CPLM-009404

Genbank Nucleotide ID

14-3-3 protein gamma

Protein Synonyms/Alias

Protein kinase C inhibitor protein 1; KCIP-1; 14-3-3 protein gamma, N-terminally processed

Homo sapiens (Human)

Position	Peptide	Type	References
10	DREQLVQKARLAEQA	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8, 9]
28	DDMAAAMKNVTELNE	ubiquitination	[3, 7, 8]
50	NLLSVAYKNVVGARR	ubiquitination	[6, 8, 10]
69	VISSIEQKTSADGNE	acetylation	[11]
69	VISSIEQKTSADGNE	ubiquitination	[3, 7, 8, 9, 12]
77	TSADGNEKKIEMVRA	ubiquitination	[8]
120	SETQYESKVFYLKMK	ubiquitination	[6, 7, 9]
125	ESKVFYLKMKGDYYR	ubiquitination	[6, 7, 10]
127	KVFYLKMKGDYYRYL	ubiquitination	[6]
142	AEVATGEKRATVVES	acetylation	[9]
142	AEVATGEKRATVVES	ubiquitination	[3, 7, 8, 9, 12]
152	TVVESSEKAYSEAHE	ubiquitination	[3, 7, 8, 9]
162	SEAHEISKEHMQPTH	acetylation	[11]
162	SEAHEISKEHMQPTH	ubiquitination	[7, 9, 12]

[1] 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]
[2] 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]
[3] 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]
[4] 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]
[5] 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]
[6] 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]
[7] 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]
[8] 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]
[9] 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]
[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] 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]
[12] 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]

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.

MOD_RES 1 1 N-acetylmethionine; in 14-3-3 protein
MOD_RES 2 2 N-acetylvaline; in 14-3-3 protein gamma,
MOD_RES 2 2 N-acetylvaline; partial.
MOD_RES 117 117 Phosphotyrosine (By similarity).
MOD_RES 145 145 Phosphothreonine.

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:0008426; F:protein kinase C inhibitor activity; NAS:UniProtKB.
GO:0016044; P:cellular membrane organization; TAS:Reactome.
GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO:0097193; P:intrinsic apoptotic 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:0045664; P:regulation of neuron differentiation; IMP:UniProtKB.
GO:0048167; P:regulation of synaptic plasticity; IMP:UniProtKB.

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

PS00796; 1433_1
PS00797; 1433_2