RACK1_HUMAN
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 03-AUG-2022, entry version 178.
DE RecName: Full=Receptor of activated protein C kinase 1;
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=Small ribosomal subunit protein RACK1 {ECO:0000303|PubMed:24524803};
DE Contains:
DE RecName: Full=Receptor of activated protein C kinase 1, N-terminally processed;
DE AltName: Full=Guanine nucleotide-binding protein subunit beta-2-like 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 SLC9A3R1.
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 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 [32]
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 [33]
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 [34]
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 [35]
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 [36]
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 [37]
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 [38]
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 [39]
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 [40]
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 [41]
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 [42]
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 [43]
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 [44]
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 [45]
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 [46]
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 [47]
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 [48]
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 [49]
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 [50]
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 [51]
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 [52]
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 [53]
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 [54]
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 [55]
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 [56]
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 [57]
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 [58]
RP FUNCTION (MICROBIAL INFECTION), AND PHOSPHORYLATION AT SER-276; THR-277;
RP SER-278 AND SER-279 (MICROBIAL INFECTION).
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 [59]
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 [60]
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 [61]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) IN COMPLEX WITH THE 80S
RP RIBOSOME, FUNCTION, AND SUBUNIT.
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).
CC {ECO:0000269|PubMed:11884618, ECO:0000269|PubMed:12589061,
CC ECO:0000269|PubMed:12958311, ECO:0000269|PubMed:17108144,
CC ECO:0000269|PubMed:17244529, ECO:0000269|PubMed:17956333,
CC ECO:0000269|PubMed:18088317, ECO:0000269|PubMed:18258429,
CC ECO:0000269|PubMed:18621736, ECO:0000269|PubMed:19423701,
CC ECO:0000269|PubMed:19674157, ECO:0000269|PubMed:19785988,
CC ECO:0000269|PubMed:20499158, ECO:0000269|PubMed:20541605,
CC ECO:0000269|PubMed:20573744, ECO:0000269|PubMed:20976005,
CC ECO:0000269|PubMed:21212275, ECO:0000269|PubMed:21347310,
CC ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:28132843,
CC 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:20529362, PubMed:15140893). Interacts with CPNE3
CC (PubMed:20010870). May interact with ABCB4 (PubMed:19674157). Component
CC of the small (40S) ribosomal subunit (By similarity). Interacts with
CC the 80S ribosome (PubMed:23636399). Binds SLC9A3R1. 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 {ECO:0000250, ECO:0000269|PubMed:11279199, ECO:0000269|PubMed:11884618,
CC ECO:0000269|PubMed:11956211, ECO:0000269|PubMed:12958311,
CC ECO:0000269|PubMed:14500341, ECO:0000269|PubMed:14699138,
CC ECO:0000269|PubMed:15596539, ECO:0000269|PubMed:17108144,
CC ECO:0000269|PubMed:17244529, ECO:0000269|PubMed:17956333,
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: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 -!- 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=3; 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; 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=5; 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; Q0P631: TMEM131; NbExp=3; IntAct=EBI-296739, EBI-12946715;
CC P63244; Q14694: USP10; NbExp=3; 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 -!- 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}. Cytoplasm,
CC perinuclear region {ECO:0000269|PubMed:11279199,
CC ECO:0000269|PubMed:12958311}. Nucleus {ECO:0000269|PubMed:10849009}.
CC Perikaryon {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="http://atlasgeneticsoncology.org/Genes/GNB2L1ID43285ch5q35.html";
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_006098.4.
DR PDB; 4AOW; X-ray; 2.45 A; A/B/C=1-317.
DR PDB; 4UG0; EM; -; Sg=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 PDBsum; 4AOW; -.
DR PDBsum; 4UG0; -.
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 AlphaFoldDB; P63244; -.
DR SMR; P63244; -.
DR BioGRID; 115671; 383.
DR ComplexPortal; CPX-5223; 40S cytosolic small ribosomal subunit.
DR CORUM; P63244; -.
DR DIP; DIP-46736N; -.
DR IntAct; P63244; 234.
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 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 EPD; P63244; -.
DR jPOST; P63244; -.
DR MassIVE; P63244; -.
DR MaxQB; P63244; -.
DR PaxDb; P63244; -.
DR PeptideAtlas; P63244; -.
DR PRIDE; P63244; -.
DR ProteomicsDB; 57512; -.
DR TopDownProteomics; P63244; -.
DR Antibodypedia; 3802; 463 antibodies from 44 providers.
DR DNASU; 10399; -.
DR Ensembl; ENST00000512805.6; ENSP00000426909.1; ENSG00000204628.12.
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 CTD; 10399; -.
DR DisGeNET; 10399; -.
DR GeneCards; RACK1; -.
DR HGNC; HGNC:4399; RACK1.
DR HPA; ENSG00000204628; Low tissue specificity.
DR MIM; 176981; gene.
DR neXtProt; NX_P63244; -.
DR OpenTargets; ENSG00000204628; -.
DR PharmGKB; PA28779; -.
DR VEuPathDB; HostDB:ENSG00000204628; -.
DR eggNOG; KOG0279; Eukaryota.
DR GeneTree; ENSGT00940000154461; -.
DR InParanoid; P63244; -.
DR OMA; CKAMLWD; -.
DR OrthoDB; 805365at2759; -.
DR PhylomeDB; P63244; -.
DR TreeFam; TF300600; -.
DR PathwayCommons; P63244; -.
DR Reactome; R-HSA-5357905; Regulation of TNFR1 signaling.
DR Reactome; R-HSA-5357956; TNFR1-induced NFkappaB signaling pathway.
DR Reactome; R-HSA-5626978; TNFR1-mediated ceramide production.
DR SignaLink; P63244; -.
DR SIGNOR; P63244; -.
DR BioGRID-ORCS; 10399; 819 hits in 1077 CRISPR screens.
DR ChiTaRS; RACK1; human.
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 214 other tissues.
DR ExpressionAtlas; P63244; baseline and differential.
DR Genevisible; P63244; HS.
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; IC: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:0019899; F:enzyme binding; IPI:BHF-UCL.
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; IDA: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: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:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
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; IC: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:1903208; P:negative regulation of hydrogen peroxide-induced neuron death; IGI:ParkinsonsUK-UCL.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IMP:ParkinsonsUK-UCL.
DR GO; GO:0050765; P:negative regulation of phagocytosis; IMP:UniProtKB.
DR GO; GO:0032091; P:negative regulation of protein binding; IDA:UniProtKB.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; IMP: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: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:0051343; P:positive regulation of cyclic-nucleotide phosphodiesterase activity; IMP:BHF-UCL.
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: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 Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR045223; Asc1/RACK1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR19868; PTHR19868; 1.
DR Pfam; PF00400; WD40; 7.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 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 Reference proteome; Repeat; Ribonucleoprotein; Ribosomal protein;
KW Translation regulation; WD repeat.
FT CHAIN 1..317
FT /note="Receptor of activated protein C kinase 1"
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="Receptor of activated protein C kinase 1, N-
FT terminally 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 poly-
FT 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 F-
FT 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:4AOW"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:4AOW"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:6ZV6"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:4AOW"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:6ZXH"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:4AOW"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:4AOW"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:4AOW"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:4AOW"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:4AOW"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:4AOW"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:4AOW"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:4AOW"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:4AOW"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:6ZXG"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:4AOW"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:4AOW"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:6ZLW"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:4AOW"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:4AOW"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:4AOW"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:4AOW"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:4AOW"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:6ZXE"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:4AOW"
FT TURN 179..182
FT /evidence="ECO:0007829|PDB:4AOW"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:4AOW"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:4AOW"
FT STRAND 204..211
FT /evidence="ECO:0007829|PDB:4AOW"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:4AOW"
FT TURN 221..224
FT /evidence="ECO:0007829|PDB:4AOW"
FT STRAND 225..231
FT /evidence="ECO:0007829|PDB:4AOW"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:4AOW"
FT STRAND 243..252
FT /evidence="ECO:0007829|PDB:4AOW"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:4AOW"
FT TURN 261..264
FT /evidence="ECO:0007829|PDB:4AOW"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:4AOW"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:6ZOJ"
FT STRAND 286..291
FT /evidence="ECO:0007829|PDB:4AOW"
FT STRAND 295..302
FT /evidence="ECO:0007829|PDB:4AOW"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:6ZMT"
FT STRAND 307..313
FT /evidence="ECO:0007829|PDB:4AOW"
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
