ID RACK1_HUMAN Reviewed; 317 AA. AC P63244; B3KTJ0; D3DWS0; P25388; P99049; Q53HU2; Q5J8M6; Q5VLR4; Q6FH47; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 28-JAN-2026, entry version 195. DE RecName: Full=Small ribosomal subunit protein RACK1 {ECO:0000303|PubMed:24524803}; DE AltName: Full=Cell proliferation-inducing gene 21 protein; DE AltName: Full=Guanine nucleotide-binding protein subunit beta-2-like 1; DE AltName: Full=Guanine nucleotide-binding protein subunit beta-like protein 12.3; DE AltName: Full=Human lung cancer oncogene 7 protein; DE Short=HLC-7; DE AltName: Full=Receptor for activated C kinase; DE AltName: Full=Receptor for activated C kinase 1 {ECO:0000303|PubMed:38157925}; DE AltName: Full=Receptor of activated protein C kinase 1; 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|HGNC:HGNC:4399}; Synonyms=GNB2L1; GN ORFNames=HLC7, PIG21; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2499885; DOI=10.1073/pnas.86.12.4594; RA Guillemot F., Billault A., Auffray C.; RT "Physical linkage of a guanine nucleotide-binding protein-related gene to RT the chicken major histocompatibility complex."; RL Proc. Natl. Acad. Sci. U.S.A. 86:4594-4598(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kim J.W.; RT "Identification of new tumor-related gene in human lung cancer."; RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kim J.W.; RT "Identification of a proliferation-inducing gene."; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Adipose tissue; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=B-cell, Brain, Cervix, Lung, Lymph, Ovary, and Skin; 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 [9] RP PROTEIN SEQUENCE OF 2-11; 48-57; 107-118; 258-280 AND 309-317, CLEAVAGE OF RP INITIATOR METHIONINE, ACETYLATION AT THR-2, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=B-cell lymphoma, and T-cell; RA Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.; RL Submitted (MAY-2006) to UniProtKB. RN [10] RP PROTEIN SEQUENCE OF 48-57; 107-118; 140-155 AND 226-245, AND IDENTIFICATION RP BY MASS SPECTROMETRY. RC TISSUE=Brain, and Cajal-Retzius cell; RA Lubec G., Afjehi-Sadat L.; RL Submitted (MAR-2007) to UniProtKB. RN [11] RP FUNCTION, AND INTERACTION WITH SRC. RX PubMed=9584165; DOI=10.1128/mcb.18.6.3245; RA Chang B.Y., Conroy K.B., Machleder E.M., Cartwright C.A.; RT "RACK1, a receptor for activated C kinase and a homolog of the beta subunit RT of G proteins, inhibits activity of src tyrosine kinases and growth of NIH RT 3T3 cells."; RL Mol. Cell. Biol. 18:3245-3256(1998). RN [12] RP INTERACTION WITH EPSTEIN-BARR VIRUS BZLF1 (MICROBIAL INFECTION), AND RP SUBCELLULAR LOCATION. RX PubMed=10849009; DOI=10.1046/j.1432-1327.2000.01430.x; RA Baumann M., Gires O., Kolch W., Mischak H., Zeidler R., Pich D., RA Hammerschmidt W.; RT "The PKC targeting protein RACK1 interacts with the Epstein-Barr virus RT activator protein BZLF1."; RL Eur. J. Biochem. 267:3891-3901(2000). RN [13] RP INTERACTION WITH SRC, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-228, AND RP MUTAGENESIS OF TYR-52; TYR-140; TYR-194; TYR-228; TYR-246 AND TYR-302. RX PubMed=11279199; DOI=10.1074/jbc.m101375200; RA Chang B.Y., Chiang M., Cartwright C.A.; RT "The interaction of Src and RACK1 is enhanced by activation of protein RT kinase C and tyrosine phosphorylation of RACK1."; RL J. Biol. Chem. 276:20346-20356(2001). RN [14] RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH HIV-1 NEF (MICROBIAL RP INFECTION), AND SUBCELLULAR LOCATION. RX PubMed=11312657; DOI=10.1006/viro.2001.0855; RA Gallina A., Rossi F., Milanesi G.; RT "Rack1 binds HIV-1 Nef and can act as a Nef-protein kinase C adaptor."; RL Virology 283:7-18(2001). RN [15] RP INTERACTION WITH NHERF1. RX PubMed=11956211; DOI=10.1074/jbc.m201917200; RA Liedtke C.M., Yun C.H.C., Kyle N., Wang D.; RT "Protein kinase C epsilon-dependent regulation of cystic fibrosis RT transmembrane regulator involves binding to a receptor for activated C RT kinase (RACK1) and RACK1 binding to Na+/H+ exchange regulatory factor."; RL J. Biol. Chem. 277:22925-22933(2002). RN [16] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH IGF1R. RX PubMed=11884618; DOI=10.1128/mcb.22.7.2345-2365.2002; RA Hermanto U., Zong C.S., Li W., Wang L.H.; RT "RACK1, an insulin-like growth factor I (IGF-I) receptor-interacting RT protein, modulates IGF-I-dependent integrin signaling and promotes cell RT spreading and contact with extracellular matrix."; RL Mol. Cell. Biol. 22:2345-2365(2002). RN [17] RP PHOSPHORYLATION, AND MUTAGENESIS OF TYR-52; TYR-140; TYR-194; TYR-228; RP TYR-246 AND TYR-302. RX PubMed=12400005; DOI=10.1038/sj.onc.1206002; RA Chang B.Y., Harte R.A., Cartwright C.A.; RT "RACK1: a novel substrate for the Src protein-tyrosine kinase."; RL Oncogene 21:7619-7629(2002). RN [18] RP INTERACTION WITH HRAS. RX PubMed=14500341; RA Guil S., de La Iglesia N., Fernandez-Larrea J., Cifuentes D., Ferrer J.C., RA Guinovart J.J., Bach-Elias M.; RT "Alternative splicing of the human proto-oncogene c-H-ras renders a new Ras RT family protein that trafficks to cytoplasm and nucleus."; RL Cancer Res. 63:5178-5187(2003). RN [19] RP FUNCTION, INTERACTION WITH AR, AND SUBCELLULAR LOCATION. RX PubMed=12958311; DOI=10.1074/jbc.m306219200; RA Rigas A.C., Ozanne D.M., Neal D.E., Robson C.N.; RT "The scaffolding protein RACK1 interacts with androgen receptor and RT promotes cross-talk through a protein kinase C signaling pathway."; RL J. Biol. Chem. 278:46087-46093(2003). RN [20] RP FUNCTION. RX PubMed=12589061; DOI=10.1091/mbc.e02-03-0142; RA Cox E.A., Bennin D., Doan A.T., O'Toole T., Huttenlocher A.; RT "RACK1 regulates integrin-mediated adhesion, protrusion, and chemotactic RT cell migration via its Src-binding site."; RL Mol. Biol. Cell 14:658-669(2003). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [22] RP SUBUNIT, AND DOMAIN. RX PubMed=15140893; DOI=10.1074/jbc.m402316200; RA Thornton C., Tang K.C., Phamluong K., Luong K., Vagts A., Nikanjam D., RA Yaka R., Ron D.; RT "Spatial and temporal regulation of RACK1 function and N-methyl-D-aspartate RT receptor activity through WD40 motif-mediated dimerization."; RL J. Biol. Chem. 279:31357-31364(2004). RN [23] RP INTERACTION WITH TRIM63 AND PRKCE. RX PubMed=15596539; DOI=10.1083/jcb.200402033; RA Arya R., Kedar V., Hwang J.R., McDonough H., Li H.-H., Taylor J., RA Patterson C.; RT "Muscle ring finger protein-1 inhibits PKC-epsilon activation and prevents RT cardiomyocyte hypertrophy."; RL J. Cell Biol. 167:1147-1159(2004). RN [24] RP INTERACTION WITH HABP4. RX PubMed=14699138; DOI=10.1074/jbc.m306672200; RA Nery F.C., Passos D.O., Garcia V.S., Kobarg J.; RT "Ki-1/57 interacts with RACK1 and is a substrate for the phosphorylation by RT phorbol 12-myristate 13-acetate-activated protein kinase C."; RL J. Biol. Chem. 279:11444-11455(2004). RN [25] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [26] RP FUNCTION, AND INTERACTION WITH AR. RX PubMed=17108144; DOI=10.1158/0008-5472.can-06-0596; RA Kraus S., Gioeli D., Vomastek T., Gordon V., Weber M.J.; RT "Receptor for activated C kinase 1 (RACK1) and Src regulate the tyrosine RT phosphorylation and function of the androgen receptor."; RL Cancer Res. 66:11047-11054(2006). RN [27] RP FUNCTION, INTERACTION WITH KRT1, AND SUBCELLULAR LOCATION. RX PubMed=17956333; DOI=10.1042/bst0351292; RA Chuang N.N., Huang C.C.; RT "Interaction of integrin beta1 with cytokeratin 1 in neuroblastoma NMB7 RT cells."; RL Biochem. Soc. Trans. 35:1292-1294(2007). RN [28] RP FUNCTION, INTERACTION WITH HIF1A, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=17244529; DOI=10.1016/j.molcel.2007.01.001; RA Liu Y.V., Baek J.H., Zhang H., Diez R., Cole R.N., Semenza G.L.; RT "RACK1 competes with HSP90 for binding to HIF-1alpha and is required for RT O(2)-independent and HSP90 inhibitor-induced degradation of HIF-1alpha."; RL Mol. Cell 25:207-217(2007). RN [29] 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 [30] RP FUNCTION, INTERACTION WITH ADAM12, AND TISSUE SPECIFICITY. RX PubMed=18621736; DOI=10.1074/jbc.m709829200; RA Bourd-Boittin K., Le Pabic H., Bonnier D., L'Helgoualc'h A., Theret N.; RT "RACK1, a new ADAM12 interacting protein. Contribution to liver RT fibrogenesis."; RL J. Biol. Chem. 283:26000-26009(2008). RN [31] RP INTERACTION WITH SLC9A6. RX PubMed=18057008; DOI=10.1074/jbc.m705146200; RA Ohgaki R., Fukura N., Matsushita M., Mitsui K., Kanazawa H.; RT "Cell surface levels of organellar Na+/H+ exchanger isoform 6 are regulated RT by interaction with RACK1."; RL J. Biol. Chem. 283:4417-4429(2008). RN [32] RP FUNCTION, AND INTERACTION WITH TBXA2R. RX PubMed=18088317; DOI=10.1111/j.1600-0854.2007.00692.x; RA Parent A., Laroche G., Hamelin E., Parent J.L.; RT "RACK1 regulates the cell surface expression of the G protein-coupled RT receptor for thromboxane A(2)."; RL Traffic 9:394-407(2008). RN [33] RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [34] RP FUNCTION, INTERACTION WITH CLEC1B, AND SUBCELLULAR LOCATION. RX PubMed=19785988; DOI=10.1016/j.bbrc.2009.09.087; RA Ruan Y., Guo L., Qiao Y., Hong Y., Zhou L., Sun L., Wang L., Zhu H., RA Wang L., Yun X., Xie J., Gu J.; RT "RACK1 associates with CLEC-2 and promotes its ubiquitin-proteasome RT degradation."; RL Biochem. Biophys. Res. Commun. 390:217-222(2009). RN [35] RP INTERACTION WITH OTUB1. RX PubMed=18954305; DOI=10.1042/bj20081318; RA Edelmann M.J., Iphoefer A., Akutsu M., Altun M., di Gleria K., Kramer H.B., RA Fiebiger E., Dhe-Paganon S., Kessler B.M.; RT "Structural basis and specificity of human otubain 1-mediated RT deubiquitination."; RL Biochem. J. 418:379-390(2009). RN [36] RP FUNCTION, AND INTERACTION WITH ABCB4. RX PubMed=19674157; DOI=10.1111/j.1872-034x.2009.00544.x; RA Ikebuchi Y., Takada T., Ito K., Yoshikado T., Anzai N., Kanai Y., RA Suzuki H.; RT "Receptor for activated C-kinase 1 regulates the cellular localization and RT function of ABCB4."; RL Hepatol. Res. 39:1091-1107(2009). RN [37] RP FUNCTION, INTERACTION WITH PTK2/FAK1, PHOSPHORYLATION AT TYR-52, AND RP MUTAGENESIS OF TYR-52; ARG-57; ARG-60; LYS-127 AND LYS-130. RX PubMed=19423701; DOI=10.1074/jbc.m109.017640; RA Kiely P.A., Baillie G.S., Barrett R., Buckley D.A., Adams D.R., RA Houslay M.D., O'Connor R.; RT "Phosphorylation of RACK1 on tyrosine 52 by c-Abl is required for insulin- RT like growth factor I-mediated regulation of focal adhesion kinase."; RL J. Biol. Chem. 284:20263-20274(2009). RN [38] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-130, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [39] RP FUNCTION, AND INTERACTION WITH BAX. RX PubMed=20541605; DOI=10.1016/j.cellsig.2010.05.018; RA Wu Y., Wang Y., Sun Y., Zhang L., Wang D., Ren F., Chang D., Chang Z., RA Jia B.; RT "RACK1 promotes Bax oligomerization and dissociates the interaction of Bax RT and Bcl-XL."; RL Cell. Signal. 22:1495-1501(2010). RN [40] RP INTERACTION WITH CPNE3. RX PubMed=20010870; DOI=10.1038/onc.2009.456; RA Heinrich C., Keller C., Boulay A., Vecchi M., Bianchi M., Sack R., RA Lienhard S., Duss S., Hofsteenge J., Hynes N.E.; RT "Copine-III interacts with ErbB2 and promotes tumor cell migration."; RL Oncogene 29:1598-1610(2010). RN [41] RP FUNCTION, INTERACTION WITH CHRM2, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=20976005; DOI=10.1371/journal.pone.0013517; RA Reiner C.L., McCullar J.S., Kow R.L., Le J.H., Goodlett D.R., RA Nathanson N.M.; RT "RACK1 associates with muscarinic receptors and regulates M(2) receptor RT trafficking."; RL PLoS ONE 5:E13517-E13517(2010). RN [42] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PABPC1 AND RACK1. RX PubMed=20573744; DOI=10.1261/rna.2146910; RA Schaffler K., Schulz K., Hirmer A., Wiesner J., Grimm M., Sickmann A., RA Fischer U.; RT "A stimulatory role for the La-related protein 4B in translation."; RL RNA 16:1488-1499(2010). RN [43] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [44] RP FUNCTION, INTERACTION WITH RHOA, AND SUBCELLULAR LOCATION. RX PubMed=20499158; DOI=10.1007/s10549-010-0955-3; RA Cao X.X., Xu J.D., Xu J.W., Liu X.L., Cheng Y.Y., Li Q.Q., Xu Z.D., RA Liu X.P.; RT "RACK1 promotes breast carcinoma migration/metastasis via activation of the RT RhoA/Rho kinase pathway."; RL Breast Cancer Res. Treat. 126:555-563(2011). RN [45] RP FUNCTION, AND INTERACTION WITH FLT1. RX PubMed=21212275; DOI=10.1074/jbc.m110.165605; RA Wang F., Yamauchi M., Muramatsu M., Osawa T., Tsuchida R., Shibuya M.; RT "RACK1 regulates VEGF/Flt1-mediated cell migration via activation of a PI3- RT K/Akt pathway."; RL J. Biol. Chem. 286:9097-9106(2011). RN [46] RP INTERACTION WITH LARP4. RX PubMed=21098120; DOI=10.1128/mcb.01162-10; RA Yang R., Gaidamakov S.A., Xie J., Lee J., Martino L., Kozlov G., RA Crawford A.K., Russo A.N., Conte M.R., Gehring K., Maraia R.J.; RT "La-related protein 4 binds poly(A), interacts with the poly(A)-binding RT protein MLLE domain via a variant PAM2w motif, and can promote mRNA RT stability."; RL Mol. Cell. Biol. 31:542-556(2011). RN [47] RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH YERSINIA RP PSEUDOTUBERCULOSIS YOPK, AND SUBCELLULAR LOCATION. RX PubMed=21347310; DOI=10.1371/journal.pone.0016784; RA Thorslund S.E., Edgren T., Pettersson J., Nordfelth R., Sellin M.E., RA Ivanova E., Francis M.S., Isaksson E.L., Wolf-Watz H., Fallman M.; RT "The RACK1 signaling scaffold protein selectively interacts with Yersinia RT pseudotuberculosis virulence function."; RL PLoS ONE 6:E16784-E16784(2011). RN [48] RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [49] RP INTERACTION WITH PKD2L1. RX PubMed=22174419; DOI=10.1074/jbc.m111.305854; RA Yang J., Wang Q., Zheng W., Tuli J., Li Q., Wu Y., Hussein S., Dai X.Q., RA Shafiei S., Li X.G., Shen P.Y., Tu J.C., Chen X.Z.; RT "Receptor for activated C kinase 1 (RACK1) inhibits function of transient RT receptor potential (TRP)-type channel Pkd2L1 through physical RT interaction."; RL J. Biol. Chem. 287:6551-6561(2012). RN [50] RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [51] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, CLEAVAGE OF RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [52] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6; THR-10; THR-96 AND RP SER-276, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [53] RP INTERACTION WITH SLC9A5. RX PubMed=24006492; DOI=10.1091/mbc.e12-06-0445; RA Diering G.H., Numata Y., Fan S., Church J., Numata M.; RT "Endosomal acidification by Na+/H+ exchanger NHE5 regulates TrkA cell- RT surface targeting and NGF-induced PI3K signaling."; RL Mol. Biol. Cell 24:3435-3448(2013). RN [54] RP NOMENCLATURE. RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002; RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R., RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A., RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V., RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J., RA Williamson J.R., Wilson D., Yonath A., Yusupov M.; RT "A new system for naming ribosomal proteins."; RL Curr. Opin. Struct. Biol. 24:165-169(2014). RN [55] RP FUNCTION (MICROBIAL INFECTION). RX PubMed=25416947; DOI=10.1016/j.cell.2014.10.041; RA Majzoub K., Hafirassou M.L., Meignin C., Goto A., Marzi S., Fedorova A., RA Verdier Y., Vinh J., Hoffmann J.A., Martin F., Baumert T.F., Schuster C., RA Imler J.L.; RT "RACK1 controls IRES-mediated translation of viruses."; RL Cell 159:1086-1095(2014). RN [56] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [57] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [58] RP FUNCTION, AND MUTAGENESIS OF 36-ARG--GLU-38. RX PubMed=28132843; DOI=10.1016/j.molcel.2016.12.026; RA Sundaramoorthy E., Leonard M., Mak R., Liao J., Fulzele A., Bennett E.J.; RT "ZNF598 and RACK1 regulate mammalian ribosome-associated quality control RT function by mediating regulatory 40S ribosomal ubiquitylation."; RL Mol. Cell 65:751-760(2017). RN [59] RP REVIEW. RX PubMed=28161490; DOI=10.1016/j.cellsig.2017.01.026; RA Nielsen M.H., Flygaard R.K., Jenner L.B.; RT "Structural analysis of ribosomal RACK1 and its role in translational RT control."; RL Cell. Signal. 35:272-281(2017). RN [60] RP FUNCTION (MICROBIAL INFECTION), PHOSPHORYLATION AT SER-276; THR-277; RP SER-278 AND SER-279 (MICROBIAL INFECTION), AND MUTAGENESIS OF RP 276-SER--SER-279 AND SER-278. RX PubMed=28636603; DOI=10.1038/nature22814; RA Jha S., Rollins M.G., Fuchs G., Procter D.J., Hall E.A., Cozzolino K., RA Sarnow P., Savas J.N., Walsh D.; RT "Trans-kingdom mimicry underlies ribosome customization by a poxvirus RT kinase."; RL Nature 546:651-655(2017). RN [61] RP SUBCELLULAR LOCATION, AND INTERACTION WITH SLC4A7. RX PubMed=29743600; DOI=10.1038/s41598-018-25059-7; RA Olesen C.W., Vogensen J., Axholm I., Severin M., Schnipper J., RA Pedersen I.S., von Stemann J.H., Schroeder J.M., Christensen D.P., RA Pedersen S.F.; RT "Trafficking, localization and degradation of the Na+,HCO3- co-transporter RT NBCn1 in kidney and breast epithelial cells."; RL Sci. Rep. 8:7435-7435(2018). RN [62] RP INTERACTION WITH LACC1. RX PubMed=33606008; DOI=10.1084/jem.20201006; RA Omarjee O., Mathieu A.L., Quiniou G., Moreews M., Ainouze M., Frachette C., RA Melki I., Dumaine C., Gerfaud-Valentin M., Duquesne A., Kallinich T., RA Tahir Turanli E., Malcus C., Viel S., Pescarmona R., Georgin-Lavialle S., RA Jamilloux Y., Larbre J.P., Sarrabay G., Magnotti F., Rice G.I., RA Bleicher F., Reboulet J., Merabet S., Henry T., Crow Y.J., Faure M., RA Walzer T., Belot A.; RT "LACC1 deficiency links juvenile arthritis with autophagy and metabolism in RT macrophages."; RL J. Exp. Med. 218:0-0(2021). RN [63] RP INTERACTION WITH HUMAN RESPIRATORY SYNCYTIAL VIRUS MATRIX PROTEIN M RP (MICROBIAL INFECTION), AND SUBCELLULAR LOCATION. RX PubMed=37712706; DOI=10.1128/jvi.00747-23; RA Cao J., Shi M., Zhu L., Li X., Li A., Wu S.Y., Chiang C.M., Zhang Y.; RT "The matrix protein of respiratory syncytial virus suppresses interferon RT signaling via RACK1 association."; RL J. Virol. 0:0-0(2023). RN [64] RP INTERACTION WITH INFLUENZA PROTEIN PA-X (MICROBIAL INFECTION). RX PubMed=37758692; DOI=10.1038/s41467-023-41442-z; RA Haas K.M., McGregor M.J., Bouhaddou M., Polacco B.J., Kim E.Y., RA Nguyen T.T., Newton B.W., Urbanowski M., Kim H., Williams M.A.P., RA Rezelj V.V., Hardy A., Fossati A., Stevenson E.J., Sukerman E., Kim T., RA Penugonda S., Moreno E., Braberg H., Zhou Y., Metreveli G., Harjai B., RA Tummino T.A., Melnyk J.E., Soucheray M., Batra J., Pache L., RA Martin-Sancho L., Carlson-Stevermer J., Jureka A.S., Basler C.F., RA Shokat K.M., Shoichet B.K., Shriver L.P., Johnson J.R., Shaw M.L., RA Chanda S.K., Roden D.M., Carter T.C., Kottyan L.C., Chisholm R.L., RA Pacheco J.A., Smith M.E., Schrodi S.J., Albrecht R.A., Vignuzzi M., RA Zuliani-Alvarez L., Swaney D.L., Eckhardt M., Wolinsky S.M., White K.M., RA Hultquist J.F., Kaake R.M., Garcia-Sastre A., Krogan N.J.; RT "Proteomic and genetic analyses of influenza A viruses identify pan-viral RT host targets."; RL Nat. Commun. 14:6030-6030(2023). RN [65] RP INTERACTION WITH TOXOPLASMA GONDII SAG1 (MICROBIAL INFECTION). RX PubMed=38157925; DOI=10.1016/j.actatropica.2023.107112; RA Wang D., Liu Y., Yang B., Zhang Z., El-Ashram S., Liu X., Li B.; RT "Toxoplasma gondii surface antigen 1 (SAG1) interacts in vitro with host RT cell receptor for activated C kinase 1 (RACK1)."; RL Acta Trop. 251:107112-107112(2024). RN [66] RP X-RAY SCATTERING SOLUTION STRUCTURE, AND INTERACTION WITH HABP4. RX PubMed=20529362; DOI=10.1186/1472-6807-10-15; RA Goncalves K.A., Borges J.C., Silva J.C., Papa P.F., Bressan G.C., RA Torriani I.L., Kobarg J.; RT "Solution structure of the human signaling protein RACK1."; RL BMC Struct. Biol. 10:15-15(2010). RN [67] RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS). RX PubMed=22869111; DOI=10.1107/s1744309112027480; RA Ruiz Carrillo D., Chandrasekaran R., Nilsson M., Cornvik T., Liew C.W., RA Tan S.M., Lescar J.; RT "Structure of human Rack1 protein at a resolution of 2.45 A."; RL Acta Crystallogr. F 68:867-872(2012). RN [68] RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) IN COMPLEX WITH THE 80S RP RIBOSOME, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=23636399; DOI=10.1038/nature12104; RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M., RA Wilson D.N., Beckmann R.; RT "Structures of the human and Drosophila 80S ribosome."; RL Nature 497:80-85(2013). CC -!- FUNCTION: Scaffolding protein involved in the recruitment, assembly CC and/or regulation of a variety of signaling molecules. Interacts with a CC wide variety of proteins and plays a role in many cellular processes. CC Component of the 40S ribosomal subunit involved in translational CC repression (PubMed:23636399). Involved in the initiation of the CC ribosome quality control (RQC), a pathway that takes place when a CC ribosome has stalled during translation, by promoting ubiquitination of CC a subset of 40S ribosomal subunits (PubMed:28132843). Binds to and CC stabilizes activated protein kinase C (PKC), increasing PKC-mediated CC phosphorylation. May recruit activated PKC to the ribosome, leading to CC phosphorylation of EIF6. Inhibits the activity of SRC kinases including CC SRC, LCK and YES1. Inhibits cell growth by prolonging the G0/G1 phase CC of the cell cycle. Enhances phosphorylation of BMAL1 by PRKCA and CC inhibits transcriptional activity of the BMAL1-CLOCK heterodimer. CC Facilitates ligand-independent nuclear translocation of AR following CC PKC activation, represses AR transactivation activity and is required CC for phosphorylation of AR by SRC. Modulates IGF1R-dependent integrin CC signaling and promotes cell spreading and contact with the CC extracellular matrix. Involved in PKC-dependent translocation of ADAM12 CC to the cell membrane. Promotes the ubiquitination and proteasome- CC mediated degradation of proteins such as CLEC1B and HIF1A. Required for CC VANGL2 membrane localization, inhibits Wnt signaling, and regulates CC cellular polarization and oriented cell division during gastrulation. CC Required for PTK2/FAK1 phosphorylation and dephosphorylation. Regulates CC internalization of the muscarinic receptor CHRM2. Promotes apoptosis by CC increasing oligomerization of BAX and disrupting the interaction of BAX CC with the anti-apoptotic factor BCL2L. Inhibits TRPM6 channel activity. CC Regulates cell surface expression of some GPCRs such as TBXA2R. Plays a CC role in regulation of FLT1-mediated cell migration. Involved in the CC transport of ABCB4 from the Golgi to the apical bile canalicular CC membrane (PubMed:19674157). Promotes migration of breast carcinoma CC cells by binding to and activating RHOA (PubMed:20499158). Acts as an CC adapter for the dephosphorylation and inactivation of AKT1 by promoting CC recruitment of PP2A phosphatase to AKT1 (By similarity). CC {ECO:0000250|UniProtKB:P68040, ECO:0000269|PubMed:11884618, CC ECO:0000269|PubMed:12589061, ECO:0000269|PubMed:12958311, CC ECO:0000269|PubMed:17108144, ECO:0000269|PubMed:17244529, CC ECO:0000269|PubMed:17956333, ECO:0000269|PubMed:18088317, CC ECO:0000269|PubMed:18258429, ECO:0000269|PubMed:18621736, CC ECO:0000269|PubMed:19423701, ECO:0000269|PubMed:19674157, CC ECO:0000269|PubMed:19785988, ECO:0000269|PubMed:20499158, CC ECO:0000269|PubMed:20541605, ECO:0000269|PubMed:20573744, CC ECO:0000269|PubMed:20976005, ECO:0000269|PubMed:21212275, CC ECO:0000269|PubMed:21347310, ECO:0000269|PubMed:23636399, CC ECO:0000269|PubMed:28132843, ECO:0000269|PubMed:9584165}. CC -!- FUNCTION: (Microbial infection) Binds to Y.pseudotuberculosis yopK CC which leads to inhibition of phagocytosis and survival of bacteria CC following infection of host cells. {ECO:0000269|PubMed:21347310}. CC -!- FUNCTION: (Microbial infection) Enhances phosphorylation of HIV-1 Nef CC by PKCs. {ECO:0000269|PubMed:11312657}. CC -!- FUNCTION: (Microbial infection) In case of poxvirus infection, remodels CC the ribosomes so that they become optimal for the viral mRNAs CC (containing poly-A leaders) translation but not for host mRNAs. CC {ECO:0000269|PubMed:28636603}. CC -!- FUNCTION: (Microbial infection) Contributes to the cap-independent CC internal ribosome entry site (IRES)-mediated translation by some RNA CC viruses. {ECO:0000269|PubMed:25416947}. CC -!- SUBUNIT: Monomer; also forms homodimers and homooligomers CC (PubMed:15140893, PubMed:20529362). Interacts with CPNE3 CC (PubMed:20010870). May interact with ABCB4 (PubMed:19674157). Component CC of the small (40S) ribosomal subunit (PubMed:23636399). Interacts with CC the 80S ribosome (PubMed:23636399). Binds NHERF1. Forms a ternary CC complex with TRIM63 and PRKCE. Interacts with HABP4, KRT1 and OTUB1. CC Interacts with SRC (via SH2 domain); the interaction is enhanced by CC tyrosine phosphorylation of RACK1. Recruited in a circadian manner into CC a nuclear complex which also includes BMAL1 and PRKCA. Interacts with CC AR. Interacts with IGF1R but not with INSR. Interacts with ADAM12. CC Interacts with CLEC1B (via N-terminal region) and with HIF1A; the CC interaction promotes their degradation. Interacts with RHOA; this CC enhances RHOA activation and promotes cell migration. Interacts with CC CHRM2; the interaction regulates CHRM2 internalization. Interacts with CC TRPM6 (via kinase domain). Interacts with PTK2/FAK1; required for CC PTK2/FAK1 phosphorylation and dephosphorylation. Interacts with FLT1. CC Interacts with TBXA2R isoform 2. Interacts with HRAS. Interacts with CC LARP4B. Interacts with LARP4 (PubMed:21098120). Interacts with PKD2L1. CC Interacts with isoform 2 of SLC4A7 (PubMed:29743600). Interacts with CC SLC9A5; this interaction regulates SLC9A5 cell-surface targeting and CC SLC9A5 activity (PubMed:24006492). Interacts with SLC9A6; this CC interaction regulates the distribution of SLC9A6 between endosomes and CC the plasma membrane (PubMed:18057008). Interacts with LACC1; this CC interaction may regulate macrophage autophagic flux. {ECO:0000250, CC ECO:0000250|UniProtKB:P68040, ECO:0000269|PubMed:11279199, CC ECO:0000269|PubMed:11884618, ECO:0000269|PubMed:11956211, CC ECO:0000269|PubMed:12958311, ECO:0000269|PubMed:14500341, CC ECO:0000269|PubMed:14699138, ECO:0000269|PubMed:15596539, CC ECO:0000269|PubMed:17108144, ECO:0000269|PubMed:17244529, CC ECO:0000269|PubMed:17956333, ECO:0000269|PubMed:18057008, CC ECO:0000269|PubMed:18088317, ECO:0000269|PubMed:18258429, CC ECO:0000269|PubMed:18621736, ECO:0000269|PubMed:18954305, CC ECO:0000269|PubMed:19423701, ECO:0000269|PubMed:19674157, CC ECO:0000269|PubMed:19785988, ECO:0000269|PubMed:20010870, CC ECO:0000269|PubMed:20499158, ECO:0000269|PubMed:20529362, CC ECO:0000269|PubMed:20541605, ECO:0000269|PubMed:20573744, CC ECO:0000269|PubMed:20976005, ECO:0000269|PubMed:21098120, CC ECO:0000269|PubMed:21212275, ECO:0000269|PubMed:22174419, CC ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:24006492, CC ECO:0000269|PubMed:29743600, ECO:0000269|PubMed:33606008, CC ECO:0000269|PubMed:9584165}. CC -!- SUBUNIT: (Microbial infection) Interacts with Y.pseudotuberculosis CC yopK. {ECO:0000269|PubMed:21347310}. CC -!- SUBUNIT: (Microbial infection) Interacts with Y.pseudotuberculosis CC yopK. Interacts with a number of viral proteins including Epstein-Barr CC virus BZLF1 and HIV-1 Nef; interaction with Nef increases Nef CC phosphorylation by PKC. {ECO:0000269|PubMed:10849009, CC ECO:0000269|PubMed:11312657}. CC -!- SUBUNIT: (Microbial infection) Interacts with human respiratory CC syncytial virus matrix protein M; this interaction suppresses CC interferon signaling. {ECO:0000269|PubMed:37712706}. CC -!- SUBUNIT: (Microbial infection) Interacts with Influenza protein PA-X. CC {ECO:0000269|PubMed:37712706}. CC -!- SUBUNIT: (Microbial infection) Interacts with Toxoplasma gondii SAG1; CC the interaction promotes viability of host cells. CC {ECO:0000269|PubMed:38157925}. CC -!- INTERACTION: CC P63244; P22303: ACHE; NbExp=2; IntAct=EBI-296739, EBI-1637793; CC P63244; P35609: ACTN2; NbExp=3; IntAct=EBI-296739, EBI-77797; CC P63244; Q9UKV8: AGO2; NbExp=2; IntAct=EBI-296739, EBI-528269; CC P63244; Q96B67: ARRDC3; NbExp=3; IntAct=EBI-296739, EBI-2875665; CC P63244; O43521: BCL2L11; NbExp=2; IntAct=EBI-296739, EBI-526406; CC P63244; Q13895: BYSL; NbExp=5; IntAct=EBI-296739, EBI-358049; CC P63244; Q9NZN8: CNOT2; NbExp=3; IntAct=EBI-296739, EBI-743033; CC P63244; Q14194: CRMP1; NbExp=3; IntAct=EBI-296739, EBI-473101; CC P63244; P63167: DYNLL1; NbExp=6; IntAct=EBI-296739, EBI-349105; CC P63244; O75530: EED; NbExp=3; IntAct=EBI-296739, EBI-923794; CC P63244; Q9UKT8: FBXW2; NbExp=11; IntAct=EBI-296739, EBI-914727; CC P63244; Q86UU5: GGN; NbExp=3; IntAct=EBI-296739, EBI-10259069; CC P63244; Q86WP2: GPBP1; NbExp=3; IntAct=EBI-296739, EBI-2349758; CC P63244; P42694: HELZ; NbExp=6; IntAct=EBI-296739, EBI-1210654; CC P63244; P48551: IFNAR2; NbExp=4; IntAct=EBI-296739, EBI-958408; CC P63244; Q0VD86: INCA1; NbExp=2; IntAct=EBI-296739, EBI-6509505; CC P63244; Q92615: LARP4B; NbExp=8; IntAct=EBI-296739, EBI-1052558; CC P63244; Q9Y561: LRP12; NbExp=2; IntAct=EBI-296739, EBI-296693; CC P63244; P07948: LYN; NbExp=2; IntAct=EBI-296739, EBI-79452; CC P63244; Q9H000: MKRN2; NbExp=3; IntAct=EBI-296739, EBI-2341005; CC P63244; Q9NWQ8: PAG1; NbExp=2; IntAct=EBI-296739, EBI-2828115; CC P63244; Q99497: PARK7; NbExp=4; IntAct=EBI-296739, EBI-1164361; CC P63244; O75928: PIAS2; NbExp=2; IntAct=EBI-296739, EBI-348555; CC P63244; Q08752: PPID; NbExp=4; IntAct=EBI-296739, EBI-716596; CC P63244; P63244: RACK1; NbExp=2; IntAct=EBI-296739, EBI-296739; CC P63244; Q0P631: TMEM131; NbExp=3; IntAct=EBI-296739, EBI-12946715; CC P63244; Q14694: USP10; NbExp=4; IntAct=EBI-296739, EBI-2510389; CC P63244; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-296739, EBI-11975223; CC P63244; P40337: VHL; NbExp=9; IntAct=EBI-296739, EBI-301246; CC P63244; O43309: ZSCAN12; NbExp=3; IntAct=EBI-296739, EBI-1210440; CC P63244; O54918-1: Bcl2l11; Xeno; NbExp=2; IntAct=EBI-296739, EBI-526076; CC P63244; P03206: BZLF1; Xeno; NbExp=5; IntAct=EBI-296739, EBI-2621186; CC P63244; O96871; Xeno; NbExp=3; IntAct=EBI-296739, EBI-52321959; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11312657, CC ECO:0000269|PubMed:17956333}; Peripheral membrane protein. Cytoplasm CC {ECO:0000269|PubMed:10849009, ECO:0000269|PubMed:11279199, CC ECO:0000269|PubMed:12958311, ECO:0000269|PubMed:19785988, CC ECO:0000269|PubMed:20499158, ECO:0000269|PubMed:20573744, CC ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:29743600, CC ECO:0000269|PubMed:37712706}. Cytoplasm, perinuclear region CC {ECO:0000269|PubMed:11279199, ECO:0000269|PubMed:12958311}. Nucleus CC {ECO:0000269|PubMed:10849009}. Perikaryon CC {ECO:0000250|UniProtKB:P68040}. Cell projection, dendrite CC {ECO:0000250|UniProtKB:P68040}. Cell projection, phagocytic cup CC {ECO:0000269|PubMed:21347310}. Note=Recruited to the plasma membrane CC through interaction with KRT1 which binds to membrane-bound ITGB1 CC (PubMed:17956333). Also associated with the membrane in oncogene- CC transformed cells (PubMed:11884618). PKC activation induces CC translocation from the perinuclear region to the cell periphery CC (PubMed:11279199). In the brain, detected mainly in cell bodies and CC dendrites with little expression in axonal fibers or nuclei (By CC similarity). Localized to phagocytic cups following infection by CC Y.pestis (PubMed:21347310). {ECO:0000250|UniProtKB:P68040, CC ECO:0000269|PubMed:11279199, ECO:0000269|PubMed:11884618, CC ECO:0000269|PubMed:17956333, ECO:0000269|PubMed:21347310}. CC -!- TISSUE SPECIFICITY: In the liver, expressed at higher levels in CC activated hepatic stellate cells than in hepatocytes or Kupffer cells. CC Up-regulated in hepatocellular carcinomas and in the adjacent non-tumor CC liver tissue. {ECO:0000269|PubMed:18621736}. CC -!- DOMAIN: The 7 WD repeats mediate protein-protein interactions with CC binding partners. {ECO:0000269|PubMed:15140893}. CC -!- PTM: Phosphorylated on Tyr-228 and/or Tyr-246 by SRC. This is required CC for binding to SRC. {ECO:0000269|PubMed:11279199, CC ECO:0000269|PubMed:12400005, ECO:0000269|PubMed:19423701}. CC -!- PTM: (Microbial infection) Phosphorylated by vaccinia virus B1 kinase CC on serine and threonine residues; this phosphorylation remodels the CC ribosome properties, favoring the viral mRNA translation. CC {ECO:0000269|PubMed:28636603}. CC -!- SIMILARITY: Belongs to the WD repeat G protein beta family. Ribosomal CC protein RACK1 subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAO21313.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAR24619.1; Type=Frameshift; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/43285/GNB2L1"; 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; M24194; AAA59626.1; -; mRNA. DR EMBL; AY159316; AAO21313.1; ALT_INIT; mRNA. DR EMBL; AY336089; AAR24619.1; ALT_FRAME; mRNA. DR EMBL; AK095666; BAG53102.1; -; mRNA. DR EMBL; CR456978; CAG33259.1; -; mRNA. DR EMBL; CR541909; CAG46707.1; -; mRNA. DR EMBL; AK222488; BAD96208.1; -; mRNA. DR EMBL; CH471165; EAW53692.1; -; Genomic_DNA. DR EMBL; CH471165; EAW53702.1; -; Genomic_DNA. DR EMBL; BC000214; AAH00214.1; -; mRNA. DR EMBL; BC000366; AAH00366.1; -; mRNA. DR EMBL; BC010119; AAH10119.1; -; mRNA. DR EMBL; BC014256; AAH14256.1; -; mRNA. DR EMBL; BC014788; AAH14788.1; -; mRNA. DR EMBL; BC017287; AAH17287.1; -; mRNA. DR EMBL; BC019093; AAH19093.1; -; mRNA. DR EMBL; BC019362; AAH19362.1; -; mRNA. DR EMBL; BC021993; AAH21993.1; -; mRNA. DR EMBL; BC032006; AAH32006.1; -; mRNA. DR CCDS; CCDS34324.1; -. DR PIR; B33928; B33928. DR RefSeq; NP_006089.1; NM_006098.5. DR PDB; 4AOW; X-ray; 2.45 A; A/B/C=1-317. DR PDB; 4UG0; EM; -; Sg=1-317. DR PDB; 4V5Z; EM; 8.70 A; Aa=1-317. DR PDB; 4V6X; EM; 5.00 A; Ag=1-317. DR PDB; 5A2Q; EM; 3.90 A; g=1-315. DR PDB; 5AJ0; EM; 3.50 A; Bg=1-317. DR PDB; 5FLX; EM; 3.90 A; g=1-317. DR PDB; 5LKS; EM; 3.60 A; Sg=1-317. DR PDB; 5OA3; EM; 4.30 A; g=1-315. DR PDB; 5T2C; EM; 3.60 A; AI=1-317. DR PDB; 5VYC; X-ray; 6.00 A; g1/g2/g3/g4/g5/g6=1-317. DR PDB; 6FEC; EM; 6.30 A; m=2-314. DR PDB; 6G18; EM; 3.60 A; g=1-317. DR PDB; 6G51; EM; 4.10 A; g=1-317. DR PDB; 6G53; EM; 4.50 A; g=1-317. DR PDB; 6G5H; EM; 3.60 A; g=1-317. DR PDB; 6G5I; EM; 3.50 A; g=1-317. DR PDB; 6IP5; EM; 3.90 A; 3F=1-317. DR PDB; 6IP6; EM; 4.50 A; 3F=1-317. DR PDB; 6IP8; EM; 3.90 A; 3F=1-317. DR PDB; 6OLE; EM; 3.10 A; Sg=3-314. DR PDB; 6OLF; EM; 3.90 A; Sg=3-314. DR PDB; 6OLG; EM; 3.40 A; Bg=2-315. DR PDB; 6OLI; EM; 3.50 A; Sg=3-314. DR PDB; 6OLZ; EM; 3.90 A; Bg=2-315. DR PDB; 6OM0; EM; 3.10 A; Sg=3-314. DR PDB; 6OM7; EM; 3.70 A; Sg=3-314. DR PDB; 6QZP; EM; 2.90 A; Sg=2-314. DR PDB; 6XA1; EM; 2.80 A; Sg=2-314. DR PDB; 6Y0G; EM; 3.20 A; Sg=1-317. DR PDB; 6Y2L; EM; 3.00 A; Sg=1-317. DR PDB; 6Y57; EM; 3.50 A; Sg=1-317. DR PDB; 6YBS; EM; 3.10 A; c=1-317. DR PDB; 6Z6L; EM; 3.00 A; Sg=1-317. DR PDB; 6Z6M; EM; 3.10 A; Sg=1-317. DR PDB; 6Z6N; EM; 2.90 A; Sg=1-317. DR PDB; 6ZLW; EM; 2.60 A; j=1-317. DR PDB; 6ZM7; EM; 2.70 A; Sg=1-317. DR PDB; 6ZME; EM; 3.00 A; Sg=1-317. DR PDB; 6ZMI; EM; 2.60 A; Sg=1-317. DR PDB; 6ZMO; EM; 3.10 A; Sg=1-317. DR PDB; 6ZMT; EM; 3.00 A; j=1-317. DR PDB; 6ZMW; EM; 3.70 A; c=1-317. DR PDB; 6ZN5; EM; 3.20 A; j=2-315. DR PDB; 6ZOJ; EM; 2.80 A; g=1-315. DR PDB; 6ZOL; EM; 2.80 A; g=1-315. DR PDB; 6ZON; EM; 3.00 A; V=1-317. DR PDB; 6ZP4; EM; 2.90 A; V=1-317. DR PDB; 6ZUO; EM; 3.10 A; g=1-317. DR PDB; 6ZV6; EM; 2.90 A; g=1-317. DR PDB; 6ZVH; EM; 2.90 A; g=2-314. DR PDB; 6ZVJ; EM; 3.80 A; V=4-312. DR PDB; 6ZXD; EM; 3.20 A; g=1-317. DR PDB; 6ZXE; EM; 3.00 A; g=1-317. DR PDB; 6ZXF; EM; 3.70 A; g=1-317. DR PDB; 6ZXG; EM; 2.60 A; g=1-317. DR PDB; 6ZXH; EM; 2.70 A; g=1-317. DR PDB; 7A09; EM; 3.50 A; V=1-317. DR PDB; 7K5I; EM; 2.90 A; g=1-317. DR PDB; 7QP6; EM; 4.70 A; c=1-317. DR PDB; 7QP7; EM; 3.70 A; c=1-317. DR PDB; 7R4X; EM; 2.15 A; g=1-317. DR PDB; 7TQL; EM; 3.40 A; j=2-315. DR PDB; 7XNX; EM; 2.70 A; Sg=1-317. DR PDB; 7XNY; EM; 2.50 A; Sg=1-317. DR PDB; 8G5Y; EM; 2.29 A; Sg=1-317. DR PDB; 8G5Z; EM; 2.64 A; Sg=2-314. DR PDB; 8G60; EM; 2.54 A; Sg=1-317. DR PDB; 8G61; EM; 2.94 A; Sg=1-317. DR PDB; 8G6J; EM; 2.80 A; Sg=1-317. DR PDB; 8GLP; EM; 1.67 A; Sg=1-317. DR PDB; 8IFD; EM; 2.59 A; 3F=1-317. DR PDB; 8IFE; EM; 2.57 A; 3F=1-317. DR PDB; 8JDJ; EM; 2.50 A; AR=1-317. DR PDB; 8JDK; EM; 2.26 A; AR=1-317. DR PDB; 8JDL; EM; 2.42 A; AR=1-317. DR PDB; 8JDM; EM; 2.67 A; AR=1-317. DR PDB; 8K2C; EM; 2.40 A; Sg=1-317. DR PDB; 8OZ0; EM; 3.50 A; k=1-317. DR PDB; 8PJ1; EM; 3.40 A; c=1-317. DR PDB; 8PJ2; EM; 3.40 A; c=1-317. DR PDB; 8PJ3; EM; 3.70 A; c=1-317. DR PDB; 8PJ4; EM; 3.20 A; c=1-317. DR PDB; 8PJ5; EM; 2.90 A; c=1-317. DR PDB; 8PJ6; EM; 2.90 A; c=1-317. DR PDB; 8PPK; EM; 2.98 A; g=1-317. DR PDB; 8PPL; EM; 2.65 A; Ag=1-317. DR PDB; 8QOI; EM; 1.90 A; Sg=1-317. DR PDB; 8T4S; EM; 2.60 A; g=1-317. DR PDB; 8UIK; EM; 2.96 A; Sg=2-314. DR PDB; 8UIY; EM; 2.97 A; Sg=2-314. DR PDB; 8UIZ; EM; 3.43 A; Sg=2-314. DR PDB; 8UJ9; EM; 3.64 A; Sg=2-314. DR PDB; 8UJB; EM; 2.67 A; Sg=2-314. DR PDB; 8UJJ; EM; 3.56 A; Sg=2-314. DR PDB; 8UJK; EM; 3.54 A; Sg=2-314. DR PDB; 8UKB; EM; 3.05 A; Sg=2-314. DR PDB; 8XP2; EM; 3.20 A; Sg=1-317. DR PDB; 8XP3; EM; 3.40 A; Sg=1-317. DR PDB; 8XSX; EM; 2.40 A; Sg=1-317. DR PDB; 8XSY; EM; 3.00 A; Sg=1-317. DR PDB; 8XSZ; EM; 3.20 A; Sg=1-317. DR PDB; 8XXL; EM; 2.90 A; Sg=1-317. DR PDB; 8XXM; EM; 3.20 A; Sg=1-317. DR PDB; 8XXN; EM; 3.60 A; Sg=1-317. DR PDB; 8Y0W; EM; 3.40 A; Sg=1-317. DR PDB; 8Y0X; EM; 3.30 A; Sg=1-317. DR PDB; 8YOO; EM; 2.00 A; Sg=1-317. DR PDB; 8YOP; EM; 2.20 A; Sg=1-317. DR PDB; 8ZDB; EM; 3.60 A; g=1-317. DR PDB; 8ZDC; EM; 3.80 A; g=1-317. DR PDB; 8ZDD; EM; 3.70 A; g=1-317. DR PDB; 9AZC; EM; 2.19 A; Sg=2-314. DR PDB; 9AZM; EM; 2.68 A; Sg=2-314. DR PDB; 9AZN; EM; 2.98 A; Sg=2-314. DR PDB; 9AZS; EM; 2.80 A; Sg=2-314. DR PDB; 9B0F; EM; 2.78 A; Sg=2-314. DR PDB; 9B0G; EM; 2.57 A; Sg=2-314. DR PDB; 9B0H; EM; 2.59 A; Sg=2-314. DR PDB; 9B0J; EM; 2.84 A; Sg=2-314. DR PDB; 9B0N; EM; 2.92 A; Sg=2-314. DR PDB; 9B0O; EM; 2.83 A; Sg=2-314. DR PDB; 9B0P; EM; 2.82 A; Sg=2-314. DR PDB; 9B0Q; EM; 3.20 A; Sg/sg=2-314. DR PDB; 9B0R; EM; 2.81 A; Sg=2-314. DR PDB; 9B0S; EM; 3.80 A; Sg/sg=2-314. DR PDB; 9B0W; EM; 2.66 A; Sg=2-314. DR PDB; 9B11; EM; 2.77 A; Sg=2-314. DR PDB; 9BKD; EM; 2.60 A; c=1-317. DR PDB; 9BLN; EM; 3.90 A; c=1-317. DR PDB; 9C3H; EM; 2.00 A; Sg=1-317. DR PDB; 9ED0; EM; 2.80 A; g=1-317. DR PDB; 9G8M; EM; 3.30 A; Sg=1-317. DR PDB; 9G8O; EM; 3.40 A; Sg=1-317. DR PDBsum; 4AOW; -. DR PDBsum; 4UG0; -. DR PDBsum; 4V5Z; -. DR PDBsum; 4V6X; -. DR PDBsum; 5A2Q; -. DR PDBsum; 5AJ0; -. DR PDBsum; 5FLX; -. DR PDBsum; 5LKS; -. DR PDBsum; 5OA3; -. DR PDBsum; 5T2C; -. DR PDBsum; 5VYC; -. DR PDBsum; 6FEC; -. DR PDBsum; 6G18; -. DR PDBsum; 6G51; -. DR PDBsum; 6G53; -. DR PDBsum; 6G5H; -. DR PDBsum; 6G5I; -. DR PDBsum; 6IP5; -. DR PDBsum; 6IP6; -. DR PDBsum; 6IP8; -. DR PDBsum; 6OLE; -. DR PDBsum; 6OLF; -. DR PDBsum; 6OLG; -. DR PDBsum; 6OLI; -. DR PDBsum; 6OLZ; -. DR PDBsum; 6OM0; -. DR PDBsum; 6OM7; -. DR PDBsum; 6QZP; -. DR PDBsum; 6XA1; -. DR PDBsum; 6Y0G; -. DR PDBsum; 6Y2L; -. DR PDBsum; 6Y57; -. DR PDBsum; 6YBS; -. DR PDBsum; 6Z6L; -. DR PDBsum; 6Z6M; -. DR PDBsum; 6Z6N; -. DR PDBsum; 6ZLW; -. DR PDBsum; 6ZM7; -. DR PDBsum; 6ZME; -. DR PDBsum; 6ZMI; -. DR PDBsum; 6ZMO; -. DR PDBsum; 6ZMT; -. DR PDBsum; 6ZMW; -. DR PDBsum; 6ZN5; -. DR PDBsum; 6ZOJ; -. DR PDBsum; 6ZOL; -. DR PDBsum; 6ZON; -. DR PDBsum; 6ZP4; -. DR PDBsum; 6ZUO; -. DR PDBsum; 6ZV6; -. DR PDBsum; 6ZVH; -. DR PDBsum; 6ZVJ; -. DR PDBsum; 6ZXD; -. DR PDBsum; 6ZXE; -. DR PDBsum; 6ZXF; -. DR PDBsum; 6ZXG; -. DR PDBsum; 6ZXH; -. DR PDBsum; 7A09; -. DR PDBsum; 7K5I; -. DR PDBsum; 7QP6; -. DR PDBsum; 7QP7; -. DR PDBsum; 7R4X; -. DR PDBsum; 7TQL; -. DR PDBsum; 7XNX; -. DR PDBsum; 7XNY; -. DR PDBsum; 8G5Y; -. DR PDBsum; 8G5Z; -. DR PDBsum; 8G60; -. DR PDBsum; 8G61; -. DR PDBsum; 8G6J; -. DR PDBsum; 8GLP; -. DR PDBsum; 8IFD; -. DR PDBsum; 8IFE; -. DR PDBsum; 8JDJ; -. DR PDBsum; 8JDK; -. DR PDBsum; 8JDL; -. DR PDBsum; 8JDM; -. DR PDBsum; 8K2C; -. DR PDBsum; 8OZ0; -. DR PDBsum; 8PJ1; -. DR PDBsum; 8PJ2; -. DR PDBsum; 8PJ3; -. DR PDBsum; 8PJ4; -. DR PDBsum; 8PJ5; -. DR PDBsum; 8PJ6; -. DR PDBsum; 8PPK; -. DR PDBsum; 8PPL; -. DR PDBsum; 8QOI; -. DR PDBsum; 8T4S; -. DR PDBsum; 8UIK; -. DR PDBsum; 8UIY; -. DR PDBsum; 8UIZ; -. DR PDBsum; 8UJ9; -. DR PDBsum; 8UJB; -. DR PDBsum; 8UJJ; -. DR PDBsum; 8UJK; -. DR PDBsum; 8UKB; -. DR PDBsum; 8XP2; -. DR PDBsum; 8XP3; -. DR PDBsum; 8XSX; -. DR PDBsum; 8XSY; -. DR PDBsum; 8XSZ; -. DR PDBsum; 8XXL; -. DR PDBsum; 8XXM; -. DR PDBsum; 8XXN; -. DR PDBsum; 8Y0W; -. DR PDBsum; 8Y0X; -. DR PDBsum; 8YOO; -. DR PDBsum; 8YOP; -. DR PDBsum; 8ZDB; -. DR PDBsum; 8ZDC; -. DR PDBsum; 8ZDD; -. DR PDBsum; 9AZC; -. DR PDBsum; 9AZM; -. DR PDBsum; 9AZN; -. DR PDBsum; 9AZS; -. DR PDBsum; 9B0F; -. DR PDBsum; 9B0G; -. DR PDBsum; 9B0H; -. DR PDBsum; 9B0J; -. DR PDBsum; 9B0N; -. DR PDBsum; 9B0O; -. DR PDBsum; 9B0P; -. DR PDBsum; 9B0Q; -. DR PDBsum; 9B0R; -. DR PDBsum; 9B0S; -. DR PDBsum; 9B0W; -. DR PDBsum; 9B11; -. DR PDBsum; 9BKD; -. DR PDBsum; 9BLN; -. DR PDBsum; 9C3H; -. DR PDBsum; 9ED0; -. DR PDBsum; 9G8M; -. DR PDBsum; 9G8O; -. DR AlphaFoldDB; P63244; -. DR EMDB; EMD-10668; -. DR EMDB; EMD-10674; -. DR EMDB; EMD-10690; -. DR EMDB; EMD-10772; -. DR EMDB; EMD-11098; -. DR EMDB; EMD-11099; -. DR EMDB; EMD-11100; -. DR EMDB; EMD-11276; -. DR EMDB; EMD-11288; -. DR EMDB; EMD-11289; -. DR EMDB; EMD-11292; -. DR EMDB; EMD-11299; -. DR EMDB; EMD-11301; -. DR EMDB; EMD-11302; -. DR EMDB; EMD-11310; -. DR EMDB; EMD-11320; -. DR EMDB; EMD-11322; -. DR EMDB; EMD-11325; -. DR EMDB; EMD-11335; -. DR EMDB; EMD-11440; -. DR EMDB; EMD-11441; -. DR EMDB; EMD-11456; -. DR EMDB; EMD-11458; -. DR EMDB; EMD-11517; -. DR EMDB; EMD-11518; -. DR EMDB; EMD-11519; -. DR EMDB; EMD-11520; -. DR EMDB; EMD-11521; -. DR EMDB; EMD-11602; -. DR EMDB; EMD-14113; -. DR EMDB; EMD-14114; -. DR EMDB; EMD-14317; -. DR EMDB; EMD-17297; -. DR EMDB; EMD-17696; -. DR EMDB; EMD-17697; -. DR EMDB; EMD-17698; -. DR EMDB; EMD-17699; -. DR EMDB; EMD-17700; -. DR EMDB; EMD-17701; -. DR EMDB; EMD-17804; -. DR EMDB; EMD-17805; -. DR EMDB; EMD-18539; -. DR EMDB; EMD-22681; -. DR EMDB; EMD-26067; -. DR EMDB; EMD-29757; -. DR EMDB; EMD-29758; -. DR EMDB; EMD-29759; -. DR EMDB; EMD-29760; -. DR EMDB; EMD-29771; -. DR EMDB; EMD-33329; -. DR EMDB; EMD-33330; -. DR EMDB; EMD-35413; -. DR EMDB; EMD-35414; -. DR EMDB; EMD-36178; -. DR EMDB; EMD-36179; -. DR EMDB; EMD-36180; -. DR EMDB; EMD-36181; -. DR EMDB; EMD-36838; -. DR EMDB; EMD-3770; -. DR EMDB; EMD-38548; -. DR EMDB; EMD-38549; -. DR EMDB; EMD-38629; -. DR EMDB; EMD-38630; -. DR EMDB; EMD-38631; -. DR EMDB; EMD-38752; -. DR EMDB; EMD-38753; -. DR EMDB; EMD-38754; -. DR EMDB; EMD-3883; -. DR EMDB; EMD-39455; -. DR EMDB; EMD-39456; -. DR EMDB; EMD-39956; -. DR EMDB; EMD-39957; -. DR EMDB; EMD-39958; -. DR EMDB; EMD-40205; -. DR EMDB; EMD-4070; -. DR EMDB; EMD-41039; -. DR EMDB; EMD-42297; -. DR EMDB; EMD-42305; -. DR EMDB; EMD-42306; -. DR EMDB; EMD-42316; -. DR EMDB; EMD-42317; -. DR EMDB; EMD-42320; -. DR EMDB; EMD-42321; -. DR EMDB; EMD-42351; -. DR EMDB; EMD-4242; -. DR EMDB; EMD-4337; -. DR EMDB; EMD-4350; -. DR EMDB; EMD-4351; -. DR EMDB; EMD-4352; -. DR EMDB; EMD-4353; -. DR EMDB; EMD-44014; -. DR EMDB; EMD-44016; -. DR EMDB; EMD-44017; -. DR EMDB; EMD-44021; -. DR EMDB; EMD-44039; -. DR EMDB; EMD-44040; -. DR EMDB; EMD-44041; -. DR EMDB; EMD-44043; -. DR EMDB; EMD-44047; -. DR EMDB; EMD-44048; -. DR EMDB; EMD-44049; -. DR EMDB; EMD-44050; -. DR EMDB; EMD-44051; -. DR EMDB; EMD-44052; -. DR EMDB; EMD-44060; -. DR EMDB; EMD-44063; -. DR EMDB; EMD-44641; -. DR EMDB; EMD-44671; -. DR EMDB; EMD-45170; -. DR EMDB; EMD-47929; -. DR EMDB; EMD-51132; -. DR EMDB; EMD-51134; -. DR EMDB; EMD-9701; -. DR EMDB; EMD-9702; -. DR EMDB; EMD-9703; -. DR SMR; P63244; -. DR BioGRID; 115671; 713. DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit. DR CORUM; P63244; -. DR DIP; DIP-46736N; -. DR FunCoup; P63244; 1792. DR IntAct; P63244; 434. DR MINT; P63244; -. DR STRING; 9606.ENSP00000426909; -. DR DrugBank; DB09130; Copper. DR TCDB; 8.A.92.1.4; the g-protein AlphaBetaGama complex (gpc) family. DR GlyCosmos; P63244; 4 sites, 1 glycan. DR GlyGen; P63244; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; P63244; -. DR MetOSite; P63244; -. DR PhosphoSitePlus; P63244; -. DR SwissPalm; P63244; -. DR BioMuta; RACK1; -. DR DMDM; 54037168; -. DR REPRODUCTION-2DPAGE; IPI00848226; -. DR REPRODUCTION-2DPAGE; P63244; -. DR CPTAC; CPTAC-379; -. DR CPTAC; CPTAC-380; -. DR jPOST; P63244; -. DR MassIVE; P63244; -. DR PaxDb; 9606-ENSP00000426909; -. DR PeptideAtlas; P63244; -. DR PRIDE; P63244; -. DR ProteomicsDB; 57512; -. DR Pumba; P63244; -. DR TopDownProteomics; P63244; -. DR Antibodypedia; 3802; 466 antibodies from 45 providers. DR DNASU; 10399; -. DR Ensembl; ENST00000512805.6; ENSP00000426909.1; ENSG00000204628.13. DR GeneID; 10399; -. DR KEGG; hsa:10399; -. DR MANE-Select; ENST00000512805.6; ENSP00000426909.1; NM_006098.5; NP_006089.1. DR UCSC; uc003mni.2; human. DR AGR; HGNC:4399; -. DR ClinPGx; PA28779; -. DR CTD; 10399; -. DR DisGeNET; 10399; -. DR GeneCards; RACK1; -. DR HGNC; HGNC:4399; RACK1. DR HPA; ENSG00000204628; Low tissue specificity. DR MIM; 176981; gene. DR OpenTargets; ENSG00000204628; -. DR VEuPathDB; HostDB:ENSG00000204628; -. DR eggNOG; KOG0279; Eukaryota. DR GeneTree; ENSGT00940000154461; -. DR InParanoid; P63244; -. DR OMA; NCKLKIN; -. DR OrthoDB; 7875889at2759; -. DR PAN-GO; P63244; 6 GO annotations based on evolutionary models. DR PhylomeDB; P63244; -. DR PathwayCommons; P63244; -. DR Reactome; R-HSA-5357905; Regulation of TNFR1 signaling. DR Reactome; R-HSA-5357956; TNFR1-induced NF-kappa-B signaling pathway. DR Reactome; R-HSA-5626978; TNFR1-mediated ceramide production. DR Reactome; R-HSA-9766229; Degradation of CDH1. DR SignaLink; P63244; -. DR SIGNOR; P63244; -. DR Agora; ENSG00000204628; -. DR BioGRID-ORCS; 10399; 855 hits in 1158 CRISPR screens. DR CD-CODE; 91857CE7; Nucleolus. DR CD-CODE; DEE660B4; Stress granule. DR ChiTaRS; RACK1; human. DR EvolutionaryTrace; P63244; -. DR GeneWiki; GNB2L1; -. DR GenomeRNAi; 10399; -. DR Pharos; P63244; Tbio. DR PRO; PR:P63244; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; P63244; protein. DR Bgee; ENSG00000204628; Expressed in pericardium and 216 other cell types or tissues. DR ExpressionAtlas; P63244; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; NAS:ComplexPortal. DR GO; GO:0030425; C:dendrite; ISS:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:1990630; C:IRE1-RACK1-PP2A complex; IDA:ParkinsonsUK-UCL. DR GO; GO:0030496; C:midbody; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IMP:UniProtKB. DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB. DR GO; GO:0001891; C:phagocytic cup; IDA:UniProtKB. DR GO; GO:0015935; C:small ribosomal subunit; ISS:UniProtKB. DR GO; GO:0051434; F:BH3 domain binding; IDA:UniProtKB. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0030332; F:cyclin binding; IPI:UniProtKB. DR GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; IMP:UniProtKB. DR GO; GO:0008047; F:enzyme activator activity; IDA:BHF-UCL. DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0008200; F:ion channel inhibitor activity; ISS:UniProtKB. DR GO; GO:0060090; F:molecular adaptor activity; TAS:BHF-UCL. DR GO; GO:0042803; F:protein homodimerization activity; IPI:ParkinsonsUK-UCL. DR GO; GO:0005080; F:protein kinase C binding; IDA:UniProtKB. DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB. DR GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; IMP:ParkinsonsUK-UCL. DR GO; GO:0030292; F:protein tyrosine kinase inhibitor activity; IDA:UniProtKB. DR GO; GO:0030971; F:receptor tyrosine kinase binding; IDA:UniProtKB. DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0042169; F:SH2 domain binding; IDA:UniProtKB. DR GO; GO:0035591; F:signaling adaptor activity; IMP:ParkinsonsUK-UCL. DR GO; GO:0005102; F:signaling receptor binding; NAS:UniProtKB. DR GO; GO:0045182; F:translation regulator activity; IEA:InterPro. DR GO; GO:0071333; P:cellular response to glucose stimulus; IDA:ParkinsonsUK-UCL. DR GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:UniProtKB. DR GO; GO:0002181; P:cytoplasmic translation; NAS:ComplexPortal. DR GO; GO:0007369; P:gastrulation; IEA:UniProtKB-KW. DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB. DR GO; GO:1900102; P:negative regulation of endoplasmic reticulum unfolded protein response; TAS:ParkinsonsUK-UCL. DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB. 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; IMP:UniProtKB. DR GO; GO:0051898; P:negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IMP:UniProtKB. DR GO; GO:0032091; P:negative regulation of protein binding; IDA:UniProtKB. DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IDA:FlyBase. DR GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB. 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; IEA:Ensembl. DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB. DR GO; GO:0030335; P:positive regulation of cell migration; IDA: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; IMP:UniProtKB. DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB. DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB. DR GO; GO:0051901; P:positive regulation of mitochondrial depolarization; IMP:UniProtKB. DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB. DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IDA:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; IMP:UniProtKB. DR GO; GO:0106070; P:regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:BHF-UCL. DR GO; GO:0051726; P:regulation of cell cycle; IDA: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:0072344; P:rescue of stalled ribosome; IMP:UniProtKB. DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW. 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; KW Host-virus interaction; Membrane; Nucleus; Phosphoprotein; KW Proteomics identification; 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_0000424480" FT INIT_MET 1 FT /note="Removed; alternate" FT /evidence="ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..317 FT /note="Small ribosomal subunit protein RACK1, N-terminally FT processed" FT /id="PRO_0000127731" 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:0007744|PubMed:22814378" 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.9, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT MOD_RES 6 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 10 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 52 FT /note="Phosphotyrosine; by ABL1" FT /evidence="ECO:0000305|PubMed:19423701" FT MOD_RES 96 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 130 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 183 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P68040" FT MOD_RES 228 FT /note="Phosphotyrosine" FT /evidence="ECO:0000269|PubMed:11279199" FT MOD_RES 276 FT /note="Phosphoserine; by viral VacV B1 kinase" FT /evidence="ECO:0000269|PubMed:28636603, FT ECO:0007744|PubMed:23186163" FT MOD_RES 277 FT /note="Phosphothreonine; by viral VacV B1 kinase" FT /evidence="ECO:0000269|PubMed:28636603" FT MOD_RES 278 FT /note="Phosphoserine; by viral VacV B1 kinase" FT /evidence="ECO:0000269|PubMed:28636603" FT MOD_RES 279 FT /note="Phosphoserine; by viral VacV B1 kinase" FT /evidence="ECO:0000269|PubMed:28636603" FT MOD_RES 316 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P68040" FT MUTAGEN 36..38 FT /note="RDK->DDE: In DEmut; abolishes association with the FT ribosome and ability to initiate the ribosome quality FT control (RQC)." FT /evidence="ECO:0000269|PubMed:28132843" FT MUTAGEN 52 FT /note="Y->F: No effect on binding to SRC. Abolishes binding FT to PTK2/FAK1 and reduces cell adhesion and foci formation." FT /evidence="ECO:0000269|PubMed:11279199, FT ECO:0000269|PubMed:12400005, ECO:0000269|PubMed:19423701" FT MUTAGEN 57 FT /note="R->A: Decreased binding to PTK2/FAK1; when FT associated with A-60." FT /evidence="ECO:0000269|PubMed:19423701" FT MUTAGEN 60 FT /note="R->A: Decreased binding to PTK2/FAK1; when FT associated with A-57." FT /evidence="ECO:0000269|PubMed:19423701" FT MUTAGEN 127 FT /note="K->A: Decreased binding to PTK2/FAK1; when FT associated with A-130." FT /evidence="ECO:0000269|PubMed:19423701" FT MUTAGEN 130 FT /note="K->A: Decreased binding to PTK2/FAK1; when FT associated with A-127." FT /evidence="ECO:0000269|PubMed:19423701" FT MUTAGEN 140 FT /note="Y->F: No effect on binding to SRC." FT /evidence="ECO:0000269|PubMed:11279199, FT ECO:0000269|PubMed:12400005" FT MUTAGEN 194 FT /note="Y->F: No effect on binding to SRC." FT /evidence="ECO:0000269|PubMed:11279199, FT ECO:0000269|PubMed:12400005" FT MUTAGEN 228 FT /note="Y->F: No effect on binding to SRC. Does not abolish FT phosphorylation by SRC. Abolishes phosphorylation by SRC; FT when associated with F-246 and F-302." FT /evidence="ECO:0000269|PubMed:11279199, FT ECO:0000269|PubMed:12400005" FT MUTAGEN 246 FT /note="Y->F: Abolishes binding to SRC. Does not abolish FT phosphorylation by SRC. Abolishes phosphorylation by SRC; FT when associated with F-228 and F-302." FT /evidence="ECO:0000269|PubMed:11279199, FT ECO:0000269|PubMed:12400005" FT MUTAGEN 276..279 FT /note="STSS->EEEE: Enhanced translation of mRNAs containing FT poly-A leaders." FT /evidence="ECO:0000269|PubMed:28636603" FT MUTAGEN 278 FT /note="S->E: Enhanced translation of mRNAs containing FT poly-A leaders." FT /evidence="ECO:0000269|PubMed:28636603" FT MUTAGEN 302 FT /note="Y->F: No effect on binding to SRC. Abolishes FT phosphorylation by SRC; when associated with F-228 and FT F-246." FT /evidence="ECO:0000269|PubMed:11279199, FT ECO:0000269|PubMed:12400005" FT CONFLICT 70..111 FT /note="Missing (in Ref. 4; BAG53102)" FT /evidence="ECO:0000305" FT CONFLICT 94 FT /note="T -> TRK (in Ref. 3; AAR24619)" FT /evidence="ECO:0000305" FT CONFLICT 221 FT /note="L -> F (in Ref. 6; BAD96208)" FT /evidence="ECO:0000305" FT STRAND 4..11 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 18..23 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 25..27 FT /evidence="ECO:0007829|PDB:6ZV6" FT STRAND 30..35 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 36..38 FT /evidence="ECO:0007829|PDB:6ZXH" FT STRAND 40..45 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 48..50 FT /evidence="ECO:0007829|PDB:4AOW" FT STRAND 52..59 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 66..71 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 75..82 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 83..85 FT /evidence="ECO:0007829|PDB:6ZV6" FT STRAND 87..91 FT /evidence="ECO:0007829|PDB:7R4X" FT TURN 92..95 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 96..101 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 108..113 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 115..118 FT /evidence="ECO:0007829|PDB:6ZXG" FT STRAND 120..124 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 129..132 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 134..136 FT /evidence="ECO:0007829|PDB:6ZLW" FT STRAND 138..142 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 144..146 FT /evidence="ECO:0007829|PDB:4AOW" FT STRAND 151..156 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 160..162 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 164..169 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 170..172 FT /evidence="ECO:0007829|PDB:6ZXE" FT STRAND 174..178 FT /evidence="ECO:0007829|PDB:7R4X" FT TURN 179..182 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 184..188 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 195..200 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 202..204 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 207..211 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 215..220 FT /evidence="ECO:0007829|PDB:7R4X" FT TURN 221..224 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 225..231 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 236..241 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 243..252 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 255..260 FT /evidence="ECO:0007829|PDB:7R4X" FT TURN 261..264 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 265..270 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 278..280 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 286..291 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 293..305 FT /evidence="ECO:0007829|PDB:7R4X" FT STRAND 307..313 FT /evidence="ECO:0007829|PDB:7R4X" 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 //