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: 2JO9
<a href="http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=2JO9" title="" target="_blank"><img src="/media/pdb.ico.png"/>2JO9</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)
Acc., Gene-, NameStartEndSubsequenceLogic#Ev.OrganismNotes
P97764 Wbp1
WBP1_MOUSE
173 176 VVHHPGTPPPPYTVGPGYPW TP 1 Mus musculus (House mouse)
Q14118 DAG1
DAG1_HUMAN
889 892 KGSRPKNMTPYRSPPPYVPP TP 1 Homo sapiens (Human)
4 
P08363 S10
VP8_BTV10
36 39 RVDDTISQPPRYAPSAPMPS TP 3 Bluetongue virus (serotype 10 / American isolate)
1 
P07567 gag
GAG_MPMV
202 205 DWPPFLTRPPPYNKATPSAP U 2 Mason-Pfizer monkey virus
P13285 LMP2
LMP2_EBVB9
57 60 ERESNEEPPPPYEDPYWGNG TP 2 Human herpesvirus 4 (strain B95-8) (Epstein-Barr virus (strain B95-8))
1 
2 
P03322 gag-pro
GAG_RSVP
172 175 NCATASAPPPPYVGSGLYPS U 2 Rous sarcoma virus - Prague C
P13285 LMP2
LMP2_EBVB9
98 101 HDGNDGLPPPPYSPRDDSSQ TP 3 Human herpesvirus 4 (strain B95-8) (Epstein-Barr virus (strain B95-8))
1 
1 
P16287 M
MATRX_RABVS
35 38 DDDDLWLPPPEYVPLKELTG U 2 Rabies virus SAD B19
P03276 PIII
CAPSP_ADE02
12 15 AAMYEEGPPPSYESVVSAAP TP 4 Human adenovirus 2
1 
P28282 UL56
UL56_HHV2H
23 26 GDDSVIDAPPPYESVAGASA TP 5 Human herpesvirus 2 strain HG52
1 
P35260 VP40
VP40_MABVM
16 19 NTYMQYLNPPPYADHGANQL TP 3 Marburg virus - Musoke, Kenya, 1980
1 
Q05128 VP40
VP40_EBOZM
10 13 RRVILPTAPPEYMEAIYPVR TP 3 Ebola virus - Mayinga, Zaire, 1976
2 
O73557 Z
Z_LASSJ
94 97 APTAPPTGAADSIRPPPYSP U 1 Lassa virus Josiah
P18541 Z
Z_LYCVA
85 88 PLPTRLKISTAPSSPPPYEE U 2 Lymphocytic choriomeningitis virus (strain Armstrong)
Q15797 SMAD1
SMAD1_HUMAN
224 227 FQMPADTPPPAYLPPEDPMT TP 1 Homo sapiens (Human)
Q15303 ERBB4
ERBB4_HUMAN
1053 1056 RSEIGHSPPPAYTPMSGNQF TP 4 Homo sapiens (Human)
3 
P51170 SCNN1G
SCNNG_HUMAN
624 627 GTQVPGTPPPKYNTLRLERA TP 5 Homo sapiens (Human)
1 
P37091 Scnn1g
SCNNG_RAT
625 628 GSTVPGTPPPRYNTLRLDRA TP 4 Rattus norvegicus (Norway rat)
P51168 SCNN1B
SCNNB_HUMAN
617 620 ALPIPGTPPPNYDSLRLQPL TP 5 Homo sapiens (Human)
P37088 SCNN1A
SCNNA_HUMAN
641 644 PSPALTAPPPAYATLGPRPS TP 6 Homo sapiens (Human)
O15350 TP73
P73_HUMAN
484 487 VSGSHCTPPPPYHADPSLVS TP 8 Homo sapiens (Human)
2 
1 
O88898 Tp63
P63_MOUSE
540 543 PSTSHCTPPPPYPTDCSIVS TP 1 Mus musculus (House mouse)
1 
P03345 gag
GAG_HTL1A
118 121 PPDSDPQIPPPYVEPTAPQV TP 2 Human T-cell lymphotrophic virus type 1 (strain ATK)
P03519 M
MATRX_VSIVA
24 27 KSKKLGIAPPPYEEDTSMEY U 1 Vesicular stomatitis Indiana virus strain San Juan
P28282 UL56
UL56_HHV2H
49 52 DIDTPTDSPPPYSAGTSPVG TP 5 Human herpesvirus 2 strain HG52
1 
Q4VCS5 AMOT
AMOT_HUMAN
239 242 KGMEHRGPPPEYPFKGMPPQ TP 3 Homo sapiens (Human)
3 
P05627 Jun
JUN_MOUSE
167 170 YSASLHSEPPVYANLSNFNP TP 6 Mus musculus (House mouse)
1 
1 
P09450 Junb
JUNB_MOUSE
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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