CPLM-005575

Genbank Nucleotide ID

14-3-3 protein theta

Protein Synonyms/Alias

14-3-3 protein T-cell; 14-3-3 protein tau; Protein HS1

Homo sapiens (Human)

Position	Peptide	Type	References
3	*****MEKTELIQKA	acetylation	[1]
3	*****MEKTELIQKA	ubiquitination	[2, 3]
9	EKTELIQKAKLAEQA	acetylation	[1]
9	EKTELIQKAKLAEQA	ubiquitination	[2, 3, 4, 5, 6, 7]
11	TELIQKAKLAEQAER	ubiquitination	[2, 3, 8, 9]
27	DDMATCMKAVTEQGA	ubiquitination	[3, 5, 9]
49	NLLSVAYKNVVGGRR	acetylation	[1]
49	NLLSVAYKNVVGGRR	ubiquitination	[2, 3, 4, 5, 6, 7, 8, 9, 10]
68	VISSIEQKTDTSDKK	acetylation	[1]
68	VISSIEQKTDTSDKK	ubiquitination	[3, 5, 9]
74	QKTDTSDKKLQLIKD	ubiquitination	[2, 4]
75	KTDTSDKKLQLIKDY	ubiquitination	[2, 3, 4]
80	DKKLQLIKDYREKVE	ubiquitination	[2, 3, 4, 5]
85	LIKDYREKVESELRS	ubiquitination	[3]
103	TVLELLDKYLIANAT	ubiquitination	[9]
115	NATNPESKVFYLKMK	acetylation	[1]
115	NATNPESKVFYLKMK	ubiquitination	[2, 4, 5, 7]
120	ESKVFYLKMKGDYFR	acetylation	[1]
120	ESKVFYLKMKGDYFR	ubiquitination	[3, 4, 6]
122	KVFYLKMKGDYFRYL	ubiquitination	[3, 4, 5]
139	VACGDDRKQTIDNSQ	ubiquitination	[3, 4, 5, 7, 9, 11]
157	QEAFDISKKEMQPTH	acetylation	[12]
157	QEAFDISKKEMQPTH	ubiquitination	[3, 4, 5, 7, 9]
158	EAFDISKKEMQPTHP	ubiquitination	[2, 3, 5, 8]

[1] 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]
[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] 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]
[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] 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]
[7] 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]
[8] 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]
[9] 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]
[10] 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]
[11] 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]
[12] 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. Negatively regulates the kinase activity of PDPK1.

MOD_RES 1 1 N-acetylmethionine.
MOD_RES 3 3 N6-acetyllysine.
MOD_RES 49 49 N6-acetyllysine.
MOD_RES 68 68 N6-acetyllysine.
MOD_RES 115 115 N6-acetyllysine.
MOD_RES 232 232 Phosphoserine.

3D-structure; Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Phosphoprotein; Reference proteome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
GO:0005829; C:cytosol; TAS:Reactome.
GO:0043234; C:protein complex; IEA:Compara.
GO:0016044; P:cellular membrane organization; TAS:Reactome.
GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:Reactome.
GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:BHF-UCL.
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:0007264; P:small GTPase mediated signal transduction; IEA:Compara.

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

PS00796; 1433_1
PS00797; 1433_2