Protein detail
ANK2
Ankyrin-2 (ANK-2) (Ankyrin-B) (Brain ankyrin) (Non-erythroid ankyrin)
Protein symbol ANK2 | UniProt ID | EVMP score 0.50 |
Frequency 1 | Transmembrane count | Protein classification Disease related genesHuman disease related genesPlasma proteinsPotential drug targetsPredicted intracellular proteinsTransporters |
EVMP score: annotation confidence score.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information
Protein Names
Ankyrin-2 (ANK-2) (Ankyrin-B) (Brain ankyrin) (Non-erythroid ankyrin)
Protein Class
Disease related genesHuman disease related genesPlasma proteinsPotential drug targetsPredicted intracellular proteinsTransporters
Protein Function
- Predicted intracellular proteins
- Potential drug targets
- Transporters:Accessory Factors Involved in Transport
- Disease related genes
- Human disease related genes:Cardiovascular diseases:Cardiac diseases
Ensembl
Entrez Gene Symbol
Gene Synonym
CFAP87FAP87LQT4
Gene Description
Ankyrin 2
Chromosome
4
Position
112818032-113384221
Frequency
1
EVMP Score
0.50
Fluorescence & Localization
Tissue Specificparathyroid glandBrain Regional SpecificcerebellumCell SpecificAdrenal medulla cellsSingle-Nuclei Brain Specificupper rhombic lipBlood Cell SpecificbasophilBlood Lineage Specificgranulocytes
Function & Pathway
Protein Function
- Predicted intracellular proteins
- Potential drug targets
- Transporters:Accessory Factors Involved in Transport
- Disease related genes
- Human disease related genes:Cardiovascular diseases:Cardiac diseases
Cellular Component
- GO:0005739 mitochondrion
- GO:0005764 lysosome
- GO:0005769 early endosome
- GO:0005829 cytosol
- GO:0005856 cytoskeleton
- GO:0005886 plasma membrane
- GO:0014704 intercalated disc
- GO:0016323 basolateral plasma membrane
- GO:0016324 apical plasma membrane
- GO:0030018 Z disc
- GO:0030315 T-tubule
- GO:0031430 M band
- GO:0031672 A band
- GO:0042383 sarcolemma
- GO:0043005 neuron projection
- GO:0043034 costamere
- GO:0045211 postsynaptic membrane
- GO:0055037 recycling endosome
Molecular Function
- GO:0005200 structural constituent of cytoskeleton
- GO:0005515 protein binding
- GO:0008093 cytoskeletal anchor activity
- GO:0019899 enzyme binding
- GO:0019901 protein kinase binding
- GO:0030507 spectrin binding
- GO:0030674 protein-macromolecule adaptor activity
- GO:0044325 transmembrane transporter binding
- GO:0051117 ATPase binding
- GO:0140031 phosphorylation-dependent protein binding
Biological Process
KEGG
Reactome
- R-hsa-446203 asparagine n linked glycosylation
- R-hsa-6807878 copi mediated anterograde transport
- R-hsa-199977 er to golgi anterograde transport
- R-hsa-445095 interaction between l1 and ankyrins
- R-hsa-373760 l1cam interactions
- R-hsa-199991 membrane trafficking
- R-hsa-9675108 nervous system development
- R-hsa-597592 post translational protein modification
- R-hsa-948021 transport to the golgi and subsequent modification
- R-hsa-5653656 vesicle mediated transport
Canonical Pathways
- M190 Pid tcr jnk pathway
- M1718 Sig il4receptor in b lyphocytes
- M8626 Sig bcr signaling pathway
Mediation Categories
Fusion and delivery mediationImmune mediationMetabolism mediationReceptor-signaling mediation
Relations & Evidence
Enzyme-Mediated Modification
3 records.
| Substrate Gene Symbol | Enzyme Gene Symbol | Enzyme UniProt ID | Residue Type | Residue Offset | Modification | Database | References |
|---|---|---|---|---|---|---|---|
| ANK2 | CDK2 | P24941 | S | 309 | phosphorylation | KEA | KEA:17570479 |
| ANK2 | CSNK1E | P49674 | T | 819 | phosphorylation | KEA | KEA:17570479 |
| ANK2 | GSK3B | P49841 | S | 309 | phosphorylation | KEA | KEA:17570479 |
Ligand-Receptor Signaling
11 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| intracellular | intracellular | LOCATE | No | No | No | No | No |
| intracellular | intracellular | ComPPI | No | No | No | No | No |
| intracellular | intracellular | GO_Intercell | No | No | No | No | No |
| intracellular | intracellular | UniProt_location | No | No | No | No | No |
| intracellular | intracellular | OmniPath | No | No | No | No | No |
| ion_channel | ion_channel | DGIdb | No | Yes | No | No | No |
| transporter | transporter | OmniPath | No | Yes | No | No | No |
| ion_channel | ion_channel | OmniPath | No | Yes | No | No | No |
| plasma_membrane | plasma_membrane | UniProt_location | No | No | No | No | No |
| apical_cell_membrane | plasma_membrane | UniProt_location | No | No | No | No | No |
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Regulatory Interaction Network
9 records.
| Source Protein Symbol | Source UniProt ID | Target Protein Symbol | Target UniProt ID | Is Directed | Is Stimulation | Is Inhibition | Database | References |
|---|---|---|---|---|---|---|---|---|
| NCHL1 | O00533 | ANK2 | Q01484 | Yes | Yes | No | SIGNOR | SIGNOR:7961622 |
| NFASC | O94856 | ANK2 | Q01484 | Yes | Yes | No | SIGNOR | SIGNOR:7961622 |
| OBSCN | Q5VST9 | ANK2 | Q01484 | Yes | Yes | No | HPRDSPIKE_LCPhosphoPointSIGNOR | HPRD:12527750SPIKE_LC:12527750SIGNOR:19840192 |
| ANK2 | Q01484 | CAC1A | O00555 | Yes | Yes | No | SIGNOR | SIGNOR:24394417 |
| ANK2 | Q01484 | CAC1B | Q00975 | Yes | Yes | No | SIGNOR | SIGNOR:24394417 |
| ANK2 | Q01484 | 2A5A | Q15172 | Yes | Yes | No | SIGNOR | SIGNOR:19840192 |
| ANK2 | Q01484 | DMD | P11532 | Yes | Yes | No | SIGNOR | SIGNOR:19109891 |
| NRCAM | Q92823 | ANK2 | Q01484 | Yes | Yes | No | HPRDSIGNOR | SIGNOR:7961622HPRD:11449000 |
| ANK2 | Q01484 | DCTN4 | Q9UJW0 | Yes | Yes | No | SIGNOR | SIGNOR:19109891 |
Protein Complex Composition
7 records.
| Component Name | Component Gene Symbols | Component UniProt ID | Stoichiometry | Database | Database IDs | References |
|---|---|---|---|---|---|---|
| FAM83BKANK2PKP2SEC16A | O15027Q5T0W9Q63ZY3Q99959 | 0:0:0:0 | hu.MAP | |||
| DNM2PANK2QRICH1 | P50570Q2TAL8Q9BZ23 | 0:0:0 | hu.MAP | |||
| ANK2 | Q01484 | 2 | PDB | PDB:5y4fPDB:5y4e | ||
| ANK2FPGS | Q01484Q05932 | 0:0 | hu.MAP2 | |||
| KANK2KIF21A | Q63ZY3Q7Z4S6 | 2:2 | PDB | PDB:5ybv | ||
| PANK2SAT2 | Q96F10Q9BZ23 | 0:0 | hu.MAP2 | |||
| PANK2 | Q9BZ23 | 4 | PDB | PDB:5e26 |
Isolation & Detection Technology
1 record.
| EV Isolation Method | Detection Method | Number of References | References |
|---|---|---|---|
| PRotein Organic Solvent Precipitation๏ผDifferential Ultracentrifugation | Mass spectrometry | 1 | 32384937 |
Sequence, Structure & Domains
Sequences
Length
3,957
Mass
433,715
Sequence
MMNEDAAQKSDSGEKFNGSSQRRKRPKKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKMMVNRTTESGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTLKVVTEEVTTTTTTITEKHKLNVPETMTEVLDVSDEEGDDTMTGDGGEYLRPEDLKELGDDSLPSSQFLDGMNYLRYSLEGGRSDSLRSFSSDRSHTLSHASYLRDSAVMDDSVVIPSHQVSTLAKEAERNSYRLSWGTENLDNVALSSSPIHSGFLVSFMVDARGGAMRGCRHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGKLHLPTAPPPLNEGESLVSRILQLGPPGTKFLGPVIVEIPHFAALRGKERELVVLRSENGDSWKEHFCDYTEDELNEILNGMDEVLDSPEDLEKKRICRIITRDFPQYFAVVSRIKQDSNLIGPEGGVLSSTVVPQVQAVFPEGALTKRIRVGLQAQPMHSELVKKILGNKATFSPIVTLEPRRRKFHKPITMTIPVPKASSDVMLNGFGGDAPTLRLLCSITGGTTPAQWEDITGTTPLTFVNECVSFTTNVSARFWLIDCRQIQESVTFASQVYREIICVPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSFFAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLPIYTKESESDQEQEEEIDMTSEKNDETESTETSVLKSHLVNEVPVLASPDLLSEVSEMKQDLIKMTAILTTDVSDKAGSIKVKELVKAAEEEPGEPFEIVERVKEDLEKVNEILRSGTCTRDESSVQSSRSERGLVEEEWVIVSDEEIEEARQKAPLEITEYPCVEVRIDKEIKGKVEKDSTGLVNYLTDDLNTCVPLPKEQLQTVQDKAGKKCEALAVGRSSEKEGKDIPPDETQSTQKQHKPSLGIKKPVRRKLKEKQKQKEEGLQASAEKAELKKGSSEESLGEDPGLAPEPLPTVKATSPLIEETPIGSIKDKVKALQKRVEDEQKGRSKLPIRVKGKEDVPKKTTHRPHPAASPSLKSERHAPGSPSPKTERHSTLSSSAKTERHPPVSPSSKTEKHSPVSPSAKTERHSPASSSSKTEKHSPVSPSTKTERHSPVSSTKTERHPPVSPSGKTDKRPPVSPSGRTEKHPPVSPGRTEKRLPVSPSGRTDKHQPVSTAGKTEKHLPVSPSGKTEKQPPVSPTSKTERIEETMSVRELMKAFQSGQDPSKHKTGLFEHKSAKQKQPQEKGKVRVEKEKGPILTQREAQKTENQTIKRGQRLPVTGTAESKRGVRVSSIGVKKEDAAGGKEKVLSHKIPEPVQSVPEEESHRESEVPKEKMADEQGDMDLQISPDRKTSTDFSEVIKQELEDNDKYQQFRLSEETEKAQLHLDQVLTSPFNTTFPLDYMKDEFLPALSLQSGALDGSSESLKNEGVAGSPCGSLMEGTPQISSEESYKHEGLAETPETSPESLSFSPKKSEEQTGETKESTKTETTTEIRSEKEHPTTKDITGGSEERGATVTEDSETSTESFQKEATLGSPKDTSPKRQDDCTGSCSVALAKETPTGLTEEAACDEGQRTFGSSAHKTQTDSEVQESTATSDETKALPLPEASVKTDTGTESKPQGVIRSPQGLELALPSRDSEVLSAVADDSLAVSHKDSLEASPVLEDNSSHKTPDSLEPSPLKESPCRDSLESSPVEPKMKAGIFPSHFPLPAAVAKTELLTEVASVRSRLLRDPDGSAEDDSLEQTSLMESSGKSPLSPDTPSSEEVSYEVTPKTTDVSTPKPAVIHECAEEDDSENGEKKRFTPEEEMFKMVTKIKMFDELEQEAKQKRDYKKEPKQEESSSSSDPDADCSVDVDEPKHTGSGEDESGVPVLVTSESRKVSSSSESEPELAQLKKGADSGLLPEPVIRVQPPSPLPSSMDSNSSPEEVQFQPVVSKQYTFKMNEDTQEEPGKSEEEKDSESHLAEDRHAVSTEAEDRSYDKLNRDTDQPKICDGHGCEAMSPSSSAAPVSSGLQSPTGDDVDEQPVIYKESLALQGTHEKDTEGEELDVSRAESPQADCPSESFSSSSSLPHCLVSEGKELDEDISATSSIQKTEVTKTDETFENLPKDCPSQDSSITTQTDRFSMDVPVSDLAENDEIYDPQITSPYENVPSQSFFSSEESKTQTDANHTTSFHSSEVYSVTITSPVEDVVVASSSSGTVLSKESNFEGQDIKMESQQESTLWEMQSDSVSSSFEPTMSATTTVVGEQISKVIITKTDVDSDSWSEIREDDEAFEARVKEEEQKIFGLMVDRQSQGTTPDTTPARTPTEEGTPTSEQNPFLFQEGKLFEMTRSGAIDMTKRSYADESFHFFQIGQESREETLSEDVKEGATGADPLPLETSAESLALSESKETVDDEADLLPDDVSEEVEEIPASDAQLNSQMGISASTETPTKEAVSVGTKDLPTVQTGDIPPLSGVKQISCPDSSEPAVQVQLDFSTLTRSVYSDRGDDSPDSSPEEQKSVIEIPTAPMENVPFTESKSKIPVRTMPTSTPAPPSAEYESSVSEDFLSSVDEENKADEAKPKSKLPVKVPLQRVEQQLSDLDTSVQKTVAPQGQDMASIAPDNRSKSESDASSLDSKTKCPVKTRSYTETETESRERAEELELESEEGATRPKILTSRLPVKSRSTTSSCRGGTSPTKESKEHFFDLYRNSIEFFEEISDEASKLVDRLTQSEREQEIVSDDESSSALEVSVIENLPPVETEHSVPEDIFDTRPIWDESIETLIERIPDENGHDHAEDPQDEQERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIVHLMETNTEPLQERISHSYAEIEQTITLDHSEGFSVLQEELCTAQHKQKEEQAVSKESETCDHPPIVSEEDISVGYSTFQDGVPKTEGDSSATALFPQTHKEQVQQDFSGKMQDLPEESSLEYQQEYFVTTPGTETSETQKAMIVPSSPSKTPEEVSTPAEEEKLYLQTPTSSERGGSPIIQEPEEPSEHREESSPRKTSLVIVESADNQPETCERLDEDAAFEKGDDMPEIPPETVTEEEYIDEHGHTVVKKVTRKIIRRYVSSEGTEKEEIMVQGMPQEPVNIEEGDGYSKVIKRVVLKSDTEQSEDNNE
Alternative Products
Event=Alternative splicing; Named isoforms=4; Name=3; IsoId=Q01484-4; Sequence=Displayed; Name=2; IsoId=Q01484-2; Sequence=VSP_000268; Name=4; IsoId=Q01484-5; Sequence=VSP_037058, VSP_037059, VSP_000268; Name=5; IsoId=Q01484-7; Sequence=VSP_037057, VSP_000268, VSP_037060
Alternative Sequence
1..1348; Missing (in isoform 5); 1..27; MMNEDAAQKSDSGEKFNGSSQRRKRPK -> MTTMLQ (in isoform 4); 967; G -> GRASPCLERDNSS (in isoform 4); 1477..3561; Missing (in isoform 2, isoform 4 and isoform 5); 3870; K -> KELTEELGELEASSDEEAMVTTRVVRRRVIIQ (in isoform 5)
3D Structural Models
Turn
151..153; 184..186; 221..223; 831..833; 1088..1091
Helix
30..41; 44..52; 67..74; 77..86; 100..106; 110..118; 133..139; 143..150; 166..172; 176..183; 195..202; 205..211; 212..214; 225..227; 236..243; 246..254; 264..266; 269..275; 279..287; 302..308; 312..320; 335..341; 345..353; 368..375; 378..386; 396..398; 401..407; 411..419; 434..441; 444..452; 467..473; 477..485; 495..497; 500..506; 510..518; 533..540; 543..551; 566..573; 576..584; 599..605; 609..617; 632..639; 642..650; 665..672; 675..683; 698..705; 708..716; 731..738; 741..749; 764..770; 774..782; 797..803; 807..814; 1114..1121; 1131..1137; 1203..1210; 1277..1279; 1307..1309; 1310..1321; 1357..1359; 1484..1491; 1501..1521; 1534..1543; 1548..1568; 1597..1601; 3583..3590; 3595..3604; 3609..3624; 3625..3627; 3630..3639; 3643..3646
Beta Strand
693..695; 759..761; 960..962; 969..974; 979..982; 984..986; 990..993; 998..1000; 1002..1009; 1025..1028; 1031..1035; 1039..1042; 1076..1082; 1092..1103; 1139..1146; 1149..1157; 1159..1165; 1168..1172; 1174..1176; 1180..1183; 1192..1199; 1213..1216; 1219..1226; 1228..1238; 1258..1263; 1283..1285; 1288..1295; 1298..1305; 1325..1335; 1338..1349; 1365..1369; 1373..1376; 1380..1391; 1399..1402; 1410..1418; 1420..1422; 1424..1432; 1445..1451; 1592..1594; 1606..1609
3D Structure
X-ray crystallography (11)
Domain & Motif Annotations
Compositional Bias
1..14; Basic and acidic residues; 1461..1471; Acidic residues; 1674..1683; Basic and acidic residues; 1711..1733; Basic and acidic residues; 1766..1783; Basic and acidic residues; 1886..1902; Basic and acidic residues; 1921..1937; Basic and acidic residues; 1980..1994; Basic and acidic residues; 2003..2034; Basic and acidic residues; 2075..2093; Basic and acidic residues; 2102..2117; Basic and acidic residues; 2128..2137; Basic and acidic residues; 2240..2251; Polar residues; 2252..2282; Basic and acidic residues; 2355..2376; Polar residues; 2523..2545; Polar residues; 2576..2586; Basic and acidic residues; 2604..2619; Basic and acidic residues; 2696..2705; Low complexity; 2729..2776; Basic and acidic residues; 2781..2791; Low complexity; 2892..2903; Polar residues; 2998..3016; Polar residues; 3078..3087; Low complexity; 3090..3099; Polar residues; 3137..3149; Basic and acidic residues; 3157..3169; Low complexity; 3175..3194; Acidic residues; 3198..3212; Polar residues; 3256..3265; Polar residues; 3335..3344; Basic and acidic residues; 3357..3374; Polar residues; 3409..3423; Basic and acidic residues; 3446..3460; Low complexity; 3832..3841; Basic and acidic residues
Repeat
30..62; ANK 1; 63..92; ANK 2; 96..125; ANK 3; 129..158; ANK 4; 162..191; ANK 5; 193..220; ANK 6; 232..261; ANK 7; 265..294; ANK 8; 298..327; ANK 9; 331..360; ANK 10; 364..393; ANK 11; 397..426; ANK 12; 430..459; ANK 13; 463..492; ANK 14; 496..525; ANK 15; 529..558; ANK 16; 562..591; ANK 17; 595..624; ANK 18; 628..657; ANK 19; 661..690; ANK 20; 694..723; ANK 21; 727..756; ANK 22; 760..789; ANK 23; 793..822; ANK 24; 1806..1817; Repeat A; 1818..1829; Repeat A; 1830..1841; Repeat A; 1842..1853; Repeat A; 1854..1865; Repeat A; 1866..1877; Repeat A; 1878..1889; Repeat A; 1890..1900; Repeat A; approximate; 1901..1912; Repeat A; 1913..1924; Repeat A; 1925..1935; Repeat A; approximate; 1936..1947; Repeat A; 1948..1959; Repeat A; 1960..1971; Repeat A; 1972..1983; Repeat A
Domain (CC)
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.
Domain (FT)
968..1156; ZU5 1; 1158..1304; ZU5 2; 1450..1535; Death 1; 3569..3653; Death 2
Region
1..34; Disordered; 966..1125; Interaction with SPTBN1; 1289..1423; UPA domain; 1457..1486; Disordered; 1670..2137; Disordered; 1806..1983; Repeat-rich region; 2197..2411; Disordered; 2430..2484; Disordered; 2507..2586; Disordered; 2604..2852; Disordered; 2864..2904; Disordered; 2923..2951; Disordered; 2987..3016; Disordered; 3069..3099; Disordered; 3136..3462; Disordered; 3777..3858; Disordered
Clinical Relevance
Disease Involvement
Disease variantLong QT syndrome
Drugs
AGOMELATINEUCSF3384DIFLUOROAGOMELATINES221536-HYDROXYMELATONINK185LY 156735UCSF7447MELATONINGR 196429S26131UCM 793N-[2-(2-IODO-5-METHOXY-1H-INDOL-3-YL)ETHYL]ACETAMIDEEFPPEAICOA-13GR 1281072-[125I]MELATONINAAE-M-PBP-AMINEUCM 724S262845-HEAT4P-PDOTUCM 549TASIMELTEONS24014AZD73252-METHOXY-&ALPHA,&BETA-DIDEHYDRO-AGOMELATINEUCM13416-CL-MLTLUZINDOLERAMELTEONS20928CBOBNEA[125I]SD6S24773UCSF4226IIK7
Interaction Protein
ENSG00000125844ENSG00000168944ENSG00000197102
Interaction Count
3
Interaction Dataset
intact_biogrid