ID 1433G_MOUSE Reviewed; 247 AA. AC P61982; O70457; P35214; Q3UFD6; Q4FK44; Q9UDP2; Q9UN99; DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 177. DE RecName: Full=14-3-3 protein gamma; DE Contains: DE RecName: Full=14-3-3 protein gamma, N-terminally processed; GN Name=Ywhag; 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; RA Karpitskiy V.V., Shaw A.S.; RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., RA Wiemann S., Schick M., Korn B.; RT "Cloning of mouse full open reading frames in Gateway(R) system entry RT vector (pDONR201)."; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=NOD; TISSUE=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 [4] 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 [5] RP PROTEIN SEQUENCE OF 13-50; 43-56; 62-69; 78-83; 92-120 AND 133-247, 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., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=18034455; DOI=10.1021/pr0701254; RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; RT "Large-scale identification and evolution indexing of tyrosine RT phosphorylation sites from murine brain."; RL J. Proteome Res. 7:311-318(2008). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, 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 [8] 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 [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. Promotes inactivation of WDR24 CC component of the GATOR2 complex by binding to phosphorylated WDR24. CC {ECO:0000250|UniProtKB:P61981}. CC -!- SUBUNIT: Homodimer (By similarity). Interacts with SAMSN1 CC (PubMed:20478393). Interacts with RAF1, SSH1 and CRTC2/TORC2 (By CC similarity). Interacts with ABL1 (phosphorylated form); the interaction CC retains it in the cytoplasm (By similarity). Interacts with GAB2 (By CC similarity). Interacts with MDM4 (phosphorylated); negatively regulates CC MDM4 activity toward TP53 (By similarity). Interacts with PKA- CC phosphorylated AANAT and SIRT2 (By similarity). Interacts with the CC 'Thr-369' phosphorylated form of DAPK2 (PubMed:26047703). Interacts CC with PI4KB, TBC1D22A and TBC1D22B (By similarity). Interacts with CC SLITRK1 (By similarity). Interacts with LRRK2; this interaction is CC dependent on LRRK2 phosphorylation (By similarity). Interacts with CC MARK2 and MARK3 (By similarity). Interacts with MEFV (By similarity). CC Interacts with ENDOG, TSC2 and PIK3C3; interaction with ENDOG weakens CC its interaction with TSC2 and PIK3C3 (By similarity). Interacts with CC (phosphorylated) WDR24 (By similarity). {ECO:0000250|UniProtKB:P61981, CC ECO:0000250|UniProtKB:P61983, ECO:0000269|PubMed:20478393, CC ECO:0000269|PubMed:26047703}. CC -!- INTERACTION: CC P61982; Q08460: Kcnma1; NbExp=4; IntAct=EBI-359843, EBI-1633915; CC P61982; Q5S006: Lrrk2; NbExp=10; IntAct=EBI-359843, EBI-2693710; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P68252}. CC -!- PTM: Phosphorylated by various PKC isozymes. CC {ECO:0000250|UniProtKB:P61981}. CC -!- SIMILARITY: Belongs to the 14-3-3 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAE28625.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AF058799; AAC14345.1; -; mRNA. DR EMBL; CT010208; CAJ18416.1; -; mRNA. DR EMBL; AK088847; BAC40609.1; -; mRNA. DR EMBL; AK148618; BAE28625.1; ALT_INIT; mRNA. DR EMBL; AK153307; BAE31888.1; -; mRNA. DR EMBL; AK164356; BAE37756.1; -; mRNA. DR EMBL; BC008129; AAH08129.1; -; mRNA. DR CCDS; CCDS19748.1; -. DR RefSeq; NP_061359.2; NM_018871.3. DR AlphaFoldDB; P61982; -. DR SMR; P61982; -. DR BioGRID; 204620; 62. DR IntAct; P61982; 31. DR MINT; P61982; -. DR STRING; 10090.ENSMUSP00000051223; -. DR GlyGen; P61982; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P61982; -. DR PhosphoSitePlus; P61982; -. DR SwissPalm; P61982; -. DR REPRODUCTION-2DPAGE; P61982; -. DR CPTAC; non-CPTAC-3956; -. DR CPTAC; non-CPTAC-3957; -. DR EPD; P61982; -. DR jPOST; P61982; -. DR MaxQB; P61982; -. DR PaxDb; 10090-ENSMUSP00000051223; -. DR ProteomicsDB; 285812; -. DR Pumba; P61982; -. DR Antibodypedia; 4339; 621 antibodies from 41 providers. DR DNASU; 22628; -. DR Ensembl; ENSMUST00000055808.6; ENSMUSP00000051223.6; ENSMUSG00000051391.10. DR Ensembl; ENSMUST00000198270.2; ENSMUSP00000143631.2; ENSMUSG00000051391.10. DR GeneID; 22628; -. DR KEGG; mmu:22628; -. DR UCSC; uc008zzf.2; mouse. DR AGR; MGI:108109; -. DR CTD; 7532; -. DR MGI; MGI:108109; Ywhag. DR VEuPathDB; HostDB:ENSMUSG00000051391; -. DR eggNOG; KOG0841; Eukaryota. DR GeneTree; ENSGT01090000260061; -. DR InParanoid; P61982; -. DR OMA; AYGEAHE; -. DR OrthoDB; 920089at2759; -. DR PhylomeDB; P61982; -. DR TreeFam; TF102003; -. DR Reactome; R-MMU-111447; Activation of BAD and translocation to mitochondria. DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition. DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes. DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes. DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome. DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes. DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane. 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-8854518; AURKA Activation by TPX2. DR Reactome; R-MMU-9614399; Regulation of localization of FOXO transcription factors. DR BioGRID-ORCS; 22628; 6 hits in 113 CRISPR screens. DR ChiTaRS; Ywhag; mouse. DR PRO; PR:P61982; -. DR Proteomes; UP000000589; Chromosome 5. DR RNAct; P61982; Protein. DR Bgee; ENSMUSG00000051391; Expressed in CA3 field of hippocampus and 274 other cell types or tissues. DR ExpressionAtlas; P61982; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB. DR GO; GO:0098793; C:presynapse; ISO:MGI. DR GO; GO:0045202; C:synapse; ISO:MGI. DR GO; GO:0031982; C:vesicle; ISO:MGI. DR GO; GO:0003779; F:actin binding; ISS:UniProtKB. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0005159; F:insulin-like growth factor receptor binding; ISS:UniProtKB. DR GO; GO:0050815; F:phosphoserine residue binding; ISS:UniProtKB. DR GO; GO:0019904; F:protein domain specific binding; IDA:MGI. DR GO; GO:0005080; F:protein kinase C binding; ISS:UniProtKB. DR GO; GO:0140311; F:protein sequestering activity; ISS:UniProtKB. DR GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:MGI. DR GO; GO:0042149; P:cellular response to glucose starvation; ISO:MGI. DR GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI. DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProt. DR GO; GO:1904262; P:negative regulation of TORC1 signaling; ISO:MGI. DR GO; GO:0006605; P:protein targeting; IDA:MGI. DR GO; GO:0045664; P:regulation of neuron differentiation; ISS:UniProtKB. DR GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR CDD; cd10024; 14-3-3_gamma; 1. 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:SF22; 14-3-3 PROTEIN GAMMA; 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; P61982; -. DR Genevisible; P61982; MM. PE 1: Evidence at protein level; KW Acetylation; Cytoplasm; Direct protein sequencing; Phosphoprotein; KW Reference proteome. FT CHAIN 1..247 FT /note="14-3-3 protein gamma" FT /id="PRO_0000058607" FT INIT_MET 1 FT /note="Removed; alternate" FT /evidence="ECO:0000250|UniProtKB:P61981" FT CHAIN 2..247 FT /note="14-3-3 protein gamma, N-terminally processed" FT /id="PRO_0000367908" FT SITE 57 FT /note="Interaction with phosphoserine on interacting FT protein" FT /evidence="ECO:0000250|UniProtKB:P61981" FT SITE 132 FT /note="Interaction with phosphoserine on interacting FT protein" FT /evidence="ECO:0000250|UniProtKB:P61981" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:P61981" FT MOD_RES 2 FT /note="N-acetylvaline; in 14-3-3 protein gamma, N- FT terminally processed" FT /evidence="ECO:0000250|UniProtKB:P61981" FT MOD_RES 71 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 133 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P61983" FT MOD_RES 145 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P61981" FT MOD_RES 215 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P61983" FT MOD_RES 234 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P61981" FT MOD_RES 235 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P61981" FT CONFLICT 150 FT /note="S -> F (in Ref. 1; AAC14345)" FT /evidence="ECO:0000305" SQ SEQUENCE 247 AA; 28303 MW; B0D16C6DE1F4455D CRC64; MVDREQLVQK ARLAEQAERY DDMAAAMKNV TELNEPLSNE ERNLLSVAYK NVVGARRSSW RVISSIEQKT SADGNEKKIE MVRAYREKIE KELEAVCQDV LSLLDNYLIK NCSETQYESK VFYLKMKGDY YRYLAEVATG EKRATVVESS EKAYSEAHEI SKEHMQPTHP IRLGLALNYS VFYYEIQNAP EQACHLAKTA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDD DGGEGNN //