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Protein

14-3-3 protein zeta/delta

Gene

YWHAZ

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -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

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

Organism-specific databases

VGNCiVGNC:53885 YWHAZ

Subcellular locationi

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). Interacts with SLITRK1 (By similarity).By similarity2 Publications

Sites

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

Binary interactionsi

WithEntry#Exp.IntActNotes
IGF1RP080693EBI-347095,EBI-475981From Homo sapiens.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi160005, 1 interactor
IntActiP63103, 11 interactors
MINTiP63103
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

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
OMAiLWTSSDS
OrthoDBiEOG091G0VKY
TreeFamiTF102003

Family and domain databases

Gene3Di1.20.190.20, 1 hit
InterProiView protein in InterPro
IPR000308 14-3-3
IPR023409 14-3-3_CS
IPR036815 14-3-3_dom_sf
IPR023410 14-3-3_domain
PANTHERiPTHR18860 PTHR18860, 1 hit
PfamiView protein in Pfam
PF00244 14-3-3, 1 hit
PIRSFiPIRSF000868 14-3-3, 1 hit
PRINTSiPR00305 1433ZETA
SMARTiView protein in SMART
SM00101 14_3_3, 1 hit
SUPFAMiSSF48445 SSF48445, 1 hit
PROSITEiView protein in PROSITE
PS00796 1433_1, 1 hit
PS00797 1433_2, 1 hit

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

Similar proteinsi

Entry informationi

Entry namei1433Z_BOVIN
AccessioniPrimary (citable) accession number: P63103
Secondary accession number(s): P29213, P29312, Q3ZCF9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: September 13, 2004
Last modified: July 18, 2018
This is version 129 of the entry and version 1 of the sequence. See 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

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