Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

14-3-3 protein beta/alpha (Protein 1054) (Protein kinase C inhibitor protein 1) (KCIP-1) [Cleaved into: 14-3-3 protein beta/alpha, N-terminally processed]

 1433B_HUMAN             Reviewed;         246 AA.
P31946; A8K9K2; E1P616;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 202.
RecName: Full=14-3-3 protein beta/alpha;
AltName: Full=Protein 1054;
AltName: Full=Protein kinase C inhibitor protein 1;
Short=KCIP-1;
Contains:
RecName: Full=14-3-3 protein beta/alpha, N-terminally processed;
Name=YWHAB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Keratinocyte;
PubMed=8515476; DOI=10.1006/jmbi.1993.1346;
Leffers H., Madsen P., Rasmussen H.H., Honore B., Andersen A.H.,
Walbum E., Vandekerckhove J., Celis J.E.;
"Molecular cloning and expression of the transformation sensitive
epithelial marker stratifin. A member of a protein family that has
been involved in the protein kinase C signalling pathway.";
J. Mol. Biol. 231:982-998(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
TISSUE=Thymus;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[4]
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=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).
[6]
PROTEIN SEQUENCE OF 1-11; 30-51; 63-73 AND 130-159, INTERACTION WITH
PI4KB; TBC1D22A AND TBC1D22B, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=23572552; DOI=10.1128/mBio.00098-13;
Greninger A.L., Knudsen G.M., Betegon M., Burlingame A.L.,
DeRisi J.L.;
"ACBD3 interaction with TBC1 domain 22 protein is differentially
affected by enteroviral and kobuviral 3A protein binding.";
MBio 4:E00098-E00098(2013).
[7]
PROTEIN SEQUENCE OF 1-11; 14-57; 63-70; 106-117; 130-169 AND 215-246,
CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1 AND THR-2, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Colon carcinoma;
Bienvenut W.V., Zebisch A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[8]
PROTEIN SEQUENCE OF 3-20.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[9]
INTERACTION WITH AANAT.
PubMed=11427721; DOI=10.1073/pnas.141118798;
Ganguly S., Gastel J.A., Weller J.L., Schwartz C., Jaffe H.,
Namboodiri M.A., Coon S.L., Hickman A.B., Rollag M., Obsil T.,
Beauverger P., Ferry G., Boutin J.A., Klein D.C.;
"Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-
3-3-binding switch in melatonin synthesis.";
Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001).
[10]
INTERACTION WITH CRTC2.
PubMed=15454081; DOI=10.1016/j.cell.2004.09.015;
Screaton R.A., Conkright M.D., Katoh Y., Best J.L., Canettieri G.,
Jeffries S., Guzman E., Niessen S., Yates J.R. III, Takemori H.,
Okamoto M., Montminy M.;
"The CREB coactivator TORC2 functions as a calcium- and cAMP-sensitive
coincidence detector.";
Cell 119:61-74(2004).
[11]
INTERACTION WITH YWHAB.
PubMed=15538381; DOI=10.1038/sj.emboj.7600477;
Schmidlin M., Lu M., Leuenberger S.A., Stoecklin G., Mallaun M.,
Gross B., Gherzi R., Hess D., Hemmings B.A., Moroni C.;
"The ARE-dependent mRNA-destabilizing activity of BRF1 is regulated by
protein kinase B.";
EMBO J. 23:4760-4769(2004).
[12]
INTERACTION WITH SSH1.
PubMed=15159416; DOI=10.1083/jcb.200401136;
Nagata-Ohashi K., Ohta Y., Goto K., Chiba S., Mori R., Nishita M.,
Ohashi K., Kousaka K., Iwamatsu A., Niwa R., Uemura T., Mizuno K.;
"A pathway of neuregulin-induced activation of cofilin-phosphatase
Slingshot and cofilin in lamellipodia.";
J. Cell Biol. 165:465-471(2004).
[13]
INTERACTION WITH ABL1.
PubMed=15696159; DOI=10.1038/ncb1228;
Yoshida K., Yamaguchi T., Natsume T., Kufe D., Miki Y.;
"JNK phosphorylation of 14-3-3 proteins regulates nuclear targeting of
c-Abl in the apoptotic response to DNA damage.";
Nat. Cell Biol. 7:278-285(2005).
[14]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[15]
INTERACTION WITH YAP1.
PubMed=17974916; DOI=10.1101/gad.1602907;
Zhao B., Wei X., Li W., Udan R.S., Yang Q., Kim J., Xie J.,
Ikenoue T., Yu J., Li L., Zheng P., Ye K., Chinnaiyan A., Halder G.,
Lai Z.C., Guan K.L.;
"Inactivation of YAP oncoprotein by the Hippo pathway is involved in
cell contact inhibition and tissue growth control.";
Genes Dev. 21:2747-2761(2007).
[16]
INTERACTION WITH ROR2, FUNCTION, PHOSPHORYLATION, DIMERIZATION, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17717073; DOI=10.1210/me.2007-0323;
Liu Y., Ross J.F., Bodine P.V.N., Billiard J.;
"Homodimerization of Ror2 tyrosine kinase receptor induces 14-3-
3(beta) phosphorylation and promotes osteoblast differentiation and
bone formation.";
Mol. Endocrinol. 21:3050-3061(2007).
[17]
INTERACTION WITH SIRT2.
PubMed=18249187; DOI=10.1016/j.bbrc.2008.01.114;
Jin Y.H., Kim Y.J., Kim D.W., Baek K.H., Kang B.Y., Yeo C.Y.,
Lee K.Y.;
"Sirt2 interacts with 14-3-3 beta/gamma and down-regulates the
activity of p53.";
Biochem. Biophys. Res. Commun. 368:690-695(2008).
[18]
INTERACTION WITH GAB2.
PubMed=19172738; DOI=10.1038/emboj.2008.159;
Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P.,
Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D.,
Guilhaus M., James D.E., Daly R.J.;
"Phosphorylation-dependent binding of 14-3-3 terminates signalling by
the Gab2 docking protein.";
EMBO J. 27:2305-2316(2008).
[19]
INTERACTION WITH SLITRK1.
PubMed=19640509; DOI=10.1016/j.biopsych.2009.05.033;
Kajiwara Y., Buxbaum J.D., Grice D.E.;
"SLITRK1 binds 14-3-3 and regulates neurite outgrowth in a
phosphorylation-dependent manner.";
Biol. Psychiatry 66:918-925(2009).
[20]
FUNCTION, AND INTERACTION WITH SRPK2.
PubMed=19592491; DOI=10.1074/jbc.M109.026237;
Jang S.W., Liu X., Fu H., Rees H., Yepes M., Levey A., Ye K.;
"Interaction of Akt-phosphorylated SRPK2 with 14-3-3 mediates cell
cycle and cell death in neurons.";
J. Biol. Chem. 284:24512-24525(2009).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70 AND LYS-117, 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).
[23]
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).
[24]
FUNCTION, AND INTERACTION WITH AKAP13.
PubMed=21224381; DOI=10.1074/jbc.M110.185645;
Cariolato L., Cavin S., Diviani D.;
"A-kinase anchoring protein (AKAP)-Lbc anchors a PKN-based signaling
complex involved in alpha1-adrenergic receptor-induced p38
activation.";
J. Biol. Chem. 286:7925-7937(2011).
[25]
INTERACTION WITH SOS1.
PubMed=22827337; DOI=10.1042/BJ20120938;
Saha M., Carriere A., Cheerathodi M., Zhang X., Lavoie G., Rush J.,
Roux P.P., Ballif B.A.;
"RSK phosphorylates SOS1 creating 14-3-3-docking sites and negatively
regulating MAPK activation.";
Biochem. J. 447:159-166(2012).
[26]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, ACETYLATION
[LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM SHORT), 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).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
[28]
INTERACTION WITH HERPES SIMPLEX VIRUS 1 UL46 (MICROBIAL INFECTION).
PubMed=23938468; DOI=10.1074/mcp.M113.030866;
Lin A.E., Greco T.M., Dohner K., Sodeik B., Cristea I.M.;
"A proteomic perspective of inbuilt viral protein regulation: pUL46
tegument protein is targeted for degradation by ICP0 during herpes
simplex virus type 1 infection.";
Mol. Cell. Proteomics 12:3237-3252(2013).
[29]
INTERACTION WITH MYO1C.
PubMed=24636949; DOI=10.1016/j.jmb.2014.03.004;
Stefan Munnich M.H., Manstein D.J.;
"Crystal structure of human myosin 1c - the motor in GLUT4 exocytosis:
implications for Ca(2+)-regulation and 14-3-3 binding.";
J. Mol. Biol. 426:2070-2081(2014).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND 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).
[31]
INTERACTION WITH DAPK2.
PubMed=26047703; DOI=10.1016/j.bbrc.2015.05.105;
Yuasa K., Ota R., Matsuda S., Isshiki K., Inoue M., Tsuji A.;
"Suppression of death-associated protein kinase 2 by interaction with
14-3-3 proteins.";
Biochem. Biophys. Res. Commun. 464:70-75(2015).
[32]
INTERACTION WITH RIPOR2.
PubMed=25588844; DOI=10.1242/jcs.161497;
Gao K., Tang W., Li Y., Zhang P., Wang D., Yu L., Wang C., Wu D.;
"Front-signal-dependent accumulation of the RHOA inhibitor FAM65B at
leading edges polarizes neutrophils.";
J. Cell Sci. 128:992-1000(2015).
[33]
ACETYLATION AT THR-2, AND CLEAVAGE OF INITIATOR METHIONINE.
PubMed=25489052; DOI=10.1093/hmg/ddu611;
Myklebust L.M., Van Damme P., Stoeve S.I., Doerfel M.J., Abboud A.,
Kalvik T.V., Grauffel C., Jonckheere V., Wu Y., Swensen J., Kaasa H.,
Liszczak G., Marmorstein R., Reuter N., Lyon G.J., Gevaert K.,
Arnesen T.;
"Biochemical and cellular analysis of Ogden syndrome reveals
downstream Nt-acetylation defects.";
Hum. Mol. Genet. 24:1956-1976(2015).
[34]
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).
[35]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-239, IDENTIFICATION BY MASS
SPECTROMETRY, INTERACTION WITH PHOSPHOSERINE MOTIFS, AND SUBUNIT.
PubMed=17085597; DOI=10.1073/pnas.0605779103;
Yang X., Lee W.H., Sobott F., Papagrigoriou E., Robinson C.V.,
Grossmann J.G., Sundstroem M., Doyle D.A., Elkins J.M.;
"Structural basis for protein-protein interactions in the 14-3-3
protein family.";
Proc. Natl. Acad. Sci. U.S.A. 103:17237-17242(2006).
[36]
VARIANT ILE-99.
PubMed=21248752; DOI=10.1038/nature09639;
Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P.,
Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A.,
Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C.,
Jia M., Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A.,
Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S.,
Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A.,
Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C.,
Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R.,
Futreal P.A.;
"Exome sequencing identifies frequent mutation of the SWI/SNF complex
gene PBRM1 in renal carcinoma.";
Nature 469:539-542(2011).
-!- FUNCTION: Adapter protein implicated in the regulation of a large
spectrum of both general and specialized signaling pathways. Binds
to a large number of partners, usually by recognition of a
phosphoserine or phosphothreonine motif. Binding generally results
in the modulation of the activity of the binding partner. Negative
regulator of osteogenesis. Blocks the nuclear translocation of the
phosphorylated form (by AKT1) of SRPK2 and antagonizes its
stimulatory effect on cyclin D1 expression resulting in blockage
of neuronal apoptosis elicited by SRPK2. Negative regulator of
signaling cascades that mediate activation of MAP kinases via
AKAP13. {ECO:0000269|PubMed:17717073, ECO:0000269|PubMed:19592491,
ECO:0000269|PubMed:21224381}.
-!- SUBUNIT: Homodimer (PubMed:17717073). Interacts with SAMSN1 and
PRKCE (By similarity). Interacts with AKAP13 (PubMed:21224381).
Interacts with SSH1 and TORC2/CRTC2 (PubMed:15454081,
PubMed:15159416). Interacts with ABL1; the interaction results in
cytoplasmic location of ABL1 and inhibition of cABL-mediated
apoptosis (PubMed:15696159). Interacts with ROR2 (dimer); the
interaction results in phosphorylation of YWHAB on tyrosine
residues (PubMed:17717073). Interacts with GAB2 (PubMed:19172738).
Interacts with YAP1 (phosphorylated form) (PubMed:17974916).
Interacts with the phosphorylated (by AKT1) form of SRPK2
(PubMed:19592491). Interacts with PKA-phosphorylated AANAT
(PubMed:11427721). Interacts with MYO1C (PubMed:24636949).
Interacts with SIRT2 (PubMed:18249187). Interacts with the 'Thr-
369' phosphorylated form of DAPK2 (PubMed:26047703). Interacts
with PI4KB, TBC1D22A and TBC1D22B (PubMed:23572552). Interacts
with the 'Ser-1134' and 'Ser-1161' phosphorylated form of SOS1
(PubMed:22827337). Interacts (via phosphorylated form) with YWHAB;
this interaction occurs in a protein kinase AKT1-dependent manner
(PubMed:15538381). Interacts with SLITRK1 (PubMed:19640509).
Interacts with SYNPO2 (phosphorylated form); YWHAB competes with
ACTN2 for interaction with SYNPO2 (By similarity). Interacts with
RIPOR2 (via phosphorylated form) isoform 2; this interaction
occurs in a chemokine-dependent manner and does not compete for
binding of RIPOR2 with RHOA nor blocks inhibition of RIPOR2-
mediated RHOA activity (PubMed:25588844).
{ECO:0000250|UniProtKB:Q9CQV8, ECO:0000269|PubMed:11427721,
ECO:0000269|PubMed:15159416, ECO:0000269|PubMed:15454081,
ECO:0000269|PubMed:15538381, ECO:0000269|PubMed:15696159,
ECO:0000269|PubMed:17085597, ECO:0000269|PubMed:17717073,
ECO:0000269|PubMed:17974916, ECO:0000269|PubMed:18249187,
ECO:0000269|PubMed:19172738, ECO:0000269|PubMed:19592491,
ECO:0000269|PubMed:19640509, ECO:0000269|PubMed:21224381,
ECO:0000269|PubMed:22827337, ECO:0000269|PubMed:23572552,
ECO:0000269|PubMed:24636949, ECO:0000269|PubMed:25588844,
ECO:0000269|PubMed:26047703}.
-!- SUBUNIT: (Microbial infection) Interacts with herpes simplex virus
1 protein UL46. {ECO:0000269|PubMed:23938468}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-359815, EBI-359815;
Q76353:- (xeno); NbExp=3; IntAct=EBI-359815, EBI-6248077;
Q9P0K1-3:ADAM22; NbExp=2; IntAct=EBI-359815, EBI-1567267;
P15056:BRAF; NbExp=3; IntAct=EBI-359815, EBI-365980;
P22681:CBL; NbExp=3; IntAct=EBI-359815, EBI-518228;
O00257:CBX4; NbExp=2; IntAct=EBI-359815, EBI-722425;
P30304:CDC25A; NbExp=10; IntAct=EBI-359815, EBI-747671;
P30305:CDC25B; NbExp=5; IntAct=EBI-359815, EBI-1051746;
P30307:CDC25C; NbExp=4; IntAct=EBI-359815, EBI-974439;
O94921:CDK14; NbExp=5; IntAct=EBI-359815, EBI-1043945;
P67828:CSNK1A1 (xeno); NbExp=3; IntAct=EBI-359815, EBI-7540603;
Q9NYF0:DACT1; NbExp=4; IntAct=EBI-359815, EBI-3951744;
Q13627-2:DYRK1A; NbExp=3; IntAct=EBI-359815, EBI-1053621;
Q9UQC2:GAB2; NbExp=4; IntAct=EBI-359815, EBI-975200;
P55040:GEM; NbExp=3; IntAct=EBI-359815, EBI-744104;
P55041:Gem (xeno); NbExp=3; IntAct=EBI-359815, EBI-7082069;
P56524:HDAC4; NbExp=3; IntAct=EBI-359815, EBI-308629;
Q11184:let-756 (xeno); NbExp=2; IntAct=EBI-359815, EBI-3843983;
Q5S007:LRRK2; NbExp=5; IntAct=EBI-359815, EBI-5323863;
Q99759:MAP3K3; NbExp=2; IntAct=EBI-359815, EBI-307281;
Q99683:MAP3K5; NbExp=3; IntAct=EBI-359815, EBI-476263;
Q7KZI7:MARK2; NbExp=3; IntAct=EBI-359815, EBI-516560;
P27448:MARK3; NbExp=4; IntAct=EBI-359815, EBI-707595;
P26045:PTPN3; NbExp=4; IntAct=EBI-359815, EBI-1047946;
P04049:RAF1; NbExp=18; IntAct=EBI-359815, EBI-365996;
Q96TC7:RMDN3; NbExp=5; IntAct=EBI-359815, EBI-1056589;
P61587:RND3; NbExp=2; IntAct=EBI-359815, EBI-1111534;
P61588:Rnd3 (xeno); NbExp=5; IntAct=EBI-359815, EBI-6930266;
P78362:SRPK2; NbExp=2; IntAct=EBI-359815, EBI-593303;
Q8WYL5:SSH1; NbExp=3; IntAct=EBI-359815, EBI-1222387;
Q91YE8:Synpo2 (xeno); NbExp=3; IntAct=EBI-359815, EBI-7623057;
P49815:TSC2; NbExp=4; IntAct=EBI-359815, EBI-396587;
P46937:YAP1; NbExp=6; IntAct=EBI-359815, EBI-1044059;
P62258:YWHAE; NbExp=4; IntAct=EBI-359815, EBI-356498;
P61981:YWHAG; NbExp=2; IntAct=EBI-359815, EBI-359832;
P27348:YWHAQ; NbExp=2; IntAct=EBI-359815, EBI-359854;
P22893:Zfp36 (xeno); NbExp=5; IntAct=EBI-359815, EBI-647803;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17081065}.
Melanosome {ECO:0000269|PubMed:17081065}. Note=Identified by mass
spectrometry in melanosome fractions from stage I to stage IV.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=Long;
IsoId=P31946-1; Sequence=Displayed;
Name=Short;
IsoId=P31946-2; Sequence=VSP_018632;
Note=Contains a N-acetylmethionine at position 1.
{ECO:0000244|PubMed:22814378};
-!- PTM: The alpha, brain-specific form differs from the beta form in
being phosphorylated. Phosphorylated on Ser-60 by protein kinase C
delta type catalytic subunit in a sphingosine-dependent fashion.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X57346; CAA40621.1; -; mRNA.
EMBL; AK292717; BAF85406.1; -; mRNA.
EMBL; AL008725; CAA15497.1; -; Genomic_DNA.
EMBL; CH471077; EAW75893.1; -; Genomic_DNA.
EMBL; CH471077; EAW75894.1; -; Genomic_DNA.
EMBL; CH471077; EAW75896.1; -; Genomic_DNA.
EMBL; BC001359; AAH01359.1; -; mRNA.
CCDS; CCDS13339.1; -. [P31946-1]
PIR; S34755; S34755.
RefSeq; NP_003395.1; NM_003404.4. [P31946-1]
RefSeq; NP_647539.1; NM_139323.3. [P31946-1]
RefSeq; XP_016883528.1; XM_017028039.1. [P31946-1]
UniGene; Hs.643544; -.
PDB; 2BQ0; X-ray; 2.50 A; A/B=2-239.
PDB; 2C23; X-ray; 2.65 A; A=2-239.
PDB; 4DNK; X-ray; 2.20 A; A/B=1-246.
PDB; 5N10; X-ray; 1.60 A; A/B=1-246.
PDBsum; 2BQ0; -.
PDBsum; 2C23; -.
PDBsum; 4DNK; -.
PDBsum; 5N10; -.
ProteinModelPortal; P31946; -.
SMR; P31946; -.
BioGrid; 113361; 353.
CORUM; P31946; -.
DIP; DIP-743N; -.
ELM; P31946; -.
IntAct; P31946; 270.
MINT; MINT-99570; -.
STRING; 9606.ENSP00000300161; -.
ChEMBL; CHEMBL3710403; -.
iPTMnet; P31946; -.
PhosphoSitePlus; P31946; -.
SwissPalm; P31946; -.
DMDM; 1345590; -.
OGP; P31946; -.
REPRODUCTION-2DPAGE; IPI00216318; -.
EPD; P31946; -.
PaxDb; P31946; -.
PeptideAtlas; P31946; -.
PRIDE; P31946; -.
TopDownProteomics; P31946-1; -. [P31946-1]
TopDownProteomics; P31946-2; -. [P31946-2]
DNASU; 7529; -.
Ensembl; ENST00000353703; ENSP00000300161; ENSG00000166913. [P31946-1]
Ensembl; ENST00000372839; ENSP00000361930; ENSG00000166913. [P31946-1]
GeneID; 7529; -.
KEGG; hsa:7529; -.
CTD; 7529; -.
DisGeNET; 7529; -.
EuPathDB; HostDB:ENSG00000166913.12; -.
GeneCards; YWHAB; -.
HGNC; HGNC:12849; YWHAB.
HPA; CAB003759; -.
HPA; HPA007925; -.
HPA; HPA011212; -.
MIM; 601289; gene.
neXtProt; NX_P31946; -.
OpenTargets; ENSG00000166913; -.
PharmGKB; PA37438; -.
eggNOG; KOG0841; Eukaryota.
eggNOG; COG5040; LUCA.
GeneTree; ENSGT00760000119116; -.
HOGENOM; HOG000240379; -.
HOVERGEN; HBG050423; -.
InParanoid; P31946; -.
KO; K16197; -.
OMA; KKQQMGR; -.
OrthoDB; EOG091G0VKY; -.
PhylomeDB; P31946; -.
TreeFam; TF102003; -.
Reactome; R-HSA-111447; Activation of BAD and translocation to mitochondria.
Reactome; R-HSA-1445148; Translocation of GLUT4 to the plasma membrane.
Reactome; R-HSA-165159; mTOR signalling.
Reactome; R-HSA-166208; mTORC1-mediated signalling.
Reactome; R-HSA-170968; Frs2-mediated activation.
Reactome; R-HSA-170984; ARMS-mediated activation.
Reactome; R-HSA-2028269; Signaling by Hippo.
Reactome; R-HSA-392517; Rap1 signalling.
Reactome; R-HSA-450385; Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA.
Reactome; R-HSA-450513; Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA.
Reactome; R-HSA-5625740; RHO GTPases activate PKNs.
Reactome; R-HSA-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-HSA-5673000; RAF activation.
Reactome; R-HSA-5674135; MAP2K and MAPK activation.
Reactome; R-HSA-5675221; Negative regulation of MAPK pathway.
Reactome; R-HSA-6802946; Signaling by moderate kinase activity BRAF mutants.
Reactome; R-HSA-6802948; Signaling by high-kinase activity BRAF mutants.
Reactome; R-HSA-6802949; Signaling by RAS mutants.
Reactome; R-HSA-6802952; Signaling by BRAF and RAF fusions.
Reactome; R-HSA-6802955; Paradoxical activation of RAF signaling by kinase inactive BRAF.
Reactome; R-HSA-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
SignaLink; P31946; -.
SIGNOR; P31946; -.
ChiTaRS; YWHAB; human.
EvolutionaryTrace; P31946; -.
GeneWiki; YWHAB; -.
GenomeRNAi; 7529; -.
PRO; PR:P31946; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000166913; -.
CleanEx; HS_YWHAB; -.
ExpressionAtlas; P31946; baseline and differential.
Genevisible; P31946; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:GOC.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0017053; C:transcriptional repressor complex; IEA:Ensembl.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0051219; F:phosphoprotein binding; IPI:BHF-UCL.
GO; GO:0050815; F:phosphoserine residue binding; IPI:BHF-UCL.
GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
GO; GO:0051220; P:cytoplasmic sequestering of protein; IDA:BHF-UCL.
GO; GO:0035329; P:hippo signaling; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0045744; P:negative regulation of G-protein coupled receptor protein signaling pathway; IMP:UniProtKB.
GO; GO:0035308; P:negative regulation of protein dephosphorylation; IDA:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:0043085; P:positive regulation of catalytic activity; IDA:BHF-UCL.
GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
GO; GO:0051291; P:protein heterooligomerization; IEA:Ensembl.
GO; GO:0006605; P:protein targeting; IEA:Ensembl.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 1.20.190.20; -; 1.
InterPro; IPR000308; 14-3-3.
InterPro; IPR023409; 14-3-3_CS.
InterPro; IPR036815; 14-3-3_dom_sf.
InterPro; IPR023410; 14-3-3_domain.
PANTHER; PTHR18860; PTHR18860; 1.
Pfam; PF00244; 14-3-3; 1.
PIRSF; PIRSF000868; 14-3-3; 1.
PRINTS; PR00305; 1433ZETA.
SMART; SM00101; 14_3_3; 1.
SUPFAM; SSF48445; SSF48445; 1.
PROSITE; PS00796; 1433_1; 1.
PROSITE; PS00797; 1433_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative initiation; Complete proteome;
Cytoplasm; Direct protein sequencing; Host-virus interaction;
Isopeptide bond; Nitration; Phosphoprotein; Polymorphism;
Reference proteome; Ubl conjugation.
CHAIN 1 246 14-3-3 protein beta/alpha.
/FTId=PRO_0000367900.
INIT_MET 1 1 Removed; alternate.
{ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:25489052,
ECO:0000269|Ref.7}.
CHAIN 2 246 14-3-3 protein beta/alpha, N-terminally
processed.
/FTId=PRO_0000000003.
SITE 58 58 Interaction with phosphoserine on
interacting protein. {ECO:0000250}.
SITE 129 129 Interaction with phosphoserine on
interacting protein. {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine; in 14-3-3 protein
beta/alpha; alternate.
{ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.7}.
MOD_RES 2 2 N-acetylthreonine; in 14-3-3 protein
beta/alpha, N-terminally processed.
{ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:25489052,
ECO:0000269|Ref.7}.
MOD_RES 2 2 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 5 5 N6-acetyllysine.
{ECO:0000250|UniProtKB:P27348}.
MOD_RES 51 51 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P27348}.
MOD_RES 60 60 Phosphoserine.
{ECO:0000250|UniProtKB:Q9CQV8}.
MOD_RES 70 70 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 84 84 Nitrated tyrosine.
{ECO:0000250|UniProtKB:Q9CQV8}.
MOD_RES 106 106 Nitrated tyrosine.
{ECO:0000250|UniProtKB:Q9CQV8}.
MOD_RES 117 117 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 186 186 Phosphoserine.
{ECO:0000250|UniProtKB:P68251}.
MOD_RES 232 232 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
CROSSLNK 51 51 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P27348}.
VAR_SEQ 1 2 Missing (in isoform Short).
{ECO:0000305}.
/FTId=VSP_018632.
VARIANT 99 99 V -> I (found in a renal cell carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:21248752}.
/FTId=VAR_064762.
HELIX 5 17 {ECO:0000244|PDB:4DNK}.
HELIX 21 33 {ECO:0000244|PDB:4DNK}.
HELIX 40 69 {ECO:0000244|PDB:4DNK}.
HELIX 75 105 {ECO:0000244|PDB:4DNK}.
HELIX 107 110 {ECO:0000244|PDB:4DNK}.
HELIX 114 133 {ECO:0000244|PDB:4DNK}.
HELIX 139 161 {ECO:0000244|PDB:4DNK}.
HELIX 167 182 {ECO:0000244|PDB:4DNK}.
HELIX 187 202 {ECO:0000244|PDB:4DNK}.
HELIX 203 207 {ECO:0000244|PDB:4DNK}.
TURN 210 212 {ECO:0000244|PDB:4DNK}.
HELIX 213 232 {ECO:0000244|PDB:4DNK}.
SEQUENCE 246 AA; 28082 MW; 6BE1A9BF97468017 CRC64;
MTMDKSELVQ KAKLAEQAER YDDMAAAMKA VTEQGHELSN EERNLLSVAY KNVVGARRSS
WRVISSIEQK TERNEKKQQM GKEYREKIEA ELQDICNDVL ELLDKYLIPN ATQPESKVFY
LKMKGDYFRY LSEVASGDNK QTTVSNSQQA YQEAFEISKK EMQPTHPIRL GLALNFSVFY
YEILNSPEKA CSLAKTAFDE AIAELDTLNE ESYKDSTLIM QLLRDNLTLW TSENQGDEGD
AGEGEN


Related products :

Catalog number Product name Quantity
20-272-190770 14 - 3 - 3 beta - Mouse monoclonal [4E1] to 14 - 3 - 3 beta; Protein kinase C inhibitor protein 1; KCIP-1; Protein 1054 Monoclonal 0.05 mg
18-272-196318 14 - 3 - 3 beta - Rabbit polyclonal to 14 - 3 - 3 beta; Protein kinase C inhibitor protein 1; KCIP-1; Protein 1054 Polyclonal 0.5 ml
18-272-196319 14 - 3 - 3 beta prediluted - Rabbit polyclonal to 14 - 3 - 3 beta prediluted; Protein kinase C inhibitor protein 1; KCIP-1; Protein 1054 Polyclonal 7 ml
18-003-43288 14-3-3 protein beta_alpha - Protein kinase C inhibitor protein 1; KCIP-1; Protein 1054 Polyclonal 0.05 mg Aff Pur
E1111b ELISA kit 14-3-3 protein beta_alpha,Bos taurus,Bovine,KCIP-1,Protein kinase C inhibitor protein 1,YWHAB 96T
E1111b ELISA 14-3-3 protein beta_alpha,Bos taurus,Bovine,KCIP-1,Protein kinase C inhibitor protein 1,YWHAB 96T
U1111b CLIA 14-3-3 protein beta_alpha,Bos taurus,Bovine,KCIP-1,Protein kinase C inhibitor protein 1,YWHAB 96T
10-288-22342F 14-3-3 protein zeta_delta - Protein kinase C inhibitor protein 1; KCIP-1 0.05 mg
10-288-22342F 14-3-3 protein zeta_delta - Protein kinase C inhibitor protein 1; KCIP-1 0.1 mg
20-272-191983 AP2 alpha + beta - Mouse monoclonal [A6 _ 2 _ 2] to AP2 alpha + beta; AP2-alpha; Activating enhancer-binding protein 2 alpha; AP-2 transcription factor; Activator protein 2; AP-2 Monoclonal 0.1 mg
18-272-195567 AP2 alpha + beta - Rabbit polyclonal to AP2 alpha + beta; AP2-alpha; Activating enhancer-binding protein 2 alpha; AP-2 transcription factor; Activator protein 2; AP-2 Polyclonal 0.05 ml
18-785-210002 14-3-3 zeta (Ab-58) - Protein kinase C inhibitor protein 1; KCIP-1 Polyclonal 0.1 mg
18-785-210002 14-3-3 zeta (Ab-58) - Protein kinase C inhibitor protein 1; KCIP-1 Polyclonal 0.05 mg
EIAAB14705 F1aa,F1A-alpha,FEM1b,Fem1b,FEM1-beta,Fem-1-like death receptor-binding protein alpha,Fem-1-like in apoptotic pathway protein alpha,Kiaa0396,Mouse,mt-Fem,Mus musculus,Protein fem-1 homolog B
18-785-210001 14-3-3 zeta (Phospho-Ser58) - Protein kinase C inhibitor protein 1; KCIP-1 Polyclonal 0.05 mg
18-785-210001 14-3-3 zeta (Phospho-Ser58) - Protein kinase C inhibitor protein 1; KCIP-1 Polyclonal 0.1 mg
EIAAB14702 F1AA,F1A-alpha,FEM1b,FEM1B,FEM1-beta,Fem-1-like death receptor-binding protein alpha,Fem-1-like in apoptotic pathway protein alpha,Homo sapiens,Human,KIAA0396,Protein fem-1 homolog B
EIAAB31334 Bos taurus,Bovine,PKN,PKN1,PRK1,PRKCL1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein kinase PKN-alpha,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine
EIAAB05849 C-C motif chemokine 4-like,CCL4L,CCL4L1,Homo sapiens,Human,LAG1,LAG-1,Lymphocyte activation gene 1 protein,Macrophage inflammatory protein 1-beta,MIP-1-beta,Monocyte adherence-induced protein 5-alpha,
10-782-55114 Ribosomal protein S6 kinase beta-1 - EC 2.7.11.1; Ribosomal protein S6 kinase I; S6K; S6K1; 70 kDa ribosomal protein S6 kinase 1; p70 S6 kinase alpha; p70(S6K)-alpha; p70-S6K; P70S6K; p70-alpha N_A 0.01 mg
10-782-55114 Ribosomal protein S6 kinase beta-1 - EC 2.7.11.1; Ribosomal protein S6 kinase I; S6K; S6K1; 70 kDa ribosomal protein S6 kinase 1; p70 S6 kinase alpha; p70(S6K)-alpha; p70-S6K; P70S6K; p70-alpha N_A 0.02 mg
10-782-55114 Ribosomal protein S6 kinase beta-1 - EC 2.7.11.1; Ribosomal protein S6 kinase I; S6K; S6K1; 70 kDa ribosomal protein S6 kinase 1; p70 S6 kinase alpha; p70(S6K)-alpha; p70-S6K; P70S6K; p70-alpha N_A 0.005 mg
10-782-55114 Ribosomal protein S6 kinase beta-1 - EC 2.7.11.1; Ribosomal protein S6 kinase I; S6K; S6K1; 70 kDa ribosomal protein S6 kinase 1; p70 S6 kinase alpha; p70(S6K)-alpha; p70-S6K; P70S6K; p70-alpha N_A 0.001 mg
U0094h CLIA C-X-C motif chemokine 2,CXCL2,GRO2,GROB,Gro-beta,Growth-regulated protein beta,Homo sapiens,Human,Macrophage inflammatory protein 2-alpha,MIP2A,MIP2-alpha,SCYB2 96T
E0094h ELISA C-X-C motif chemokine 2,CXCL2,GRO2,GROB,Gro-beta,Growth-regulated protein beta,Homo sapiens,Human,Macrophage inflammatory protein 2-alpha,MIP2A,MIP2-alpha,SCYB2 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur