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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.
30-AUG-2017, entry version 143.
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]
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).
[22]
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).
[23]
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).
[24]
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).
[25]
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).
[26]
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).
[27]
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).
[28]
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).
[29]
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).
[30]
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).
[31]
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).
[32]
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).
[33]
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).
[34]
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).
[35]
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).
[36]
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).
[37]
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).
[38]
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).
[39]
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).
[40]
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).
[41]
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).
[42]
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).
[43]
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).
[44]
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).
[45]
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).
[46]
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).
[47]
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).
[48]
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).
[49]
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).
[50]
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).
[51]
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).
[52]
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).
[53]
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).
[54]
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).
[55]
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).
[56]
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: 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}.
-!- SUBUNIT: 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). Exists as a monomer and also forms oligomers.
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:
P22303:ACHE; NbExp=2; IntAct=EBI-296739, EBI-1637793;
P35609:ACTN2; NbExp=3; IntAct=EBI-296739, EBI-77797;
Q9UKV8:AGO2; NbExp=2; IntAct=EBI-296739, EBI-528269;
O43521:BCL2L11; NbExp=2; IntAct=EBI-296739, EBI-526406;
O54918-1:Bcl2l11 (xeno); NbExp=2; IntAct=EBI-296739, EBI-526076;
P03206:BZLF1 (xeno); NbExp=5; IntAct=EBI-296739, EBI-2621186;
P63167:DYNLL1; NbExp=6; IntAct=EBI-296739, EBI-349105;
P48551:IFNAR2; NbExp=4; IntAct=EBI-296739, EBI-958408;
Q92615:LARP4B; NbExp=3; IntAct=EBI-296739, EBI-1052558;
Q9Y561:LRP12; NbExp=2; IntAct=EBI-296739, EBI-296693;
P07948:LYN; NbExp=2; IntAct=EBI-296739, EBI-79452;
Q9NWQ8:PAG1; NbExp=2; IntAct=EBI-296739, EBI-2828115;
Q99497:PARK7; NbExp=4; IntAct=EBI-296739, EBI-1164361;
O75928:PIAS2; NbExp=2; IntAct=EBI-296739, EBI-348555;
Q08752:PPID; NbExp=4; IntAct=EBI-296739, EBI-716596;
Q70EL1-9:USP54; NbExp=4; IntAct=EBI-296739, EBI-11975223;
P40337:VHL; NbExp=9; IntAct=EBI-296739, EBI-301246;
-!- 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}.
-!- 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}.
-!- 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=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAR24619.1; Type=Frameshift; Positions=94; 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.
UniGene; Hs.5662; -.
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; 5T2C; EM; 3.60 A; AI=1-317.
PDBsum; 4AOW; -.
PDBsum; 4UG0; -.
PDBsum; 4V6X; -.
PDBsum; 5A2Q; -.
PDBsum; 5AJ0; -.
PDBsum; 5FLX; -.
PDBsum; 5LKS; -.
PDBsum; 5T2C; -.
ProteinModelPortal; P63244; -.
SMR; P63244; -.
BioGrid; 115671; 210.
DIP; DIP-46736N; -.
IntAct; P63244; 97.
MINT; MINT-105673; -.
STRING; 9606.ENSP00000426909; -.
iPTMnet; P63244; -.
PhosphoSitePlus; P63244; -.
SwissPalm; P63244; -.
BioMuta; GNB2L1; -.
DMDM; 54037168; -.
REPRODUCTION-2DPAGE; IPI00848226; -.
REPRODUCTION-2DPAGE; P63244; -.
EPD; P63244; -.
MaxQB; P63244; -.
PaxDb; P63244; -.
PeptideAtlas; P63244; -.
PRIDE; P63244; -.
TopDownProteomics; P63244; -.
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; CAB004288; -.
HPA; HPA021676; -.
MIM; 176981; gene.
neXtProt; NX_P63244; -.
OpenTargets; ENSG00000204628; -.
PharmGKB; PA28779; -.
eggNOG; KOG0279; Eukaryota.
eggNOG; ENOG410XQGZ; LUCA.
GeneTree; ENSGT00890000139419; -.
HOVERGEN; HBG000277; -.
InParanoid; P63244; -.
KO; K14753; -.
OMA; QYGYPKR; -.
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; GNB2L1; human.
GeneWiki; GNB2L1; -.
GenomeRNAi; 10399; -.
PRO; PR:P63244; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000204628; -.
CleanEx; HS_GNB2L1; -.
ExpressionAtlas; P63244; baseline and differential.
Genevisible; P63244; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
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:0045296; F:cadherin binding; IDA:BHF-UCL.
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:0032947; F:protein complex scaffold 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:0005102; F:receptor binding; NAS: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; IDA:UniProtKB.
GO; GO:0042169; F:SH2 domain binding; IDA:UniProtKB.
GO; GO:0035591; F:signaling adaptor activity; IMP:ParkinsonsUK-UCL.
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: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:0001649; P:osteoblast differentiation; IEA:Ensembl.
GO; GO:0043473; P:pigmentation; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0030822; P:positive regulation of cAMP catabolic process; IMP:BHF-UCL.
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:0032464; P:positive regulation of protein homooligomerization; IDA:UniProtKB.
GO; GO:0001934; P:positive regulation of protein phosphorylation; 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; -; 2.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
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; Complete proteome; 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 Receptor of activated protein C kinase 1.
/FTId=PRO_0000424480.
INIT_MET 1 1 Removed; alternate.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.9}.
CHAIN 2 317 Receptor of activated protein C kinase 1,
N-terminally processed.
/FTId=PRO_0000127731.
REPEAT 13 44 WD 1.
REPEAT 61 91 WD 2.
REPEAT 103 133 WD 3.
REPEAT 146 178 WD 4.
REPEAT 190 220 WD 5.
REPEAT 231 260 WD 6.
REPEAT 281 311 WD 7.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 2 2 N-acetylthreonine; in Guanine nucleotide-
binding protein subunit beta-2-like 1, N-
terminally processed.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.9}.
MOD_RES 6 6 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 10 10 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 52 52 Phosphotyrosine; by ABL1.
{ECO:0000305|PubMed:19423701}.
MOD_RES 96 96 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 130 130 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 183 183 N6-acetyllysine.
{ECO:0000250|UniProtKB:P68040}.
MOD_RES 228 228 Phosphotyrosine.
{ECO:0000269|PubMed:11279199}.
MOD_RES 276 276 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 316 316 Phosphothreonine.
{ECO:0000250|UniProtKB:P68040}.
MUTAGEN 36 38 RDK->DDE: In DEmut; abolishes association
with the ribosome and ability to initiate
the ribosome quality control (RQC).
{ECO:0000269|PubMed:28132843}.
MUTAGEN 52 52 Y->F: No effect on binding to SRC.
Abolishes binding to PTK2/FAK1 and
reduces cell adhesion and foci formation.
{ECO:0000269|PubMed:11279199,
ECO:0000269|PubMed:12400005,
ECO:0000269|PubMed:19423701}.
MUTAGEN 57 57 R->A: Decreased binding to PTK2/FAK1;
when associated with A-60.
{ECO:0000269|PubMed:19423701}.
MUTAGEN 60 60 R->A: Decreased binding to PTK2/FAK1;
when associated with A-57.
{ECO:0000269|PubMed:19423701}.
MUTAGEN 127 127 K->A: Decreased binding to PTK2/FAK1;
when associated with A-130.
{ECO:0000269|PubMed:19423701}.
MUTAGEN 130 130 K->A: Decreased binding to PTK2/FAK1;
when associated with A-127.
{ECO:0000269|PubMed:19423701}.
MUTAGEN 140 140 Y->F: No effect on binding to SRC.
{ECO:0000269|PubMed:11279199,
ECO:0000269|PubMed:12400005}.
MUTAGEN 194 194 Y->F: No effect on binding to SRC.
{ECO:0000269|PubMed:11279199,
ECO:0000269|PubMed:12400005}.
MUTAGEN 228 228 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.
{ECO:0000269|PubMed:11279199,
ECO:0000269|PubMed:12400005}.
MUTAGEN 246 246 Y->F: Abolishes binding to SRC. Does not
abolish phosphorylation by SRC. Abolishes
phosphorylation by SRC; when associated
with F-228 and F-302.
{ECO:0000269|PubMed:11279199,
ECO:0000269|PubMed:12400005}.
MUTAGEN 302 302 Y->F: No effect on binding to SRC.
Abolishes phosphorylation by SRC; when
associated with F-228 and F-246.
{ECO:0000269|PubMed:11279199,
ECO:0000269|PubMed:12400005}.
CONFLICT 70 111 Missing (in Ref. 4; BAG53102).
{ECO:0000305}.
CONFLICT 94 94 T -> TRK (in Ref. 3; AAR24619).
{ECO:0000305}.
CONFLICT 221 221 L -> F (in Ref. 6; BAD96208).
{ECO:0000305}.
STRAND 4 11 {ECO:0000244|PDB:4AOW}.
STRAND 18 23 {ECO:0000244|PDB:4AOW}.
STRAND 30 35 {ECO:0000244|PDB:4AOW}.
STRAND 40 45 {ECO:0000244|PDB:4AOW}.
STRAND 48 50 {ECO:0000244|PDB:4AOW}.
STRAND 52 59 {ECO:0000244|PDB:4AOW}.
STRAND 66 71 {ECO:0000244|PDB:4AOW}.
STRAND 75 82 {ECO:0000244|PDB:4AOW}.
STRAND 85 91 {ECO:0000244|PDB:4AOW}.
TURN 92 95 {ECO:0000244|PDB:4AOW}.
STRAND 96 102 {ECO:0000244|PDB:4AOW}.
STRAND 108 113 {ECO:0000244|PDB:4AOW}.
STRAND 120 124 {ECO:0000244|PDB:4AOW}.
STRAND 129 132 {ECO:0000244|PDB:4AOW}.
STRAND 138 142 {ECO:0000244|PDB:4AOW}.
STRAND 144 146 {ECO:0000244|PDB:4AOW}.
STRAND 151 156 {ECO:0000244|PDB:4AOW}.
STRAND 160 162 {ECO:0000244|PDB:4AOW}.
STRAND 164 169 {ECO:0000244|PDB:4AOW}.
STRAND 174 178 {ECO:0000244|PDB:4AOW}.
TURN 179 182 {ECO:0000244|PDB:4AOW}.
STRAND 183 188 {ECO:0000244|PDB:4AOW}.
STRAND 195 200 {ECO:0000244|PDB:4AOW}.
STRAND 204 211 {ECO:0000244|PDB:4AOW}.
STRAND 215 220 {ECO:0000244|PDB:4AOW}.
TURN 221 224 {ECO:0000244|PDB:4AOW}.
STRAND 225 231 {ECO:0000244|PDB:4AOW}.
STRAND 236 241 {ECO:0000244|PDB:4AOW}.
STRAND 243 252 {ECO:0000244|PDB:4AOW}.
STRAND 255 260 {ECO:0000244|PDB:4AOW}.
TURN 261 264 {ECO:0000244|PDB:4AOW}.
STRAND 265 270 {ECO:0000244|PDB:4AOW}.
STRAND 286 291 {ECO:0000244|PDB:4AOW}.
STRAND 295 302 {ECO:0000244|PDB:4AOW}.
STRAND 307 313 {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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