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281  structures 1664  species 16  interactions 12100  sequences 2689  architectures

Family: Ank (PF00023)

Summary: Ankyrin repeat

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This is the Wikipedia entry entitled "Ankyrin repeat". More...

Ankyrin repeat Edit Wikipedia article

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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Ankyrin repeat Provide feedback

Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity [2].

Literature references

  1. Lux SE, John KM, Bennett V; , Nature 1990;345:736-739.: Hereditary spherocytosis associated with deletion of human erythrocyte ankyrin gene on chromosome 8. PUBMED:2141669 EPMC:2141669

  2. Michaely P, Tomchick DR, Machius M, Anderson RG;, EMBO J. 2002;21:6387-6396.: Crystal structure of a 12 ANK repeat stack from human ankyrinR. PUBMED:12456646 EPMC:12456646

  3. Michaely P, Bennett V;, Trends Cell Biol. 1992;2:127-129.: The ANK repeat: a ubiquitous motif involved in macromolecular recognition. PUBMED:14731966 EPMC:14731966


Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR002110

The ankyrin repeat is one of the most common protein-protein interaction motifs in nature. Ankyrin repeats 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 [PUBMED:8108379]. The repeat has been found in proteins of diverse function such as transcriptional initiators, cell-cycle regulators, cytoskeletal, ion transporters and signal transducers. The ankyrin fold appears to be defined by its structure rather than its function since there is no specific sequence or structure which is universally recognised by it.

The conserved fold of the ankyrin repeat unit is known from several crystal and solution structures [PUBMED:8875926, PUBMED:9353127, PUBMED:9461436, PUBMED:9865693]. Each repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90o angle. The repeats stack together to form an L-shaped structure [PUBMED:8875926, PUBMED:12461176].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan Ank (CL0465), which has the following description:

The ankyrin repeat is a short sequence region that is about 30-34 amino-acids in length. Multiple copies of the repeat composed of two beta strands and two alpha helices combine to form long arrays. In general these repeats are involved in protein-protein interactions. This superfamily also includes some families that are arrays of several repeats.

The clan contains the following 8 members:

Ank Ank_2 Ank_3 Ank_4 Ank_5 AnkUBD DUF3420 DUF3447

Alignments

We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the UniProtKB sequence database, the NCBI sequence database, and our metagenomics sequence database. More...

View options

We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(1063)
Full
(12100)
Representative proteomes UniProt
(20276)
NCBI
(800309)
Meta
(5803)
RP15
(3948)
RP35
(6919)
RP55
(9764)
RP75
(12023)
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PP/heatmap 1                

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(1063)
Full
(12100)
Representative proteomes UniProt
(20276)
NCBI
(800309)
Meta
(5803)
RP15
(3948)
RP35
(6919)
RP55
(9764)
RP75
(12023)
Alignment:
Format:
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Sequence:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(1063)
Full
(12100)
Representative proteomes UniProt
(20276)
NCBI
(800309)
Meta
(5803)
RP15
(3948)
RP35
(6919)
RP55
(9764)
RP75
(12023)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download     Download  
Gzipped Download   Download   Download   Download   Download   Download   Download     Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Swissprot_feature_table
Previous IDs: ank;
Type: Repeat
Sequence Ontology: SO:0001068
Author: Bateman A , Sonnhammer ELL
Number in seed: 1063
Number in full: 12100
Average length of the domain: 33.70 aa
Average identity of full alignment: 30 %
Average coverage of the sequence by the domain: 4.67 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.1 14.7
Trusted cut-off 21.1 14.7
Noise cut-off 21.0 14.6
Model length: 32
Family (HMM) version: 30
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence

Selections

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Interactions

There are 16 interactions for this family. More...

P53 Ank Ank_2 Ank_2 SH3_1 Activator_LAG-3 Cupin_8 Ank_5 LAG1-DNAbind ArfGap Ank_4 Ank_4 LIM SOCS_box Pkinase Adeno_knob

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 PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Ank domain has been found. There are 281 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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