LIG_WW_4
ELM server details
ELM
blue dot
Functional site class:
WW ligand
Functional site description:
the motif is implicated in protein-protein interactions mediated WW domains
ELM(s): LIG_WW_4, LIG_WW_1, LIG_WW_2, LIG_WW_3
LIG_WW_4 description: Class IV WW domains interaction motif; phosphorylation-dependent interaction.
Pattern: ...[ST]P.
Present in taxon(s): Homo sapiens  Eukaryota  Saccharomyces cerevisiae  
Not represented in taxon(s):

o Abstract

WW are small modular domains of 38-40 residues long that mediate protein-protein interaction through binding of short proline rich regions within proteins. WW domain-containing proteins are involved in many cellular processes such as ubiquitin mediated protein degradation and mitotic regulation and they are also implicated directly or indirectly in several human diseases such as muscular distrophy and Alzheimer’s and Huntington’s diseases. Based on their ligand specificity, the WW domains can be devided in five class. Group I WW domains bind proteins containing the PPXY motif, while the group II recognizes the PPLP motif. Group IV recognition is serine-phosphorylation dependent.

o Selected references

Kato Y, Ito M, Kawai K, Nagata K, Tanokura M
Determinants of ligand specificity in groups I and IV WW domains as studied by surface plasmon resonance and model building.
J Biol Chem 2002 Mar 22;277(12) : 10173-7.
PMID: 11751914

Lu PJ, Zhou XZ, Shen M, Lu KP
Function of WW domains as phosphoserine- or phosphothreonine-binding modules.
Science 1999 Feb 26;283(5406) : 1325-8.
PMID: 10037602

Morris DP, Phatnani HP, Greenleaf AL
Phospho-carboxyl-terminal domain binding and the role of a prolyl isomerase in pre-mRNA 3'-End formation.
J Biol Chem 1999 Oct 29;274(44) : 31583-7.
PMID: 10531363

Myers JK, Morris DP, Greenleaf AL, Oas TG
Phosphorylation of RNA polymerase II CTD fragments results in tight binding to the WW domain from the yeast prolyl isomerase Ess1.
Biochemistry 2001 Jul 24;40(29) : 8479-86.
PMID: 11456485

Sudol M, Sliwa K, Russo T
Functions of WW domains in the nucleus.
FEBS Lett 2001 Feb 16;490(3) : 190-5.
PMID: 11223034

Verdecia MA, Bowman ME, Lu KP, Hunter T, Noel JP
Structural basis for phosphoserine-proline recognition by group IV WW domains.
Nat Struct Biol 2000 Aug;7(8) : 639-43.
PMID: 10932246

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

Biological Process
  start control point of mitotic cell cycle
  transcription from Pol II promoter
  cell cycle control
  cell proliferation
  mitotic metaphase/anaphase transition
  regulation of mitosis
Cellular Component
  cytosol
  nucleus
Molecular Function
  DNA-directed RNA polymerase II
  DNA binding
  protein kinase

 

o Instances for LIG_WW_4

No instances annotated