Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ankyrin-2

Gene

ANK2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

In skeletal muscle, required for proper localization of DMD and DCTN4 and for the formation and/or stability of a special subset of microtubules associated with costameres and neuromuscular junctions (By similarity). Attaches integral membrane proteins to cytoskeletal elements. Also binds to cytoskeletal proteins. Required for coordinate assembly of Na/Ca exchanger, Na/K ATPase and InsP3 receptor at sarcoplasmic reticulum sites in cardiomyocytes. Required for the coordinated expression of the Na/K ATPase, Na/Ca exchanger and beta-2-spectrin (SPTBN1) in the inner segment of rod photoreceptors. Required for expression and targeting of SPTBN1 in neonatal cardiomyocytes and for the regulation of neonatal cardiomyocyte contraction rate.By similarity1 Publication

GO - Molecular functioni

  • ATPase binding Source: BHF-UCL
  • cytoskeletal adaptor activity Source: GO_Central
  • enzyme binding Source: UniProtKB
  • ion channel binding Source: BHF-UCL
  • protein binding, bridging Source: BHF-UCL
  • protein kinase binding Source: BHF-UCL
  • spectrin binding Source: BHF-UCL
  • structural constituent of cytoskeleton Source: Ensembl

GO - Biological processi

  • atrial cardiac muscle cell action potential Source: BHF-UCL
  • atrial cardiac muscle cell to AV node cell communication Source: BHF-UCL
  • atrial septum development Source: BHF-UCL
  • cellular calcium ion homeostasis Source: BHF-UCL
  • cellular protein localization Source: BHF-UCL
  • ER to Golgi vesicle-mediated transport Source: Reactome
  • membrane depolarization during SA node cell action potential Source: BHF-UCL
  • paranodal junction assembly Source: Ensembl
  • positive regulation of calcium ion transmembrane transporter activity Source: BHF-UCL
  • positive regulation of calcium ion transport Source: BHF-UCL
  • positive regulation of cation channel activity Source: BHF-UCL
  • positive regulation of gene expression Source: BHF-UCL
  • positive regulation of potassium ion transmembrane transporter activity Source: BHF-UCL
  • positive regulation of potassium ion transport Source: BHF-UCL
  • protein localization to cell surface Source: BHF-UCL
  • protein localization to endoplasmic reticulum Source: BHF-UCL
  • protein localization to M-band Source: BHF-UCL
  • protein localization to organelle Source: BHF-UCL
  • protein localization to plasma membrane Source: BHF-UCL
  • protein localization to T-tubule Source: BHF-UCL
  • protein stabilization Source: BHF-UCL
  • protein targeting to plasma membrane Source: GO_Central
  • regulation of atrial cardiac muscle cell action potential Source: BHF-UCL
  • regulation of calcium ion transmembrane transporter activity Source: BHF-UCL
  • regulation of calcium ion transport Source: BHF-UCL
  • regulation of cardiac muscle cell contraction Source: BHF-UCL
  • regulation of cardiac muscle contraction Source: BHF-UCL
  • regulation of cardiac muscle contraction by calcium ion signaling Source: BHF-UCL
  • regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: BHF-UCL
  • regulation of heart rate Source: BHF-UCL
  • regulation of heart rate by cardiac conduction Source: BHF-UCL
  • regulation of protein stability Source: BHF-UCL
  • regulation of release of sequestered calcium ion into cytosol Source: BHF-UCL
  • regulation of SA node cell action potential Source: BHF-UCL
  • regulation of ventricular cardiac muscle cell membrane repolarization Source: BHF-UCL
  • response to methylmercury Source: Ensembl
  • SA node cell action potential Source: BHF-UCL
  • SA node cell to atrial cardiac muscle cell communication Source: BHF-UCL
  • sarcoplasmic reticulum calcium ion transport Source: BHF-UCL
  • T-tubule organization Source: BHF-UCL
  • ventricular cardiac muscle cell action potential Source: BHF-UCL
Complete GO annotation...

Enzyme and pathway databases

BioCyciZFISH:ENSG00000145362-MONOMER.
ReactomeiR-HSA-445095. Interaction between L1 and Ankyrins.
R-HSA-6807878. COPI-mediated anterograde transport.

Protein family/group databases

TCDBi8.A.28.1.1. the ankyrin (ankyrin) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Ankyrin-2
Short name:
ANK-2
Alternative name(s):
Ankyrin-B
Brain ankyrin
Non-erythroid ankyrin
Gene namesi
Name:ANK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:493. ANK2.

Subcellular locationi

  • Cytoplasmcytoskeleton 1 Publication
  • Membrane 1 Publication
  • CytoplasmmyofibrilsarcomereM line By similarity
  • Apical cell membrane By similarity
  • Cell membrane 1 Publication
  • Cell junctionsynapsepostsynaptic cell membrane By similarity

  • Note: Expressed at the apical membrane of airway lung epithelial cells (By similarity). Localized to the plasma membrane of the inner segments of photoreceptors in retina. Colocalizes with SPTBN1 in a distict intracellular compartment of neonatal cardiomyocytes (By similarity). In skeletal muscle, localizes to neuromuscular junctions (By similarity).By similarity

GO - Cellular componenti

  • A band Source: BHF-UCL
  • apical plasma membrane Source: UniProtKB-SubCell
  • basolateral plasma membrane Source: UniProtKB
  • costamere Source: BHF-UCL
  • cytoskeleton Source: UniProtKB-SubCell
  • cytosol Source: Reactome
  • intercalated disc Source: BHF-UCL
  • intracellular Source: BHF-UCL
  • M band Source: BHF-UCL
  • membrane raft Source: Ensembl
  • neuron projection Source: Ensembl
  • plasma membrane Source: BHF-UCL
  • postsynaptic membrane Source: UniProtKB-SubCell
  • sarcolemma Source: BHF-UCL
  • T-tubule Source: BHF-UCL
  • Z disc Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Involvement in diseasei

Long QT syndrome 4 (LQT4)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy. Long QT syndrome type 4 shows many atypical features compared to classical long QT syndromes, including pronounced sinus bradycardia, polyphasic T waves and atrial fibrillation. Cardiac repolarization defects may be not as severe as in classical LQT syndromes and prolonged QT interval on EKG is not a consistent feature.
See also OMIM:600919
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0229341458E → G in LQT4; loss of function. 2 PublicationsCorresponds to variant rs72544141dbSNPEnsembl.1
Natural variantiVAR_0229353740L → I in LQT4; loss of function. 1 PublicationCorresponds to variant rs35530544dbSNPEnsembl.1
Natural variantiVAR_0229363744T → N in LQT4; loss of function. 1 PublicationCorresponds to variant rs121912705dbSNPEnsembl.1
Natural variantiVAR_0229373906R → W in LQT4; loss of function. 1 PublicationCorresponds to variant rs121912706dbSNPEnsembl.1
Natural variantiVAR_0229383931E → K in LQT4; loss of function. 1 PublicationCorresponds to variant rs45454496dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi975 – 977DAR → AAA: Prevents binding to SPTBN1. 1 Publication3
Mutagenesisi1000A → P: Prevents binding to SPTBN1. 1 Publication1
Mutagenesisi1100 – 1103ENGD → AAGA: Weak binding to SPTBN1. 1 Publication4

Keywords - Diseasei

Disease mutation, Long QT syndrome

Organism-specific databases

DisGeNETi287.
MalaCardsiANK2.
MIMi600919. phenotype.
OpenTargetsiENSG00000145362.
Orphaneti101016. Romano-Ward syndrome.
PharmGKBiPA24799.

Polymorphism and mutation databases

BioMutaiANK2.
DMDMi387912917.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000668851 – 3957Ankyrin-2Add BLAST3957

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei31PhosphoserineBy similarity1
Modified residuei34PhosphoserineBy similarity1
Modified residuei378PhosphotyrosineBy similarity1
Modified residuei531PhosphotyrosineBy similarity1
Modified residuei846PhosphoserineCombined sources1
Modified residuei853PhosphothreonineBy similarity1
Modified residuei874PhosphoserineBy similarity1
Modified residuei1382PhosphotyrosineBy similarity1
Modified residuei1459PhosphoserineBy similarity1
Modified residuei1461PhosphoserineBy similarity1
Modified residuei1473PhosphoserineBy similarity1
Modified residuei1500PhosphoserineBy similarity1
Modified residuei1596PhosphoserineBy similarity1
Modified residuei1732PhosphoserineBy similarity1
Modified residuei1733PhosphoserineBy similarity1
Modified residuei1736PhosphoserineBy similarity1
Modified residuei1855PhosphoserineBy similarity1
Modified residuei1858PhosphoserineBy similarity1
Modified residuei1929PhosphoserineBy similarity1
Modified residuei2127PhosphoserineBy similarity1
Modified residuei2239PhosphothreonineBy similarity1
Modified residuei2243PhosphoserineBy similarity1
Modified residuei2269PhosphothreonineBy similarity1
Modified residuei2275PhosphoserineBy similarity1
Modified residuei2405PhosphoserineBy similarity1
Modified residuei2440PhosphoserineBy similarity1
Modified residuei2454PhosphoserineBy similarity1
Modified residuei2516PhosphoserineBy similarity1
Modified residuei2521PhosphoserineBy similarity1
Modified residuei2583PhosphothreonineBy similarity1
Modified residuei2679PhosphoserineBy similarity1
Modified residuei2701PhosphoserineBy similarity1
Modified residuei2781PhosphoserineBy similarity1
Modified residuei2795PhosphoserineBy similarity1
Modified residuei2956PhosphoserineBy similarity1
Modified residuei3075PhosphoserineBy similarity1
Modified residuei3078PhosphothreonineBy similarity1
Modified residuei3273PhosphoserineBy similarity1
Modified residuei3276PhosphoserineBy similarity1
Modified residuei3277PhosphoserineBy similarity1
Modified residuei3390PhosphoserineBy similarity1
Modified residuei3409PhosphoserineBy similarity1
Modified residuei3474PhosphoserineBy similarity1
Modified residuei3735PhosphoserineBy similarity1
Modified residuei3776PhosphothreonineBy similarity1
Modified residuei3797PhosphothreonineBy similarity1
Modified residuei3803PhosphothreonineBy similarity1
Modified residuei3814PhosphothreonineBy similarity1
Modified residuei3823PhosphoserineBy similarity1
Modified residuei3909PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylated at multiple sites by different protein kinases and each phosphorylation event regulates the protein's structure and function.Curated

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ01484.
MaxQBiQ01484.
PaxDbiQ01484.
PeptideAtlasiQ01484.
PRIDEiQ01484.

PTM databases

iPTMnetiQ01484.
PhosphoSitePlusiQ01484.
SwissPalmiQ01484.

Expressioni

Tissue specificityi

Present in plasma membrane of neurons as well as glial cells throughout the brain. Expressed in fetal brain and in temporal cortex of adult brain. Also expressed in the inner segments of rod photoreceptors in retina.3 Publications

Gene expression databases

BgeeiENSG00000145362.
CleanExiHS_ANK2.
ExpressionAtlasiQ01484. baseline and differential.
GenevisibleiQ01484. HS.

Organism-specific databases

HPAiCAB015178.
HPA007570.
HPA008007.
HPA035970.

Interactioni

Subunit structurei

Interacts with RHBG and SPTBN1 (PubMed:15262991, PubMed:15611082). Colocalizes with Na/K ATPase, Na/Ca exchanger and SPTBN1 (PubMed:19007774). Directly interacts with DMD; this interaction is necessary for DMD localization at the sarcolemma. Interacts with DCTN4; this interaction is required for DCTN4 retention at costameres. Identified in complexes that contain VIM, EZR, AHNAK, BFSP1, BFSP2, ANK2, PLEC, PRX and spectrin (By similarity).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CEP120Q8N9602EBI-941975,EBI-2563015
DMDP11532-52EBI-941975,EBI-1018651
EHD3Q9NZN32EBI-941975,EBI-2870749
GRB2P629932EBI-941975,EBI-401755

GO - Molecular functioni

  • ATPase binding Source: BHF-UCL
  • cytoskeletal adaptor activity Source: GO_Central
  • enzyme binding Source: UniProtKB
  • ion channel binding Source: BHF-UCL
  • protein binding, bridging Source: BHF-UCL
  • protein kinase binding Source: BHF-UCL
  • spectrin binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi106784. 21 interactors.
DIPiDIP-37425N.
IntActiQ01484. 21 interactors.
STRINGi9606.ENSP00000349588.

Structurei

Secondary structure

13957
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi30 – 41Combined sources12
Helixi44 – 52Combined sources9
Helixi67 – 74Combined sources8
Helixi77 – 86Combined sources10
Helixi100 – 106Combined sources7
Helixi110 – 118Combined sources9
Helixi133 – 139Combined sources7
Helixi143 – 150Combined sources8
Turni151 – 153Combined sources3
Helixi166 – 172Combined sources7
Helixi176 – 183Combined sources8
Turni184 – 186Combined sources3
Helixi195 – 202Combined sources8
Helixi205 – 211Combined sources7
Helixi212 – 214Combined sources3
Helixi225 – 227Combined sources3
Helixi236 – 243Combined sources8
Helixi246 – 254Combined sources9
Helixi264 – 266Combined sources3
Helixi269 – 275Combined sources7
Helixi279 – 287Combined sources9
Helixi302 – 307Combined sources6
Turni308 – 310Combined sources3
Helixi312 – 318Combined sources7
Helixi434 – 441Combined sources8
Helixi444 – 452Combined sources9
Helixi467 – 474Combined sources8
Helixi477 – 485Combined sources9
Helixi495 – 497Combined sources3
Helixi500 – 507Combined sources8
Helixi510 – 518Combined sources9
Helixi533 – 540Combined sources8
Helixi543 – 550Combined sources8
Turni551 – 553Combined sources3
Helixi566 – 573Combined sources8
Helixi576 – 583Combined sources8
Turni584 – 586Combined sources3
Helixi599 – 605Combined sources7
Helixi609 – 617Combined sources9
Helixi741 – 748Combined sources8
Turni749 – 751Combined sources3
Beta strandi759 – 761Combined sources3
Helixi764 – 767Combined sources4
Turni768 – 772Combined sources5
Helixi774 – 780Combined sources7
Turni781 – 784Combined sources4
Helixi797 – 800Combined sources4
Turni801 – 805Combined sources5
Turni807 – 815Combined sources9
Beta strandi969 – 974Combined sources6
Beta strandi979 – 982Combined sources4
Beta strandi984 – 986Combined sources3
Beta strandi990 – 993Combined sources4
Beta strandi1002 – 1009Combined sources8
Beta strandi1025 – 1028Combined sources4
Beta strandi1031 – 1035Combined sources5
Beta strandi1039 – 1042Combined sources4
Beta strandi1076 – 1082Combined sources7
Turni1088 – 1091Combined sources4
Beta strandi1092 – 1103Combined sources12
Helixi1131 – 1137Combined sources7
Beta strandi1139 – 1146Combined sources8
Beta strandi1149 – 1157Combined sources9
Beta strandi1159 – 1165Combined sources7
Beta strandi1168 – 1172Combined sources5
Beta strandi1174 – 1176Combined sources3
Beta strandi1180 – 1183Combined sources4
Beta strandi1192 – 1199Combined sources8
Helixi1203 – 1210Combined sources8
Beta strandi1213 – 1216Combined sources4
Beta strandi1219 – 1226Combined sources8
Beta strandi1228 – 1238Combined sources11
Beta strandi1258 – 1263Combined sources6
Helixi1277 – 1279Combined sources3
Beta strandi1283 – 1285Combined sources3
Beta strandi1288 – 1295Combined sources8
Beta strandi1298 – 1305Combined sources8
Helixi1307 – 1309Combined sources3
Helixi1310 – 1321Combined sources12
Beta strandi1325 – 1335Combined sources11
Beta strandi1338 – 1349Combined sources12
Helixi1357 – 1359Combined sources3
Beta strandi1365 – 1369Combined sources5
Beta strandi1373 – 1376Combined sources4
Beta strandi1380 – 1391Combined sources12
Beta strandi1399 – 1402Combined sources4
Beta strandi1410 – 1418Combined sources9
Beta strandi1424 – 1432Combined sources9
Beta strandi1445 – 1451Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4D8OX-ray2.20A966-1476[»]
4RLVX-ray3.49A28-873[»]
4RLYX-ray2.50A28-318[»]
DisProtiDP00467.
ProteinModelPortaliQ01484.
SMRiQ01484.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati30 – 62ANK 1Add BLAST33
Repeati63 – 92ANK 2Add BLAST30
Repeati96 – 125ANK 3Add BLAST30
Repeati129 – 158ANK 4Add BLAST30
Repeati162 – 191ANK 5Add BLAST30
Repeati193 – 220ANK 6Add BLAST28
Repeati232 – 261ANK 7Add BLAST30
Repeati265 – 294ANK 8Add BLAST30
Repeati298 – 327ANK 9Add BLAST30
Repeati331 – 360ANK 10Add BLAST30
Repeati364 – 393ANK 11Add BLAST30
Repeati397 – 426ANK 12Add BLAST30
Repeati430 – 459ANK 13Add BLAST30
Repeati463 – 492ANK 14Add BLAST30
Repeati496 – 525ANK 15Add BLAST30
Repeati529 – 558ANK 16Add BLAST30
Repeati562 – 591ANK 17Add BLAST30
Repeati595 – 624ANK 18Add BLAST30
Repeati628 – 657ANK 19Add BLAST30
Repeati661 – 690ANK 20Add BLAST30
Repeati694 – 723ANK 21Add BLAST30
Repeati727 – 756ANK 22Add BLAST30
Repeati760 – 789ANK 23Add BLAST30
Repeati793 – 822ANK 24Add BLAST30
Domaini966 – 1124ZU5 1PROSITE-ProRule annotationAdd BLAST159
Domaini1125 – 1288ZU5 2PROSITE-ProRule annotationAdd BLAST164
Domaini1450 – 1535Death 1PROSITE-ProRule annotationAdd BLAST86
Repeati1806 – 1817Repeat AAdd BLAST12
Repeati1818 – 1829Repeat AAdd BLAST12
Repeati1830 – 1841Repeat AAdd BLAST12
Repeati1842 – 1853Repeat AAdd BLAST12
Repeati1854 – 1865Repeat AAdd BLAST12
Repeati1866 – 1877Repeat AAdd BLAST12
Repeati1878 – 1889Repeat AAdd BLAST12
Repeati1890 – 1900Repeat A; approximateAdd BLAST11
Repeati1901 – 1912Repeat AAdd BLAST12
Repeati1913 – 1924Repeat AAdd BLAST12
Repeati1925 – 1935Repeat A; approximateAdd BLAST11
Repeati1936 – 1947Repeat AAdd BLAST12
Repeati1948 – 1959Repeat AAdd BLAST12
Repeati1960 – 1971Repeat AAdd BLAST12
Repeati1972 – 1983Repeat AAdd BLAST12
Domaini3569 – 3653Death 2PROSITE-ProRule annotationAdd BLAST85

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni966 – 1125Interaction with SPTBN11 PublicationAdd BLAST160
Regioni1289 – 1423UPA domainAdd BLAST135
Regioni1806 – 1983Repeat-rich regionAdd BLAST178

Domaini

The tandem configuration of the two ZU5 and the UPA domains forms a structural supramodule termed ZZU. ZU5-1 mediates interaction with beta-spectrin, and the ZU5-1/UPA interface is required for ankyrin's function other than binding to spectrin.1 Publication

Sequence similaritiesi

Contains 24 ANK repeats.PROSITE-ProRule annotation
Contains 2 death domains.PROSITE-ProRule annotation
Contains 2 ZU5 domains.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiKOG4177. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00840000129677.
HOGENOMiHOG000169277.
HOVERGENiHBG100442.
InParanoidiQ01484.
KOiK10380.
OrthoDBiEOG091G00GN.
PhylomeDBiQ01484.
TreeFamiTF351263.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
1.25.40.20. 3 hits.
InterProiIPR030301. Ankyrin-B.
IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR000906. ZU5_dom.
[Graphical view]
PANTHERiPTHR24123:SF17. PTHR24123:SF17. 4 hits.
PfamiPF00023. Ank. 2 hits.
PF12796. Ank_2. 6 hits.
PF00531. Death. 1 hit.
PF00791. ZU5. 3 hits.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 23 hits.
SM00005. DEATH. 1 hit.
SM00218. ZU5. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF48403. SSF48403. 3 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 20 hits.
PS50017. DEATH_DOMAIN. 1 hit.
PS51145. ZU5. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 3 (identifier: Q01484-4) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MMNEDAAQKS DSGEKFNGSS QRRKRPKKSD SNASFLRAAR AGNLDKVVEY
60 70 80 90 100
LKGGIDINTC NQNGLNALHL AAKEGHVGLV QELLGRGSSV DSATKKGNTA
110 120 130 140 150
LHIASLAGQA EVVKVLVKEG ANINAQSQNG FTPLYMAAQE NHIDVVKYLL
160 170 180 190 200
ENGANQSTAT EDGFTPLAVA LQQGHNQAVA ILLENDTKGK VRLPALHIAA
210 220 230 240 250
RKDDTKSAAL LLQNDHNADV QSKMMVNRTT ESGFTPLHIA AHYGNVNVAT
260 270 280 290 300
LLLNRGAAVD FTARNGITPL HVASKRGNTN MVKLLLDRGG QIDAKTRDGL
310 320 330 340 350
TPLHCAARSG HDQVVELLLE RGAPLLARTK NGLSPLHMAA QGDHVECVKH
360 370 380 390 400
LLQHKAPVDD VTLDYLTALH VAAHCGHYRV TKLLLDKRAN PNARALNGFT
410 420 430 440 450
PLHIACKKNR IKVMELLVKY GASIQAITES GLTPIHVAAF MGHLNIVLLL
460 470 480 490 500
LQNGASPDVT NIRGETALHM AARAGQVEVV RCLLRNGALV DARAREEQTP
510 520 530 540 550
LHIASRLGKT EIVQLLLQHM AHPDAATTNG YTPLHISARE GQVDVASVLL
560 570 580 590 600
EAGAAHSLAT KKGFTPLHVA AKYGSLDVAK LLLQRRAAAD SAGKNGLTPL
610 620 630 640 650
HVAAHYDNQK VALLLLEKGA SPHATAKNGY TPLHIAAKKN QMQIASTLLN
660 670 680 690 700
YGAETNIVTK QGVTPLHLAS QEGHTDMVTL LLDKGANIHM STKSGLTSLH
710 720 730 740 750
LAAQEDKVNV ADILTKHGAD QDAHTKLGYT PLIVACHYGN VKMVNFLLKQ
760 770 780 790 800
GANVNAKTKN GYTPLHQAAQ QGHTHIINVL LQHGAKPNAT TANGNTALAI
810 820 830 840 850
AKRLGYISVV DTLKVVTEEV TTTTTTITEK HKLNVPETMT EVLDVSDEEG
860 870 880 890 900
DDTMTGDGGE YLRPEDLKEL GDDSLPSSQF LDGMNYLRYS LEGGRSDSLR
910 920 930 940 950
SFSSDRSHTL SHASYLRDSA VMDDSVVIPS HQVSTLAKEA ERNSYRLSWG
960 970 980 990 1000
TENLDNVALS SSPIHSGFLV SFMVDARGGA MRGCRHNGLR IIIPPRKCTA
1010 1020 1030 1040 1050
PTRVTCRLVK RHRLATMPPM VEGEGLASRL IEVGPSGAQF LGKLHLPTAP
1060 1070 1080 1090 1100
PPLNEGESLV SRILQLGPPG TKFLGPVIVE IPHFAALRGK ERELVVLRSE
1110 1120 1130 1140 1150
NGDSWKEHFC DYTEDELNEI LNGMDEVLDS PEDLEKKRIC RIITRDFPQY
1160 1170 1180 1190 1200
FAVVSRIKQD SNLIGPEGGV LSSTVVPQVQ AVFPEGALTK RIRVGLQAQP
1210 1220 1230 1240 1250
MHSELVKKIL GNKATFSPIV TLEPRRRKFH KPITMTIPVP KASSDVMLNG
1260 1270 1280 1290 1300
FGGDAPTLRL LCSITGGTTP AQWEDITGTT PLTFVNECVS FTTNVSARFW
1310 1320 1330 1340 1350
LIDCRQIQES VTFASQVYRE IICVPYMAKF VVFAKSHDPI EARLRCFCMT
1360 1370 1380 1390 1400
DDKVDKTLEQ QENFAEVARS RDVEVLEGKP IYVDCFGNLV PLTKSGQHHI
1410 1420 1430 1440 1450
FSFFAFKENR LPLFVKVRDT TQEPCGRLSF MKEPKSTRGL VHQAICNLNI
1460 1470 1480 1490 1500
TLPIYTKESE SDQEQEEEID MTSEKNDETE STETSVLKSH LVNEVPVLAS
1510 1520 1530 1540 1550
PDLLSEVSEM KQDLIKMTAI LTTDVSDKAG SIKVKELVKA AEEEPGEPFE
1560 1570 1580 1590 1600
IVERVKEDLE KVNEILRSGT CTRDESSVQS SRSERGLVEE EWVIVSDEEI
1610 1620 1630 1640 1650
EEARQKAPLE ITEYPCVEVR IDKEIKGKVE KDSTGLVNYL TDDLNTCVPL
1660 1670 1680 1690 1700
PKEQLQTVQD KAGKKCEALA VGRSSEKEGK DIPPDETQST QKQHKPSLGI
1710 1720 1730 1740 1750
KKPVRRKLKE KQKQKEEGLQ ASAEKAELKK GSSEESLGED PGLAPEPLPT
1760 1770 1780 1790 1800
VKATSPLIEE TPIGSIKDKV KALQKRVEDE QKGRSKLPIR VKGKEDVPKK
1810 1820 1830 1840 1850
TTHRPHPAAS PSLKSERHAP GSPSPKTERH STLSSSAKTE RHPPVSPSSK
1860 1870 1880 1890 1900
TEKHSPVSPS AKTERHSPAS SSSKTEKHSP VSPSTKTERH SPVSSTKTER
1910 1920 1930 1940 1950
HPPVSPSGKT DKRPPVSPSG RTEKHPPVSP GRTEKRLPVS PSGRTDKHQP
1960 1970 1980 1990 2000
VSTAGKTEKH LPVSPSGKTE KQPPVSPTSK TERIEETMSV RELMKAFQSG
2010 2020 2030 2040 2050
QDPSKHKTGL FEHKSAKQKQ PQEKGKVRVE KEKGPILTQR EAQKTENQTI
2060 2070 2080 2090 2100
KRGQRLPVTG TAESKRGVRV SSIGVKKEDA AGGKEKVLSH KIPEPVQSVP
2110 2120 2130 2140 2150
EEESHRESEV PKEKMADEQG DMDLQISPDR KTSTDFSEVI KQELEDNDKY
2160 2170 2180 2190 2200
QQFRLSEETE KAQLHLDQVL TSPFNTTFPL DYMKDEFLPA LSLQSGALDG
2210 2220 2230 2240 2250
SSESLKNEGV AGSPCGSLME GTPQISSEES YKHEGLAETP ETSPESLSFS
2260 2270 2280 2290 2300
PKKSEEQTGE TKESTKTETT TEIRSEKEHP TTKDITGGSE ERGATVTEDS
2310 2320 2330 2340 2350
ETSTESFQKE ATLGSPKDTS PKRQDDCTGS CSVALAKETP TGLTEEAACD
2360 2370 2380 2390 2400
EGQRTFGSSA HKTQTDSEVQ ESTATSDETK ALPLPEASVK TDTGTESKPQ
2410 2420 2430 2440 2450
GVIRSPQGLE LALPSRDSEV LSAVADDSLA VSHKDSLEAS PVLEDNSSHK
2460 2470 2480 2490 2500
TPDSLEPSPL KESPCRDSLE SSPVEPKMKA GIFPSHFPLP AAVAKTELLT
2510 2520 2530 2540 2550
EVASVRSRLL RDPDGSAEDD SLEQTSLMES SGKSPLSPDT PSSEEVSYEV
2560 2570 2580 2590 2600
TPKTTDVSTP KPAVIHECAE EDDSENGEKK RFTPEEEMFK MVTKIKMFDE
2610 2620 2630 2640 2650
LEQEAKQKRD YKKEPKQEES SSSSDPDADC SVDVDEPKHT GSGEDESGVP
2660 2670 2680 2690 2700
VLVTSESRKV SSSSESEPEL AQLKKGADSG LLPEPVIRVQ PPSPLPSSMD
2710 2720 2730 2740 2750
SNSSPEEVQF QPVVSKQYTF KMNEDTQEEP GKSEEEKDSE SHLAEDRHAV
2760 2770 2780 2790 2800
STEAEDRSYD KLNRDTDQPK ICDGHGCEAM SPSSSAAPVS SGLQSPTGDD
2810 2820 2830 2840 2850
VDEQPVIYKE SLALQGTHEK DTEGEELDVS RAESPQADCP SESFSSSSSL
2860 2870 2880 2890 2900
PHCLVSEGKE LDEDISATSS IQKTEVTKTD ETFENLPKDC PSQDSSITTQ
2910 2920 2930 2940 2950
TDRFSMDVPV SDLAENDEIY DPQITSPYEN VPSQSFFSSE ESKTQTDANH
2960 2970 2980 2990 3000
TTSFHSSEVY SVTITSPVED VVVASSSSGT VLSKESNFEG QDIKMESQQE
3010 3020 3030 3040 3050
STLWEMQSDS VSSSFEPTMS ATTTVVGEQI SKVIITKTDV DSDSWSEIRE
3060 3070 3080 3090 3100
DDEAFEARVK EEEQKIFGLM VDRQSQGTTP DTTPARTPTE EGTPTSEQNP
3110 3120 3130 3140 3150
FLFQEGKLFE MTRSGAIDMT KRSYADESFH FFQIGQESRE ETLSEDVKEG
3160 3170 3180 3190 3200
ATGADPLPLE TSAESLALSE SKETVDDEAD LLPDDVSEEV EEIPASDAQL
3210 3220 3230 3240 3250
NSQMGISAST ETPTKEAVSV GTKDLPTVQT GDIPPLSGVK QISCPDSSEP
3260 3270 3280 3290 3300
AVQVQLDFST LTRSVYSDRG DDSPDSSPEE QKSVIEIPTA PMENVPFTES
3310 3320 3330 3340 3350
KSKIPVRTMP TSTPAPPSAE YESSVSEDFL SSVDEENKAD EAKPKSKLPV
3360 3370 3380 3390 3400
KVPLQRVEQQ LSDLDTSVQK TVAPQGQDMA SIAPDNRSKS ESDASSLDSK
3410 3420 3430 3440 3450
TKCPVKTRSY TETETESRER AEELELESEE GATRPKILTS RLPVKSRSTT
3460 3470 3480 3490 3500
SSCRGGTSPT KESKEHFFDL YRNSIEFFEE ISDEASKLVD RLTQSEREQE
3510 3520 3530 3540 3550
IVSDDESSSA LEVSVIENLP PVETEHSVPE DIFDTRPIWD ESIETLIERI
3560 3570 3580 3590 3600
PDENGHDHAE DPQDEQERIE ERLAYIADHL GFSWTELARE LDFTEEQIHQ
3610 3620 3630 3640 3650
IRIENPNSLQ DQSHALLKYW LERDGKHATD TNLVECLTKI NRMDIVHLME
3660 3670 3680 3690 3700
TNTEPLQERI SHSYAEIEQT ITLDHSEGFS VLQEELCTAQ HKQKEEQAVS
3710 3720 3730 3740 3750
KESETCDHPP IVSEEDISVG YSTFQDGVPK TEGDSSATAL FPQTHKEQVQ
3760 3770 3780 3790 3800
QDFSGKMQDL PEESSLEYQQ EYFVTTPGTE TSETQKAMIV PSSPSKTPEE
3810 3820 3830 3840 3850
VSTPAEEEKL YLQTPTSSER GGSPIIQEPE EPSEHREESS PRKTSLVIVE
3860 3870 3880 3890 3900
SADNQPETCE RLDEDAAFEK GDDMPEIPPE TVTEEEYIDE HGHTVVKKVT
3910 3920 3930 3940 3950
RKIIRRYVSS EGTEKEEIMV QGMPQEPVNI EEGDGYSKVI KRVVLKSDTE

QSEDNNE
Length:3,957
Mass (Da):433,715
Last modified:May 16, 2012 - v4
Checksum:i41C1A240CC5A3B72
GO
Isoform 2 (identifier: Q01484-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1477-3561: Missing.

Show »
Length:1,872
Mass (Da):205,795
Checksum:i425D5422CF5CE930
GO
Isoform 4 (identifier: Q01484-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-27: MMNEDAAQKSDSGEKFNGSSQRRKRPK → MTTMLQ
     967-967: G → GRASPCLERDNSS
     1477-3561: Missing.

Note: No experimental confirmation available.
Show »
Length:1,863
Mass (Da):204,752
Checksum:i4E2B2DB97E1DDC0A
GO
Isoform 5 (identifier: Q01484-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1348: Missing.
     1477-3561: Missing.
     3870-3870: K → KELTEELGELEASSDEEAMVTTRVVRRRVIIQ

Show »
Length:555
Mass (Da):63,361
Checksum:iC0C03881D8E0EFD9
GO

Sequence cautioni

The sequence AAI25237 differs from that shown. Reason: Frameshift at position 1405.Curated
The sequence CAB42644 differs from that shown. CDS lacks C-terminal region which is nevertheless present in the underlying cDNA.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti220V → I in CAD97827 (PubMed:17974005).Curated1
Sequence conflicti475 – 476GQ → PE in AAA62828 (PubMed:1833308).Curated2
Sequence conflicti2787A → R in CAB42644 (PubMed:8253844).Curated1
Sequence conflicti2999Q → L in CAB42644 (PubMed:8253844).Curated1
Sequence conflicti3140 – 3141EE → RY in AC093879 (PubMed:15815621).Curated2
Sequence conflicti3185D → S in CAB42644 (PubMed:8253844).Curated1
Sequence conflicti3699V → A in CAD97827 (PubMed:17974005).Curated1
Sequence conflicti3737A → S in CAA40279 (PubMed:1830053).Curated1
Sequence conflicti3737A → S in CAB42644 (PubMed:8253844).Curated1
Sequence conflicti3955 – 3956NN → SM in AC093879 (PubMed:15815621).Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_035606685G → E in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_055504687N → S.Corresponds to variant rs29372dbSNPEnsembl.1
Natural variantiVAR_0356071267G → R in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_0229341458E → G in LQT4; loss of function. 2 PublicationsCorresponds to variant rs72544141dbSNPEnsembl.1
Natural variantiVAR_0555052369V → A.Corresponds to variant rs28377576dbSNPEnsembl.1
Natural variantiVAR_0356083653T → K in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_0229353740L → I in LQT4; loss of function. 1 PublicationCorresponds to variant rs35530544dbSNPEnsembl.1
Natural variantiVAR_0229363744T → N in LQT4; loss of function. 1 PublicationCorresponds to variant rs121912705dbSNPEnsembl.1
Natural variantiVAR_0229373906R → W in LQT4; loss of function. 1 PublicationCorresponds to variant rs121912706dbSNPEnsembl.1
Natural variantiVAR_0229383931E → K in LQT4; loss of function. 1 PublicationCorresponds to variant rs45454496dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0370571 – 1348Missing in isoform 5. 1 PublicationAdd BLAST1348
Alternative sequenceiVSP_0370581 – 27MMNED…RKRPK → MTTMLQ in isoform 4. 1 PublicationAdd BLAST27
Alternative sequenceiVSP_037059967G → GRASPCLERDNSS in isoform 4. 1 Publication1
Alternative sequenceiVSP_0002681477 – 3561Missing in isoform 2, isoform 4 and isoform 5. 3 PublicationsAdd BLAST2085
Alternative sequenceiVSP_0370603870K → KELTEELGELEASSDEEAMV TTRVVRRRVIIQ in isoform 5. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56957 mRNA. Translation: CAA40278.1.
X56958 mRNA. Translation: CAA40279.2.
Z26634 mRNA. Translation: CAB42644.1. Sequence problems.
BX537758 mRNA. Translation: CAD97827.1.
AC004057 Genomic DNA. No translation available.
AC093617 Genomic DNA. No translation available.
AC093879 Genomic DNA. No translation available.
AC093900 Genomic DNA. No translation available.
BC125235 mRNA. Translation: AAI25236.1.
BC125236 mRNA. Translation: AAI25237.1. Frameshift.
M37123 Genomic DNA. Translation: AAA62828.1.
CCDSiCCDS3702.1. [Q01484-4]
CCDS43261.1. [Q01484-2]
CCDS54796.1. [Q01484-5]
PIRiS37431.
RefSeqiNP_001120965.1. NM_001127493.1. [Q01484-5]
NP_001139.3. NM_001148.4. [Q01484-4]
NP_066187.2. NM_020977.3. [Q01484-2]
UniGeneiHs.620557.

Genome annotation databases

EnsembliENST00000357077; ENSP00000349588; ENSG00000145362. [Q01484-4]
ENST00000394537; ENSP00000378044; ENSG00000145362. [Q01484-2]
ENST00000506722; ENSP00000421067; ENSG00000145362. [Q01484-5]
ENST00000510275; ENSP00000421023; ENSG00000145362. [Q01484-7]
GeneIDi287.
KEGGihsa:287.
UCSCiuc003ibd.5. human. [Q01484-4]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Ankyrin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56957 mRNA. Translation: CAA40278.1.
X56958 mRNA. Translation: CAA40279.2.
Z26634 mRNA. Translation: CAB42644.1. Sequence problems.
BX537758 mRNA. Translation: CAD97827.1.
AC004057 Genomic DNA. No translation available.
AC093617 Genomic DNA. No translation available.
AC093879 Genomic DNA. No translation available.
AC093900 Genomic DNA. No translation available.
BC125235 mRNA. Translation: AAI25236.1.
BC125236 mRNA. Translation: AAI25237.1. Frameshift.
M37123 Genomic DNA. Translation: AAA62828.1.
CCDSiCCDS3702.1. [Q01484-4]
CCDS43261.1. [Q01484-2]
CCDS54796.1. [Q01484-5]
PIRiS37431.
RefSeqiNP_001120965.1. NM_001127493.1. [Q01484-5]
NP_001139.3. NM_001148.4. [Q01484-4]
NP_066187.2. NM_020977.3. [Q01484-2]
UniGeneiHs.620557.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4D8OX-ray2.20A966-1476[»]
4RLVX-ray3.49A28-873[»]
4RLYX-ray2.50A28-318[»]
DisProtiDP00467.
ProteinModelPortaliQ01484.
SMRiQ01484.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106784. 21 interactors.
DIPiDIP-37425N.
IntActiQ01484. 21 interactors.
STRINGi9606.ENSP00000349588.

Protein family/group databases

TCDBi8.A.28.1.1. the ankyrin (ankyrin) family.

PTM databases

iPTMnetiQ01484.
PhosphoSitePlusiQ01484.
SwissPalmiQ01484.

Polymorphism and mutation databases

BioMutaiANK2.
DMDMi387912917.

Proteomic databases

EPDiQ01484.
MaxQBiQ01484.
PaxDbiQ01484.
PeptideAtlasiQ01484.
PRIDEiQ01484.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000357077; ENSP00000349588; ENSG00000145362. [Q01484-4]
ENST00000394537; ENSP00000378044; ENSG00000145362. [Q01484-2]
ENST00000506722; ENSP00000421067; ENSG00000145362. [Q01484-5]
ENST00000510275; ENSP00000421023; ENSG00000145362. [Q01484-7]
GeneIDi287.
KEGGihsa:287.
UCSCiuc003ibd.5. human. [Q01484-4]

Organism-specific databases

CTDi287.
DisGeNETi287.
GeneCardsiANK2.
H-InvDBHIX0164018.
HGNCiHGNC:493. ANK2.
HPAiCAB015178.
HPA007570.
HPA008007.
HPA035970.
MalaCardsiANK2.
MIMi106410. gene.
600919. phenotype.
neXtProtiNX_Q01484.
OpenTargetsiENSG00000145362.
Orphaneti101016. Romano-Ward syndrome.
PharmGKBiPA24799.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4177. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00840000129677.
HOGENOMiHOG000169277.
HOVERGENiHBG100442.
InParanoidiQ01484.
KOiK10380.
OrthoDBiEOG091G00GN.
PhylomeDBiQ01484.
TreeFamiTF351263.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000145362-MONOMER.
ReactomeiR-HSA-445095. Interaction between L1 and Ankyrins.
R-HSA-6807878. COPI-mediated anterograde transport.

Miscellaneous databases

ChiTaRSiANK2. human.
GenomeRNAii287.
PROiQ01484.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000145362.
CleanExiHS_ANK2.
ExpressionAtlasiQ01484. baseline and differential.
GenevisibleiQ01484. HS.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
1.25.40.20. 3 hits.
InterProiIPR030301. Ankyrin-B.
IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR000906. ZU5_dom.
[Graphical view]
PANTHERiPTHR24123:SF17. PTHR24123:SF17. 4 hits.
PfamiPF00023. Ank. 2 hits.
PF12796. Ank_2. 6 hits.
PF00531. Death. 1 hit.
PF00791. ZU5. 3 hits.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 23 hits.
SM00005. DEATH. 1 hit.
SM00218. ZU5. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF48403. SSF48403. 3 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 20 hits.
PS50017. DEATH_DOMAIN. 1 hit.
PS51145. ZU5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiANK2_HUMAN
AccessioniPrimary (citable) accession number: Q01484
Secondary accession number(s): Q01485
, Q08AC7, Q08AC8, Q7Z3L5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: May 16, 2012
Last modified: November 30, 2016
This is version 179 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.