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Q01484 (ANK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ankyrin-2

Short name=ANK-2
Alternative name(s):
Ankyrin-B
Brain ankyrin
Non-erythroid ankyrin
Gene names
Name:ANK2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length3957 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8

Subunit structure

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 By similarity. Interacts with RHBG and SPTBN1. Ref.9 Ref.10 Ref.11

Subcellular location

Cytoplasmcytoskeleton. Membrane. CytoplasmmyofibrilsarcomereM line By similarity. Apical cell membrane By similarity. Cell membrane. 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. Ref.11

Tissue specificity

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. Ref.1 Ref.7 Ref.11

Domain

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. Ref.14

Post-translational modification

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

Involvement in disease

Long QT syndrome 4 (LQT4) [MIM:600919]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.15

Sequence similarities

Contains 24 ANK repeats.

Contains 2 death domains.

Contains 2 ZU5 domains.

Sequence caution

The sequence AAI25237.1 differs from that shown. Reason: Frameshift at position 1405.

The sequence CAB42644.1 differs from that shown. Reason: CDS lacks C-terminal region which is nevertheless present in the underlying cDNA.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Long QT syndrome
   DomainANK repeat
Repeat
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processSA node cell action potential

Inferred from sequence or structural similarity. Source: BHF-UCL

SA node cell to atrial cardiac muscle cell communication

Inferred from mutant phenotype Ref.8PubMed 18832177PubMed 21859974. Source: BHF-UCL

T-tubule organization

Inferred from sequence or structural similarity. Source: BHF-UCL

atrial cardiac muscle cell action potential

Inferred from mutant phenotype PubMed 17242276PubMed 18832177PubMed 21859974. Source: BHF-UCL

atrial cardiac muscle cell to AV node cell communication

Inferred from sequence or structural similarity. Source: BHF-UCL

atrial septum development

Inferred from mutant phenotype PubMed 18832177. Source: BHF-UCL

axon guidance

Traceable author statement. Source: Reactome

cardiac muscle contraction

Inferred from electronic annotation. Source: Ensembl

cellular calcium ion homeostasis

Inferred from sequence or structural similarity. Source: BHF-UCL

cellular protein localization

Inferred from genetic interaction Ref.9PubMed 17242276. Source: BHF-UCL

membrane depolarization during SA node cell action potential

Traceable author statement PubMed 19098452. Source: BHF-UCL

paranodal junction assembly

Inferred from electronic annotation. Source: Ensembl

positive regulation of calcium ion transmembrane transporter activity

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of calcium ion transport

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cation channel activity

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of gene expression

Inferred from genetic interaction PubMed 17242276. Source: BHF-UCL

positive regulation of potassium ion transmembrane transporter activity

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of potassium ion transport

Inferred from sequence or structural similarity. Source: BHF-UCL

protein localization to M-band

Inferred from sequence or structural similarity. Source: BHF-UCL

protein localization to T-tubule

Inferred from sequence or structural similarity. Source: BHF-UCL

protein localization to cell surface

Inferred from sequence or structural similarity. Source: BHF-UCL

protein localization to endoplasmic reticulum

Inferred from genetic interaction Ref.15. Source: BHF-UCL

protein localization to organelle

Inferred from genetic interaction Ref.15. Source: BHF-UCL

protein localization to plasma membrane

Inferred from genetic interaction PubMed 17178715. Source: BHF-UCL

protein stabilization

Inferred from sequence or structural similarity PubMed 17178715. Source: BHF-UCL

protein targeting to plasma membrane

Inferred from electronic annotation. Source: Ensembl

regulation of calcium ion transmembrane transporter activity

Inferred from sequence or structural similarity PubMed 21859974. Source: BHF-UCL

regulation of calcium ion transport

Inferred from genetic interaction Ref.8Ref.15. Source: BHF-UCL

regulation of cardiac muscle cell contraction

Inferred from genetic interaction PubMed 17242276. Source: BHF-UCL

regulation of cardiac muscle cell membrane potential

Inferred from electronic annotation. Source: Ensembl

regulation of cardiac muscle contraction

Inferred from mutant phenotype Ref.15. Source: BHF-UCL

regulation of cardiac muscle contraction by calcium ion signaling

Inferred from mutant phenotype Ref.8. Source: BHF-UCL

regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion

Inferred from genetic interaction PubMed 17178715. Source: BHF-UCL

regulation of heart rate

Inferred from mutant phenotype PubMed 18832177. Source: BHF-UCL

regulation of heart rate by cardiac conduction

Inferred from mutant phenotype Ref.8Ref.15PubMed 17242276PubMed 21859974. Source: BHF-UCL

regulation of protein stability

Inferred by curator PubMed 18832177. Source: BHF-UCL

regulation of release of sequestered calcium ion into cytosol

Inferred from genetic interaction PubMed 17242276. Source: BHF-UCL

regulation of ventricular cardiac muscle cell membrane repolarization

Inferred from mutant phenotype PubMed 18832177. Source: BHF-UCL

response to methylmercury

Inferred from electronic annotation. Source: Ensembl

sarcoplasmic reticulum calcium ion transport

Traceable author statement PubMed 19098452. Source: BHF-UCL

ventricular cardiac muscle cell action potential

Inferred from mutant phenotype PubMed 17242276. Source: BHF-UCL

   Cellular_componentA band

Inferred from sequence or structural similarity. Source: BHF-UCL

M band

Inferred from sequence or structural similarity. Source: BHF-UCL

T-tubule

Inferred from sequence or structural similarity. Source: BHF-UCL

Z disc

Inferred from sequence or structural similarity. Source: BHF-UCL

apical plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

basolateral plasma membrane

Inferred from direct assay Ref.10. Source: UniProtKB

costamere

Inferred from sequence or structural similarity. Source: BHF-UCL

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

integral component of plasma membrane

Inferred from electronic annotation. Source: Ensembl

intercalated disc

Inferred from sequence or structural similarity. Source: BHF-UCL

intracellular

Inferred from genetic interaction PubMed 17178715. Source: BHF-UCL

membrane raft

Inferred from electronic annotation. Source: Ensembl

neuron projection

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

sarcolemma

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular_functionATPase binding

Inferred from sequence or structural similarity. Source: BHF-UCL

enzyme binding

Inferred from physical interaction PubMed 21177872. Source: UniProtKB

ion channel binding

Inferred from physical interaction PubMed 20610380PubMed 21859974. Source: BHF-UCL

potassium channel regulator activity

Inferred from electronic annotation. Source: Ensembl

protein binding, bridging

Inferred from sequence or structural similarity. Source: BHF-UCL

protein kinase binding

Inferred from physical interaction PubMed 18782775. Source: BHF-UCL

spectrin binding

Inferred from physical interaction Ref.9. Source: BHF-UCL

structural constituent of cytoskeleton

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 3 (identifier: Q01484-4)

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.
Isoform 2 (identifier: Q01484-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1477-3561: Missing.
Isoform 4 (identifier: Q01484-5)

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.
Isoform 5 (identifier: Q01484-7)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 39573957Ankyrin-2
PRO_0000066885

Regions

Repeat30 – 6233ANK 1
Repeat63 – 9230ANK 2
Repeat96 – 12530ANK 3
Repeat129 – 15830ANK 4
Repeat162 – 19130ANK 5
Repeat193 – 22028ANK 6
Repeat232 – 26130ANK 7
Repeat265 – 29430ANK 8
Repeat298 – 32730ANK 9
Repeat331 – 36030ANK 10
Repeat364 – 39330ANK 11
Repeat397 – 42630ANK 12
Repeat430 – 45930ANK 13
Repeat463 – 49230ANK 14
Repeat496 – 52530ANK 15
Repeat529 – 55830ANK 16
Repeat562 – 59130ANK 17
Repeat595 – 62430ANK 18
Repeat628 – 65730ANK 19
Repeat661 – 69030ANK 20
Repeat694 – 72330ANK 21
Repeat727 – 75630ANK 22
Repeat760 – 78930ANK 23
Repeat793 – 82230ANK 24
Domain966 – 1124159ZU5 1
Domain1125 – 1288164ZU5 2
Domain1450 – 153586Death 1
Repeat1806 – 181712Repeat A
Repeat1818 – 182912Repeat A
Repeat1830 – 184112Repeat A
Repeat1842 – 185312Repeat A
Repeat1854 – 186512Repeat A
Repeat1866 – 187712Repeat A
Repeat1878 – 188912Repeat A
Repeat1890 – 190011Repeat A; approximate
Repeat1901 – 191212Repeat A
Repeat1913 – 192412Repeat A
Repeat1925 – 193511Repeat A; approximate
Repeat1936 – 194712Repeat A
Repeat1948 – 195912Repeat A
Repeat1960 – 197112Repeat A
Repeat1972 – 198312Repeat A
Domain3569 – 365385Death 2
Region966 – 1125160Interaction with SPTBN1
Region1289 – 1423135UPA domain
Region1806 – 1983178Repeat-rich region

Amino acid modifications

Modified residue3781Phosphotyrosine By similarity
Modified residue5311Phosphotyrosine By similarity
Modified residue13821Phosphotyrosine By similarity
Modified residue37761Phosphothreonine By similarity

Natural variations

Alternative sequence1 – 13481348Missing in isoform 5.
VSP_037057
Alternative sequence1 – 2727MMNED…RKRPK → MTTMLQ in isoform 4.
VSP_037058
Alternative sequence9671G → GRASPCLERDNSS in isoform 4.
VSP_037059
Alternative sequence1477 – 35612085Missing in isoform 2, isoform 4 and isoform 5.
VSP_000268
Alternative sequence38701K → KELTEELGELEASSDEEAMV TTRVVRRRVIIQ in isoform 5.
VSP_037060
Natural variant6851G → E in a breast cancer sample; somatic mutation. Ref.16
VAR_035606
Natural variant6871N → S.
Corresponds to variant rs29372 [ dbSNP | Ensembl ].
VAR_055504
Natural variant12671G → R in a colorectal cancer sample; somatic mutation. Ref.16
VAR_035607
Natural variant14581E → G in LQT4; loss of function. Ref.8 Ref.15
Corresponds to variant rs72544141 [ dbSNP | Ensembl ].
VAR_022934
Natural variant23691V → A.
Corresponds to variant rs28377576 [ dbSNP | Ensembl ].
VAR_055505
Natural variant36531T → K in a colorectal cancer sample; somatic mutation. Ref.16
VAR_035608
Natural variant37401L → I in LQT4; loss of function. Ref.15
Corresponds to variant rs35530544 [ dbSNP | Ensembl ].
VAR_022935
Natural variant37441T → N in LQT4; loss of function. Ref.15
VAR_022936
Natural variant39061R → W in LQT4; loss of function. Ref.15
Corresponds to variant rs121912706 [ dbSNP | Ensembl ].
VAR_022937
Natural variant39311E → K in LQT4; loss of function. Ref.15
Corresponds to variant rs45454496 [ dbSNP | Ensembl ].
VAR_022938

Experimental info

Mutagenesis975 – 9773DAR → AAA: Prevents binding to SPTBN1. Ref.9
Mutagenesis10001A → P: Prevents binding to SPTBN1. Ref.9
Mutagenesis1100 – 11034ENGD → AAGA: Weak binding to SPTBN1. Ref.9
Sequence conflict2201V → I in CAD97827. Ref.4
Sequence conflict475 – 4762GQ → PE in AAA62828. Ref.7
Sequence conflict27871A → R in CAB42644. Ref.3
Sequence conflict29991Q → L in CAB42644. Ref.3
Sequence conflict3140 – 31412EE → RY in AC093879. Ref.5
Sequence conflict31851D → S in CAB42644. Ref.3
Sequence conflict36991V → A in CAD97827. Ref.4
Sequence conflict37371A → S in CAA40279. Ref.1
Sequence conflict37371A → S in CAB42644. Ref.3
Sequence conflict3955 – 39562NN → SM in AC093879. Ref.5

Secondary structure

............................................................................... 3957
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 3 [UniParc].

Last modified May 16, 2012. Version 4.
Checksum: 41C1A240CC5A3B72

FASTA3,957433,715
        10         20         30         40         50         60 
MMNEDAAQKS DSGEKFNGSS QRRKRPKKSD SNASFLRAAR AGNLDKVVEY LKGGIDINTC 

        70         80         90        100        110        120 
NQNGLNALHL AAKEGHVGLV QELLGRGSSV DSATKKGNTA LHIASLAGQA EVVKVLVKEG 

       130        140        150        160        170        180 
ANINAQSQNG FTPLYMAAQE NHIDVVKYLL ENGANQSTAT EDGFTPLAVA LQQGHNQAVA 

       190        200        210        220        230        240 
ILLENDTKGK VRLPALHIAA RKDDTKSAAL LLQNDHNADV QSKMMVNRTT ESGFTPLHIA 

       250        260        270        280        290        300 
AHYGNVNVAT LLLNRGAAVD FTARNGITPL HVASKRGNTN MVKLLLDRGG QIDAKTRDGL 

       310        320        330        340        350        360 
TPLHCAARSG HDQVVELLLE RGAPLLARTK NGLSPLHMAA QGDHVECVKH LLQHKAPVDD 

       370        380        390        400        410        420 
VTLDYLTALH VAAHCGHYRV TKLLLDKRAN PNARALNGFT PLHIACKKNR IKVMELLVKY 

       430        440        450        460        470        480 
GASIQAITES GLTPIHVAAF MGHLNIVLLL LQNGASPDVT NIRGETALHM AARAGQVEVV 

       490        500        510        520        530        540 
RCLLRNGALV DARAREEQTP LHIASRLGKT EIVQLLLQHM AHPDAATTNG YTPLHISARE 

       550        560        570        580        590        600 
GQVDVASVLL EAGAAHSLAT KKGFTPLHVA AKYGSLDVAK LLLQRRAAAD SAGKNGLTPL 

       610        620        630        640        650        660 
HVAAHYDNQK VALLLLEKGA SPHATAKNGY TPLHIAAKKN QMQIASTLLN YGAETNIVTK 

       670        680        690        700        710        720 
QGVTPLHLAS QEGHTDMVTL LLDKGANIHM STKSGLTSLH LAAQEDKVNV ADILTKHGAD 

       730        740        750        760        770        780 
QDAHTKLGYT PLIVACHYGN VKMVNFLLKQ GANVNAKTKN GYTPLHQAAQ QGHTHIINVL 

       790        800        810        820        830        840 
LQHGAKPNAT TANGNTALAI AKRLGYISVV DTLKVVTEEV TTTTTTITEK HKLNVPETMT 

       850        860        870        880        890        900 
EVLDVSDEEG DDTMTGDGGE YLRPEDLKEL GDDSLPSSQF LDGMNYLRYS LEGGRSDSLR 

       910        920        930        940        950        960 
SFSSDRSHTL SHASYLRDSA VMDDSVVIPS HQVSTLAKEA ERNSYRLSWG TENLDNVALS 

       970        980        990       1000       1010       1020 
SSPIHSGFLV SFMVDARGGA MRGCRHNGLR IIIPPRKCTA PTRVTCRLVK RHRLATMPPM 

      1030       1040       1050       1060       1070       1080 
VEGEGLASRL IEVGPSGAQF LGKLHLPTAP PPLNEGESLV SRILQLGPPG TKFLGPVIVE 

      1090       1100       1110       1120       1130       1140 
IPHFAALRGK ERELVVLRSE NGDSWKEHFC DYTEDELNEI LNGMDEVLDS PEDLEKKRIC 

      1150       1160       1170       1180       1190       1200 
RIITRDFPQY FAVVSRIKQD SNLIGPEGGV LSSTVVPQVQ AVFPEGALTK RIRVGLQAQP 

      1210       1220       1230       1240       1250       1260 
MHSELVKKIL GNKATFSPIV TLEPRRRKFH KPITMTIPVP KASSDVMLNG FGGDAPTLRL 

      1270       1280       1290       1300       1310       1320 
LCSITGGTTP AQWEDITGTT PLTFVNECVS FTTNVSARFW LIDCRQIQES VTFASQVYRE 

      1330       1340       1350       1360       1370       1380 
IICVPYMAKF VVFAKSHDPI EARLRCFCMT DDKVDKTLEQ QENFAEVARS RDVEVLEGKP 

      1390       1400       1410       1420       1430       1440 
IYVDCFGNLV PLTKSGQHHI FSFFAFKENR LPLFVKVRDT TQEPCGRLSF MKEPKSTRGL 

      1450       1460       1470       1480       1490       1500 
VHQAICNLNI TLPIYTKESE SDQEQEEEID MTSEKNDETE STETSVLKSH LVNEVPVLAS 

      1510       1520       1530       1540       1550       1560 
PDLLSEVSEM KQDLIKMTAI LTTDVSDKAG SIKVKELVKA AEEEPGEPFE IVERVKEDLE 

      1570       1580       1590       1600       1610       1620 
KVNEILRSGT CTRDESSVQS SRSERGLVEE EWVIVSDEEI EEARQKAPLE ITEYPCVEVR 

      1630       1640       1650       1660       1670       1680 
IDKEIKGKVE KDSTGLVNYL TDDLNTCVPL PKEQLQTVQD KAGKKCEALA VGRSSEKEGK 

      1690       1700       1710       1720       1730       1740 
DIPPDETQST QKQHKPSLGI KKPVRRKLKE KQKQKEEGLQ ASAEKAELKK GSSEESLGED 

      1750       1760       1770       1780       1790       1800 
PGLAPEPLPT VKATSPLIEE TPIGSIKDKV KALQKRVEDE QKGRSKLPIR VKGKEDVPKK 

      1810       1820       1830       1840       1850       1860 
TTHRPHPAAS PSLKSERHAP GSPSPKTERH STLSSSAKTE RHPPVSPSSK TEKHSPVSPS 

      1870       1880       1890       1900       1910       1920 
AKTERHSPAS SSSKTEKHSP VSPSTKTERH SPVSSTKTER HPPVSPSGKT DKRPPVSPSG 

      1930       1940       1950       1960       1970       1980 
RTEKHPPVSP GRTEKRLPVS PSGRTDKHQP VSTAGKTEKH LPVSPSGKTE KQPPVSPTSK 

      1990       2000       2010       2020       2030       2040 
TERIEETMSV RELMKAFQSG QDPSKHKTGL FEHKSAKQKQ PQEKGKVRVE KEKGPILTQR 

      2050       2060       2070       2080       2090       2100 
EAQKTENQTI KRGQRLPVTG TAESKRGVRV SSIGVKKEDA AGGKEKVLSH KIPEPVQSVP 

      2110       2120       2130       2140       2150       2160 
EEESHRESEV PKEKMADEQG DMDLQISPDR KTSTDFSEVI KQELEDNDKY QQFRLSEETE 

      2170       2180       2190       2200       2210       2220 
KAQLHLDQVL TSPFNTTFPL DYMKDEFLPA LSLQSGALDG SSESLKNEGV AGSPCGSLME 

      2230       2240       2250       2260       2270       2280 
GTPQISSEES YKHEGLAETP ETSPESLSFS PKKSEEQTGE TKESTKTETT TEIRSEKEHP 

      2290       2300       2310       2320       2330       2340 
TTKDITGGSE ERGATVTEDS ETSTESFQKE ATLGSPKDTS PKRQDDCTGS CSVALAKETP 

      2350       2360       2370       2380       2390       2400 
TGLTEEAACD EGQRTFGSSA HKTQTDSEVQ ESTATSDETK ALPLPEASVK TDTGTESKPQ 

      2410       2420       2430       2440       2450       2460 
GVIRSPQGLE LALPSRDSEV LSAVADDSLA VSHKDSLEAS PVLEDNSSHK TPDSLEPSPL 

      2470       2480       2490       2500       2510       2520 
KESPCRDSLE SSPVEPKMKA GIFPSHFPLP AAVAKTELLT EVASVRSRLL RDPDGSAEDD 

      2530       2540       2550       2560       2570       2580 
SLEQTSLMES SGKSPLSPDT PSSEEVSYEV TPKTTDVSTP KPAVIHECAE EDDSENGEKK 

      2590       2600       2610       2620       2630       2640 
RFTPEEEMFK MVTKIKMFDE LEQEAKQKRD YKKEPKQEES SSSSDPDADC SVDVDEPKHT 

      2650       2660       2670       2680       2690       2700 
GSGEDESGVP VLVTSESRKV SSSSESEPEL AQLKKGADSG LLPEPVIRVQ PPSPLPSSMD 

      2710       2720       2730       2740       2750       2760 
SNSSPEEVQF QPVVSKQYTF KMNEDTQEEP GKSEEEKDSE SHLAEDRHAV STEAEDRSYD 

      2770       2780       2790       2800       2810       2820 
KLNRDTDQPK ICDGHGCEAM SPSSSAAPVS SGLQSPTGDD VDEQPVIYKE SLALQGTHEK 

      2830       2840       2850       2860       2870       2880 
DTEGEELDVS RAESPQADCP SESFSSSSSL PHCLVSEGKE LDEDISATSS IQKTEVTKTD 

      2890       2900       2910       2920       2930       2940 
ETFENLPKDC PSQDSSITTQ TDRFSMDVPV SDLAENDEIY DPQITSPYEN VPSQSFFSSE 

      2950       2960       2970       2980       2990       3000 
ESKTQTDANH TTSFHSSEVY SVTITSPVED VVVASSSSGT VLSKESNFEG QDIKMESQQE 

      3010       3020       3030       3040       3050       3060 
STLWEMQSDS VSSSFEPTMS ATTTVVGEQI SKVIITKTDV DSDSWSEIRE DDEAFEARVK 

      3070       3080       3090       3100       3110       3120 
EEEQKIFGLM VDRQSQGTTP DTTPARTPTE EGTPTSEQNP FLFQEGKLFE MTRSGAIDMT 

      3130       3140       3150       3160       3170       3180 
KRSYADESFH FFQIGQESRE ETLSEDVKEG ATGADPLPLE TSAESLALSE SKETVDDEAD 

      3190       3200       3210       3220       3230       3240 
LLPDDVSEEV EEIPASDAQL NSQMGISAST ETPTKEAVSV GTKDLPTVQT GDIPPLSGVK 

      3250       3260       3270       3280       3290       3300 
QISCPDSSEP AVQVQLDFST LTRSVYSDRG DDSPDSSPEE QKSVIEIPTA PMENVPFTES 

      3310       3320       3330       3340       3350       3360 
KSKIPVRTMP TSTPAPPSAE YESSVSEDFL SSVDEENKAD EAKPKSKLPV KVPLQRVEQQ 

      3370       3380       3390       3400       3410       3420 
LSDLDTSVQK TVAPQGQDMA SIAPDNRSKS ESDASSLDSK TKCPVKTRSY TETETESRER 

      3430       3440       3450       3460       3470       3480 
AEELELESEE GATRPKILTS RLPVKSRSTT SSCRGGTSPT KESKEHFFDL YRNSIEFFEE 

      3490       3500       3510       3520       3530       3540 
ISDEASKLVD RLTQSEREQE IVSDDESSSA LEVSVIENLP PVETEHSVPE DIFDTRPIWD 

      3550       3560       3570       3580       3590       3600 
ESIETLIERI PDENGHDHAE DPQDEQERIE ERLAYIADHL GFSWTELARE LDFTEEQIHQ 

      3610       3620       3630       3640       3650       3660 
IRIENPNSLQ DQSHALLKYW LERDGKHATD TNLVECLTKI NRMDIVHLME TNTEPLQERI 

      3670       3680       3690       3700       3710       3720 
SHSYAEIEQT ITLDHSEGFS VLQEELCTAQ HKQKEEQAVS KESETCDHPP IVSEEDISVG 

      3730       3740       3750       3760       3770       3780 
YSTFQDGVPK TEGDSSATAL FPQTHKEQVQ QDFSGKMQDL PEESSLEYQQ EYFVTTPGTE 

      3790       3800       3810       3820       3830       3840 
TSETQKAMIV PSSPSKTPEE VSTPAEEEKL YLQTPTSSER GGSPIIQEPE EPSEHREESS 

      3850       3860       3870       3880       3890       3900 
PRKTSLVIVE SADNQPETCE RLDEDAAFEK GDDMPEIPPE TVTEEEYIDE HGHTVVKKVT 

      3910       3920       3930       3940       3950 
RKIIRRYVSS EGTEKEEIMV QGMPQEPVNI EEGDGYSKVI KRVVLKSDTE QSEDNNE 

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Isoform 2 [UniParc].

Checksum: 425D5422CF5CE930
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FASTA1,872205,795
Isoform 4 [UniParc].

Checksum: 4E2B2DB97E1DDC0A
Show »

FASTA1,863204,752
Isoform 5 [UniParc].

Checksum: C0C03881D8E0EFD9
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FASTA55563,361

References

« Hide 'large scale' references
[1]"Isolation and characterization of cDNAs encoding human brain ankyrins reveal a family of alternatively spliced genes."
Otto E., Kunimoto M., McLaughlin T., Bennett V.
J. Cell Biol. 114:241-253(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 1477-2110 (ISOFORM 3), TISSUE SPECIFICITY.
Tissue: Brain stem.
[2]Carpenter S.
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"440-kD ankyrinB: structure of the major developmentally regulated domain and selective localization in unmyelinated axons."
Chan W., Kordeli E., Bennett V.
J. Cell Biol. 123:1463-1473(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Brain stem.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Retina.
[5]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
[7]"Isolation and chromosomal localization of a novel nonerythroid ankyrin gene."
Tse W.T., Menninger J.C., Yang-Feng T.L., Francke U., Sahr K.E., Lux S.E., Ward D.C., Forget B.G.
Genomics 10:858-866(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 463-495, TISSUE SPECIFICITY.
[8]"Ankyrin-B mutation causes type 4 long-QT cardiac arrhythmia and sudden cardiac death."
Mohler P.J., Schott J.-J., Gramolini A.O., Dilly K.W., Guatimosim S., duBell W.H., Song L.-S., Haurogne K., Kyndt F., Ali M.E., Rogers T.B., Lederer W.J., Escande D., Le Marec H., Bennett V.
Nature 421:634-639(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, VARIANT LQT4 GLY-1458.
[9]"Ankyrin-B targets beta2-spectrin to an intracellular compartment in neonatal cardiomyocytes."
Mohler P.J., Yoon W., Bennett V.
J. Biol. Chem. 279:40185-40193(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SPTBN1, MUTAGENESIS OF 975-ASP--ARG-977; ALA-1000 AND 1100-GLU--ASP-1103.
[10]"The ammonium transporter RhBG: requirement of a tyrosine-based signal and ankyrin-G for basolateral targeting and membrane anchorage in polarized kidney epithelial cells."
Lopez C., Metral S., Eladari D., Drevensek S., Gane P., Chambrey R., Bennett V., Cartron J.-P., Le Van Kim C., Colin Y.
J. Biol. Chem. 280:8221-8228(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RHBG.
[11]"Ankyrin-B is required for coordinated expression of beta-2-spectrin, the Na/K-ATPase and the Na/Ca exchanger in the inner segment of rod photoreceptors."
Kizhatil K., Sandhu N.K., Peachey N.S., Bennett V.
Exp. Eye Res. 88:57-64(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Structure of the ZU5-ZU5-UPA-DD tandem of ankyrin-B reveals interaction surfaces necessary for ankyrin function."
Wang C., Yu C., Ye F., Wei Z., Zhang M.
Proc. Natl. Acad. Sci. U.S.A. 109:4822-4827(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 966-3620, DOMAIN DEATH 1, DOMAIN UPA, DOMAINS ZU5.
[15]"A cardiac arrhythmia syndrome caused by loss of ankyrin-B function."
Mohler P.J., Splawski I., Napolitano C., Bottelli G., Sharpe L., Timothy K., Priori S.G., Keating M.T., Bennett V.
Proc. Natl. Acad. Sci. U.S.A. 101:9137-9142(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LQT4 GLY-1458; ILE-3740; ASN-3744; TRP-3906 AND LYS-3931, CHARACTERIZATION OF VARIANTS LQT4.
[16]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLU-685; ARG-1267 AND LYS-3653.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS37431.
RefSeqNP_001120965.1. NM_001127493.1.
NP_001139.3. NM_001148.4.
NP_066187.2. NM_020977.3.
UniGeneHs.620557.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4D8OX-ray2.20A966-3653[»]
DisProtDP00467.
ProteinModelPortalQ01484.
SMRQ01484. Positions 432-841, 3570-3647.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106784. 8 interactions.
DIPDIP-37425N.
IntActQ01484. 16 interactions.
STRING9606.ENSP00000349588.

Protein family/group databases

TCDB8.A.28.1.1. the ankyrin (ankyrin) family.

PTM databases

PhosphoSiteQ01484.

Polymorphism databases

DMDM387912917.

Proteomic databases

PaxDbQ01484.
PRIDEQ01484.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000357077; ENSP00000349588; ENSG00000145362. [Q01484-4]
ENST00000394537; ENSP00000378044; ENSG00000145362. [Q01484-2]
ENST00000506722; ENSP00000421067; ENSG00000145362. [Q01484-5]
ENST00000510275; ENSP00000421023; ENSG00000145362. [Q01484-7]
GeneID287.
KEGGhsa:287.
UCSCuc003ibd.4. human. [Q01484-5]
uc003ibe.4. human. [Q01484-4]
uc003ibf.4. human. [Q01484-2]
uc003ibh.4. human. [Q01484-7]

Organism-specific databases

CTD287.
GeneCardsGC04P113739.
H-InvDBHIX0164018.
HGNCHGNC:493. ANK2.
HPACAB015178.
HPA007570.
HPA008007.
HPA035970.
MIM106410. gene.
600919. phenotype.
neXtProtNX_Q01484.
Orphanet101016. Romano-Ward syndrome.
PharmGKBPA24799.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0666.
HOGENOMHOG000169277.
HOVERGENHBG100442.
KOK10380.
PhylomeDBQ01484.
TreeFamTF351263.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.

Gene expression databases

ArrayExpressQ01484.
BgeeQ01484.
CleanExHS_ANK2.
GenevestigatorQ01484.

Family and domain databases

Gene3D1.10.533.10. 1 hit.
1.25.40.20. 3 hits.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR000906. ZU5.
[Graphical view]
PfamPF00023. Ank. 19 hits.
PF12796. Ank_2. 1 hit.
PF00531. Death. 1 hit.
PF00791. ZU5. 2 hits.
[Graphical view]
PRINTSPR01415. ANKYRIN.
SMARTSM00248. ANK. 23 hits.
SM00005. DEATH. 1 hit.
[Graphical view]
SUPFAMSSF47986. SSF47986. 1 hit.
SSF48403. SSF48403. 3 hits.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 20 hits.
PS50017. DEATH_DOMAIN. 1 hit.
PS51145. ZU5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAnk2. human.
GenomeRNAi287.
NextBio1169.
PROQ01484.
SOURCESearch...

Entry information

Entry nameANK2_HUMAN
AccessionPrimary (citable) accession number: Q01484
Secondary accession number(s): Q01485 expand/collapse secondary AC list , Q08AC7, Q08AC8, Q7Z3L5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: May 16, 2012
Last modified: April 16, 2014
This is version 150 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM