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:
PPXY is the motif recognized by WW domains of Group I
Pattern: PP.Y
Pattern Probability: 0.0001257
Present in taxons: Eukaryota Homo sapiens Mus musculus Rattus norvegicus
Interaction Domain:
WW (PF00397) WW domain (Stochiometry: 1 : 1)
PDB Structure: 1EG4
<a href="http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1EG4" title="" target="_blank"><img src="/media/pdb.ico.png"/>1EG4</a>
o See 28 Instances for LIG_WW_1
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 12 selected references:

o 9 GO-Terms:

o 28 Instances for LIG_WW_1
(click table headers for sorting; Notes column: =Number of Switches, =Number of Interactions)
Protein NameGene NameStartEndSubsequenceLogic#Ev.OrganismNotes
WBP1_MOUSE Wbp1 173 176 VVHHPGTPPPPYTVGPGYPW TP 1 Mus musculus (House mouse)
DAG1_HUMAN DAG1 889 892 KGSRPKNMTPYRSPPPYVPP TP 1 Homo sapiens (Human)
4 
VP8_BTV10 S10 36 39 RVDDTISQPPRYAPSAPMPS TP 3 Bluetongue virus (serotype 10 / American isolate)
1 
GAG_MPMV gag 202 205 DWPPFLTRPPPYNKATPSAP U 2 Mason-Pfizer monkey virus
LMP2_EBVB9 LMP2 57 60 ERESNEEPPPPYEDPYWGNG TP 2 Human herpesvirus 4 (strain B95-8) (Epstein-Barr virus (strain B95-8))
1 
2 
GAG_RSVP gag-pro 172 175 NCATASAPPPPYVGSGLYPS U 2 Rous sarcoma virus - Prague C
LMP2_EBVB9 LMP2 98 101 HDGNDGLPPPPYSPRDDSSQ TP 3 Human herpesvirus 4 (strain B95-8) (Epstein-Barr virus (strain B95-8))
1 
1 
MATRX_RABVS M 35 38 DDDDLWLPPPEYVPLKELTG U 2 Rabies virus SAD B19
CAPSP_ADE02 PIII 12 15 AAMYEEGPPPSYESVVSAAP TP 4 Human adenovirus 2
1 
UL56_HHV2H UL56 23 26 GDDSVIDAPPPYESVAGASA TP 5 Human herpesvirus 2 strain HG52
1 
VP40_MABVM VP40 16 19 NTYMQYLNPPPYADHGANQL TP 3 Marburg virus - Musoke, Kenya, 1980
1 
VP40_EBOZM VP40 10 13 RRVILPTAPPEYMEAIYPVR TP 3 Ebola virus - Mayinga, Zaire, 1976
2 
Z_LASSJ Z 94 97 APTAPPTGAADSIRPPPYSP U 1 Lassa virus Josiah
Z_LYCVA Z 85 88 PLPTRLKISTAPSSPPPYEE U 2 Lymphocytic choriomeningitis virus (strain Armstrong)
SMAD1_HUMAN SMAD1 224 227 FQMPADTPPPAYLPPEDPMT TP 1 Homo sapiens (Human)
ERBB4_HUMAN ERBB4 1053 1056 RSEIGHSPPPAYTPMSGNQF TP 4 Homo sapiens (Human)
3 
SCNNG_HUMAN SCNN1G 624 627 GTQVPGTPPPKYNTLRLERA TP 5 Homo sapiens (Human)
1 
SCNNG_RAT Scnn1g 625 628 GSTVPGTPPPRYNTLRLDRA TP 4 Rattus norvegicus (Norway rat)
SCNNB_HUMAN SCNN1B 617 620 ALPIPGTPPPNYDSLRLQPL TP 5 Homo sapiens (Human)
SCNNA_HUMAN SCNN1A 641 644 PSPALTAPPPAYATLGPRPS TP 6 Homo sapiens (Human)
P73_HUMAN TP73 484 487 VSGSHCTPPPPYHADPSLVS TP 8 Homo sapiens (Human)
2 
1 
P63_MOUSE Tp63 540 543 PSTSHCTPPPPYPTDCSIVS TP 1 Mus musculus (House mouse)
1 
GAG_HTL1A gag 118 121 PPDSDPQIPPPYVEPTAPQV TP 2 Human T-cell lymphotrophic virus type 1 (strain ATK)
MATRX_VSIVA M 24 27 KSKKLGIAPPPYEEDTSMEY U 1 Vesicular stomatitis Indiana virus strain San Juan
UL56_HHV2H UL56 49 52 DIDTPTDSPPPYSAGTSPVG TP 5 Human herpesvirus 2 strain HG52
1 
AMOT_HUMAN AMOT 239 242 KGMEHRGPPPEYPFKGMPPQ TP 3 Homo sapiens (Human)
3 
JUN_MOUSE Jun 167 170 YSASLHSEPPVYANLSNFNP TP 6 Mus musculus (House mouse)
1 
1 
JUNB_MOUSE Junb 176 179 GVYAGPEPPPVYTNLSSYSP TP 5 Mus musculus (House mouse)
1 
Please cite: The Eukaryotic Linear Motif Resource ELM: 10 Years and Counting (PMID:24214962)

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