UniProt Accession

 1433Z_HUMAN; P63104; A8K1N0; B7Z465; P29213; P29312; Q32P43; Q5XJ08; Q6GPI2; Q6IN74; Q6NUR9; Q6P3U9; Q86V33 

Genbank Protein ID

 M86400; U28964; AK289945; AK296902; CH471060; BC003623; BC051814; BC063824; BC068456; BC072426; BC073141; BC083508; BC099904; BC101483; BC108281; BC111951 

Genbank Nucleotide ID

 AAA36446.1; AAC52052.1; BAF82634.1; BAH12451.1; EAW91823.1; AAH03623.3; AAH51814.1; AAH63824.2; AAH68456.2; AAH72426.2; AAH73141.1; AAH83508.2; AAH99904.1; AAI01484.1; AAI08282.1; AAI11952.1 

Protein Name

 14-3-3 protein zeta/delta 

Protein Synonyms/Alias

 Protein kinase C inhibitor protein 1; KCIP-1 

Gene Name

 YWHAZ 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
3	*****MDKNELVQKA	acetylation	[1]
3	*****MDKNELVQKA	ubiquitination	[2, 3]
9	DKNELVQKAKLAEQA	ubiquitination	[2, 3, 4, 5, 6, 7]
11	NELVQKAKLAEQAER	ubiquitination	[2, 3, 4, 6, 7]
49	NLLSVAYKNVVGARR	ubiquitination	[2, 3, 4, 6, 7, 8]
68	VVSSIEQKTEGAEKK	acetylation	[1]
68	VVSSIEQKTEGAEKK	ubiquitination	[3, 6, 7, 8]
74	QKTEGAEKKQQMARE	ubiquitination	[7]
85	MAREYREKIETELRD	ubiquitination	[3]
115	NASQAESKVFYLKMK	acetylation	[1]
115	NASQAESKVFYLKMK	ubiquitination	[3, 5, 7]
120	ESKVFYLKMKGDYYR	ubiquitination	[3, 6, 7]
122	KVFYLKMKGDYYRYL	ubiquitination	[6, 7]
138	EVAAGDDKKGIVDQS	ubiquitination	[2, 3, 4, 6, 7, 8]
139	VAAGDDKKGIVDQSQ	ubiquitination	[3, 4, 5, 6, 7, 8]
157	QEAFEISKKEMQPTH	ubiquitination	[3, 4, 6, 7]
158	EAFEISKKEMQPTHP	ubiquitination	[3, 4, 5, 6, 7]
193	EKACSLAKTAFDEAI	ubiquitination	[6, 8]

Reference

 [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] 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]
 [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] 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]
 [5] 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]
 [6] 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]
 [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] 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. 

Sequence Annotation

 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 3 3 N6-acetyllysine.
 MOD_RES 58 58 Phosphoserine; by PKA and PKB/AKT1.
 MOD_RES 68 68 N6-acetyllysine.
 MOD_RES 184 184 Phosphoserine; by MAPK8.
 MOD_RES 207 207 Phosphoserine.
 MOD_RES 232 232 Phosphothreonine; by CK1.  

Keyword

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

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 245 AA 

Protein Sequence

Gene Ontology

 GO:0031252; C:cell leading edge; IEA:Compara.
 GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
 GO:0014069; C:postsynaptic density; IEA:Compara.
 GO:0043234; C:protein complex; IEA:Compara.
 GO:0016044; P:cellular membrane organization; TAS:Reactome.
 GO:0010467; P:gene expression; TAS:Reactome.
 GO:0002553; P:histamine secretion by mast cell; IEA:Compara.
 GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:Reactome.
 GO:0016071; P:mRNA metabolic process; TAS:Reactome.
 GO:0043066; P:negative regulation of apoptotic process; TAS:ProtInc.
 GO:0030168; P:platelet activation; TAS:Reactome.
 GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
 GO:0006626; P:protein targeting to mitochondrion; IEA:Compara. 

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.