1433Z_MOUSE
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 03-AUG-2022, entry version 179.
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, 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 [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. Induces ARHGEF7 activity on RAC1
CC as well as lamellipodia and membrane ruffle formation (By similarity).
CC In neurons, regulates spine maturation through the modulation of
CC ARHGEF7 activity (By similarity). {ECO:0000250|UniProtKB:O55043,
CC 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). {ECO:0000250|UniProtKB:P63104,
CC ECO:0000250|UniProtKB:Q9ES28, ECO:0000269|PubMed:10455159,
CC ECO:0000269|PubMed:12176995, ECO:0000269|PubMed:16959763,
CC ECO:0000269|PubMed:20478393, ECO:0000269|PubMed:21478148,
CC ECO:0000269|PubMed:22701344, ECO:0000269|PubMed:26047703,
CC ECO:0000269|PubMed:9016762, 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. Melanosome. Note=Located to stage I to
CC stage IV melanosomes. {ECO:0000250}.
CC -!- PTM: The delta, brain-specific form differs from the zeta form in being
CC phosphorylated (By similarity). Phosphorylation on Ser-184 by MAPK8;
CC promotes dissociation of BAX and translocation of BAX to mitochondria.
CC Phosphorylation on Thr-232; inhibits binding of RAF1 (By similarity).
CC Phosphorylated on Ser-58 by PKA and protein kinase C delta type
CC catalytic subunit in a sphingosine-dependent fashion. Phosphorylation
CC on Ser-58 by PKA; disrupts homodimerization and heterodimerization with
CC YHAE and TP53. {ECO:0000250, ECO:0000269|PubMed:9705322}.
CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}.
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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; 208.
DR ComplexPortal; CPX-1148; Foxo3-Ywhaz complex.
DR CORUM; P63101; -.
DR DIP; DIP-31894N; -.
DR IntAct; P63101; 186.
DR MINT; P63101; -.
DR STRING; 10090.ENSMUSP00000022894; -.
DR iPTMnet; P63101; -.
DR PhosphoSitePlus; P63101; -.
DR SwissPalm; P63101; -.
DR REPRODUCTION-2DPAGE; P63101; -.
DR UCD-2DPAGE; P63101; -.
DR EPD; P63101; -.
DR jPOST; P63101; -.
DR MaxQB; P63101; -.
DR PaxDb; P63101; -.
DR PeptideAtlas; P63101; -.
DR PRIDE; P63101; -.
DR ProteomicsDB; 285983; -.
DR TopDownProteomics; P63101; -.
DR Antibodypedia; 3905; 1027 antibodies from 43 providers.
DR DNASU; 22631; -.
DR Ensembl; ENSMUST00000022894; ENSMUSP00000022894; ENSMUSG00000022285.
DR Ensembl; ENSMUST00000110361; ENSMUSP00000105990; ENSMUSG00000022285.
DR Ensembl; ENSMUST00000110362; ENSMUSP00000105991; ENSMUSG00000022285.
DR GeneID; 22631; -.
DR KEGG; mmu:22631; -.
DR UCSC; uc007vmz.2; mouse.
DR CTD; 7534; -.
DR MGI; MGI:109484; Ywhaz.
DR VEuPathDB; HostDB:ENSMUSG00000022285; -.
DR eggNOG; KOG0841; Eukaryota.
DR GeneTree; ENSGT01050000244817; -.
DR HOGENOM; CLU_058290_1_0_1; -.
DR InParanoid; P63101; -.
DR OMA; ERVCQDV; -.
DR OrthoDB; 1176818at2759; -.
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; 11 hits in 114 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 277 other tissues.
DR ExpressionAtlas; P63101; baseline and differential.
DR Genevisible; P63101; MM.
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; TAS:Reactome.
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:0014069; C:postsynaptic density; 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:0019904; F:protein domain specific binding; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
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: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:0030324; P:lung development; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
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:0010941; P:regulation of cell death; IGI:MGI.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
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 DisProt; DP02943; -.
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 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"
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: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
