Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

14-3-3 protein zeta/delta

Gene

YWHAZ

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Activates the ADP-ribosyltransferase (exoS) activity of bacterial origin.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-BTA-111447. Activation of BAD and translocation to mitochondria.
R-BTA-1445148. Translocation of GLUT4 to the plasma membrane.
R-BTA-3769402. Deactivation of the beta-catenin transactivating complex.
R-BTA-392517. Rap1 signalling.
R-BTA-430116. GP1b-IX-V activation signalling.
R-BTA-450604. KSRP (KHSRP) binds and destabilizes mRNA.
R-BTA-512988. Interleukin-3, 5 and GM-CSF signaling.
R-BTA-5625740. RHO GTPases activate PKNs.
R-BTA-5628897. TP53 Regulates Metabolic Genes.
R-BTA-75035. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.

Names & Taxonomyi

Protein namesi
Recommended name:
14-3-3 protein zeta/delta
Alternative name(s):
Factor activating exoenzyme S
Short name:
FAS
Protein kinase C inhibitor protein 1
Short name:
KCIP-1
Gene namesi
Name:YWHAZ
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 14

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000586261 – 24514-3-3 protein zeta/deltaAdd BLAST245

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei3N6-acetyllysineBy similarity1
Modified residuei58Phosphoserine; by PKABy similarity1
Modified residuei68N6-acetyllysineBy similarity1
Modified residuei184PhosphoserineBy similarity1
Modified residuei207PhosphoserineBy similarity1
Modified residuei210PhosphoserineBy similarity1
Modified residuei232Phosphothreonine; by CK1By similarity1

Post-translational modificationi

The delta, brain-specific form differs from the zeta form in being phosphorylated (By similarity). Phosphorylation on Ser-184 by MAPK8; promotes dissociation of BAX and translocation of BAX to mitochondria. Phosphorylation on Thr-232; inhibits binding of RAF1 (By similarity). Phosphorylated on Ser-58 by PKA and protein kinase C delta type catalytic subunit in a sphingosine-dependent fashion. Phosphorylation on Ser-58 by PKA; disrupts homodimerization and heterodimerization with YHAE and TP53 (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP63103.
PeptideAtlasiP63103.
PRIDEiP63103.

Expressioni

Gene expression databases

BgeeiENSBTAG00000000236.

Interactioni

Subunit structurei

Homodimer. Heterodimerizes with YWHAE (By similarity). Homo- and hetero-dimerization is inhibited by phosphorylation on Ser-58 (By similarity). Interacts with FOXO4, NOXA1, SSH1 ARHGEF2, CDK16 and BSPRY. Interacts with WEE1 (C-terminal). Interacts with MLF1 (phosphorylated form); the interaction retains it in the cytoplasm. Interacts with BAX; the interaction occurs in the cytoplasm. Under stress conditions, MAPK8-mediated phosphorylation releases BAX to mitochondria. Interacts with TP53; the interaction enhances p53 transcriptional activity. The Ser-58 phosphorylated form inhibits this interaction and p53 transcriptional activity. Interacts with ABL1 (phosphorylated form); the interaction retains ABL1 in the cytoplasm. Interacts with PKA-phosphorylated AANAT; the interaction modulates AANAT enzymatic activity by increasing affinity for arylalkylamines and acetyl-CoA and protecting the enzyme from dephosphorylation and proteasomal degradation. It may also prevent thiol-dependent inactivation (By similarity). Interacts with AKT1; the interaction phosphorylates YWHAZ and modulates dimerization (By similarity). Interacts with GAB2. Interacts with BCL2L11, SAMSN1 and TLK2 (By similarity). Interacts with phosphorylated RAF1; the interaction is inhibited when YWHAZ is phosphorylated on Thr-232. Interacts with Thr-phosphorylated ITGB2. Interacts with the 'Thr-369' phosphorylated form of DAPK2 (By similarity). Interacts with PI4KB, TBC1D22A and TBC1D22B (By similarity). Interacts with ZFP36L1 (via phosphorylated form); this interaction occurs in a p38 MAPK- and AKT-signaling pathways (By similarity).By similarity2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei56Interaction with phosphoserine on interacting protein1
Sitei127Interaction with phosphoserine on interacting protein1

Protein-protein interaction databases

BioGridi160005. 1 interactor.
IntActiP63103. 10 interactors.
MINTiMINT-99823.
STRINGi9913.ENSBTAP00000000289.

Structurei

Secondary structure

1245
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 15Combined sources13
Helixi19 – 30Combined sources12
Turni31 – 33Combined sources3
Helixi38 – 67Combined sources30
Helixi74 – 103Combined sources30
Turni104 – 107Combined sources4
Helixi112 – 115Combined sources4
Helixi117 – 131Combined sources15
Helixi137 – 156Combined sources20
Turni157 – 159Combined sources3
Helixi165 – 180Combined sources16
Helixi185 – 201Combined sources17
Turni202 – 205Combined sources4
Turni208 – 210Combined sources3
Helixi211 – 226Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A37X-ray3.60A/B1-245[»]
1A38X-ray3.35A/B1-245[»]
1A4OX-ray2.80A/B/C/D1-245[»]
2V7DX-ray2.50A/B/C/D1-245[»]
ProteinModelPortaliP63103.
SMRiP63103.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63103.

Family & Domainsi

Sequence similaritiesi

Belongs to the 14-3-3 family.Curated

Phylogenomic databases

eggNOGiKOG0841. Eukaryota.
COG5040. LUCA.
GeneTreeiENSGT00760000119116.
HOGENOMiHOG000240379.
HOVERGENiHBG050423.
InParanoidiP63103.
KOiK16197.
OMAiEHPVMDK.
OrthoDBiEOG091G0VKY.
TreeFamiTF102003.

Family and domain databases

InterProiIPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view]
PANTHERiPTHR18860. PTHR18860. 1 hit.
PfamiPF00244. 14-3-3. 1 hit.
[Graphical view]
PIRSFiPIRSF000868. 14-3-3. 1 hit.
PRINTSiPR00305. 1433ZETA.
SMARTiSM00101. 14_3_3. 1 hit.
[Graphical view]
SUPFAMiSSF48445. SSF48445. 1 hit.
PROSITEiPS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P63103-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDKNELVQKA KLAEQAERYD DMAACMKSVT EQGAELSNEE RNLLSVAYKN
60 70 80 90 100
VVGARRSSWR VVSSIEQKTE GAEKKQQMAR EYREKIETEL RDICNDVLSL
110 120 130 140 150
LEKFLIPNAS QAESKVFYLK MKGDYYRYLA EVAAGDDKKG IVDQSQQAYQ
160 170 180 190 200
EAFEISKKEM QPTHPIRLGL ALNFSVFYYE ILNSPEKACS LAKTAFDEAI
210 220 230 240
AELDTLSEES YKDSTLIMQL LRDNLTLWTS DTQGDEAEAG EGGEN
Length:245
Mass (Da):27,745
Last modified:September 13, 2004 - v1
Checksum:iD464DF2286BBFE60
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti25C → A AA sequence (PubMed:1499718).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07955 mRNA. Translation: AAA30514.1.
BC102382 mRNA. Translation: AAI02383.1.
PIRiA47389.
S65013.
RefSeqiNP_777239.1. NM_174814.2.
UniGeneiBt.111451.

Genome annotation databases

EnsembliENSBTAT00000000289; ENSBTAP00000000289; ENSBTAG00000000236.
GeneIDi287022.
KEGGibta:287022.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07955 mRNA. Translation: AAA30514.1.
BC102382 mRNA. Translation: AAI02383.1.
PIRiA47389.
S65013.
RefSeqiNP_777239.1. NM_174814.2.
UniGeneiBt.111451.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A37X-ray3.60A/B1-245[»]
1A38X-ray3.35A/B1-245[»]
1A4OX-ray2.80A/B/C/D1-245[»]
2V7DX-ray2.50A/B/C/D1-245[»]
ProteinModelPortaliP63103.
SMRiP63103.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi160005. 1 interactor.
IntActiP63103. 10 interactors.
MINTiMINT-99823.
STRINGi9913.ENSBTAP00000000289.

Proteomic databases

PaxDbiP63103.
PeptideAtlasiP63103.
PRIDEiP63103.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000000289; ENSBTAP00000000289; ENSBTAG00000000236.
GeneIDi287022.
KEGGibta:287022.

Organism-specific databases

CTDi7534.

Phylogenomic databases

eggNOGiKOG0841. Eukaryota.
COG5040. LUCA.
GeneTreeiENSGT00760000119116.
HOGENOMiHOG000240379.
HOVERGENiHBG050423.
InParanoidiP63103.
KOiK16197.
OMAiEHPVMDK.
OrthoDBiEOG091G0VKY.
TreeFamiTF102003.

Enzyme and pathway databases

ReactomeiR-BTA-111447. Activation of BAD and translocation to mitochondria.
R-BTA-1445148. Translocation of GLUT4 to the plasma membrane.
R-BTA-3769402. Deactivation of the beta-catenin transactivating complex.
R-BTA-392517. Rap1 signalling.
R-BTA-430116. GP1b-IX-V activation signalling.
R-BTA-450604. KSRP (KHSRP) binds and destabilizes mRNA.
R-BTA-512988. Interleukin-3, 5 and GM-CSF signaling.
R-BTA-5625740. RHO GTPases activate PKNs.
R-BTA-5628897. TP53 Regulates Metabolic Genes.
R-BTA-75035. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.

Miscellaneous databases

EvolutionaryTraceiP63103.
PROiP63103.

Gene expression databases

BgeeiENSBTAG00000000236.

Family and domain databases

InterProiIPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view]
PANTHERiPTHR18860. PTHR18860. 1 hit.
PfamiPF00244. 14-3-3. 1 hit.
[Graphical view]
PIRSFiPIRSF000868. 14-3-3. 1 hit.
PRINTSiPR00305. 1433ZETA.
SMARTiSM00101. 14_3_3. 1 hit.
[Graphical view]
SUPFAMiSSF48445. SSF48445. 1 hit.
PROSITEiPS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry namei1433Z_BOVIN
AccessioniPrimary (citable) accession number: P63103
Secondary accession number(s): P29213, P29312, Q3ZCF9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: September 13, 2004
Last modified: November 30, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.