The Eukaryote Linear Motif resource for Functional Sites in Proteins
Accession:
Functional site class:
WW domain ligands
Functional site description:
WW Domains are small but abundant domains found in diverse regulatory situations. The binding peptide motifs appear always to involve proline residues. Specific motifs vary for different WW domains and in some cases must be phosphorylated on a serine or threonine.
ELMs with same func. site: DOC_WW_Pin1_4  LIG_WW_1  LIG_WW_2  LIG_WW_3 
ELM Description:
PPLP is the motif recognized by WW domains of Group II
Pattern: PPLP
Pattern Probability: 0.0000613
Present in taxons: Eukaryota Homo sapiens Mus musculus Rattus norvegicus
Interaction Domain:
WW (PF00397) WW domain (Stochiometry: 1 : 1)
o See 3 Instances for LIG_WW_2
o Abstract
WW are small modular domains of 38-40 residues long that mediate protein-protein interaction through binding of short proline-containing peptides that are typically in regions of native disordered polypeptide. WW are named after a pair of tryptophan residues that are important for structure-function. WW domains can occur singly or in clusters of up to four, as in the ubiquitin ligase Nedd4. 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 specificities, the WW domains have been divided into four classes. Group I WW domains bind proteins containing the PPXY motif, while group II recognize the PPLP motif. Group III recognise PPR motifs. There may be some overlap between the group II and III specificities. Group IV recognition is of p(ST)P sites and is dependent on phosphorylation by proline-directed kinases.
The peptidyl-prolyl cis/trans isomerases (PPIase) are evolutionarily conserved enzymes that catalyse the cis/trans isomerization of peptidyl-prolyl peptide bonds. Pin1 is a unique PPIase that recognizes only the phosphorylated S/T motif preceding a proline residue. It is a multidomain protein contains a WW domain and PPIase domain and both domains work together to target the p(S/T)P sequence. Pin1 acts a mitotic regulator by catalyzing the isomerization of p(S/T)P motifs present in a defined subset of mitosis-specific phosphoproteins and also plays essential roles in transcription, DNA damage response, neuronal survival etc. The consequence of Pin1-mediated isomerization varies in individual substrates and phosphorylation sites which make them amenable to different processes like dephosphorylation, protein degradation, cleavage and targeting to different sub cellular localization etc. It is also found that the aberrant function of pin1 is linked to many diseases like cancer, AD, asthma, ageing and microbial infection and thus it represents a major therapeutic target.
o 6 selected references:

o 9 GO-Terms:

o 3 Instances for LIG_WW_2
(click table headers for sorting; Notes column: =Number of Switches, =Number of Interactions)
Protein NameGene NameStartEndSubsequenceLogic#Ev.OrganismNotes
SF01_MOUSE Sf1 575 578 VPLPPGVQPPLPPGAPPPPP TP 2 Mus musculus (House mouse)
1 
FMN1_MOUSE Fmn1 877 880 SPPAPPTPPPLPPPLIPPPP TP 6 Mus musculus (House mouse)
2 
ENAH_MOUSE Enah 602 605 PPPPPPPAPPLPASGIFSGS TP 6 Mus musculus (House mouse)
1 
Please cite: The Eukaryotic Linear Motif Resource ELM: 10 Years and Counting (PMID:24214962)

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