targeting and SLC9A5 activity (By similarity). CC Interacts with SLC9A6; this interaction regulates the distribution of CC SLC9A6 between endosomes and the plasma membrane (By similarity). CC Interacts with AIM2; promoting association with PP2A phosphatase and CC dephosphorylation of AKT1 (PubMed:33505023). Interacts with LACC1; this CC interaction may regulate macrophage autophagic flux. CC {ECO:0000250|UniProtKB:P63244, ECO:0000269|PubMed:18258429, CC ECO:0000269|PubMed:20093473, ECO:0000269|PubMed:33505023, CC ECO:0000269|PubMed:36517592}. CC -!- INTERACTION: CC P68040; O88351: Ikbkb; NbExp=4; IntAct=EBI-296749, EBI-447960; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P63244}; CC Peripheral membrane protein {ECO:0000250|UniProtKB:P63244}. Cytoplasm CC {ECO:0000269|PubMed:20093473}. Cytoplasm, perinuclear region CC {ECO:0000250|UniProtKB:P63244}. Nucleus {ECO:0000269|PubMed:20093473}. CC Perikaryon {ECO:0000269|PubMed:16414032}. Cell projection, dendrite CC {ECO:0000269|PubMed:16414032}. Note=Recruited to the plasma membrane CC through interaction with KRT1 which binds to membrane-bound ITGB1. PKC CC activation induces translocation from the perinuclear region to the CC cell periphery (By similarity). In the brain, detected mainly in cell CC bodies and dendrites with little expression in axonal fibers or nuclei CC (PubMed:16414032). {ECO:0000250|UniProtKB:P63244, CC ECO:0000269|PubMed:16414032}. CC -!- TISSUE SPECIFICITY: Strongly and ubiquitously expressed in the CC embryonic and early postnatal brain. At 11.5 dpc, expressed in a high- CC dorsal to low-ventral gradient throughout the brain. At 13.5 dpc, most CC abundant in the telecephalon. At 18.5 dpc, expressed most abundantly in CC layers 1-4 of the cortex, striatum, hippocampus, dentate gyrus, and CC specific thalamic nuclei. This expression decreases during postnatal CC development and is localized in the dentate gyrus, habenula, piriform CC cortex, paraventricular nucleus of the hypothalamus and supraoptic CC nucleus of the adult brain. {ECO:0000269|PubMed:16414032, CC ECO:0000269|PubMed:7968370}. CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryonic brain development CC with high levels detected at 11.5 dpc, 13.5 dpc and 18.5 dpc. Also CC detected at high levels in the adult brain. CC {ECO:0000269|PubMed:16414032}. CC -!- DOMAIN: The 7 WD repeats mediate protein-protein interactions with CC binding partners. {ECO:0000250|UniProtKB:P63244}. CC -!- PTM: Phosphorylated on Tyr-228 and/or Tyr-246 by SRC. This is required CC for binding to SRC (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the WD repeat G protein beta family. Ribosomal CC protein RACK1 subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAG29506.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D29802; BAA06185.1; -; mRNA. DR EMBL; X75313; CAA53062.1; -; mRNA. DR EMBL; AK002493; BAB22141.1; -; mRNA. DR EMBL; AK012242; BAB28114.1; -; mRNA. DR EMBL; AK017772; BAB30920.1; -; mRNA. DR EMBL; AK051226; BAC34564.1; -; mRNA. DR EMBL; AK159797; BAE35378.1; -; mRNA. DR EMBL; AK160528; BAE35846.1; -; mRNA. DR EMBL; AK160739; BAE35980.1; -; mRNA. DR EMBL; AK161234; BAE36257.1; -; mRNA. DR EMBL; AK166417; BAE38762.1; -; mRNA. DR EMBL; AK166786; BAE39017.1; -; mRNA. DR EMBL; AK166800; BAE39028.1; -; mRNA. DR EMBL; AK166889; BAE39095.1; -; mRNA. DR EMBL; AK166945; BAE39133.1; -; mRNA. DR EMBL; AK168086; BAE40059.1; -; mRNA. DR EMBL; AK168096; BAE40068.1; -; mRNA. DR EMBL; AK168196; BAE40156.1; -; mRNA. DR EMBL; AK168349; BAE40286.1; -; mRNA. DR EMBL; AL645849; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH466575; EDL33791.1; -; Genomic_DNA. DR EMBL; BC046760; AAH46760.1; -; mRNA. DR EMBL; AF295529; AAG29506.1; ALT_FRAME; Genomic_DNA. DR CCDS; CCDS24585.1; -. DR PIR; S38398; S38398. DR RefSeq; NP_032169.1; NM_008143.3. DR PDB; 7CPU; EM; 2.82 A; Sg=1-317. DR PDB; 7CPV; EM; 3.03 A; Sg=1-317. DR PDB; 7LS1; EM; 3.30 A; I3=1-317. DR PDB; 7LS2; EM; 3.10 A; I3=1-317. DR PDB; 9H4N; EM; 2.46 A; I3=12-314. DR PDB; 9KDT; EM; 2.63 A; Sg=1-317. DR PDB; 9KDU; EM; 2.96 A; Sg=1-317. DR PDB; 9KDV; EM; 3.33 A; Sg=1-317. DR PDB; 9KDW; EM; 2.67 A; Sg=1-317. DR PDB; 9QOH; EM; 2.78 A; I3=1-317. DR PDB; 9QQL; EM; 3.09 A; I3=1-317. DR PDB; 9QQP; EM; 2.80 A; I3=1-317. DR PDB; 9QSA; EM; 3.40 A; I3=1-317. DR PDB; 9QWT; EM; 3.10 A; I3=1-317. DR PDB; 9QZP; EM; 3.43 A; I3=1-317. DR AlphaFoldDB; P68040; -. DR EMDB; EMD-23500; -. DR EMDB; EMD-23501; -. DR EMDB; EMD-30432; -. DR EMDB; EMD-30433; -. DR EMDB; EMD-51865; -. DR EMDB; EMD-53262; -. DR EMDB; EMD-53307; -. DR EMDB; EMD-53310; -. DR EMDB; EMD-53333; -. DR EMDB; EMD-53427; -. DR EMDB; EMD-53473; -. DR EMDB; EMD-62285; -. DR EMDB; EMD-62286; -. DR EMDB; EMD-62287; -. DR EMDB; EMD-62288; -. DR SMR; P68040; -. DR BioGRID; 199978; 109. DR CORUM; P68040; -. DR FunCoup; P68040; 2584. DR IntAct; P68040; 23. DR STRING; 10090.ENSMUSP00000020640; -. DR GlyCosmos; P68040; 1 site, 1 glycan. DR GlyGen; P68040; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P68040; -. DR PhosphoSitePlus; P68040; -. DR SwissPalm; P68040; -. DR REPRODUCTION-2DPAGE; P68040; -. DR jPOST; P68040; -. DR PaxDb; 10090-ENSMUSP00000020640; -. DR PeptideAtlas; P68040; -. DR ProteomicsDB; 300295; -. DR Pumba; P68040; -. DR TopDownProteomics; P68040; -. DR Antibodypedia; 3802; 530 antibodies from 48 providers. DR DNASU; 14694; -. DR Ensembl; ENSMUST00000020640.8; ENSMUSP00000020640.8; ENSMUSG00000020372.16. DR GeneID; 14694; -. DR KEGG; mmu:14694; -. DR UCSC; uc007ipa.1; mouse. DR AGR; MGI:101849; -. DR CTD; 10399; -. DR MGI; MGI:101849; Rack1. DR VEuPathDB; HostDB:ENSMUSG00000020372; -. DR eggNOG; KOG0279; Eukaryota. DR GeneTree; ENSGT00940000154461; -. DR HOGENOM; CLU_000288_57_7_1; -. DR InParanoid; P68040; -. DR OMA; AACGPTI; -. DR OrthoDB; 7875889at2759; -. DR PhylomeDB; P68040; -. DR Reactome; R-MMU-5357905; Regulation of TNFR1 signaling. DR Reactome; R-MMU-5357956; TNFR1-induced NF-kappa-B signaling pathway. DR Reactome; R-MMU-5626978; TNFR1-mediated ceramide production. DR Reactome; R-MMU-9766229; Degradation of CDH1. DR BioGRID-ORCS; 14694; 31 hits in 76 CRISPR screens. DR CD-CODE; 453FB656; Mast cell extracellular granules (MCEGs). DR PRO; PR:P68040; -. DR Proteomes; UP000000589; Chromosome 11. DR RNAct; P68040; protein. DR Bgee; ENSMUSG00000020372; Expressed in epiblast (generic) and 73 other cell types or tissues. DR GO; GO:0044297; C:cell body; IDA:ParkinsonsUK-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005829; C:cytosol; ISO:GO_Central. DR GO; GO:0030425; C:dendrite; IDA:UniProtKB. DR GO; GO:1990630; C:IRE1-RACK1-PP2A complex; ISO:GO_Central. DR GO; GO:0030496; C:midbody; ISS:UniProtKB. DR GO; GO:0005739; C:mitochondrion; ISO:GO_Central. DR GO; GO:0043005; C:neuron projection; IDA:ParkinsonsUK-UCL. DR GO; GO:0043025; C:neuronal cell body; IDA:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:GO_Central. DR GO; GO:0005634; C:nucleus; EXP:UniProtKB. DR GO; GO:0043204; C:perikaryon; EXP:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB. DR GO; GO:0001891; C:phagocytic cup; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0015935; C:small ribosomal subunit; IDA:UniProtKB. DR GO; GO:0051434; F:BH3 domain binding; ISO:GO_Central. DR GO; GO:0030332; F:cyclin binding; ISO:GO_Central. DR GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; ISO:GO_Central. DR GO; GO:0008047; F:enzyme activator activity; ISO:GO_Central. DR GO; GO:0019899; F:enzyme binding; ISO:GO_Central. DR GO; GO:0042802; F:identical protein binding; ISO:GO_Central. DR GO; GO:0008200; F:ion channel inhibitor activity; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; ISO:GO_Central. DR GO; GO:0005080; F:protein kinase C binding; ISS:UniProtKB. DR GO; GO:0019903; F:protein phosphatase binding; ISO:GO_Central. DR GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; ISO:GO_Central. DR GO; GO:0030292; F:protein tyrosine kinase inhibitor activity; ISS:UniProtKB. DR GO; GO:0030971; F:receptor tyrosine kinase binding; ISS:UniProtKB. DR GO; GO:0043022; F:ribosome binding; ISS:UniProtKB. DR GO; GO:0042169; F:SH2 domain binding; ISS:UniProtKB. DR GO; GO:0035591; F:signaling adaptor activity; ISO:GO_Central. DR GO; GO:0038023; F:signaling receptor activity; ISO:MGI. DR GO; GO:0045182; F:translation regulator activity; IEA:InterPro. DR GO; GO:0071333; P:cellular response to glucose stimulus; ISO:GO_Central. DR GO; GO:0071363; P:cellular response to growth factor stimulus; ISS:UniProtKB. DR GO; GO:0008104; P:intracellular protein localization; ISO:MGI. DR GO; GO:0035556; P:intracellular signal transduction; ISO:MGI. DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB. DR GO; GO:0010629; P:negative regulation of gene expression; ISO:GO_Central. DR GO; GO:1903751; P:negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide; IGI:ParkinsonsUK-UCL. DR GO; GO:0050765; P:negative regulation of phagocytosis; ISS:UniProtKB. DR GO; GO:0051898; P:negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISO:GO_Central. DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; ISO:GO_Central. DR GO; GO:0017148; P:negative regulation of translation; ISO:GO_Central. DR GO; GO:2001125; P:negative regulation of translational frameshifting; IBA:GO_Central. DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISS:UniProtKB. DR GO; GO:0043473; P:pigmentation; IMP:MGI. DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB. DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB. DR GO; GO:2000543; P:positive regulation of gastrulation; ISS:UniProtKB. DR GO; GO:0042998; P:positive regulation of Golgi to plasma membrane protein transport; ISS:UniProtKB. DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB. DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISO:GO_Central. DR GO; GO:0051901; P:positive regulation of mitochondrial depolarization; ISO:GO_Central. DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB. DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISS:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB. DR GO; GO:0106070; P:regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:GO_Central. DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB. DR GO; GO:0051302; P:regulation of cell division; ISS:UniProtKB. DR GO; GO:2000114; P:regulation of establishment of cell polarity; ISS:UniProtKB. DR GO; GO:0032880; P:regulation of protein localization; ISS:UniProtKB. DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; ISO:GO_Central. DR GO; GO:0072344; P:rescue of stalled cytosolic ribosome; ISS:UniProtKB. DR GO; GO:0006412; P:translation; IMP:MGI. DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISO:MGI. DR CDD; cd00200; WD40; 1. DR FunFam; 2.130.10.10:FF:001252; Receptor of activated protein C kinase 1; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR InterPro; IPR045223; RACK1-like. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR020472; WD40_PAC1. DR InterPro; IPR019775; WD40_repeat_CS. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR19868; RECEPTOR FOR ACTIVATED PROTEIN KINASE C RACK1; 1. DR Pfam; PF00400; WD40; 7. DR PRINTS; PR00320; GPROTEINBRPT. DR SMART; SM00320; WD40; 7. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS00678; WD_REPEATS_1; 4. DR PROSITE; PS50082; WD_REPEATS_2; 6. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Apoptosis; Biological rhythms; Cell cycle; KW Cell membrane; Cell projection; Cytoplasm; Developmental protein; KW Direct protein sequencing; Gastrulation; Growth regulation; Membrane; KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; KW Ribosomal protein; Translation regulation; WD repeat. FT CHAIN 1..317 FT /note="Small ribosomal subunit protein RACK1" FT /id="PRO_0000424482" FT INIT_MET 1 FT /note="Removed; alternate" FT /evidence="ECO:0000269|Ref.8" FT CHAIN 2..317 FT /note="Small ribosomal subunit protein RACK1, N-terminally FT processed" FT /id="PRO_0000127732" FT REPEAT 13..44 FT /note="WD 1" FT REPEAT 61..91 FT /note="WD 2" FT REPEAT 103..133 FT /note="WD 3" FT REPEAT 146..178 FT /note="WD 4" FT REPEAT 190..220 FT /note="WD 5" FT REPEAT 231..260 FT /note="WD 6" FT REPEAT 281..311 FT /note="WD 7" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:P63244" FT MOD_RES 2 FT /note="N-acetylthreonine; in Guanine nucleotide-binding FT protein subunit beta-2-like 1, N-terminally processed" FT /evidence="ECO:0000269|Ref.8" FT MOD_RES 6 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P63244" FT MOD_RES 10 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P63244" FT MOD_RES 52 FT /note="Phosphotyrosine; by ABL1" FT /evidence="ECO:0000250|UniProtKB:P63244" FT MOD_RES 96 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P63244" FT MOD_RES 130 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 183 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 228 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P63244" FT MOD_RES 276 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P63244" FT MOD_RES 277 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P63244" FT MOD_RES 278 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P63244" FT MOD_RES 279 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P63244" FT MOD_RES 316 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT CONFLICT 9 FT /note="G -> R (in Ref. 3; BAE40068/BAE40156)" FT /evidence="ECO:0000305" FT CONFLICT 125 FT /note="R -> Q (in Ref. 3; BAE40059/BAE40068/BAE40156)" FT /evidence="ECO:0000305" FT CONFLICT 248 FT /note="L -> P (in Ref. 3; BAE35378)" FT /evidence="ECO:0000305" FT CONFLICT 266 FT /note="I -> M (in Ref. 6; AAG29506)" FT /evidence="ECO:0000305" FT CONFLICT 273 FT /note="E -> A (in Ref. 1; BAA06185)" FT /evidence="ECO:0000305" FT STRAND 4..11 FT /evidence="ECO:0007829|PDB:9QOH" FT STRAND 18..23 FT /evidence="ECO:0007829|PDB:9H4N" FT STRAND 30..38 FT /evidence="ECO:0007829|PDB:9H4N" FT STRAND 41..48 FT /evidence="ECO:0007829|PDB:9H4N" FT STRAND 51..57 FT /evidence="ECO:0007829|PDB:9H4N" FT STRAND 62..64 FT /evidence="ECO:0007829|PDB:9QOH" FT STRAND 68..71 FT /evidence="ECO:0007829|PDB:9H4N" FT HELIX 73..75 FT /evidence="ECO:0007829|PDB:9H4N" FT STRAND 76..81 FT /evidence="ECO:0007829|PDB:9H4N" FT TURN 83..85 FT /evidence="ECO:0007829|PDB:7CPU" FT STRAND 87..93 FT /evidence="ECO:0007829|PDB:9H4N" FT STRAND 97..101 FT /evidence="ECO:0007829|PDB:9H4N" FT STRAND 108..112 FT /evidence="ECO:0007829|PDB:9QOH" FT STRAND 115..121 FT /evidence="ECO:0007829|PDB:9H4N" FT TURN 125..127 FT /evidence="ECO:0007829|PDB:9QOH" FT STRAND 128..133 FT /evidence="ECO:0007829|PDB:9QOH" FT STRAND 134..136 FT /evidence="ECO:0007829|PDB:9QQP" FT STRAND 138..142 FT /evidence="ECO:0007829|PDB:9QOH" FT STRAND 144..146 FT /evidence="ECO:0007829|PDB:7CPV" FT STRAND 151..156 FT /evidence="ECO:0007829|PDB:9QOH" FT STRAND 158..162 FT /evidence="ECO:0007829|PDB:9QQL" FT STRAND 164..169 FT /evidence="ECO:0007829|PDB:9QOH" FT TURN 170..172 FT /evidence="ECO:0007829|PDB:9QQP" FT STRAND 174..178 FT /evidence="ECO:0007829|PDB:9QOH" FT TURN 179..182 FT /evidence="ECO:0007829|PDB:9QOH" FT STRAND 183..188 FT /evidence="ECO:0007829|PDB:9QOH" FT STRAND 195..200 FT /evidence="ECO:0007829|PDB:9QOH" FT STRAND 202..213 FT /evidence="ECO:0007829|PDB:9QOH" FT STRAND 215..223 FT /evidence="ECO:0007829|PDB:9QOH" FT STRAND 226..231 FT /evidence="ECO:0007829|PDB:9QOH" FT STRAND 238..241 FT /evidence="ECO:0007829|PDB:9H4N" FT STRAND 243..245 FT /evidence="ECO:0007829|PDB:9H4N" FT STRAND 248..251 FT /evidence="ECO:0007829|PDB:9H4N" FT STRAND 252..254 FT /evidence="ECO:0007829|PDB:9QWT" FT STRAND 255..260 FT /evidence="ECO:0007829|PDB:9QOH" FT TURN 261..264 FT /evidence="ECO:0007829|PDB:9QOH" FT STRAND 265..271 FT /evidence="ECO:0007829|PDB:9QOH" FT STRAND 279..281 FT /evidence="ECO:0007829|PDB:7LS1" FT HELIX 282..285 FT /evidence="ECO:0007829|PDB:9QOH" FT STRAND 288..291 FT /evidence="ECO:0007829|PDB:9H4N" FT STRAND 293..295 FT /evidence="ECO:0007829|PDB:9H4N" FT STRAND 297..301 FT /evidence="ECO:0007829|PDB:9H4N" FT STRAND 303..305 FT /evidence="ECO:0007829|PDB:9H4N" FT STRAND 307..311 FT /evidence="ECO:0007829|PDB:9H4N" SQ SEQUENCE 317 AA; 35077 MW; 257F91E369ED2044 CRC64; MTEQMTLRGT LKGHNGWVTQ IATTPQFPDM ILSASRDKTI IMWKLTRDET NYGIPQRALR GHSHFVSDVV ISSDGQFALS GSWDGTLRLW DLTTGTTTRR FVGHTKDVLS VAFSSDNRQI VSGSRDKTIK LWNTLGVCKY TVQDESHSEW VSCVRFSPNS SNPIIVSCGW DKLVKVWNLA NCKLKTNHIG HTGYLNTVTV SPDGSLCASG GKDGQAMLWD LNEGKHLYTL DGGDIINALC FSPNRYWLCA ATGPSIKIWD LEGKIIVDEL KQEVISTSSK AEPPQCTSLA WSADGQTLFA GYTDNLVRVW QVTIGTR //