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191  structures 1083  species 6  interactions 25000  sequences 916  architectures

Clan: WW (CL0680)

Summary

WW domain Add an annotation

The WW domain is composed of 38 to 40 semi-conserved amino acids. They are found in many human proteins and play integral roles in systems connected to the appearance of Alzheimer’s, Huntington’s, muscular dystrophy, and cancer. In particular, loss-of-function mutations that disrupt WW domain–ligand interactions can lead to major complications. WW domains fold into a three-stranded beta sheet that binds polyproline motifs. They have been divided into four main classes, corresponding to the polyproline motif with which they interact: class 1 with PPxY motifs, class 2 with PPPL/R motifs, class 3 with (PxxGMxPP)*2 motifs, and class 4 with (pS/pT)P motifs (p=phosphorylation) [1].

This clan contains 2 families and the total number of domains in the clan is 25000. The clan was built by S El-Gebali.

Literature references

  1. Dodson EJ, Fishbain-Yoskovitz V, Rotem-Bamberger S, Schueler-Furman O;, Exp Biol Med (Maywood). 2015;240:351-360.: Versatile communication strategies among tandem WW domain repeats. PUBMED:25710931 EPMC:25710931

Members

This clan contains the following 2 member families:

WW WW_1

Domain organisation

Below is a listing of the unique domain organisations or architectures from this clan. More...

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Alignments

The table below shows the number of occurrences of each domain throughout the sequence database. More...

Pfam family Num. domains Alignment
WW (PF00397) 24972 (99.9%) View
WW_1 (PF18507) 28 (0.1%) View
Total: 2 Total: 25000 Clan alignment
 

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Family relationships

This diagram shows the relationships between members of this clan. More...

Species distribution

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This tree shows the occurrence of the domains in this clan across different species. More...

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Interactions

There are 6 interactions for this clan. More...

Interacting families
A B
DAG1 WW
WW EF-hand_2
HECT
Herpes_LMP2
Rotamase
WW

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD group, to allow us to map Pfam domains onto UniProt three-dimensional structures. The table below shows the mapping between the Pfam families in this clan, the corresponding UniProt entries, and the region of the three-dimensional structures that are available for that sequence.

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