UniProt Accession

 1433E_HUMAN; P62258; B3KY71; D3DTH5; P29360; P42655; Q4VJB6; Q53XZ5; Q63631; Q7M4R4 

Genbank Protein ID

 U20972; U54778; U43399; U43430; U28936; AB017103; AY883089; AK128785; AK295260; AK316185; BT007161; CH471108; CH471108; BC000179; BC001440 

Genbank Nucleotide ID

 AAC50175.1; AAC50710.1; AAC50625.1; AAD00026.1; AAA75301.1; BAA32538.1; AAX68683.1; BAG54733.1; BAG58249.1; BAH14556.1; AAP35825.1; EAW90628.1; EAW90629.1; AAH00179.1; AAH01440.1 

Protein Name

 14-3-3 protein epsilon 

Protein Synonyms/Alias

 14-3-3E 

Gene Name

 YWHAE 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
12	EDLVYQAKLAEQAER	ubiquitination	[1, 2, 3, 4]
28	DEMVESMKKVAGMDV	ubiquitination	[3, 5, 6]
29	EMVESMKKVAGMDVE	ubiquitination	[3, 7]
50	NLLSVAYKNVIGARR	acetylation	[8]
50	NLLSVAYKNVIGARR	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 9, 10, 11, 12]
69	IISSIEQKEENKGGE	acetylation	[8]
69	IISSIEQKEENKGGE	ubiquitination	[5, 6, 7]
73	IEQKEENKGGEDKLK	ubiquitination	[5, 6]
106	DILDVLDKHLIPAAN	acetylation	[13]
106	DILDVLDKHLIPAAN	ubiquitination	[1, 3, 4, 5, 6, 7, 9, 14, 15]
118	AANTGESKVFYYKMK	acetylation	[8, 15, 16]
118	AANTGESKVFYYKMK	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 15]
123	ESKVFYYKMKGDYHR	acetylation	[8, 17]
123	ESKVFYYKMKGDYHR	ubiquitination	[1, 2, 3, 4, 5, 6, 12, 15]
125	KVFYYKMKGDYHRYL	ubiquitination	[5, 6, 12]
142	FATGNDRKEAAENSL	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 12]
153	ENSLVAYKAASDIAM	ubiquitination	[5, 6, 7]
196	DRACRLAKAAFDDAI	ubiquitination	[1, 2, 4, 5, 6, 7, 9, 11]
244	GDGEEQNKEALQDVE	ubiquitination	[4, 5, 6, 7, 10, 14]

Reference

 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [7] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [8] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [9] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [10] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [11] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [12] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [13] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224]
 [14] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [15] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [16] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [17] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 

Functional Description

 Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. 

Sequence Annotation

 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 50 50 N6-acetyllysine.
 MOD_RES 69 69 N6-acetyllysine.
 MOD_RES 118 118 N6-acetyllysine.
 MOD_RES 123 123 N6-acetyllysine.
 MOD_RES 210 210 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Host-virus interaction; Phosphoprotein; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 255 AA 

Protein Sequence

Gene Ontology

 GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005871; C:kinesin complex; IEA:Compara.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0016044; P:cellular membrane organization; TAS:Reactome.
 GO:0021987; P:cerebral cortex development; IEA:Compara.
 GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
 GO:0035329; P:hippo signaling cascade; TAS:Reactome.
 GO:0021766; P:hippocampus development; IEA:Compara.
 GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:Reactome.
 GO:0035308; P:negative regulation of protein dephosphorylation; IEA:Compara.
 GO:0001764; P:neuron migration; IEA:Compara.
 GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
 GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
 GO:0006605; P:protein targeting; IEA:Compara.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 

Interpro

 IPR000308; 14-3-3.
 IPR023409; 14-3-3_CS.
 IPR023410; 14-3-3_domain. 

Pfam

 PF00244; 14-3-3 

SMART

 SM00101; 14_3_3 

PROSITE

 PS00796; 1433_1
 PS00797; 1433_2 

PRINTS

 PR00305; 1433ZETA.