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Receptor of activated protein C kinase 1 (Cell proliferation-inducing gene 21 protein) (Guanine nucleotide-binding protein subunit beta-2-like 1) (Guanine nucleotide-binding protein subunit beta-like protein 12.3) (Human lung cancer oncogene 7 protein) (HLC-7) (Receptor for activated C kinase) (Small ribosomal subunit protein RACK1) [Cleaved into: Receptor of activated protein C kinase 1, N-terminally processed (Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed)]

 RACK1_HUMAN             Reviewed;         317 AA.
P63244; B3KTJ0; D3DWS0; P25388; P99049; Q53HU2; Q5J8M6; Q5VLR4; Q6FH47;
11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-APR-2020, entry version 167.
RecName: Full=Receptor of activated protein C kinase 1;
AltName: Full=Cell proliferation-inducing gene 21 protein;
AltName: Full=Guanine nucleotide-binding protein subunit beta-2-like 1;
AltName: Full=Guanine nucleotide-binding protein subunit beta-like protein 12.3;
AltName: Full=Human lung cancer oncogene 7 protein;
Short=HLC-7;
AltName: Full=Receptor for activated C kinase;
AltName: Full=Small ribosomal subunit protein RACK1 {ECO:0000303|PubMed:24524803};
Contains:
RecName: Full=Receptor of activated protein C kinase 1, N-terminally processed;
AltName: Full=Guanine nucleotide-binding protein subunit beta-2-like 1, N-terminally processed;
Name=RACK1 {ECO:0000312|HGNC:HGNC:4399}; Synonyms=GNB2L1;
ORFNames=HLC7, PIG21;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2499885; DOI=10.1073/pnas.86.12.4594;
Guillemot F., Billault A., Auffray C.;
"Physical linkage of a guanine nucleotide-binding protein-related gene to
the chicken major histocompatibility complex.";
Proc. Natl. Acad. Sci. U.S.A. 86:4594-4598(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kim J.W.;
"Identification of new tumor-related gene in human lung cancer.";
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kim J.W.;
"Identification of a proliferation-inducing gene.";
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Adipose tissue;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=B-cell, Brain, Cervix, Lung, Lymph, Ovary, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 2-11; 48-57; 107-118; 258-280 AND 309-317, CLEAVAGE OF
INITIATOR METHIONINE, ACETYLATION AT THR-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=B-cell lymphoma, and T-cell;
Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
Submitted (MAY-2006) to UniProtKB.
[10]
PROTEIN SEQUENCE OF 48-57; 107-118; 140-155 AND 226-245, AND IDENTIFICATION
BY MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Afjehi-Sadat L.;
Submitted (MAR-2007) to UniProtKB.
[11]
FUNCTION, AND INTERACTION WITH SRC.
PubMed=9584165; DOI=10.1128/mcb.18.6.3245;
Chang B.Y., Conroy K.B., Machleder E.M., Cartwright C.A.;
"RACK1, a receptor for activated C kinase and a homolog of the beta subunit
of G proteins, inhibits activity of src tyrosine kinases and growth of NIH
3T3 cells.";
Mol. Cell. Biol. 18:3245-3256(1998).
[12]
INTERACTION WITH EPSTEIN-BARR VIRUS BZLF1 (MICROBIAL INFECTION), AND
SUBCELLULAR LOCATION.
PubMed=10849009; DOI=10.1046/j.1432-1327.2000.01430.x;
Baumann M., Gires O., Kolch W., Mischak H., Zeidler R., Pich D.,
Hammerschmidt W.;
"The PKC targeting protein RACK1 interacts with the Epstein-Barr virus
activator protein BZLF1.";
Eur. J. Biochem. 267:3891-3901(2000).
[13]
INTERACTION WITH SRC, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-228, AND
MUTAGENESIS OF TYR-52; TYR-140; TYR-194; TYR-228; TYR-246 AND TYR-302.
PubMed=11279199; DOI=10.1074/jbc.m101375200;
Chang B.Y., Chiang M., Cartwright C.A.;
"The interaction of Src and RACK1 is enhanced by activation of protein
kinase C and tyrosine phosphorylation of RACK1.";
J. Biol. Chem. 276:20346-20356(2001).
[14]
FUNCTION (MICROBIAL INFECTION), INTERACTION WITH HIV-1 NEF (MICROBIAL
INFECTION), AND SUBCELLULAR LOCATION.
PubMed=11312657; DOI=10.1006/viro.2001.0855;
Gallina A., Rossi F., Milanesi G.;
"Rack1 binds HIV-1 Nef and can act as a Nef-protein kinase C adaptor.";
Virology 283:7-18(2001).
[15]
INTERACTION WITH SLC9A3R1.
PubMed=11956211; DOI=10.1074/jbc.m201917200;
Liedtke C.M., Yun C.H.C., Kyle N., Wang D.;
"Protein kinase C epsilon-dependent regulation of cystic fibrosis
transmembrane regulator involves binding to a receptor for activated C
kinase (RACK1) and RACK1 binding to Na+/H+ exchange regulatory factor.";
J. Biol. Chem. 277:22925-22933(2002).
[16]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH IGF1R.
PubMed=11884618; DOI=10.1128/mcb.22.7.2345-2365.2002;
Hermanto U., Zong C.S., Li W., Wang L.H.;
"RACK1, an insulin-like growth factor I (IGF-I) receptor-interacting
protein, modulates IGF-I-dependent integrin signaling and promotes cell
spreading and contact with extracellular matrix.";
Mol. Cell. Biol. 22:2345-2365(2002).
[17]
PHOSPHORYLATION, AND MUTAGENESIS OF TYR-52; TYR-140; TYR-194; TYR-228;
TYR-246 AND TYR-302.
PubMed=12400005; DOI=10.1038/sj.onc.1206002;
Chang B.Y., Harte R.A., Cartwright C.A.;
"RACK1: a novel substrate for the Src protein-tyrosine kinase.";
Oncogene 21:7619-7629(2002).
[18]
INTERACTION WITH HRAS.
PubMed=14500341;
Guil S., de La Iglesia N., Fernandez-Larrea J., Cifuentes D., Ferrer J.C.,
Guinovart J.J., Bach-Elias M.;
"Alternative splicing of the human proto-oncogene c-H-ras renders a new Ras
family protein that trafficks to cytoplasm and nucleus.";
Cancer Res. 63:5178-5187(2003).
[19]
FUNCTION, INTERACTION WITH AR, AND SUBCELLULAR LOCATION.
PubMed=12958311; DOI=10.1074/jbc.m306219200;
Rigas A.C., Ozanne D.M., Neal D.E., Robson C.N.;
"The scaffolding protein RACK1 interacts with androgen receptor and
promotes cross-talk through a protein kinase C signaling pathway.";
J. Biol. Chem. 278:46087-46093(2003).
[20]
FUNCTION.
PubMed=12589061; DOI=10.1091/mbc.e02-03-0142;
Cox E.A., Bennin D., Doan A.T., O'Toole T., Huttenlocher A.;
"RACK1 regulates integrin-mediated adhesion, protrusion, and chemotactic
cell migration via its Src-binding site.";
Mol. Biol. Cell 14:658-669(2003).
[21]
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Lymphoblast;
PubMed=14654843; DOI=10.1038/nature02166;
Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
"Proteomic characterization of the human centrosome by protein correlation
profiling.";
Nature 426:570-574(2003).
[22]
SUBUNIT, AND DOMAIN.
PubMed=15140893; DOI=10.1074/jbc.m402316200;
Thornton C., Tang K.C., Phamluong K., Luong K., Vagts A., Nikanjam D.,
Yaka R., Ron D.;
"Spatial and temporal regulation of RACK1 function and N-methyl-D-aspartate
receptor activity through WD40 motif-mediated dimerization.";
J. Biol. Chem. 279:31357-31364(2004).
[23]
INTERACTION WITH TRIM63 AND PRKCE.
PubMed=15596539; DOI=10.1083/jcb.200402033;
Arya R., Kedar V., Hwang J.R., McDonough H., Li H.-H., Taylor J.,
Patterson C.;
"Muscle ring finger protein-1 inhibits PKC-epsilon activation and prevents
cardiomyocyte hypertrophy.";
J. Cell Biol. 167:1147-1159(2004).
[24]
INTERACTION WITH HABP4.
PubMed=14699138; DOI=10.1074/jbc.m306672200;
Nery F.C., Passos D.O., Garcia V.S., Kobarg J.;
"Ki-1/57 interacts with RACK1 and is a substrate for the phosphorylation by
phorbol 12-myristate 13-acetate-activated protein kinase C.";
J. Biol. Chem. 279:11444-11455(2004).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[26]
FUNCTION, AND INTERACTION WITH AR.
PubMed=17108144; DOI=10.1158/0008-5472.can-06-0596;
Kraus S., Gioeli D., Vomastek T., Gordon V., Weber M.J.;
"Receptor for activated C kinase 1 (RACK1) and Src regulate the tyrosine
phosphorylation and function of the androgen receptor.";
Cancer Res. 66:11047-11054(2006).
[27]
FUNCTION, INTERACTION WITH KRT1, AND SUBCELLULAR LOCATION.
PubMed=17956333; DOI=10.1042/bst0351292;
Chuang N.N., Huang C.C.;
"Interaction of integrin beta1 with cytokeratin 1 in neuroblastoma NMB7
cells.";
Biochem. Soc. Trans. 35:1292-1294(2007).
[28]
FUNCTION, INTERACTION WITH HIF1A, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17244529; DOI=10.1016/j.molcel.2007.01.001;
Liu Y.V., Baek J.H., Zhang H., Diez R., Cole R.N., Semenza G.L.;
"RACK1 competes with HSP90 for binding to HIF-1alpha and is required for
O(2)-independent and HSP90 inhibitor-induced degradation of HIF-1alpha.";
Mol. Cell 25:207-217(2007).
[29]
FUNCTION, AND INTERACTION WITH TRPM6.
PubMed=18258429; DOI=10.1016/j.cub.2007.12.058;
Cao G., Thebault S., van der Wijst J., van der Kemp A., Lasonder E.,
Bindels R.J., Hoenderop J.G.;
"RACK1 inhibits TRPM6 activity via phosphorylation of the fused alpha-
kinase domain.";
Curr. Biol. 18:168-176(2008).
[30]
FUNCTION, INTERACTION WITH ADAM12, AND TISSUE SPECIFICITY.
PubMed=18621736; DOI=10.1074/jbc.m709829200;
Bourd-Boittin K., Le Pabic H., Bonnier D., L'Helgoualc'h A., Theret N.;
"RACK1, a new ADAM12 interacting protein. Contribution to liver
fibrogenesis.";
J. Biol. Chem. 283:26000-26009(2008).
[31]
FUNCTION, AND INTERACTION WITH TBXA2R.
PubMed=18088317; DOI=10.1111/j.1600-0854.2007.00692.x;
Parent A., Laroche G., Hamelin E., Parent J.L.;
"RACK1 regulates the cell surface expression of the G protein-coupled
receptor for thromboxane A(2).";
Traffic 9:394-407(2008).
[32]
ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in a
refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[33]
FUNCTION, INTERACTION WITH CLEC1B, AND SUBCELLULAR LOCATION.
PubMed=19785988; DOI=10.1016/j.bbrc.2009.09.087;
Ruan Y., Guo L., Qiao Y., Hong Y., Zhou L., Sun L., Wang L., Zhu H.,
Wang L., Yun X., Xie J., Gu J.;
"RACK1 associates with CLEC-2 and promotes its ubiquitin-proteasome
degradation.";
Biochem. Biophys. Res. Commun. 390:217-222(2009).
[34]
INTERACTION WITH OTUB1.
PubMed=18954305; DOI=10.1042/bj20081318;
Edelmann M.J., Iphoefer A., Akutsu M., Altun M., di Gleria K., Kramer H.B.,
Fiebiger E., Dhe-Paganon S., Kessler B.M.;
"Structural basis and specificity of human otubain 1-mediated
deubiquitination.";
Biochem. J. 418:379-390(2009).
[35]
FUNCTION, AND INTERACTION WITH ABCB4.
PubMed=19674157; DOI=10.1111/j.1872-034x.2009.00544.x;
Ikebuchi Y., Takada T., Ito K., Yoshikado T., Anzai N., Kanai Y.,
Suzuki H.;
"Receptor for activated C-kinase 1 regulates the cellular localization and
function of ABCB4.";
Hepatol. Res. 39:1091-1107(2009).
[36]
FUNCTION, INTERACTION WITH PTK2/FAK1, PHOSPHORYLATION AT TYR-52, AND
MUTAGENESIS OF TYR-52; ARG-57; ARG-60; LYS-127 AND LYS-130.
PubMed=19423701; DOI=10.1074/jbc.m109.017640;
Kiely P.A., Baillie G.S., Barrett R., Buckley D.A., Adams D.R.,
Houslay M.D., O'Connor R.;
"Phosphorylation of RACK1 on tyrosine 52 by c-Abl is required for insulin-
like growth factor I-mediated regulation of focal adhesion kinase.";
J. Biol. Chem. 284:20263-20274(2009).
[37]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-130, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[38]
FUNCTION, AND INTERACTION WITH BAX.
PubMed=20541605; DOI=10.1016/j.cellsig.2010.05.018;
Wu Y., Wang Y., Sun Y., Zhang L., Wang D., Ren F., Chang D., Chang Z.,
Jia B.;
"RACK1 promotes Bax oligomerization and dissociates the interaction of Bax
and Bcl-XL.";
Cell. Signal. 22:1495-1501(2010).
[39]
INTERACTION WITH CPNE3.
PubMed=20010870; DOI=10.1038/onc.2009.456;
Heinrich C., Keller C., Boulay A., Vecchi M., Bianchi M., Sack R.,
Lienhard S., Duss S., Hofsteenge J., Hynes N.E.;
"Copine-III interacts with ErbB2 and promotes tumor cell migration.";
Oncogene 29:1598-1610(2010).
[40]
FUNCTION, INTERACTION WITH CHRM2, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=20976005; DOI=10.1371/journal.pone.0013517;
Reiner C.L., McCullar J.S., Kow R.L., Le J.H., Goodlett D.R.,
Nathanson N.M.;
"RACK1 associates with muscarinic receptors and regulates M(2) receptor
trafficking.";
PLoS ONE 5:E13517-E13517(2010).
[41]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PABPC1 AND RACK1.
PubMed=20573744; DOI=10.1261/rna.2146910;
Schaffler K., Schulz K., Hirmer A., Wiesner J., Grimm M., Sickmann A.,
Fischer U.;
"A stimulatory role for the La-related protein 4B in translation.";
RNA 16:1488-1499(2010).
[42]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[43]
FUNCTION, INTERACTION WITH RHOA, AND SUBCELLULAR LOCATION.
PubMed=20499158; DOI=10.1007/s10549-010-0955-3;
Cao X.X., Xu J.D., Xu J.W., Liu X.L., Cheng Y.Y., Li Q.Q., Xu Z.D.,
Liu X.P.;
"RACK1 promotes breast carcinoma migration/metastasis via activation of the
RhoA/Rho kinase pathway.";
Breast Cancer Res. Treat. 126:555-563(2011).
[44]
FUNCTION, AND INTERACTION WITH FLT1.
PubMed=21212275; DOI=10.1074/jbc.m110.165605;
Wang F., Yamauchi M., Muramatsu M., Osawa T., Tsuchida R., Shibuya M.;
"RACK1 regulates VEGF/Flt1-mediated cell migration via activation of a PI3-
K/Akt pathway.";
J. Biol. Chem. 286:9097-9106(2011).
[45]
INTERACTION WITH LARP4.
PubMed=21098120; DOI=10.1128/mcb.01162-10;
Yang R., Gaidamakov S.A., Xie J., Lee J., Martino L., Kozlov G.,
Crawford A.K., Russo A.N., Conte M.R., Gehring K., Maraia R.J.;
"La-related protein 4 binds poly(A), interacts with the poly(A)-binding
protein MLLE domain via a variant PAM2w motif, and can promote mRNA
stability.";
Mol. Cell. Biol. 31:542-556(2011).
[46]
FUNCTION (MICROBIAL INFECTION), INTERACTION WITH YERSINIA
PSEUDOTUBERCULOSIS YOPK, AND SUBCELLULAR LOCATION.
PubMed=21347310; DOI=10.1371/journal.pone.0016784;
Thorslund S.E., Edgren T., Pettersson J., Nordfelth R., Sellin M.E.,
Ivanova E., Francis M.S., Isaksson E.L., Wolf-Watz H., Fallman M.;
"The RACK1 signaling scaffold protein selectively interacts with Yersinia
pseudotuberculosis virulence function.";
PLoS ONE 6:E16784-E16784(2011).
[47]
ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
"System-wide temporal characterization of the proteome and phosphoproteome
of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[48]
INTERACTION WITH PKD2L1.
PubMed=22174419; DOI=10.1074/jbc.m111.305854;
Yang J., Wang Q., Zheng W., Tuli J., Li Q., Wu Y., Hussein S., Dai X.Q.,
Shafiei S., Li X.G., Shen P.Y., Tu J.C., Chen X.Z.;
"Receptor for activated C kinase 1 (RACK1) inhibits function of transient
receptor potential (TRP)-type channel Pkd2L1 through physical
interaction.";
J. Biol. Chem. 287:6551-6561(2012).
[49]
ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.m111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[50]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-terminal
acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[51]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6; THR-10; THR-96 AND
SER-276, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[52]
NOMENCLATURE.
PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
Williamson J.R., Wilson D., Yonath A., Yusupov M.;
"A new system for naming ribosomal proteins.";
Curr. Opin. Struct. Biol. 24:165-169(2014).
[53]
FUNCTION (MICROBIAL INFECTION).
PubMed=25416947; DOI=10.1016/j.cell.2014.10.041;
Majzoub K., Hafirassou M.L., Meignin C., Goto A., Marzi S., Fedorova A.,
Verdier Y., Vinh J., Hoffmann J.A., Martin F., Baumert T.F., Schuster C.,
Imler J.L.;
"RACK1 controls IRES-mediated translation of viruses.";
Cell 159:1086-1095(2014).
[54]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[55]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[56]
FUNCTION, AND MUTAGENESIS OF 36-ARG--GLU-38.
PubMed=28132843; DOI=10.1016/j.molcel.2016.12.026;
Sundaramoorthy E., Leonard M., Mak R., Liao J., Fulzele A., Bennett E.J.;
"ZNF598 and RACK1 regulate mammalian ribosome-associated quality control
function by mediating regulatory 40S ribosomal ubiquitylation.";
Mol. Cell 0:0-0(2017).
[57]
REVIEW.
PubMed=28161490; DOI=10.1016/j.cellsig.2017.01.026;
Nielsen M.H., Flygaard R.K., Jenner L.B.;
"Structural analysis of ribosomal RACK1 and its role in translational
control.";
Cell. Signal. 35:272-281(2017).
[58]
FUNCTION (MICROBIAL INFECTION), AND PHOSPHORYLATION AT SER-276; THR-277;
SER-278 AND SER-279 (MICROBIAL INFECTION).
PubMed=28636603; DOI=10.1038/nature22814;
Jha S., Rollins M.G., Fuchs G., Procter D.J., Hall E.A., Cozzolino K.,
Sarnow P., Savas J.N., Walsh D.;
"Trans-kingdom mimicry underlies ribosome customization by a poxvirus
kinase.";
Nature 546:651-655(2017).
[59]
X-RAY SCATTERING SOLUTION STRUCTURE, AND INTERACTION WITH HABP4.
PubMed=20529362; DOI=10.1186/1472-6807-10-15;
Goncalves K.A., Borges J.C., Silva J.C., Papa P.F., Bressan G.C.,
Torriani I.L., Kobarg J.;
"Solution structure of the human signaling protein RACK1.";
BMC Struct. Biol. 10:15-15(2010).
[60]
X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
PubMed=22869111; DOI=10.1107/s1744309112027480;
Ruiz Carrillo D., Chandrasekaran R., Nilsson M., Cornvik T., Liew C.W.,
Tan S.M., Lescar J.;
"Structure of human Rack1 protein at a resolution of 2.45 A.";
Acta Crystallogr. F 68:867-872(2012).
[61]
STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) IN COMPLEX WITH THE 80S
RIBOSOME, FUNCTION, AND SUBUNIT.
PubMed=23636399; DOI=10.1038/nature12104;
Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
Wilson D.N., Beckmann R.;
"Structures of the human and Drosophila 80S ribosome.";
Nature 497:80-85(2013).
-!- FUNCTION: Scaffolding protein involved in the recruitment, assembly
and/or regulation of a variety of signaling molecules. Interacts with a
wide variety of proteins and plays a role in many cellular processes.
Component of the 40S ribosomal subunit involved in translational
repression (PubMed:23636399). Involved in the initiation of the
ribosome quality control (RQC), a pathway that takes place when a
ribosome has stalled during translation, by promoting ubiquitination of
a subset of 40S ribosomal subunits (PubMed:28132843). Binds to and
stabilizes activated protein kinase C (PKC), increasing PKC-mediated
phosphorylation. May recruit activated PKC to the ribosome, leading to
phosphorylation of EIF6. Inhibits the activity of SRC kinases including
SRC, LCK and YES1. Inhibits cell growth by prolonging the G0/G1 phase
of the cell cycle. Enhances phosphorylation of BMAL1 by PRKCA and
inhibits transcriptional activity of the BMAL1-CLOCK heterodimer.
Facilitates ligand-independent nuclear translocation of AR following
PKC activation, represses AR transactivation activity and is required
for phosphorylation of AR by SRC. Modulates IGF1R-dependent integrin
signaling and promotes cell spreading and contact with the
extracellular matrix. Involved in PKC-dependent translocation of ADAM12
to the cell membrane. Promotes the ubiquitination and proteasome-
mediated degradation of proteins such as CLEC1B and HIF1A. Required for
VANGL2 membrane localization, inhibits Wnt signaling, and regulates
cellular polarization and oriented cell division during gastrulation.
Required for PTK2/FAK1 phosphorylation and dephosphorylation. Regulates
internalization of the muscarinic receptor CHRM2. Promotes apoptosis by
increasing oligomerization of BAX and disrupting the interaction of BAX
with the anti-apoptotic factor BCL2L. Inhibits TRPM6 channel activity.
Regulates cell surface expression of some GPCRs such as TBXA2R. Plays a
role in regulation of FLT1-mediated cell migration. Involved in the
transport of ABCB4 from the Golgi to the apical bile canalicular
membrane (PubMed:19674157). Promotes migration of breast carcinoma
cells by binding to and activating RHOA (PubMed:20499158).
{ECO:0000269|PubMed:11884618, ECO:0000269|PubMed:12589061,
ECO:0000269|PubMed:12958311, ECO:0000269|PubMed:17108144,
ECO:0000269|PubMed:17244529, ECO:0000269|PubMed:17956333,
ECO:0000269|PubMed:18088317, ECO:0000269|PubMed:18258429,
ECO:0000269|PubMed:18621736, ECO:0000269|PubMed:19423701,
ECO:0000269|PubMed:19674157, ECO:0000269|PubMed:19785988,
ECO:0000269|PubMed:20499158, ECO:0000269|PubMed:20541605,
ECO:0000269|PubMed:20573744, ECO:0000269|PubMed:20976005,
ECO:0000269|PubMed:21212275, ECO:0000269|PubMed:21347310,
ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:28132843,
ECO:0000269|PubMed:9584165}.
-!- FUNCTION: (Microbial infection) Binds to Y.pseudotuberculosis yopK
which leads to inhibition of phagocytosis and survival of bacteria
following infection of host cells. {ECO:0000269|PubMed:21347310}.
-!- FUNCTION: (Microbial infection) Enhances phosphorylation of HIV-1 Nef
by PKCs. {ECO:0000269|PubMed:11312657}.
-!- FUNCTION: (Microbial infection) In case of poxvirus infection, remodels
the ribosomes so that they become optimal for the viral mRNAs
(containing poly-A leaders) translation but not for host mRNAs.
{ECO:0000269|PubMed:28636603}.
-!- FUNCTION: (Microbial infection) Contributes to the cap-independent
internal ribosome entry site (IRES)-mediated translation by some RNA
viruses. {ECO:0000269|PubMed:25416947}.
-!- SUBUNIT: Monomer; also forms homodimers and homooligomers
(PubMed:20529362, PubMed:15140893). Interacts with CPNE3
(PubMed:20010870). May interact with ABCB4 (PubMed:19674157). Component
of the small (40S) ribosomal subunit (By similarity). Interacts with
the 80S ribosome (PubMed:23636399). Binds SLC9A3R1. Forms a ternary
complex with TRIM63 and PRKCE. Interacts with HABP4, KRT1 and OTUB1.
Interacts with SRC (via SH2 domain); the interaction is enhanced by
tyrosine phosphorylation of RACK1. Recruited in a circadian manner into
a nuclear complex which also includes BMAL1 and PRKCA. Interacts with
AR. Interacts with IGF1R but not with INSR. Interacts with ADAM12.
Interacts with CLEC1B (via N-terminal region) and with HIF1A; the
interaction promotes their degradation. Interacts with RHOA; this
enhances RHOA activation and promotes cell migration. Interacts with
CHRM2; the interaction regulates CHRM2 internalization. Interacts with
TRPM6 (via kinase domain). Interacts with PTK2/FAK1; required for
PTK2/FAK1 phosphorylation and dephosphorylation. Interacts with FLT1.
Interacts with TBXA2R isoform 2. Interacts with HRAS. Interacts with
LARP4B. Interacts with LARP4 (PubMed:21098120). Interacts with PKD2L1.
{ECO:0000250, ECO:0000269|PubMed:11279199, ECO:0000269|PubMed:11884618,
ECO:0000269|PubMed:11956211, ECO:0000269|PubMed:12958311,
ECO:0000269|PubMed:14500341, ECO:0000269|PubMed:14699138,
ECO:0000269|PubMed:15596539, ECO:0000269|PubMed:17108144,
ECO:0000269|PubMed:17244529, ECO:0000269|PubMed:17956333,
ECO:0000269|PubMed:18088317, ECO:0000269|PubMed:18258429,
ECO:0000269|PubMed:18621736, ECO:0000269|PubMed:18954305,
ECO:0000269|PubMed:19423701, ECO:0000269|PubMed:19674157,
ECO:0000269|PubMed:19785988, ECO:0000269|PubMed:20010870,
ECO:0000269|PubMed:20499158, ECO:0000269|PubMed:20529362,
ECO:0000269|PubMed:20541605, ECO:0000269|PubMed:20573744,
ECO:0000269|PubMed:20976005, ECO:0000269|PubMed:21098120,
ECO:0000269|PubMed:21212275, ECO:0000269|PubMed:22174419,
ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:9584165}.
-!- SUBUNIT: (Microbial infection) Interacts with Y.pseudotuberculosis
yopK. {ECO:0000269|PubMed:21347310}.
-!- SUBUNIT: (Microbial infection) Interacts with Y.pseudotuberculosis
yopK. Interacts with a number of viral proteins including Epstein-Barr
virus BZLF1 and HIV-1 Nef; interaction with Nef increases Nef
phosphorylation by PKC. {ECO:0000269|PubMed:10849009,
ECO:0000269|PubMed:11312657}.
-!- INTERACTION:
P63244; P22303: ACHE; NbExp=2; IntAct=EBI-296739, EBI-1637793;
P63244; P35609: ACTN2; NbExp=3; IntAct=EBI-296739, EBI-77797;
P63244; Q9UKV8: AGO2; NbExp=2; IntAct=EBI-296739, EBI-528269;
P63244; Q96B67: ARRDC3; NbExp=3; IntAct=EBI-296739, EBI-2875665;
P63244; O43521: BCL2L11; NbExp=2; IntAct=EBI-296739, EBI-526406;
P63244; O54918-1: Bcl2l11; Xeno; NbExp=2; IntAct=EBI-296739, EBI-526076;
P63244; Q13895: BYSL; NbExp=3; IntAct=EBI-296739, EBI-358049;
P63244; P03206: BZLF1; Xeno; NbExp=5; IntAct=EBI-296739, EBI-2621186;
P63244; Q9NZN8: CNOT2; NbExp=3; IntAct=EBI-296739, EBI-743033;
P63244; Q14194: CRMP1; NbExp=3; IntAct=EBI-296739, EBI-473101;
P63244; P63167: DYNLL1; NbExp=6; IntAct=EBI-296739, EBI-349105;
P63244; O75530: EED; NbExp=3; IntAct=EBI-296739, EBI-923794;
P63244; Q86UU5: GGN; NbExp=3; IntAct=EBI-296739, EBI-10259069;
P63244; Q86WP2: GPBP1; NbExp=3; IntAct=EBI-296739, EBI-2349758;
P63244; P48551: IFNAR2; NbExp=4; IntAct=EBI-296739, EBI-958408;
P63244; Q0VD86: INCA1; NbExp=2; IntAct=EBI-296739, EBI-6509505;
P63244; Q92615: LARP4B; NbExp=5; IntAct=EBI-296739, EBI-1052558;
P63244; Q9Y561: LRP12; NbExp=2; IntAct=EBI-296739, EBI-296693;
P63244; P07948: LYN; NbExp=2; IntAct=EBI-296739, EBI-79452;
P63244; Q9H000: MKRN2; NbExp=3; IntAct=EBI-296739, EBI-2341005;
P63244; Q9NWQ8: PAG1; NbExp=2; IntAct=EBI-296739, EBI-2828115;
P63244; Q99497: PARK7; NbExp=4; IntAct=EBI-296739, EBI-1164361;
P63244; O75928: PIAS2; NbExp=2; IntAct=EBI-296739, EBI-348555;
P63244; Q08752: PPID; NbExp=4; IntAct=EBI-296739, EBI-716596;
P63244; Q0P631: TMEM131; NbExp=3; IntAct=EBI-296739, EBI-12946715;
P63244; Q14694: USP10; NbExp=3; IntAct=EBI-296739, EBI-2510389;
P63244; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-296739, EBI-11975223;
P63244; P40337: VHL; NbExp=9; IntAct=EBI-296739, EBI-301246;
P63244; O43309: ZSCAN12; NbExp=3; IntAct=EBI-296739, EBI-1210440;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11312657,
ECO:0000269|PubMed:17956333}; Peripheral membrane protein. Cytoplasm
{ECO:0000269|PubMed:10849009, ECO:0000269|PubMed:11279199,
ECO:0000269|PubMed:12958311, ECO:0000269|PubMed:19785988,
ECO:0000269|PubMed:20499158, ECO:0000269|PubMed:20573744}. Cytoplasm,
perinuclear region {ECO:0000269|PubMed:11279199,
ECO:0000269|PubMed:12958311}. Nucleus {ECO:0000269|PubMed:10849009}.
Perikaryon {ECO:0000250|UniProtKB:P68040}. Cell projection, dendrite
{ECO:0000250|UniProtKB:P68040}. Cell projection, phagocytic cup
{ECO:0000269|PubMed:21347310}. Note=Recruited to the plasma membrane
through interaction with KRT1 which binds to membrane-bound ITGB1
(PubMed:17956333). Also associated with the membrane in oncogene-
transformed cells (PubMed:11884618). PKC activation induces
translocation from the perinuclear region to the cell periphery
(PubMed:11279199). In the brain, detected mainly in cell bodies and
dendrites with little expression in axonal fibers or nuclei (By
similarity). Localized to phagocytic cups following infection by
Y.pestis (PubMed:21347310). {ECO:0000250|UniProtKB:P68040,
ECO:0000269|PubMed:11279199, ECO:0000269|PubMed:11884618,
ECO:0000269|PubMed:17956333, ECO:0000269|PubMed:21347310}.
-!- TISSUE SPECIFICITY: In the liver, expressed at higher levels in
activated hepatic stellate cells than in hepatocytes or Kupffer cells.
Up-regulated in hepatocellular carcinomas and in the adjacent non-tumor
liver tissue. {ECO:0000269|PubMed:18621736}.
-!- DOMAIN: The 7 WD repeats mediate protein-protein interactions with
binding partners. {ECO:0000269|PubMed:15140893}.
-!- PTM: Phosphorylated on Tyr-228 and/or Tyr-246 by SRC. This is required
for binding to SRC. {ECO:0000269|PubMed:11279199,
ECO:0000269|PubMed:12400005, ECO:0000269|PubMed:19423701}.
-!- PTM: (Microbial infection) Phosphorylated by vaccinia virus B1 kinase
on serine and threonine residues; this phosphorylation remodels the
ribosome properties, favoring the viral mRNA translation.
{ECO:0000269|PubMed:28636603}.
-!- SIMILARITY: Belongs to the WD repeat G protein beta family. Ribosomal
protein RACK1 subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAO21313.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
Sequence=AAR24619.1; Type=Frameshift; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
Haematology;
URL="http://atlasgeneticsoncology.org/Genes/GNB2L1ID43285ch5q35.html";
---------------------------------------------------------------------------
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EMBL; M24194; AAA59626.1; -; mRNA.
EMBL; AY159316; AAO21313.1; ALT_INIT; mRNA.
EMBL; AY336089; AAR24619.1; ALT_FRAME; mRNA.
EMBL; AK095666; BAG53102.1; -; mRNA.
EMBL; CR456978; CAG33259.1; -; mRNA.
EMBL; CR541909; CAG46707.1; -; mRNA.
EMBL; AK222488; BAD96208.1; -; mRNA.
EMBL; CH471165; EAW53692.1; -; Genomic_DNA.
EMBL; CH471165; EAW53702.1; -; Genomic_DNA.
EMBL; BC000214; AAH00214.1; -; mRNA.
EMBL; BC000366; AAH00366.1; -; mRNA.
EMBL; BC010119; AAH10119.1; -; mRNA.
EMBL; BC014256; AAH14256.1; -; mRNA.
EMBL; BC014788; AAH14788.1; -; mRNA.
EMBL; BC017287; AAH17287.1; -; mRNA.
EMBL; BC019093; AAH19093.1; -; mRNA.
EMBL; BC019362; AAH19362.1; -; mRNA.
EMBL; BC021993; AAH21993.1; -; mRNA.
EMBL; BC032006; AAH32006.1; -; mRNA.
CCDS; CCDS34324.1; -.
PIR; B33928; B33928.
RefSeq; NP_006089.1; NM_006098.4.
PDB; 4AOW; X-ray; 2.45 A; A/B/C=1-317.
PDB; 4UG0; EM; -; Sg=1-317.
PDB; 4V6X; EM; 5.00 A; Ag=1-317.
PDB; 5A2Q; EM; 3.90 A; g=1-315.
PDB; 5AJ0; EM; 3.50 A; Bg=1-317.
PDB; 5FLX; EM; 3.90 A; g=1-317.
PDB; 5LKS; EM; 3.60 A; Sg=1-317.
PDB; 5OA3; EM; 4.30 A; g=1-315.
PDB; 5T2C; EM; 3.60 A; AI=1-317.
PDB; 5VYC; X-ray; 6.00 A; g1/g2/g3/g4/g5/g6=1-317.
PDB; 6EK0; EM; 2.90 A; Sg=1-317.
PDB; 6FEC; EM; 6.30 A; m=2-314.
PDB; 6G18; EM; 3.60 A; g=1-317.
PDB; 6G51; EM; 4.10 A; g=1-317.
PDB; 6G53; EM; 4.50 A; g=1-317.
PDB; 6G5H; EM; 3.60 A; g=1-317.
PDB; 6G5I; EM; 3.50 A; g=1-317.
PDB; 6IP5; EM; 3.90 A; 3F=1-317.
PDB; 6IP6; EM; 4.50 A; 3F=1-317.
PDB; 6IP8; EM; 3.90 A; 3F=1-317.
PDB; 6OLE; EM; 3.10 A; Sg=3-314.
PDB; 6OLF; EM; 3.90 A; Sg=3-314.
PDB; 6OLG; EM; 3.40 A; Bg=2-315.
PDB; 6OLI; EM; 3.50 A; Sg=3-314.
PDB; 6OLZ; EM; 3.90 A; Bg=2-315.
PDB; 6OM0; EM; 3.10 A; Sg=3-314.
PDB; 6OM7; EM; 3.70 A; Sg=3-314.
PDB; 6QZP; EM; 2.90 A; Sg=2-314.
PDBsum; 4AOW; -.
PDBsum; 4UG0; -.
PDBsum; 4V6X; -.
PDBsum; 5A2Q; -.
PDBsum; 5AJ0; -.
PDBsum; 5FLX; -.
PDBsum; 5LKS; -.
PDBsum; 5OA3; -.
PDBsum; 5T2C; -.
PDBsum; 5VYC; -.
PDBsum; 6EK0; -.
PDBsum; 6FEC; -.
PDBsum; 6G18; -.
PDBsum; 6G51; -.
PDBsum; 6G53; -.
PDBsum; 6G5H; -.
PDBsum; 6G5I; -.
PDBsum; 6IP5; -.
PDBsum; 6IP6; -.
PDBsum; 6IP8; -.
PDBsum; 6OLE; -.
PDBsum; 6OLF; -.
PDBsum; 6OLG; -.
PDBsum; 6OLI; -.
PDBsum; 6OLZ; -.
PDBsum; 6OM0; -.
PDBsum; 6OM7; -.
PDBsum; 6QZP; -.
SMR; P63244; -.
BioGrid; 115671; 280.
CORUM; P63244; -.
DIP; DIP-46736N; -.
IntAct; P63244; 125.
MINT; P63244; -.
STRING; 9606.ENSP00000426909; -.
DrugBank; DB09130; Copper.
TCDB; 8.A.92.1.4; the g-protein AlphaBetaGama complex (gpc) family.
iPTMnet; P63244; -.
MetOSite; P63244; -.
PhosphoSitePlus; P63244; -.
SwissPalm; P63244; -.
BioMuta; RACK1; -.
DMDM; 54037168; -.
REPRODUCTION-2DPAGE; IPI00848226; -.
REPRODUCTION-2DPAGE; P63244; -.
CPTAC; CPTAC-379; -.
CPTAC; CPTAC-380; -.
EPD; P63244; -.
jPOST; P63244; -.
MassIVE; P63244; -.
MaxQB; P63244; -.
PaxDb; P63244; -.
PeptideAtlas; P63244; -.
PRIDE; P63244; -.
ProteomicsDB; 57512; -.
TopDownProteomics; P63244; -.
Antibodypedia; 3802; 425 antibodies.
DNASU; 10399; -.
Ensembl; ENST00000512805; ENSP00000426909; ENSG00000204628.
GeneID; 10399; -.
KEGG; hsa:10399; -.
UCSC; uc003mni.2; human.
CTD; 10399; -.
DisGeNET; 10399; -.
GeneCards; RACK1; -.
HGNC; HGNC:4399; RACK1.
HPA; ENSG00000204628; Low tissue specificity.
MIM; 176981; gene.
neXtProt; NX_P63244; -.
OpenTargets; ENSG00000204628; -.
PharmGKB; PA28779; -.
eggNOG; KOG0279; Eukaryota.
eggNOG; ENOG410XQGZ; LUCA.
GeneTree; ENSGT00940000154461; -.
InParanoid; P63244; -.
KO; K14753; -.
OMA; CKAMLWD; -.
OrthoDB; 805365at2759; -.
PhylomeDB; P63244; -.
TreeFam; TF300600; -.
Reactome; R-HSA-5357905; Regulation of TNFR1 signaling.
Reactome; R-HSA-5357956; TNFR1-induced NFkappaB signaling pathway.
Reactome; R-HSA-5626978; TNFR1-mediated ceramide production.
SignaLink; P63244; -.
SIGNOR; P63244; -.
ChiTaRS; RACK1; human.
GeneWiki; GNB2L1; -.
GenomeRNAi; 10399; -.
Pharos; P63244; Tbio.
PRO; PR:P63244; -.
Proteomes; UP000005640; Chromosome 5.
RNAct; P63244; protein.
Bgee; ENSG00000204628; Expressed in female gonad and 245 other tissues.
ExpressionAtlas; P63244; baseline and differential.
Genevisible; P63244; HS.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IMP:UniProtKB.
GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:1990630; C:IRE1-RACK1-PP2A complex; IDA:ParkinsonsUK-UCL.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IMP:UniProtKB.
GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0001891; C:phagocytic cup; IDA:UniProtKB.
GO; GO:0015935; C:small ribosomal subunit; ISS:UniProtKB.
GO; GO:0051434; F:BH3 domain binding; IDA:UniProtKB.
GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
GO; GO:0030332; F:cyclin binding; IPI:UniProtKB.
GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; IMP:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0008200; F:ion channel inhibitor activity; ISS:UniProtKB.
GO; GO:0060090; F:molecular adaptor activity; TAS:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IDA:ParkinsonsUK-UCL.
GO; GO:0005080; F:protein kinase C binding; IDA:UniProtKB.
GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
GO; GO:0030292; F:protein tyrosine kinase inhibitor activity; IDA:UniProtKB.
GO; GO:0030971; F:receptor tyrosine kinase binding; IDA:UniProtKB.
GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0042169; F:SH2 domain binding; IDA:UniProtKB.
GO; GO:0035591; F:signaling adaptor activity; IMP:ParkinsonsUK-UCL.
GO; GO:0005102; F:signaling receptor binding; NAS:UniProtKB.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0071333; P:cellular response to glucose stimulus; IDA:ParkinsonsUK-UCL.
GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:UniProtKB.
GO; GO:0007369; P:gastrulation; IEA:UniProtKB-KW.
GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
GO; GO:1900102; P:negative regulation of endoplasmic reticulum unfolded protein response; TAS:ParkinsonsUK-UCL.
GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
GO; GO:1903208; P:negative regulation of hydrogen peroxide-induced neuron death; IGI:ParkinsonsUK-UCL.
GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IMP:ParkinsonsUK-UCL.
GO; GO:0050765; P:negative regulation of phagocytosis; IMP:UniProtKB.
GO; GO:0032091; P:negative regulation of protein binding; IDA:UniProtKB.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; IMP:UniProtKB.
GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISS:UniProtKB.
GO; GO:0043473; P:pigmentation; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
GO; GO:2000304; P:positive regulation of ceramide biosynthetic process; TAS:Reactome.
GO; GO:0051343; P:positive regulation of cyclic-nucleotide phosphodiesterase activity; IMP:BHF-UCL.
GO; GO:2000543; P:positive regulation of gastrulation; ISS:UniProtKB.
GO; GO:0042998; P:positive regulation of Golgi to plasma membrane protein transport; IMP:UniProtKB.
GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0051901; P:positive regulation of mitochondrial depolarization; IMP:UniProtKB.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IMP:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
GO; GO:0051302; P:regulation of cell division; ISS:UniProtKB.
GO; GO:2000114; P:regulation of establishment of cell polarity; ISS:UniProtKB.
GO; GO:0032880; P:regulation of protein localization; ISS:UniProtKB.
GO; GO:0010803; P:regulation of tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0072344; P:rescue of stalled ribosome; IMP:UniProtKB.
GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF00400; WD40; 7.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00320; WD40; 7.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS00678; WD_REPEATS_1; 4.
PROSITE; PS50082; WD_REPEATS_2; 6.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Apoptosis; Biological rhythms; Cell cycle;
Cell membrane; Cell projection; Cytoplasm; Developmental protein;
Direct protein sequencing; Gastrulation; Growth regulation;
Host-virus interaction; Membrane; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Ribonucleoprotein; Ribosomal protein;
Translation regulation; WD repeat.
CHAIN 1..317
/note="Receptor of activated protein C kinase 1"
/id="PRO_0000424480"
INIT_MET 1
/note="Removed; alternate"
/evidence="ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378, ECO:0000269|Ref.9"
CHAIN 2..317
/note="Receptor of activated protein C kinase 1, N-
terminally processed"
/id="PRO_0000127731"
REPEAT 13..44
/note="WD 1"
REPEAT 61..91
/note="WD 2"
REPEAT 103..133
/note="WD 3"
REPEAT 146..178
/note="WD 4"
REPEAT 190..220
/note="WD 5"
REPEAT 231..260
/note="WD 6"
REPEAT 281..311
/note="WD 7"
MOD_RES 1
/note="N-acetylmethionine"
/evidence="ECO:0000244|PubMed:22814378"
MOD_RES 2
/note="N-acetylthreonine; in Guanine nucleotide-binding
protein subunit beta-2-like 1, N-terminally processed"
/evidence="ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378, ECO:0000269|Ref.9"
MOD_RES 6
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 10
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 52
/note="Phosphotyrosine; by ABL1"
/evidence="ECO:0000305|PubMed:19423701"
MOD_RES 96
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:23186163"
MOD_RES 130
/note="N6-acetyllysine"
/evidence="ECO:0000244|PubMed:19608861"
MOD_RES 183
/note="N6-acetyllysine"
/evidence="ECO:0000250|UniProtKB:P68040"
MOD_RES 228
/note="Phosphotyrosine"
/evidence="ECO:0000269|PubMed:11279199"
MOD_RES 276
/note="Phosphoserine; by viral VacV B1 kinase"
/evidence="ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:28636603"
MOD_RES 277
/note="Phosphothreonine; by viral VacV B1 kinase"
/evidence="ECO:0000269|PubMed:28636603"
MOD_RES 278
/note="Phosphoserine; by viral VacV B1 kinase"
/evidence="ECO:0000269|PubMed:28636603"
MOD_RES 279
/note="Phosphoserine; by viral VacV B1 kinase"
/evidence="ECO:0000269|PubMed:28636603"
MOD_RES 316
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:P68040"
MUTAGEN 36..38
/note="RDK->DDE: In DEmut; abolishes association with the
ribosome and ability to initiate the ribosome quality
control (RQC)."
/evidence="ECO:0000269|PubMed:28132843"
MUTAGEN 52
/note="Y->F: No effect on binding to SRC. Abolishes binding
to PTK2/FAK1 and reduces cell adhesion and foci formation."
/evidence="ECO:0000269|PubMed:11279199,
ECO:0000269|PubMed:12400005, ECO:0000269|PubMed:19423701"
MUTAGEN 57
/note="R->A: Decreased binding to PTK2/FAK1; when
associated with A-60."
/evidence="ECO:0000269|PubMed:19423701"
MUTAGEN 60
/note="R->A: Decreased binding to PTK2/FAK1; when
associated with A-57."
/evidence="ECO:0000269|PubMed:19423701"
MUTAGEN 127
/note="K->A: Decreased binding to PTK2/FAK1; when
associated with A-130."
/evidence="ECO:0000269|PubMed:19423701"
MUTAGEN 130
/note="K->A: Decreased binding to PTK2/FAK1; when
associated with A-127."
/evidence="ECO:0000269|PubMed:19423701"
MUTAGEN 140
/note="Y->F: No effect on binding to SRC."
/evidence="ECO:0000269|PubMed:11279199,
ECO:0000269|PubMed:12400005"
MUTAGEN 194
/note="Y->F: No effect on binding to SRC."
/evidence="ECO:0000269|PubMed:11279199,
ECO:0000269|PubMed:12400005"
MUTAGEN 228
/note="Y->F: No effect on binding to SRC. Does not abolish
phosphorylation by SRC. Abolishes phosphorylation by SRC;
when associated with F-246 and F-302."
/evidence="ECO:0000269|PubMed:11279199,
ECO:0000269|PubMed:12400005"
MUTAGEN 246
/note="Y->F: Abolishes binding to SRC. Does not abolish
phosphorylation by SRC. Abolishes phosphorylation by SRC;
when associated with F-228 and F-302."
/evidence="ECO:0000269|PubMed:11279199,
ECO:0000269|PubMed:12400005"
MUTAGEN 276..279
/note="STSS->EEEE: Enhanced translation of mRNAs containing
poly-A leaders."
/evidence="ECO:0000269|PubMed:28636603"
MUTAGEN 278
/note="S->E: Enhanced translation of mRNAs containing poly-
A leaders."
/evidence="ECO:0000269|PubMed:28636603"
MUTAGEN 302
/note="Y->F: No effect on binding to SRC. Abolishes
phosphorylation by SRC; when associated with F-228 and F-
246."
/evidence="ECO:0000269|PubMed:11279199,
ECO:0000269|PubMed:12400005"
CONFLICT 70..111
/note="Missing (in Ref. 4; BAG53102)"
/evidence="ECO:0000305"
CONFLICT 94
/note="T -> TRK (in Ref. 3; AAR24619)"
/evidence="ECO:0000305"
CONFLICT 221
/note="L -> F (in Ref. 6; BAD96208)"
/evidence="ECO:0000305"
STRAND 4..11
/evidence="ECO:0000244|PDB:4AOW"
STRAND 18..23
/evidence="ECO:0000244|PDB:4AOW"
STRAND 30..35
/evidence="ECO:0000244|PDB:4AOW"
STRAND 40..45
/evidence="ECO:0000244|PDB:4AOW"
STRAND 48..50
/evidence="ECO:0000244|PDB:4AOW"
STRAND 52..59
/evidence="ECO:0000244|PDB:4AOW"
STRAND 66..71
/evidence="ECO:0000244|PDB:4AOW"
STRAND 75..82
/evidence="ECO:0000244|PDB:4AOW"
STRAND 85..91
/evidence="ECO:0000244|PDB:4AOW"
TURN 92..95
/evidence="ECO:0000244|PDB:4AOW"
STRAND 96..102
/evidence="ECO:0000244|PDB:4AOW"
STRAND 108..113
/evidence="ECO:0000244|PDB:4AOW"
STRAND 120..124
/evidence="ECO:0000244|PDB:4AOW"
STRAND 129..132
/evidence="ECO:0000244|PDB:4AOW"
STRAND 138..142
/evidence="ECO:0000244|PDB:4AOW"
STRAND 144..146
/evidence="ECO:0000244|PDB:4AOW"
STRAND 151..156
/evidence="ECO:0000244|PDB:4AOW"
STRAND 160..162
/evidence="ECO:0000244|PDB:4AOW"
STRAND 164..169
/evidence="ECO:0000244|PDB:4AOW"
STRAND 174..178
/evidence="ECO:0000244|PDB:4AOW"
TURN 179..182
/evidence="ECO:0000244|PDB:4AOW"
STRAND 183..188
/evidence="ECO:0000244|PDB:4AOW"
STRAND 195..200
/evidence="ECO:0000244|PDB:4AOW"
STRAND 204..211
/evidence="ECO:0000244|PDB:4AOW"
STRAND 215..220
/evidence="ECO:0000244|PDB:4AOW"
TURN 221..224
/evidence="ECO:0000244|PDB:4AOW"
STRAND 225..231
/evidence="ECO:0000244|PDB:4AOW"
STRAND 236..241
/evidence="ECO:0000244|PDB:4AOW"
STRAND 243..252
/evidence="ECO:0000244|PDB:4AOW"
STRAND 255..260
/evidence="ECO:0000244|PDB:4AOW"
TURN 261..264
/evidence="ECO:0000244|PDB:4AOW"
STRAND 265..270
/evidence="ECO:0000244|PDB:4AOW"
STRAND 286..291
/evidence="ECO:0000244|PDB:4AOW"
STRAND 295..302
/evidence="ECO:0000244|PDB:4AOW"
STRAND 307..313
/evidence="ECO:0000244|PDB:4AOW"
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


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