1433T_MOUSE
ID 1433T_MOUSE Reviewed; 245 AA.
AC P68254; P35216; Q3TW69; Q3UJN5; Q5SP76; Q5U423; Q66JR6;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=14-3-3 protein theta;
DE AltName: Full=14-3-3 protein tau;
GN Name=Ywhaq;
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] (ISOFORM 1), 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] (ISOFORM 1).
RX PubMed=9211421;
RX DOI=10.1002/(sici)1098-2795(199708)47:4<370::aid-mrd3>3.0.co;2-h;
RA Perego L., Berruti G.;
RT "Molecular cloning and tissue-specific expression of the mouse homologue of
RT the rat brain 14-3-3 theta protein: characterization of its cellular and
RT developmental pattern of expression in the male germ line.";
RL Mol. Reprod. Dev. 47:370-379(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=129/Sv;
RA Takihara Y., Irie K., Nomura M., Motaleb M., Matsumoto K., Shimada K.;
RT "14-3-3 family members play an important role in tumorigenic transformation
RT of NIH 3T3 cells and retinoic acid-mediated F9 cell differentiation.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Amnion, Blastocyst, Bone marrow, and Egg;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and FVB/N;
RC TISSUE=Brain, Mammary tumor, and Olfactory epithelium;
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 12-49; 61-68; 75-80; 84-115; 128-167 AND 194-245, 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 [LARGE SCALE ANALYSIS] AT SER-92, AND IDENTIFICATION BY
RP 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 [9]
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 CDKN1B ('Thr-198'
CC phosphorylated form); the interaction translocates CDKN1B to the
CC cytoplasm. Interacts with SSH1 (By similarity). Interacts with GAB2.
CC Interacts with RGS7 (phosphorylated form) (By similarity). Interacts
CC with CDK16 (PubMed:9197417). Interacts with the 'Ser-241'
CC phosphorylated form of PDPK1 (By similarity). Interacts with the 'Thr-
CC 369' phosphorylated form of DAPK2 (PubMed:26047703). Interacts with
CC PI4KB, TBC1D22A and TBC1D22B (By similarity). Interacts with SLITRK1
CC (By similarity). Interacts with RIPOR2 (By similarity). Interacts with
CC INAVA; the interaction increases upon PRR (pattern recognition
CC receptor) stimulation and is required for cellular signaling pathway
CC activation and cytokine secretion (By similarity). Interacts with
CC MARK2, MARK3 and MARK4 (By similarity). Interacts with MEFV (By
CC similarity). {ECO:0000250|UniProtKB:P27348,
CC ECO:0000269|PubMed:26047703, ECO:0000269|PubMed:9197417}.
CC -!- INTERACTION:
CC P68254; P23242: Gja1; NbExp=3; IntAct=EBI-400675, EBI-298630;
CC P68254; P11688: Itga5; NbExp=2; IntAct=EBI-400675, EBI-6477055;
CC P68254; Q5S006: Lrrk2; NbExp=4; IntAct=EBI-400675, EBI-2693710;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P68254-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P68254-2; Sequence=VSP_016340;
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH80802.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH85299.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U57312; AAC53257.1; -; mRNA.
DR EMBL; U56243; AAB72023.1; -; mRNA.
DR EMBL; D87662; BAA13423.1; -; mRNA.
DR EMBL; AK145568; BAE26517.1; -; mRNA.
DR EMBL; AK146371; BAE27120.1; -; mRNA.
DR EMBL; AK150850; BAE29907.1; -; mRNA.
DR EMBL; AK151437; BAE30400.1; -; mRNA.
DR EMBL; AK151715; BAE30634.1; -; mRNA.
DR EMBL; AK151864; BAE30752.1; -; mRNA.
DR EMBL; AK159403; BAE35055.1; -; mRNA.
DR EMBL; AK159817; BAE35397.1; -; mRNA.
DR EMBL; AK163237; BAE37249.1; -; mRNA.
DR EMBL; AK167397; BAE39486.1; -; mRNA.
DR EMBL; AL929409; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC080802; AAH80802.1; ALT_INIT; mRNA.
DR EMBL; BC085299; AAH85299.1; ALT_INIT; mRNA.
DR EMBL; BC090838; AAH90838.1; -; mRNA.
DR EMBL; BC106164; AAI06165.1; -; mRNA.
DR CCDS; CCDS25837.1; -. [P68254-1]
DR RefSeq; NP_035869.1; NM_011739.3. [P68254-1]
DR AlphaFoldDB; P68254; -.
DR SMR; P68254; -.
DR BioGRID; 204622; 68.
DR CORUM; P68254; -.
DR ELM; P68254; -.
DR IntAct; P68254; 33.
DR MINT; P68254; -.
DR STRING; 10090.ENSMUSP00000100067; -.
DR iPTMnet; P68254; -.
DR PhosphoSitePlus; P68254; -.
DR SwissPalm; P68254; -.
DR REPRODUCTION-2DPAGE; P68254; -.
DR CPTAC; non-CPTAC-3627; -.
DR EPD; P68254; -.
DR jPOST; P68254; -.
DR MaxQB; P68254; -.
DR PaxDb; P68254; -.
DR PeptideAtlas; P68254; -.
DR PRIDE; P68254; -.
DR ProteomicsDB; 285981; -. [P68254-1]
DR ProteomicsDB; 285982; -. [P68254-2]
DR Antibodypedia; 1900; 595 antibodies from 46 providers.
DR DNASU; 22630; -.
DR Ensembl; ENSMUST00000103002; ENSMUSP00000100067; ENSMUSG00000076432. [P68254-1]
DR Ensembl; ENSMUST00000135088; ENSMUSP00000123605; ENSMUSG00000076432. [P68254-1]
DR Ensembl; ENSMUST00000155480; ENSMUSP00000117118; ENSMUSG00000076432. [P68254-2]
DR GeneID; 22630; -.
DR KEGG; mmu:22630; -.
DR UCSC; uc007ndw.1; mouse. [P68254-1]
DR UCSC; uc007ndx.1; mouse. [P68254-2]
DR CTD; 10971; -.
DR MGI; MGI:891963; Ywhaq.
DR VEuPathDB; HostDB:ENSMUSG00000076432; -.
DR eggNOG; KOG0841; Eukaryota.
DR GeneTree; ENSGT01050000244817; -.
DR HOGENOM; CLU_058290_1_0_1; -.
DR InParanoid; P68254; -.
DR OMA; FEMATTI; -.
DR PhylomeDB; P68254; -.
DR TreeFam; TF102002; -.
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 Reactome; R-MMU-9614399; Regulation of localization of FOXO transcription factors.
DR BioGRID-ORCS; 22630; 6 hits in 87 CRISPR screens.
DR ChiTaRS; Ywhaq; mouse.
DR PRO; PR:P68254; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P68254; protein.
DR Bgee; ENSMUSG00000076432; Expressed in urogenital fold and 245 other tissues.
DR ExpressionAtlas; P68254; baseline and differential.
DR Genevisible; P68254; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0071889; F:14-3-3 protein binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IDA:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR GO; GO:0034766; P:negative regulation of ion transmembrane transport; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0006605; P:protein targeting; IDA:MGI.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IPI:MGI.
DR CDD; cd10023; 14-3-3_theta; 1.
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 InterPro; IPR042584; 14-3-3_theta.
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 Acetylation; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Nitration; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..245
FT /note="14-3-3 protein theta"
FT /id="PRO_0000058637"
FT SITE 56
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000250"
FT SITE 127
FT /note="Interaction with phosphoserine on interacting
FT protein"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P27348"
FT MOD_RES 3
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P27348"
FT MOD_RES 49
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P27348"
FT MOD_RES 68
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P27348"
FT MOD_RES 82
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQV8"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 104
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQV8"
FT MOD_RES 115
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P27348"
FT MOD_RES 232
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000250|UniProtKB:P27348, ECO:0000305"
FT CROSSLNK 49
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P27348"
FT VAR_SEQ 227..245
FT /note="LWTSDSAGEECDAAEGAEN -> FTCVELETVSVCFSLLS (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016340"
FT CONFLICT 26
FT /note="M -> I (in Ref. 4; BAE35397)"
FT /evidence="ECO:0000305"
FT CONFLICT 227
FT /note="L -> S (in Ref. 4; BAE27120)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 245 AA; 27778 MW; E30471260E8B366E CRC64;
MEKTELIQKA KLAEQAERYD DMATCMKAVT EQGAELSNEE RNLLSVAYKN VVGGRRSAWR
VISSIEQKTD TSDKKLQLIK DYREKVESEL RSICTTVLEL LDKYLIANAT NPESKVFYLK
MKGDYFRYLA EVACGDDRKQ TIENSQGAYQ EAFDISKKEM QPTHPIRLGL ALNFSVFYYE
ILNNPELACT LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DSAGEECDAA
EGAEN
