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Protein Page:
14-3-3 zeta (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
14-3-3 zeta a protein of the 14-3-3 family of proteins which mediate signal transduction by binding to phosphoserine-containing proteins. A multifunctional regulator of the cell signaling processes. Phosphorylation apparently disrupts homodimerization. Note: This description may include information from UniProtKB.
Protein type: Adaptor/scaffold; Motility/polarity/chemotaxis
Cellular Component: nucleoplasm; extracellular space; protein complex; cytoplasmic vesicle membrane; mast cell granule; mitochondrion; perinuclear region of cytoplasm; postsynaptic density; leading edge; cytoplasm; melanosome; cytosol
Molecular Function: protein domain specific binding; identical protein binding; protein binding; protein complex binding; transcription factor binding; protein kinase binding
Biological Process: platelet activation; histamine secretion by mast cell; RNA metabolic process; apoptosis; gene expression; signal transduction; blood coagulation; protein targeting to mitochondrion; mRNA metabolic process; negative regulation of apoptosis
Reference #:  P63104 (UniProtKB)
Alt. Names/Synonyms: 14-3-3 protein zeta/delta; 14-3-3 protein/cytosolic phospholipase A2; 14-3-3 zeta; 14-3-3-zeta; 1433Z; KCIP-1; MGC111427; MGC126532; MGC138156; phospholipase A2; Protein kinase C inhibitor protein 1; protein kinase C inhibitor protein-1; tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, zeta polypeptide; tyrosine 3/tryptophan 5 -monooxygenase activation protein, zeta polypeptide; YWHAZ
Gene Symbols: YWHAZ
Molecular weight: 27,745 Da
Basal Isoelectric point: 4.73  Predict pI for various phosphorylation states
CST Pathways:  Actin Dynamics  |  Apoptosis Regulation  |  Crosstalk between PTMs  |  G2/M DNA Damage Checkpoint  |  Growth And Differentiation Control by MAPKs  |  Hippo Signaling  |  Mitochondrial Control of Apoptosis  |  PI3K/Akt Signaling  |  SAPK/JNK Signaling Cascades
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

14-3-3 zeta

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene


Sites Implicated In
apoptosis, altered: S58‑p
activity, inhibited: T232‑p
molecular association, regulation: S58‑p, S184‑p, T232‑p
phosphorylation: S184‑p
protein conformation: S184‑p, T232‑p
protein degradation: S58‑p
protein stabilization: S184‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 28 K3-a _____MDkNELVQkA
0 6 K9-u DkNELVQkAkLAEQA
0 37 K11-u NELVQkAkLAEQAER
0 1 S28 DMAACMKSVTEQGAE
0 1 S37-p TEQGAELsNEERNLL
0 11 S45-p NEERNLLsVAykNVV
0 7 Y48-p RNLLsVAykNVVGAR
0 4 K49-a NLLsVAykNVVGARR
0 150 K49-u NLLsVAykNVVGARR
11 6 S58-p VVGARRSsWRVVssI
0 2 S63-p RSsWRVVssIEQkTE
0 2 S64-p SsWRVVssIEQkTEG
0 4 K68-a VVssIEQkTEGAEkK
0 7 K68-u VVssIEQkTEGAEkK
0 2 K74-a QkTEGAEkKQQMARE
0 1 K74 QkTEGAEKKQQMARE
0 2 K85-u MAREYREkIETELRD
0 1 S99-p DICNDVLsLLEKFLI
0 4 S110-p KFLIPNAsQAEskVF
0 2 S114-p PNAsQAEskVFYLkM
0 62 K115-a NAsQAEskVFYLkMk
0 1 K115 NAsQAEsKVFYLkMk
0 4 K120-a EskVFYLkMkGDYyR
0 72 K120-u EskVFYLkMkGDYyR
0 9 K122-u kVFYLkMkGDYyRyL
0 31 Y126-p LkMkGDYyRyLAEVA
0 3 Y128-p MkGDYyRyLAEVAAG
0 16 K138-a EVAAGDDkkGIVDQS
0 124 K138-u EVAAGDDkkGIVDQS
0 5 K139-a VAAGDDkkGIVDQSQ
0 38 K139-u VAAGDDkkGIVDQSQ
0 21 K157-a QEAFEISkkEMQPTH
0 10 K157-u QEAFEISkkEMQPTH
0 56 K158-u EAFEISkkEMQPTHP
1 1 Y179 LNFSVFYYEILNsPE
5 4 S184-p FYYEILNsPEKACSL
0 9 K193-u EKACSLAktAFDEAI
0 1 T194-p KACSLAktAFDEAIA
0 21 S207-p IAELDTLsEESykDS
0 3 Y211-p DTLsEESykDSTLIM
0 1 K212-m2 TLsEESykDSTLIMQ
0 1 T226 QLLRDNLTLWtsDtQ
0 3 T229-p RDNLTLWtsDtQGDE
0 6 S230-p DNLTLWtsDtQGDEA
6 28 T232-p LTLWtsDtQGDEAEA
  mouse

 
K3-a _____MDkNELVQkA
K9-u DkNELVQkAkLAEQA
K11-u NELVQkAkLAEQAER
S28-p DMAACMKsVTEQGAE
S37-p TEQGAELsNEERNLL
S45-p NEERNLLsVAykNVV
Y48-p RNLLsVAykNVVGAR
K49-a NLLsVAykNVVGARR
K49-u NLLsVAykNVVGARR
S58-p VVGARRSsWRVVSsI
S63 RSsWRVVSsIEQkTE
S64-p SsWRVVSsIEQkTEG
K68-a VVSsIEQkTEGAEkK
K68-u VVSsIEQkTEGAEkK
K74 QkTEGAEKKQQMARE
K74-u QkTEGAEkKQQMARE
K85-u MAREYREkIETELRD
S99-p DICNDVLsLLEKFLI
S110-p KFLIPNAsQPEskVF
S114-p PNAsQPEskVFYLkM
K115-a NAsQPEskVFYLkMk
K115-u NAsQPEskVFYLkMk
K120-a EskVFYLkMkGDYyR
K120-u EskVFYLkMkGDYyR
K122-u kVFYLkMkGDYyRyL
Y126-p LkMkGDYyRyLAEVA
Y128-p MkGDYyRyLAEVAAG
K138-a EVAAGDDkkGIVDQS
K138-u EVAAGDDkkGIVDQS
K139 VAAGDDkKGIVDQSQ
K139-u VAAGDDkkGIVDQSQ
K157-a QEAFEISkkEMQPTH
K157-u QEAFEISkkEMQPTH
K158-u EAFEISkkEMQPTHP
Y179-p LNFSVFYyEILNSPE
S184 FYyEILNSPEKACSL
K193-u EKACSLAkTAFDEAI
T194 KACSLAkTAFDEAIA
S207-p IAELDTLsEESyKDS
Y211-p DTLsEESyKDSTLIM
K212 TLsEESyKDSTLIMQ
T226-p QLLRDNLtLWtsDtQ
T229-p RDNLtLWtsDtQGDE
S230-p DNLtLWtsDtQGDEA
T232-p LtLWtsDtQGDEAEA
  rat

 
K3 _____MDKNELVQkA
K9-u DKNELVQkAkLAEQA
K11-u NELVQkAkLAEQAER
S28 DMAACMKSVTEQGAE
S37 TEQGAELSNEERNLL
S45 NEERNLLSVAYkNVV
Y48 RNLLSVAYkNVVGAR
K49 NLLSVAYKNVVGARR
K49-u NLLSVAYkNVVGARR
S58-p VVGARRSsWRVVSSI
S63 RSsWRVVSSIEQKTE
S64 SsWRVVSSIEQKTEG
K68 VVSSIEQKTEGAEKK
K68 VVSSIEQKTEGAEKK
K74 QKTEGAEKKQQMARE
K74 QKTEGAEKKQQMARE
K85 MAREYREKIETELRD
S99 DICNDVLSLLEKFLI
S110 KFLIPNASQPESKVF
S114 PNASQPESKVFYLkM
K115 NASQPESKVFYLkMk
K115 NASQPESKVFYLkMk
K120 ESKVFYLKMkGDYYR
K120-u ESKVFYLkMkGDYYR
K122-u KVFYLkMkGDYYRyL
Y126 LkMkGDYYRyLAEVA
Y128-p MkGDYYRyLAEVAAG
K138 EVAAGDDKkGIVDQS
K138-u EVAAGDDkkGIVDQS
K139 VAAGDDkKGIVDQSQ
K139-u VAAGDDkkGIVDQSQ
K157 QEAFEISKKEMQPTH
K157 QEAFEISKKEMQPTH
K158 EAFEISKKEMQPTHP
Y179 LNFSVFYYEILNSPE
S184 FYYEILNSPEKACSL
K193 EKACSLAKTAFDEAI
T194 KACSLAKTAFDEAIA
S207 IAELDTLSEESYKDS
Y211 DTLSEESYKDSTLIM
K212 TLSEESYKDSTLIMQ
T226 QLLRDNLTLWTSDTQ
T229 RDNLTLWTSDTQGDE
S230 DNLTLWTSDTQGDEA
T232 LTLWTSDTQGDEAEA
  sheep

 
K3 _____MDKNELVQKA
K9 DKNELVQKAKLAEQA
K11 NELVQKAKLAEQAER
S28 DMAACMKSVTEQGAE
S37 TEQGAELSNEERNLL
S45 NEERNLLSVAYKNVV
Y48 RNLLSVAYKNVVGAR
K49 NLLSVAYKNVVGARR
K49 NLLSVAYKNVVGARR
S58 VVGARRSSWRVVSSI
S63 RSSWRVVSSIEQKTE
S64 SSWRVVSSIEQKTEG
K68 VVSSIEQKTEGAEKK
K68 VVSSIEQKTEGAEKK
K74 QKTEGAEKKQQMARE
K74 QKTEGAEKKQQMARE
K85 MAREYREKIETELRD
S99 DICNDVLSLLEKFLI
S110 KFLIPNRSQPESKVF
S114 PNRSQPESKVFYLKM
K115 NRSQPESKVFYLKMK
K115 NRSQPESKVFYLKMK
K120 ESKVFYLKMKGDYYR
K120 ESKVFYLKMKGDYYR
K122 KVFYLKMKGDYYRYL
Y126 LKMKGDYYRYLAEVA
Y128 MKGDYYRYLAEVAAG
K138 EVAAGDDKKGIVDQS
K138 EVAAGDDKKGIVDQS
K139 VAAGDDKKGIVDQSQ
K139 VAAGDDKKGIVDQSQ
K157 QEAFEISKKEMQPTH
K157 QEAFEISKKEMQPTH
K158 EAFEISKKEMQPTHP
Y179 LNFSVFYYEILNsPE
S184-p FYYEILNsPEKACSL
K193 EKACSLAKTAFDEAI
T194 KACSLAKTAFDEAIA
S207 IAELDTLSEESYKDS
Y211 DTLSEESYKDSTLIM
K212 TLSEESYKDSTLIMQ
T226 QLLRDNLTLWTSDTQ
T229 RDNLTLWTSDTQGDE
S230 DNLTLWTSDTQGDEA
T232 LTLWTSDTQGDEAEA
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