1433F_MOUSE
ID 1433F_MOUSE Reviewed; 246 AA.
AC P68510; P11576; P70198; Q3TGZ9;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=14-3-3 protein eta;
GN Name=Ywhah;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH CDK16.
RC TISSUE=Brain;
RX PubMed=9197417; DOI=10.1007/s004380050453;
RA Sladeczek F., Camonis J.H., Burnol A.-F., Le Bouffant F.;
RT "The Cdk-like protein PCTAIRE-1 from mouse brain associates with p11 and
RT 14-3-3 proteins.";
RL Mol. Gen. Genet. 254:571-577(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/Sv;
RA Takihara Y., Irie K., Nomura M., Motaleb M., Matsumoto K., Shimada K.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9738002; DOI=10.1074/jbc.273.39.25356;
RA Tang S.J., Seun T.-C., McInnes R.R., Buchwald M.;
RT "Association of the TLX-2 homeodomain and 14-3-3eta signaling proteins.";
RL J. Biol. Chem. 273:25356-25363(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12008017; DOI=10.1016/s0169-328x(02)00129-8;
RA Toyooka K., Muratake T., Watanabe H., Hayashi S., Ichikawa T., Usui H.,
RA Washiyama K., Kumanishi T., Takahashi Y.;
RT "Isolation and structure of the mouse 14-3-3 eta chain gene and the
RT distribution of 14-3-3 eta mRNA in the mouse brain.";
RL Brain Res. Mol. Brain Res. 100:13-20(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart, Kidney, and Sympathetic ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 13-56; 62-69; 92-106; 111-120; 133-172 AND 199-227, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [8]
RP PHOSPHORYLATION AT SER-59.
RX PubMed=9705322; DOI=10.1074/jbc.273.34.21834;
RA Megidish T., Cooper J., Zhang L., Fu H., Hakomori S.;
RT "A novel sphingosine-dependent protein kinase (SDK1) specifically
RT phosphorylates certain isoforms of 14-3-3 protein.";
RL J. Biol. Chem. 273:21834-21845(1998).
RN [9]
RP INTERACTION WITH ARHGEF28.
RX PubMed=11533041; DOI=10.1074/jbc.m107709200;
RA Zhai J., Lin H., Shamim M., Schlaepfer W.W., Canete-Soler R.;
RT "Identification of a novel interaction of 14-3-3 with p190RhoGEF.";
RL J. Biol. Chem. 276:41318-41324(2001).
RN [10]
RP INTERACTION WITH KCNK18.
RX PubMed=18397886; DOI=10.1074/jbc.m800712200;
RA Czirjak G., Vuity D., Enyedi P.;
RT "Phosphorylation-dependent binding of 14-3-3 proteins controls TRESK
RT regulation.";
RL J. Biol. Chem. 283:15672-15680(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP INTERACTION WITH SAMSN1.
RX PubMed=20478393; DOI=10.1016/j.biocel.2010.05.004;
RA Brandt S., Ellwanger K., Beuter-Gunia C., Schuster M., Hausser A.,
RA Schmitz I., Beer-Hammer S.;
RT "SLy2 targets the nuclear SAP30/HDAC1 complex.";
RL Int. J. Biochem. Cell Biol. 42:1472-1481(2010).
RN [13]
RP INTERACTION WITH DAPK2.
RX PubMed=26047703; DOI=10.1016/j.bbrc.2015.05.105;
RA Yuasa K., Ota R., Matsuda S., Isshiki K., Inoue M., Tsuji A.;
RT "Suppression of death-associated protein kinase 2 by interaction with 14-3-
RT 3 proteins.";
RL Biochem. Biophys. Res. Commun. 464:70-75(2015).
CC -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC spectrum of both general and specialized signaling pathways. Binds to a
CC large number of partners, usually by recognition of a phosphoserine or
CC phosphothreonine motif. Binding generally results in the modulation of
CC the activity of the binding partner. Negatively regulates the kinase
CC activity of PDPK1 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with many nuclear hormone
CC receptors and cofactors including AR, ESR1, ESR2, MC2R, NR3C1, NRIP1,
CC PPARBP and THRA. Interacts with ABL1 (phosphorylated form); the
CC interaction retains it in the cytoplasm. Weakly interacts with CDKN1B
CC (By similarity). Interacts with ARHGEF28 and CDK16. Interacts with
CC KCNK18 in a phosphorylation-dependent manner. Interacts with SAMSN1.
CC Interacts with the 'Ser-241' phosphorylated form of PDPK1 (By
CC similarity). Interacts with the 'Thr-369' phosphorylated form of DAPK2
CC (PubMed:26047703). Interacts with PI4KB, TBC1D22A and TBC1D22B (By
CC similarity). Interacts with SLITRK1 (By similarity). Interacts with
CC MEFV (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q04917,
CC ECO:0000269|PubMed:26047703}.
CC -!- INTERACTION:
CC P68510; Q5S006: Lrrk2; NbExp=7; IntAct=EBI-444641, EBI-2693710;
CC P68510; Q9WVS6: Prkn; NbExp=2; IntAct=EBI-444641, EBI-973635;
CC P68510; O60260: PRKN; Xeno; NbExp=6; IntAct=EBI-444641, EBI-716346;
CC P68510; P21580: TNFAIP3; Xeno; NbExp=3; IntAct=EBI-444641, EBI-527670;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: Phosphorylated on Ser-59 by protein kinase C delta type catalytic
CC subunit in a sphingosine-dependent fashion.
CC {ECO:0000269|PubMed:9705322}.
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U57311; AAC53256.1; -; mRNA.
DR EMBL; D87661; BAA13422.1; -; mRNA.
DR EMBL; AF077002; AAC36290.1; -; mRNA.
DR EMBL; AB063572; BAB79599.1; -; Genomic_DNA.
DR EMBL; AK077596; BAC36887.1; -; mRNA.
DR EMBL; AK149224; BAE28768.1; -; mRNA.
DR EMBL; AK168520; BAE40399.1; -; mRNA.
DR EMBL; AK169035; BAE40826.1; -; mRNA.
DR EMBL; AK169189; BAE40965.1; -; mRNA.
DR EMBL; BC008187; AAH08187.1; -; mRNA.
DR EMBL; BC061497; AAH61497.1; -; mRNA.
DR CCDS; CCDS19198.1; -.
DR RefSeq; NP_035868.1; NM_011738.2.
DR PDB; 5YQG; X-ray; 2.10 A; A/B/C/D=1-246.
DR PDBsum; 5YQG; -.
DR AlphaFoldDB; P68510; -.
DR SMR; P68510; -.
DR BioGRID; 204621; 41.
DR IntAct; P68510; 321.
DR MINT; P68510; -.
DR STRING; 10090.ENSMUSP00000019109; -.
DR iPTMnet; P68510; -.
DR PhosphoSitePlus; P68510; -.
DR SwissPalm; P68510; -.
DR UCD-2DPAGE; P68510; -.
DR CPTAC; non-CPTAC-3684; -.
DR EPD; P68510; -.
DR jPOST; P68510; -.
DR MaxQB; P68510; -.
DR PaxDb; P68510; -.
DR PeptideAtlas; P68510; -.
DR PRIDE; P68510; -.
DR ProteomicsDB; 285811; -.
DR TopDownProteomics; P68510; -.
DR Antibodypedia; 11204; 317 antibodies from 37 providers.
DR DNASU; 22629; -.
DR Ensembl; ENSMUST00000019109; ENSMUSP00000019109; ENSMUSG00000018965.
DR GeneID; 22629; -.
DR KEGG; mmu:22629; -.
DR UCSC; uc008xag.2; mouse.
DR CTD; 7533; -.
DR MGI; MGI:109194; Ywhah.
DR VEuPathDB; HostDB:ENSMUSG00000018965; -.
DR eggNOG; KOG0841; Eukaryota.
DR GeneTree; ENSGT01050000244817; -.
DR HOGENOM; CLU_058290_0_0_1; -.
DR InParanoid; P68510; -.
DR OMA; IKNCDES; -.
DR OrthoDB; 1176818at2759; -.
DR PhylomeDB; P68510; -.
DR TreeFam; TF102003; -.
DR Reactome; R-MMU-111447; Activation of BAD and translocation to mitochondria.
DR Reactome; R-MMU-5625740; RHO GTPases activate PKNs.
DR Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-MMU-75035; Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
DR BioGRID-ORCS; 22629; 2 hits in 111 CRISPR screens.
DR ChiTaRS; Ywhah; mouse.
DR PRO; PR:P68510; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P68510; protein.
DR Bgee; ENSMUSG00000018965; Expressed in primary visual cortex and 126 other tissues.
DR Genevisible; P68510; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0014704; C:intercalated disc; IC:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0003779; F:actin binding; IDA:ProtInc.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0035259; F:nuclear glucocorticoid receptor binding; ISS:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IDA:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0017080; F:sodium channel regulator activity; ISS:BHF-UCL.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:0007010; P:cytoskeleton organization; NAS:ProtInc.
DR GO; GO:0006713; P:glucocorticoid catabolic process; ISS:UniProtKB.
DR GO; GO:0042921; P:glucocorticoid receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IDA:MGI.
DR GO; GO:0086010; P:membrane depolarization during action potential; ISS:BHF-UCL.
DR GO; GO:0043066; P:negative regulation of apoptotic process; NAS:ProtInc.
DR GO; GO:0050774; P:negative regulation of dendrite morphogenesis; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; NAS:ProtInc.
DR GO; GO:2000649; P:regulation of sodium ion transmembrane transporter activity; ISS:BHF-UCL.
DR GO; GO:0002028; P:regulation of sodium ion transport; ISS:BHF-UCL.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 1.20.190.20; -; 1.
DR InterPro; IPR000308; 14-3-3.
DR InterPro; IPR023409; 14-3-3_CS.
DR InterPro; IPR036815; 14-3-3_dom_sf.
DR InterPro; IPR023410; 14-3-3_domain.
DR PANTHER; PTHR18860; PTHR18860; 1.
DR Pfam; PF00244; 14-3-3; 1.
DR PIRSF; PIRSF000868; 14-3-3; 1.
DR PRINTS; PR00305; 1433ZETA.
DR SMART; SM00101; 14_3_3; 1.
DR SUPFAM; SSF48445; SSF48445; 1.
DR PROSITE; PS00796; 1433_1; 1.
DR PROSITE; PS00797; 1433_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q04917"
FT CHAIN 2..246
FT /note="14-3-3 protein eta"
FT /id="PRO_0000058624"
FT SITE 57
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000250"
FT SITE 132
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:Q04917"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04917"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:9705322"
FT CONFLICT 15..16
FT /note="EQ -> DE (in Ref. 2; BAA13422)"
FT /evidence="ECO:0000305"
FT HELIX 3..16
FT /evidence="ECO:0007829|PDB:5YQG"
FT HELIX 20..32
FT /evidence="ECO:0007829|PDB:5YQG"
FT HELIX 39..62
FT /evidence="ECO:0007829|PDB:5YQG"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:5YQG"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:5YQG"
FT HELIX 82..106
FT /evidence="ECO:0007829|PDB:5YQG"
FT TURN 107..111
FT /evidence="ECO:0007829|PDB:5YQG"
FT HELIX 117..137
FT /evidence="ECO:0007829|PDB:5YQG"
FT HELIX 140..164
FT /evidence="ECO:0007829|PDB:5YQG"
FT HELIX 170..185
FT /evidence="ECO:0007829|PDB:5YQG"
FT HELIX 190..207
FT /evidence="ECO:0007829|PDB:5YQG"
FT HELIX 218..232
FT /evidence="ECO:0007829|PDB:5YQG"
SQ SEQUENCE 246 AA; 28212 MW; C12F62B4ABA76DA3 CRC64;
MGDREQLLQR ARLAEQAERY DDMASAMKAV TELNEPLSNE DRNLLSVAYK NVVGARRSSW
RVISSIEQKT MADGNEKKLE KVKAYREKIE KELETVCNDV LALLDKFLIK NCNDFQYESK
VFYLKMKGDY YRYLAEVASG EKKNSVVEAS EAAYKEAFEI SKEHMQPTHP IRLGLALNFS
VFYYEIQNAP EQACLLAKQA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDE
EAGEGN
