LIG_14-3-3_1
ELM server details
ELM
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Functional site class:
14-3-3 ligand
Functional site description:
14-3-3 proteins interact with phosphoserine or phosphothreonine containing motifs.
ELM(s): LIG_14-3-3_1, LIG_14-3-3_2, LIG_14-3-3_3
LIG_14-3-3_1 description: 14-3-3 proteins interaction motif 1
Pattern: R[SFYW].S.P
Present in taxon(s): Homo sapiens  Xenopus laevis  Saccharomyces cerevisiae  Caenorhabditis elegans  Schizosaccharomyces pombe  Eukaryota  Bos taurus  Mus musculus  Gallus gallus  Petroselinum crispum  Rattus norvegicus  Arabidopsis thaliana  Dictyostelium discoideum  
Not represented in taxon(s):

o See instances for LIG_14-3-3_1


o Abstract

The 14-3-3 proteins constitute a family of conserved proteins present in all eukaryotic organisms so far investigated, including seven isotypes in human cells. They are involved in important cellular processes such as signal transduction, cell-cycle control, apoptosis, stress response and malignant transformation. More than one hundred different binding partners for these proteins have been reported yet. 14-3-3 proteins were the first signaling molecules to be identified as discrete phosphoserine/threonine binding modules, although cases of phosphorilation-independent interaction has been reported. Although the exact function of 14-3-3 proteins is still unknown, they are known to act as adaptor molecules to mediate protein-protein interactions and the subcellular localisation and to regulate enzymes activity. Though 14-3-3 proteins perform different functions for different ligands, general mechanisms of 14-3-3 action include changes in activity of bound ligands, altered association of bound ligands with other cellular components, and changes in intracellular localization of 14-3-3-bound cargo.

o Selected references

Conklin DS, Galaktionov K, Beach D
14-3-3 proteins associate with cdc25 phosphatases.
Proc Natl Acad Sci U S A 1995 Aug 15;92(17) : 7892-6.
PMID: 7644510

Fanger GR, Widmann C, Porter AC, Sather S, Johnson GL, Vaillancourt RR
14-3-3 proteins interact with specific MEK kinases.
J Biol Chem 1998 Feb 6;273(6) : 3476-83.
PMID: 9452471

Furlanetto RW, Dey BR, Lopaczynski W, Nissley SP
14-3-3 proteins interact with the insulin-like growth factor receptor but not the insulin receptor.
Biochem J 1997 Nov 1;327() : 765-71.
PMID: 9581554

Itagaki C, Isobe T, Taoka M, Natsume T, Nomura N, Horigome T, Omata S, Ichinose H, Nagatsu T, Greene LA, Ichimura T
Stimulus-coupled interaction of tyrosine hydroxylase with 14-3-3 proteins.
Biochemistry 1999 Nov 23;38(47) : 15673-80.
PMID: 10569954

Luk SC, Ngai SM, Tsui SK, Fung KP, Lee CY, Waye MM
In vivo and in vitro association of 14-3-3 epsilon isoform with calmodulin: implication for signal transduction and cell proliferation.
J Cell Biochem 1999 Apr 1;73(1) : 31-5.
PMID: 10088721

Meller N, Liu YC, Collins TL, Bonnefoy-Berard N, Baier G, Isakov N, Altman A
Direct interaction between protein kinase C theta (PKC theta) and 14-3-3 tau in T cells: 14-3-3 overexpression results in inhibition of PKC theta translocation and function.
Mol Cell Biol 1996 Oct;16(10) : 5782-91.
PMID: 8816492

Reuther GW, Fu H, Cripe LD, Collier RJ, Pendergast AM
Association of the protein kinases c-Bcr and Bcr-Abl with proteins of the 14-3-3 family.
Science 1994 Oct 7;266(5182) : 129-33.
PMID: 7939633

Sladeczek F, Camonis JH, Burnol AF, Le Bouffant F
The Cdk-like protein PCTAIRE-1 from mouse brain associates with p11 and 14-3-3 proteins.
Mol Gen Genet 1997 May 20;254(5) : 571-7.
PMID: 9197417

Sliva D, Gu M, Zhu YX, Chen J, Tsai S, Du X, Yang YC
14-3-3zeta interacts with the alpha-chain of human interleukin 9 receptor.
Biochem J 2000 Feb 1;345() : 741-7.
PMID: 10642536

Tzivion G, Avruch J
14-3-3 proteins: active cofactors in cellular regulation by serine/threonine phosphorylation.
J Biol Chem 2002 Feb 1;277(5) : 3061-4.
PMID: 11709560

Yip-Schneider MT, Miao W, Lin A, Barnard DS, Tzivion G, Marshall MS
Regulation of the Raf-1 kinase domain by phosphorylation and 14-3-3 association.
Biochem J 2000 Oct 1;351() : 151-9.
PMID: 10998357

Zha J, Harada H, Yang E, Jockel J, Korsmeyer SJ
Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L)
Cell 1996 Nov 15;87(4) : 619-28.
PMID: 8929531

Zhang L, Chen J, Fu H
Suppression of apoptosis signal-regulating kinase 1-induced cell death by 14-3-3 proteins.
Proc Natl Acad Sci U S A 1999 Jul 20;96(15) : 8511-5.
PMID: 10411906

o This ELM has been assigned the following Gene Ontology (GO) terms for biological process, cellular component and molecular function.

Biological Process
  cell proliferation
  cell cycle control
  cell cycle checkpoint
  dopamine biosynthesis from tyrosine
  heart development
  protein kinase cascade
  G-protein coupled receptor protein signaling pathway
  induction of apoptosis by DNA damage
  mismatch repair
  apoptotic program
Cellular Component
  internal side of plasma membrane
  nucleus
  cytosol
Molecular Function
  protein domain specific binding

 

o Instances for LIG_14-3-3_1

SequencePositionSubsequence
(Click for evidence information)
PDBGene NameProtein DescriptionOrganism
MT_POVM3 273-278 TYSVMRSHSYPPTRVLQ 1QJB
- Middle T antigen (MT) (MT-AG). Murine polyomavirus (strain 3) (MPyV).
MPIP3_HUMAN 213-218 RSGLYRSPSMPENLNRP - Name=CDC25C; M-phase inducer phosphatase 3 (EC 3.1.3.48) (Dual specificity phosphatase Cdc25C). Homo sapiens (Human).
RAF1_HUMAN 256-261 LSQRQRSTSTPNVHMVS - Name=RAF1; Synonyms=RAF; RAF proto-oncogene serine/threonine-protein kinase (EC 2.7.11.1) (Raf- 1) (C-RAF) (cRaf). Homo sapiens (Human).
RAF1_HUMAN 618-623 LPKINRSASEPSLHRAA - Name=RAF1; Synonyms=RAF; RAF proto-oncogene serine/threonine-protein kinase (EC 2.7.11.1) (Raf- 1) (C-RAF) (cRaf). Homo sapiens (Human).
BAD_RAT 134-139 SPFRGRSRSAPPNLWAA - Name=Bad; Bcl2 antagonist of cell death (BAD) (Bcl-2-binding component 6) (Bcl- xL/Bcl-2-associated death promoter). Rattus norvegicus (Rat).
M3K5_HUMAN 963-968 SNEYLRSISLPVPVLVE - Name=MAP3K5; Synonyms=ASK1, MAPKKK5, MEKK5; Mitogen-activated protein kinase kinase kinase 5 (EC 2.7.11.25) (MAPK/ERK kinase kinase 5) (MEK kinase 5) (MEKK 5) (Apoptosis signal- regulating kinase 1) (ASK-1). Homo sapiens (Human).