CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009688
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 14-3-3 protein zeta/delta 
Protein Synonyms/Alias
 Protein kinase C inhibitor protein 1; KCIP-1; SEZ-2 
Gene Name
 Ywhaz 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
9DKNELVQKAKLAEQAubiquitination[1]
11NELVQKAKLAEQAERubiquitination[1, 2]
49NLLSVAYKNVVGARRubiquitination[1]
68VVSSIEQKTEGAEKKubiquitination[1]
74QKTEGAEKKQQMAREubiquitination[1]
85MAREYREKIETELRDubiquitination[1]
115NASQPESKVFYLKMKacetylation[3, 4]
115NASQPESKVFYLKMKubiquitination[1]
120ESKVFYLKMKGDYYRubiquitination[1]
122KVFYLKMKGDYYRYLubiquitination[1]
138EVAAGDDKKGIVDQSubiquitination[1, 2]
139VAAGDDKKGIVDQSQubiquitination[1]
157QEAFEISKKEMQPTHacetylation[3, 4]
157QEAFEISKKEMQPTHubiquitination[1]
158EAFEISKKEMQPTHPubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] BTB-ZF factors recruit the E3 ligase cullin 3 to regulate lymphoid effector programs.
 Mathew R, Seiler MP, Scanlon ST, Mao AP, Constantinides MG, Bertozzi-Villa C, Singer JD, Bendelac A.
 Nature. 2012 Nov 22;491(7425):618-21. [PMID: 23086144]
 [3] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [4] 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 (By similarity).
 MOD_RES 3 3 N6-acetyllysine (By similarity).
 MOD_RES 58 58 Phosphoserine; by PKA.
 MOD_RES 68 68 N6-acetyllysine (By similarity).
 MOD_RES 184 184 Phosphoserine (By similarity).
 MOD_RES 207 207 Phosphoserine (By similarity).
 MOD_RES 232 232 Phosphothreonine; by CK1 (By similarity).  
Keyword
 Acetylation; Complete proteome; Cytoplasm; Direct protein sequencing; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 245 AA 
Protein Sequence
MDKNELVQKA KLAEQAERYD DMAACMKSVT EQGAELSNEE RNLLSVAYKN VVGARRSSWR 60
VVSSIEQKTE GAEKKQQMAR EYREKIETEL RDICNDVLSL LEKFLIPNAS QPESKVFYLK 120
MKGDYYRYLA EVAAGDDKKG IVDQSQQAYQ EAFEISKKEM QPTHPIRLGL ALNFSVFYYE 180
ILNSPEKACS LAKTAFDEAI AELDTLSEES YKDSTLIMQL LRDNLTLWTS DTQGDEAEAG 240
EGGEN 245 
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; IDA:MGI.
 GO:0005634; C:nucleus; IDA:MGI.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
 GO:0014069; C:postsynaptic density; IEA:Compara.
 GO:0043234; C:protein complex; IEA:Compara.
 GO:0019904; F:protein domain specific binding; IDA:UniProtKB.
 GO:0002553; P:histamine secretion by mast cell; IEA:Compara.
 GO:0006605; P:protein targeting; IDA:MGI.
 GO:0006626; P:protein targeting to mitochondrion; IEA:Compara.
 GO:0010941; P:regulation of cell death; IGI:MGI. 
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.