ID 1433Z_MOUSE Reviewed; 245 AA. AC P63101; P35215; P70197; P97286; Q3TSF1; Q5EBQ1; DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2004, sequence version 1. DT 27-MAR-2024, entry version 188. DE RecName: Full=14-3-3 protein zeta/delta; DE AltName: Full=Protein kinase C inhibitor protein 1; DE Short=KCIP-1; DE AltName: Full=SEZ-2; GN Name=Ywhaz; 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]. RC STRAIN=C57BL/6J; TISSUE=Brain; RX PubMed=8645260; DOI=10.1006/bbrc.1996.0313; RA Kajiwara K., Nagawawa H., Shimizu-Nishikawa K., Ookura T., Kimura M., RA Sugaya E.; RT "Molecular characterization of seizure-related genes isolated by RT differential screening."; RL Biochem. Biophys. Res. Commun. 219:795-799(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH CDK16. 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 [4] RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH WEE1. RX PubMed=9016762; DOI=10.1006/bbrc.1996.5933; RA Honda R., Ohba Y., Yasuda H.; RT "14-3-3 zeta protein binds to the carboxyl half of mouse wee1 kinase."; RL Biochem. Biophys. Res. Commun. 230:262-265(1997). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; RC TISSUE=Blastocyst, Bone marrow macrophage, Egg, Embryonic kidney, and RC Thymus; 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=C57BL/6J; TISSUE=Brain; 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 12-55; 61-68; 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., Klug S., Friebe K., Yang J.W., Zigmond M., Sunyer B., RA Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [8] RP PHOSPHORYLATION AT SER-58. 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 TLK2. RX PubMed=10455159; DOI=10.1074/jbc.274.35.24865; RA Zhang S., Xing H., Muslin A.J.; RT "Nuclear localization of protein kinase U-alpha is regulated by 14-3-3."; RL J. Biol. Chem. 274:24865-24872(1999). RN [10] RP INTERACTION WITH MLF1. RX PubMed=12176995; DOI=10.1074/jbc.m206041200; RA Lim R., Winteringham L.N., Williams J.H., McCulloch R.K., Ingley E., RA Tiao J.Y.-H., Lalonde J.-P., Tsai S., Tilbrook P.A., Sun Y., Wu X., RA Morris S.W., Klinken S.P.; RT "MADM, a novel adaptor protein that mediates phosphorylation of the 14-3-3 RT binding site of myeloid leukemia factor 1."; RL J. Biol. Chem. 277:40997-41008(2002). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic brain; RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200; RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; RT "Phosphoproteomic analysis of the developing mouse brain."; RL Mol. Cell. Proteomics 3:1093-1101(2004). RN [12] RP INTERACTION WITH ARHGEF7 AND GIT1. RX PubMed=16959763; DOI=10.1074/mcp.m600147-mcp200; RA Angrand P.O., Segura I., Voelkel P., Ghidelli S., Terry R., Brajenovic M., RA Vintersten K., Klein R., Superti-Furga G., Drewes G., Kuster B., RA Bouwmeester T., Acker-Palmer A.; RT "Transgenic mouse proteomics identifies new 14-3-3-associated proteins RT involved in cytoskeletal rearrangements and cell signaling."; RL Mol. Cell. Proteomics 5:2211-2227(2006). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, 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 [14] 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 [15] RP INTERACTION WITH BCL2L11. RX PubMed=21478148; DOI=10.1074/jbc.m110.197707; RA Thompson S., Pearson A.N., Ashley M.D., Jessick V., Murphy B.M., Gafken P., RA Henshall D.C., Morris K.T., Simon R.P., Meller R.; RT "Identification of a novel Bcl-2-interacting mediator of cell death (Bim) RT E3 ligase, tripartite motif-containing protein 2 (TRIM2), and its role in RT rapid ischemic tolerance-induced neuroprotection."; RL J. Biol. Chem. 286:19331-19339(2011). RN [16] RP INTERACTION WITH ZFP36L1. RX PubMed=22701344; DOI=10.7150/ijbs.4036; RA Lin N.Y., Lin T.Y., Yang W.H., Wang S.C., Wang K.T., Su Y.L., Jiang Y.W., RA Chang G.D., Chang C.J.; RT "Differential expression and functional analysis of the tristetraprolin RT family during early differentiation of 3T3-L1 preadipocytes."; RL Int. J. Biol. Sci. 8:761-777(2012). RN [17] 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. Promotes cytosolic retention and CC inactivation of TFEB transcription factor by binding to phosphorylated CC TFEB. Induces ARHGEF7 activity on RAC1 as well as lamellipodia and CC membrane ruffle formation (By similarity). In neurons, regulates spine CC maturation through the modulation of ARHGEF7 activity (By similarity). CC {ECO:0000250|UniProtKB:O55043, ECO:0000250|UniProtKB:P63104}. CC -!- SUBUNIT: Homodimer. Heterodimerizes with YWHAE (By similarity). CC Homo- and heterodimerization is inhibited by phosphorylation on Ser-58 CC (By similarity). Interacts with FOXO4, NOXA1, SSH1 and ARHGEF2. CC Interacts with CDK16 and with WEE1 (C-terminal). Interacts with MLF1 CC (phosphorylated form); the interaction retains it in the cytoplasm. CC Interacts with BSPRY. Interacts with Thr-phosphorylated ITGB2 (By CC similarity). Interacts with Pseudomonas aeruginosa exoS CC (unphosphorylated form). Interacts with BAX; the interaction occurs in CC the cytoplasm. Under stress conditions, MAPK8-mediated phosphorylation CC releases BAX to mitochondria. Interacts with phosphorylated RAF1; the CC interaction is inhibited when YWHAZ is phosphorylated on Thr-232. CC Interacts with TP53; the interaction enhances p53 transcriptional CC activity. The Ser-58 phosphorylated form inhibits this interaction and CC p53 transcriptional activity. Interacts with ABL1 (phosphorylated CC form); the interaction retains ABL1 in the cytoplasm. Interacts with CC PKA-phosphorylated AANAT; the interaction modulates AANAT enzymatic CC activity by increasing affinity for arylalkylamines and acetyl-CoA and CC protecting the enzyme from dephosphorylation and proteasomal CC degradation (By similarity). It may also prevent thiol-dependent CC inactivation (By similarity). Interacts with AKT1; the interaction CC phosphorylates YWHAZ and modulates dimerization (By similarity). CC Interacts with GAB2 (By similarity). Interacts with SAMSN1. Interacts CC with BCL2L11 and TLK2. Interacts with the 'Thr-369' phosphorylated form CC of DAPK2 (PubMed:26047703). Interacts with PI4KB, TBC1D22A and TBC1D22B CC (By similarity). Interacts with ZFP36L1 (via phosphorylated form); this CC interaction occurs in a p38 MAPK- and AKT-signaling pathways CC (PubMed:22701344). Interacts with SLITRK1 (By similarity). Interacts CC with AK5, LDB1, MADD, PDE1A and SMARCB1 (By similarity). Interacts with CC ARHGEF7 and GIT1 (PubMed:16959763). Interacts with MEFV (By CC similarity). Interacts with ADAM22 (via C-terminus) (By similarity). CC {ECO:0000250|UniProtKB:P63104, ECO:0000250|UniProtKB:Q9ES28, CC ECO:0000269|PubMed:10455159, ECO:0000269|PubMed:12176995, CC ECO:0000269|PubMed:16959763, ECO:0000269|PubMed:20478393, CC ECO:0000269|PubMed:21478148, ECO:0000269|PubMed:22701344, CC ECO:0000269|PubMed:26047703, ECO:0000269|PubMed:9016762, CC ECO:0000269|PubMed:9197417}. CC -!- INTERACTION: CC P63101; Q5S006: Lrrk2; NbExp=5; IntAct=EBI-354751, EBI-2693710; CC P63101; Q9QWV4: Mlf1; NbExp=3; IntAct=EBI-354751, EBI-354765; CC P63101; O43524: FOXO3; Xeno; NbExp=2; IntAct=EBI-354751, EBI-1644164; CC P63101; Q92945: KHSRP; Xeno; NbExp=2; IntAct=EBI-354751, EBI-1049099; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P63104}. CC Melanosome {ECO:0000250|UniProtKB:P63104}. Note=Located to stage I to CC stage IV melanosomes. {ECO:0000250|UniProtKB:P63104}. CC -!- PTM: The delta, brain-specific form differs from the zeta form in being CC phosphorylated (Probable). Phosphorylation on Ser-184 by MAPK8; CC promotes dissociation of BAX and translocation of BAX to mitochondria CC (By similarity). Phosphorylation on Thr-232; inhibits binding of RAF1 CC (By similarity). Phosphorylated on Ser-58 by PKA and protein kinase C CC delta type catalytic subunit in a sphingosine-dependent fashion CC (PubMed:9705322). Phosphorylation on Ser-58 by PKA; disrupts CC homodimerization and heterodimerization with YHAE and TP53 (By CC similarity). {ECO:0000250|UniProtKB:P63104, ECO:0000269|PubMed:9705322, CC ECO:0000305}. 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; D78647; BAA11464.1; -; mRNA. DR EMBL; D87660; BAA13421.1; -; mRNA. DR EMBL; U79231; AAC53254.1; -; mRNA. DR EMBL; D83037; BAA11751.1; -; mRNA. DR EMBL; AK083368; BAC38887.1; -; mRNA. DR EMBL; AK145657; BAE26570.1; -; mRNA. DR EMBL; AK146800; BAE27442.1; -; mRNA. DR EMBL; AK150381; BAE29512.1; -; mRNA. DR EMBL; AK151900; BAE30783.1; -; mRNA. DR EMBL; AK162099; BAE36724.1; -; mRNA. DR EMBL; AK167128; BAE39275.1; -; mRNA. DR EMBL; BC050891; AAH50891.1; -; mRNA. DR EMBL; BC089334; AAH89334.1; -; mRNA. DR CCDS; CCDS27432.1; -. DR PIR; JC5384; JC5384. DR RefSeq; NP_001240734.1; NM_001253805.1. DR RefSeq; NP_001240735.1; NM_001253806.1. DR RefSeq; NP_035870.1; NM_011740.3. DR RefSeq; XP_011243654.1; XM_011245352.2. DR PDB; 7EXE; X-ray; 2.75 A; A/B=2-245. DR PDBsum; 7EXE; -. DR AlphaFoldDB; P63101; -. DR BMRB; P63101; -. DR SMR; P63101; -. DR BioGRID; 204623; 212. DR ComplexPortal; CPX-1148; Foxo3-Ywhaz complex. DR CORUM; P63101; -. DR DIP; DIP-31894N; -. DR IntAct; P63101; 187. DR MINT; P63101; -. DR STRING; 10090.ENSMUSP00000022894; -. DR GlyGen; P63101; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P63101; -. DR MetOSite; P63101; -. DR PhosphoSitePlus; P63101; -. DR SwissPalm; P63101; -. DR REPRODUCTION-2DPAGE; P63101; -. DR EPD; P63101; -. DR jPOST; P63101; -. DR MaxQB; P63101; -. DR PaxDb; 10090-ENSMUSP00000022894; -. DR PeptideAtlas; P63101; -. DR ProteomicsDB; 285983; -. DR Pumba; P63101; -. DR TopDownProteomics; P63101; -. DR Antibodypedia; 3905; 1188 antibodies from 43 providers. DR DNASU; 22631; -. DR Ensembl; ENSMUST00000022894.14; ENSMUSP00000022894.8; ENSMUSG00000022285.18. DR Ensembl; ENSMUST00000110361.8; ENSMUSP00000105990.2; ENSMUSG00000022285.18. DR Ensembl; ENSMUST00000110362.4; ENSMUSP00000105991.4; ENSMUSG00000022285.18. DR GeneID; 22631; -. DR KEGG; mmu:22631; -. DR UCSC; uc007vmz.2; mouse. DR AGR; MGI:109484; -. DR CTD; 7534; -. DR MGI; MGI:109484; Ywhaz. DR VEuPathDB; HostDB:ENSMUSG00000022285; -. DR eggNOG; KOG0841; Eukaryota. DR GeneTree; ENSGT01090000260040; -. DR HOGENOM; CLU_058290_1_0_1; -. DR InParanoid; P63101; -. DR OMA; YDEMVNE; -. DR OrthoDB; 920089at2759; -. DR PhylomeDB; P63101; -. DR TreeFam; TF102003; -. DR Reactome; R-MMU-111447; Activation of BAD and translocation to mitochondria. DR Reactome; R-MMU-3769402; Deactivation of the beta-catenin transactivating complex. DR Reactome; R-MMU-392517; Rap1 signalling. DR Reactome; R-MMU-430116; GP1b-IX-V activation signalling. DR Reactome; R-MMU-450604; KSRP (KHSRP) binds and destabilizes mRNA. DR Reactome; R-MMU-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling. 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-9013700; NOTCH4 Activation and Transmission of Signal to the Nucleus. DR Reactome; R-MMU-9614399; Regulation of localization of FOXO transcription factors. DR BioGRID-ORCS; 22631; 12 hits in 120 CRISPR screens. DR ChiTaRS; Ywhaz; mouse. DR PRO; PR:P63101; -. DR Proteomes; UP000000589; Chromosome 15. DR RNAct; P63101; Protein. DR Bgee; ENSMUSG00000022285; Expressed in olfactory tubercle and 280 other cell types or tissues. DR ExpressionAtlas; P63101; baseline and differential. DR GO; GO:0031252; C:cell leading edge; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI. DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO. DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell. DR GO; GO:0005739; C:mitochondrion; HDA:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI. DR GO; GO:0099572; C:postsynaptic specialization; ISO:MGI. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0050815; F:phosphoserine residue binding; ISS:UniProtKB. DR GO; GO:0019904; F:protein domain specific binding; IDA:UniProtKB. DR GO; GO:0019901; F:protein kinase binding; ISO:MGI. DR GO; GO:0140311; F:protein sequestering activity; ISS:UniProtKB. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI. DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI. DR GO; GO:0001525; P:angiogenesis; IMP:MGI. DR GO; GO:0042149; P:cellular response to glucose starvation; ISO:MGI. DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IMP:MGI. DR GO; GO:0051683; P:establishment of Golgi localization; ISO:MGI. DR GO; GO:0090168; P:Golgi reassembly; ISO:MGI. DR GO; GO:0002553; P:histamine secretion by mast cell; ISO:MGI. DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProt. DR GO; GO:0030324; P:lung development; IMP:MGI. DR GO; GO:0045824; P:negative regulation of innate immune response; ISO:MGI. DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; ISO:MGI. DR GO; GO:1904262; P:negative regulation of TORC1 signaling; ISO:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ComplexPortal. DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB. DR GO; GO:0006605; P:protein targeting; IDA:MGI. DR GO; GO:0006626; P:protein targeting to mitochondrion; ISO:MGI. DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB. DR GO; GO:0043067; P:regulation of programmed cell death; IGI:MGI. DR GO; GO:0090128; P:regulation of synapse maturation; ISO:MGI. DR GO; GO:0003016; P:respiratory system process; IMP:MGI. DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI. DR GO; GO:0007165; P:signal transduction; ISS:UniProtKB. DR GO; GO:0008039; P:synaptic target recognition; IDA:SynGO. DR GO; GO:0035148; P:tube formation; IMP:MGI. DR CDD; cd10022; 14-3-3_beta_zeta; 1. DR DisProt; DP02943; -. DR Gene3D; 1.20.190.20; 14-3-3 domain; 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; 14-3-3 PROTEIN; 1. DR PANTHER; PTHR18860:SF7; 14-3-3 PROTEIN ZETA_DELTA; 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; 14-3-3 protein; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. DR UCD-2DPAGE; P63101; -. DR Genevisible; P63101; MM. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; KW Phosphoprotein; Reference proteome. FT CHAIN 1..245 FT /note="14-3-3 protein zeta/delta" FT /id="PRO_0000058628" FT SITE 56 FT /note="Interaction with phosphoserine on interacting FT protein" FT /evidence="ECO:0000250|UniProtKB:P63103" FT SITE 127 FT /note="Interaction with phosphoserine on interacting FT protein" FT /evidence="ECO:0000250|UniProtKB:P63103" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:P63104" FT MOD_RES 3 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P63104" FT MOD_RES 58 FT /note="Phosphoserine; by PKA" FT /evidence="ECO:0000269|PubMed:9705322" FT MOD_RES 68 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P63104" FT MOD_RES 184 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P63104" FT MOD_RES 207 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 210 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P63102" FT MOD_RES 232 FT /note="Phosphothreonine; by CK1" FT /evidence="ECO:0000250|UniProtKB:P63104" FT CONFLICT 78 FT /note="M -> V (in Ref. 4; BAA11751)" FT /evidence="ECO:0000305" FT CONFLICT 139 FT /note="K -> R (in Ref. 5; BAE36724)" FT /evidence="ECO:0000305" FT CONFLICT 218..219 FT /note="MQ -> IE (in Ref. 2; BAA13421)" FT /evidence="ECO:0000305" FT CONFLICT 236 FT /note="E -> D (in Ref. 4; BAA11751)" FT /evidence="ECO:0000305" FT HELIX 3..15 FT /evidence="ECO:0007829|PDB:7EXE" FT HELIX 19..31 FT /evidence="ECO:0007829|PDB:7EXE" FT HELIX 38..66 FT /evidence="ECO:0007829|PDB:7EXE" FT HELIX 73..103 FT /evidence="ECO:0007829|PDB:7EXE" FT TURN 104..108 FT /evidence="ECO:0007829|PDB:7EXE" FT HELIX 112..130 FT /evidence="ECO:0007829|PDB:7EXE" FT HELIX 137..159 FT /evidence="ECO:0007829|PDB:7EXE" FT HELIX 165..180 FT /evidence="ECO:0007829|PDB:7EXE" FT HELIX 187..200 FT /evidence="ECO:0007829|PDB:7EXE" FT TURN 208..210 FT /evidence="ECO:0007829|PDB:7EXE" FT HELIX 211..228 FT /evidence="ECO:0007829|PDB:7EXE" SQ SEQUENCE 245 AA; 27771 MW; 2164DF3793B45B7A CRC64; MDKNELVQKA KLAEQAERYD DMAACMKSVT EQGAELSNEE RNLLSVAYKN VVGARRSSWR VVSSIEQKTE GAEKKQQMAR EYREKIETEL RDICNDVLSL LEKFLIPNAS QPESKVFYLK MKGDYYRYLA EVAAGDDKKG IVDQSQQAYQ EAFEISKKEM QPTHPIRLGL ALNFSVFYYE ILNSPEKACS LAKTAFDEAI AELDTLSEES YKDSTLIMQL LRDNLTLWTS DTQGDEAEAG EGGEN //