PROSITE documentation PDOC50088

Ankyrin repeat and ankyrin repeat region profiles

Description

Ankyrin repeats (ANK) are tandemly repeated modules of about 33 amino acids. They occur in a large number of functionally diverse proteins mainly from eukaryotes. The few known examples from prokaryotes and viruses may be the result of horizontal gene transfers [1].

Many ankyrin repeat regions are known to function as protein-protein interaction domains.

The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures, e.g. from:

  • p53-binding protein 53BP2 [2],
  • Cyclin-dependent kinase inhibitor p19Ink4d [3],
  • Transcriptional regulator GABP-β [4],
  • NF-kappaB inhibitory protein IkB-α [5].

It has been described as an L-shaped structure consisting of a β-hairpin and two α-helices [2].

Two profiles were developed for this module, the first one picks up ANK repeats while the second profile is 'circular' and will thus detect a region containing adjacent ANK repeats.

Last update:

December 2001 / First entry.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

ANK_REPEAT, PS50088Ankyrin repeat profile  (MATRIX)
Sequences known to belong to this class detected by the repeat profile: ALL
Other sequence(s) detected in Swiss-Prot: NONE.
Domain architecture view of Swiss-Prot proteins matching PS50088
PS50088
• Retrieve an alignment of Swiss-Prot true positive hits:
  Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format
Retrieve the sequence logo from the alignment
Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS50088
Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS50088
Scan Swiss-Prot/TrEMBL entries against PS50088
view ligand binding statistics
Matching PDB structures: 1AP7 1AWC 1BD8 1BI7 ... [ALL]
ANK_REP_REGION, PS50297Ankyrin repeat region circular profile  (MATRIX)
Sequences known to belong to this class detected by the circular profile: ALL
Other sequence(s) detected in Swiss-Prot: NONE.
Domain architecture view of Swiss-Prot proteins matching PS50297
PS50297
Scan Swiss-Prot/TrEMBL entries against PS50297
view ligand binding statistics
Matching PDB structures: 1A5E 1AP7 1AWC 1BD8 ... [ALL]

References

1 Authors Bork P.
Title Hundreds of ankyrin-like repeats in functionally diverse proteins: mobile modules that cross phyla horizontally?
Source Proteins 17:363-374(1993).
PubMed ID 8108379
2 Authors Gorina S., Pavletich N.P.
Title Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2.
Source Science 274:1001-1005(1996).
PubMed ID 8875926
3 Authors Luh F.Y., Archer S.J., Domaille P.J., Smith B.O., Owen D., Brotherton D.H., Raine A.R., Xu X., Brizuela L., Brenner S.L., Laue E.D.
Title Structure of the cyclin-dependent kinase inhibitor p19Ink4d.
Source Nature 389:999-1003(1997).
PubMed ID 9353127
DOI 10.1038/40202
4 Authors Batchelor A.H., Piper D.E., de la Brousse F.C., McKnight S.L., Wolberger C.
Title The structure of GABPalpha/beta: an ETS domain- ankyrin repeat heterodimer bound to DNA.
Source Science 279:1037-1041(1998).
PubMed ID 9461436
5 Authors Jacobs M.D., Harrison S.C.
Title Structure of an IkappaBalpha/NF-kappaB complex.
Source Cell 95:749-758(1998).
PubMed ID 9865693

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