Q01484 (ANK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ankyrin-2
Short name=ANK-2

Alternative name(s):
Ankyrin-B
Brain ankyrin
Non-erythroid ankyrin

Gene names

Name:

ANK2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	3957 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › cytoskeleton. Membrane. Cytoplasm › myofibril › sarcomere › M line By similarity. Apical cell membrane By similarity. Cell membrane. Cell junction › synapse › postsynaptic 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 component	Cell junction Cell membrane Cytoplasm Cytoskeleton Membrane Postsynaptic cell membrane Synapse
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Long QT syndrome
Domain	ANK repeat Repeat
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	T-tubule organization 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: Compara cellular calcium ion homeostasis Inferred from sequence or structural similarity. Source: BHF-UCL membrane depolarization involved in regulation of SA node cell action potential Traceable author statement PubMed 19098452. Source: BHF-UCL 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 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 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: Compara regulation of atrial cardiac muscle cell action potential Inferred from mutant phenotype PubMed 17242276PubMed 18832177PubMed 21859974. 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 by cardiac conduction Inferred from mutant phenotype Ref.8Ref.15PubMed 17242276PubMed 21859974. Source: BHF-UCL regulation of ventricular cardiac muscle cell action potential Inferred from mutant phenotype PubMed 17242276. Source: BHF-UCL regulation of ventricular cardiac muscle cell membrane repolarization Inferred from mutant phenotype PubMed 18832177. Source: BHF-UCL sarcoplasmic reticulum calcium ion transport Traceable author statement PubMed 19098452. Source: BHF-UCL
Cellular_component	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 to plasma membrane Inferred from electronic annotation. Source: Compara intercalated disc Inferred from sequence or structural similarity. Source: BHF-UCL perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATPase binding Inferred from sequence or structural similarity. Source: BHF-UCL ion channel binding Inferred from sequence or structural similarity. Source: BHF-UCL potassium channel regulator activity Inferred from electronic annotation. Source: Compara protein binding, bridging Inferred from sequence or structural similarity. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DMD	P11532-5	2	EBI-941975,EBI-1018651
GRB2	P62993	2	EBI-941975,EBI-401755

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 3957

3957

Ankyrin-2

PRO_0000066885

Regions

Repeat

30 – 62

33

ANK 1

Repeat

63 – 92

30

ANK 2

Repeat

96 – 125

30

ANK 3

Repeat

129 – 158

30

ANK 4

Repeat

162 – 191

30

ANK 5

Repeat

193 – 220

28

ANK 6

Repeat

232 – 261

30

ANK 7

Repeat

265 – 294

30

ANK 8

Repeat

298 – 327

30

ANK 9

Repeat

331 – 360

30

ANK 10

Repeat

364 – 393

30

ANK 11

Repeat

397 – 426

30

ANK 12

Repeat

430 – 459

30

ANK 13

Repeat

463 – 492

30

ANK 14

Repeat

496 – 525

30

ANK 15

Repeat

529 – 558

30

ANK 16

Repeat

562 – 591

30

ANK 17

Repeat

595 – 624

30

ANK 18

Repeat

628 – 657

30

ANK 19

Repeat

661 – 690

30

ANK 20

Repeat

694 – 723

30

ANK 21

Repeat

727 – 756

30

ANK 22

Repeat

760 – 789

30

ANK 23

Repeat

793 – 822

30

ANK 24

Domain

966 – 1124

159

ZU5 1

Domain

1125 – 1288

164

ZU5 2

Domain

1450 – 1535

86

Death 1

Repeat

1806 – 1817

12

Repeat A

Repeat

1818 – 1829

12

Repeat A

Repeat

1830 – 1841

12

Repeat A

Repeat

1842 – 1853

12

Repeat A

Repeat

1854 – 1865

12

Repeat A

Repeat

1866 – 1877

12

Repeat A

Repeat

1878 – 1889

12

Repeat A

Repeat

1890 – 1900

11

Repeat A; approximate

Repeat

1901 – 1912

12

Repeat A

Repeat

1913 – 1924

12

Repeat A

Repeat

1925 – 1935

11

Repeat A; approximate

Repeat

1936 – 1947

12

Repeat A

Repeat

1948 – 1959

12

Repeat A

Repeat

1960 – 1971

12

Repeat A

Repeat

1972 – 1983

12

Repeat A

Domain

3569 – 3653

85

Death 2

Region

966 – 1125

160

Interaction with SPTBN1

Region

1289 – 1423

135

UPA domain

Region

1806 – 1983

178

Repeat-rich region

Amino acid modifications

Modified residue

31

1

Phosphoserine By similarity

Modified residue

34

1

Phosphoserine By similarity

Modified residue

378

1

Phosphotyrosine By similarity

Modified residue

531

1

Phosphotyrosine By similarity

Modified residue

846

1

Phosphoserine By similarity

Modified residue

898

1

Phosphoserine By similarity

Modified residue

1382

1

Phosphotyrosine By similarity

Modified residue

1461

1

Phosphoserine By similarity

Modified residue

3093

1

Phosphothreonine By similarity

Modified residue

3273

1

Phosphoserine By similarity

Modified residue

3362

1

Phosphoserine By similarity

Modified residue

3390

1

Phosphoserine By similarity

Modified residue

3409

1

Phosphoserine By similarity

Modified residue

3410

1

Phosphotyrosine By similarity

Modified residue

3735

1

Phosphoserine By similarity

Modified residue

3776

1

Phosphothreonine By similarity

Modified residue

3802

1

Phosphoserine By similarity

Modified residue

3803

1

Phosphothreonine By similarity

Modified residue

3823

1

Phosphoserine By similarity

Modified residue

3844

1

Phosphothreonine By similarity

Natural variations

Alternative sequence

1 – 1348

1348

Missing in isoform 5.

VSP_037057

Alternative sequence

1 – 27

27

MMNED…RKRPK → MTTMLQ in isoform 4.

VSP_037058

Alternative sequence

967

1

G → GRASPCLERDNSS in isoform 4.

VSP_037059

Alternative sequence

1477 – 3561

2085

Missing in isoform 2, isoform 4 and isoform 5.

VSP_000268

Alternative sequence

3870

1

K → KELTEELGELEASSDEEAMV TTRVVRRRVIIQ in isoform 5.

VSP_037060

Natural variant

685

1

G → E in a breast cancer sample; somatic mutation. Ref.16

VAR_035606

Natural variant

687

1

N → S.
Corresponds to variant rs29372 [ dbSNP | Ensembl ].

VAR_055504

Natural variant

1267

1

G → R in a colorectal cancer sample; somatic mutation. Ref.16

VAR_035607

Natural variant

1458

1

E → G in LQT4; loss of function. Ref.8 Ref.15

VAR_022934

Natural variant

2369

1

V → A.
Corresponds to variant rs28377576 [ dbSNP | Ensembl ].

VAR_055505

Natural variant

3653

1

T → K in a colorectal cancer sample; somatic mutation. Ref.16

VAR_035608

Natural variant

3740

1

L → I in LQT4; loss of function. Ref.15

VAR_022935

Natural variant

3744

1

T → N in LQT4; loss of function. Ref.15

VAR_022936

Natural variant

3906

1

R → W in LQT4; loss of function. Ref.15

VAR_022937

Natural variant

3931

1

E → K in LQT4; loss of function. Ref.15

VAR_022938

Experimental info

Mutagenesis

975 – 977

3

DAR → AAA: Prevents binding to SPTBN1. Ref.9

Mutagenesis

1000

1

A → P: Prevents binding to SPTBN1. Ref.9

Mutagenesis

1100 – 1103

4

ENGD → AAGA: Weak binding to SPTBN1. Ref.9

Sequence conflict

220

1

V → I in CAD97827. Ref.4

Sequence conflict

475 – 476

2

GQ → PE in AAA62828. Ref.7

Sequence conflict

2787

1

A → R in CAB42644. Ref.3

Sequence conflict

2999

1

Q → L in CAB42644. Ref.3

Sequence conflict

3140 – 3141

2

EE → RY in AC093879. Ref.5

Sequence conflict

3185

1

D → S in CAB42644. Ref.3

Sequence conflict

3699

1

V → A in CAD97827. Ref.4

Sequence conflict

3737

1

A → S in CAA40279. Ref.1

Sequence conflict

3737

1

A → S in CAB42644. Ref.3

Sequence conflict

3955 – 3956

2

NN → SM in AC093879. Ref.5

Secondary structure

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3957

Helix Strand Turn

Details...

Beta strand

969 – 974

6

Beta strand

979 – 982

4

Beta strand

984 – 986

3

Beta strand

990 – 993

4

Beta strand

1002 – 1009

8

Beta strand

1025 – 1028

4

Beta strand

1031 – 1035

5

Beta strand

1073 – 1082

10

Turn

1088 – 1091

4

Beta strand

1092 – 1103

12

Helix

1131 – 1137

7

Beta strand

1139 – 1146

8

Beta strand

1149 – 1157

9

Beta strand

1159 – 1165

7

Beta strand

1168 – 1172

5

Beta strand

1174 – 1176

3

Beta strand

1180 – 1183

4

Beta strand

1192 – 1199

8

Helix

1203 – 1210

8

Beta strand

1213 – 1216

4

Beta strand

1219 – 1226

8

Beta strand

1228 – 1238

11

Beta strand

1258 – 1263

6

Helix

1277 – 1279

3

Beta strand

1283 – 1285

3

Beta strand

1288 – 1295

8

Beta strand

1298 – 1305

8

Helix

1307 – 1309

3

Helix

1310 – 1321

12

Beta strand

1325 – 1335

11

Beta strand

1338 – 1349

12

Helix

1357 – 1359

3

Beta strand

1365 – 1369

5

Beta strand

1373 – 1376

4

Beta strand

1380 – 1391

12

Beta strand

1399 – 1402

4

Beta strand

1410 – 1418

9

Beta strand

1424 – 1432

9

Beta strand

1445 – 1451

7

Helix

3571 – 3580

10

Helix

3583 – 3590

8

Helix

3595 – 3604

10

Helix

3609 – 3624

16

Helix

3625 – 3627

3

Helix

3630 – 3639

10

Helix

3643 – 3646

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 3 [UniParc]. Last modified May 16, 2012. Version 4. Checksum: 41C1A240CC5A3B72	FASTA	3,957	433,715
	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
	Isoform 2 [UniParc]. Checksum: 425D5422CF5CE930	FASTA	1,872	205,795
	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 MTSEKNPQDE QERIEERLAY IADHLGFSWT 1510 1520 1530 1540 1550 1560 ELARELDFTE EQIHQIRIEN PNSLQDQSHA LLKYWLERDG KHATDTNLVE CLTKINRMDI 1570 1580 1590 1600 1610 1620 VHLMETNTEP LQERISHSYA EIEQTITLDH SEGFSVLQEE LCTAQHKQKE EQAVSKESET 1630 1640 1650 1660 1670 1680 CDHPPIVSEE DISVGYSTFQ DGVPKTEGDS SATALFPQTH KEQVQQDFSG KMQDLPEESS 1690 1700 1710 1720 1730 1740 LEYQQEYFVT TPGTETSETQ KAMIVPSSPS KTPEEVSTPA EEEKLYLQTP TSSERGGSPI 1750 1760 1770 1780 1790 1800 IQEPEEPSEH REESSPRKTS LVIVESADNQ PETCERLDED AAFEKGDDMP EIPPETVTEE 1810 1820 1830 1840 1850 1860 EYIDEHGHTV VKKVTRKIIR RYVSSEGTEK EEIMVQGMPQ EPVNIEEGDG YSKVIKRVVL 1870 KSDTEQSEDN NE
	Isoform 4 [UniParc]. Checksum: 4E2B2DB97E1DDC0A	FASTA	1,863	204,752
	10 20 30 40 50 60 MTTMLQKSDS NASFLRAARA GNLDKVVEYL KGGIDINTCN QNGLNALHLA AKEGHVGLVQ 70 80 90 100 110 120 ELLGRGSSVD SATKKGNTAL HIASLAGQAE VVKVLVKEGA NINAQSQNGF TPLYMAAQEN 130 140 150 160 170 180 HIDVVKYLLE NGANQSTATE DGFTPLAVAL QQGHNQAVAI LLENDTKGKV RLPALHIAAR 190 200 210 220 230 240 KDDTKSAALL LQNDHNADVQ SKMMVNRTTE SGFTPLHIAA HYGNVNVATL LLNRGAAVDF 250 260 270 280 290 300 TARNGITPLH VASKRGNTNM VKLLLDRGGQ IDAKTRDGLT PLHCAARSGH DQVVELLLER 310 320 330 340 350 360 GAPLLARTKN GLSPLHMAAQ GDHVECVKHL LQHKAPVDDV TLDYLTALHV AAHCGHYRVT 370 380 390 400 410 420 KLLLDKRANP NARALNGFTP LHIACKKNRI KVMELLVKYG ASIQAITESG LTPIHVAAFM 430 440 450 460 470 480 GHLNIVLLLL QNGASPDVTN IRGETALHMA ARAGQVEVVR CLLRNGALVD ARAREEQTPL 490 500 510 520 530 540 HIASRLGKTE IVQLLLQHMA HPDAATTNGY TPLHISAREG QVDVASVLLE AGAAHSLATK 550 560 570 580 590 600 KGFTPLHVAA KYGSLDVAKL LLQRRAAADS AGKNGLTPLH VAAHYDNQKV ALLLLEKGAS 610 620 630 640 650 660 PHATAKNGYT PLHIAAKKNQ MQIASTLLNY GAETNIVTKQ GVTPLHLASQ EGHTDMVTLL 670 680 690 700 710 720 LDKGANIHMS TKSGLTSLHL AAQEDKVNVA DILTKHGADQ DAHTKLGYTP LIVACHYGNV 730 740 750 760 770 780 KMVNFLLKQG ANVNAKTKNG YTPLHQAAQQ GHTHIINVLL QHGAKPNATT ANGNTALAIA 790 800 810 820 830 840 KRLGYISVVD TLKVVTEEVT TTTTTITEKH KLNVPETMTE VLDVSDEEGD DTMTGDGGEY 850 860 870 880 890 900 LRPEDLKELG DDSLPSSQFL DGMNYLRYSL EGGRSDSLRS FSSDRSHTLS HASYLRDSAV 910 920 930 940 950 960 MDDSVVIPSH QVSTLAKEAE RNSYRLSWGT ENLDNVALSS SPIHSGRASP CLERDNSSFL 970 980 990 1000 1010 1020 VSFMVDARGG AMRGCRHNGL RIIIPPRKCT APTRVTCRLV KRHRLATMPP MVEGEGLASR 1030 1040 1050 1060 1070 1080 LIEVGPSGAQ FLGKLHLPTA PPPLNEGESL VSRILQLGPP GTKFLGPVIV EIPHFAALRG 1090 1100 1110 1120 1130 1140 KERELVVLRS ENGDSWKEHF CDYTEDELNE ILNGMDEVLD SPEDLEKKRI CRIITRDFPQ 1150 1160 1170 1180 1190 1200 YFAVVSRIKQ DSNLIGPEGG VLSSTVVPQV QAVFPEGALT KRIRVGLQAQ PMHSELVKKI 1210 1220 1230 1240 1250 1260 LGNKATFSPI VTLEPRRRKF HKPITMTIPV PKASSDVMLN GFGGDAPTLR LLCSITGGTT 1270 1280 1290 1300 1310 1320 PAQWEDITGT TPLTFVNECV SFTTNVSARF WLIDCRQIQE SVTFASQVYR EIICVPYMAK 1330 1340 1350 1360 1370 1380 FVVFAKSHDP IEARLRCFCM TDDKVDKTLE QQENFAEVAR SRDVEVLEGK PIYVDCFGNL 1390 1400 1410 1420 1430 1440 VPLTKSGQHH IFSFFAFKEN RLPLFVKVRD TTQEPCGRLS FMKEPKSTRG LVHQAICNLN 1450 1460 1470 1480 1490 1500 ITLPIYTKES ESDQEQEEEI DMTSEKNPQD EQERIEERLA YIADHLGFSW TELARELDFT 1510 1520 1530 1540 1550 1560 EEQIHQIRIE NPNSLQDQSH ALLKYWLERD GKHATDTNLV ECLTKINRMD IVHLMETNTE 1570 1580 1590 1600 1610 1620 PLQERISHSY AEIEQTITLD HSEGFSVLQE ELCTAQHKQK EEQAVSKESE TCDHPPIVSE 1630 1640 1650 1660 1670 1680 EDISVGYSTF QDGVPKTEGD SSATALFPQT HKEQVQQDFS GKMQDLPEES SLEYQQEYFV 1690 1700 1710 1720 1730 1740 TTPGTETSET QKAMIVPSSP SKTPEEVSTP AEEEKLYLQT PTSSERGGSP IIQEPEEPSE 1750 1760 1770 1780 1790 1800 HREESSPRKT SLVIVESADN QPETCERLDE DAAFEKGDDM PEIPPETVTE EEYIDEHGHT 1810 1820 1830 1840 1850 1860 VVKKVTRKII RRYVSSEGTE KEEIMVQGMP QEPVNIEEGD GYSKVIKRVV LKSDTEQSED NNE
	Isoform 5 [UniParc]. Checksum: C0C03881D8E0EFD9	FASTA	555	63,361
	10 20 30 40 50 60 MTDDKVDKTL EQQENFAEVA RSRDVEVLEG KPIYVDCFGN LVPLTKSGQH HIFSFFAFKE 70 80 90 100 110 120 NRLPLFVKVR DTTQEPCGRL SFMKEPKSTR GLVHQAICNL NITLPIYTKE SESDQEQEEE 130 140 150 160 170 180 IDMTSEKNPQ DEQERIEERL AYIADHLGFS WTELARELDF TEEQIHQIRI ENPNSLQDQS 190 200 210 220 230 240 HALLKYWLER DGKHATDTNL VECLTKINRM DIVHLMETNT EPLQERISHS YAEIEQTITL 250 260 270 280 290 300 DHSEGFSVLQ EELCTAQHKQ KEEQAVSKES ETCDHPPIVS EEDISVGYST FQDGVPKTEG 310 320 330 340 350 360 DSSATALFPQ THKEQVQQDF SGKMQDLPEE SSLEYQQEYF VTTPGTETSE TQKAMIVPSS 370 380 390 400 410 420 PSKTPEEVST PAEEEKLYLQ TPTSSERGGS PIIQEPEEPS EHREESSPRK TSLVIVESAD 430 440 450 460 470 480 NQPETCERLD EDAAFEKELT EELGELEASS DEEAMVTTRV VRRRVIIQGD DMPEIPPETV 490 500 510 520 530 540 TEEEYIDEHG HTVVKKVTRK IIRRYVSSEG TEKEEIMVQG MPQEPVNIEE GDGYSKVIKR 550 VVLKSDTEQS EDNNE

References

	« Hide 'large scale' referencesShow '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. , 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, DEATH DOMAIN 1, UPA DOMAIN, ZU5 DOMAINS.
[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. , 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

GeneReviews

Wikipedia

Ankyrin entry

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.

IPI

IPI00007834.
IPI00074962.
IPI00305279.
IPI00384928.
IPI00895856.

PIR

S37431.

RefSeq

NP_001120965.1. NM_001127493.1.
NP_001139.3. NM_001148.4.
NP_066187.2. NM_020977.3.

UniGene

Hs.620557.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4D8O	X-ray	2.20	A	966-3653	[»]

DisProt

DP00467.

ProteinModelPortal

Q01484.

SMR

Q01484. Positions 432-841, 3570-3647.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-37425N.

IntAct

Q01484. 16 interactions.

MINT

MINT-254984.

STRING

9606.ENSP00000349588.

Protein family/group databases

TCDB

8.A.28.1.1. ankyrin family.

PTM databases

PhosphoSite

Q01484.

Polymorphism databases

DMDM

215274185.

Proteomic databases

PaxDb

Q01484.

PRIDE

Q01484.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000357077; ENSP00000349588; ENSG00000145362.
ENST00000394537; ENSP00000378044; ENSG00000145362.
ENST00000506722; ENSP00000421067; ENSG00000145362.
ENST00000510275; ENSP00000421023; ENSG00000145362.

GeneID

287.

KEGG

hsa:287.

UCSC

uc003ibd.4. human.
uc003ibe.4. human.
uc003ibf.4. human.
uc003ibh.4. human.

Organism-specific databases

CTD

287.

GeneCards

GC04P113739.

H-InvDB

HIX0164018.

HGNC

HGNC:493. ANK2.

MIM

106410. gene.
600919. phenotype.

neXtProt

NX_Q01484.

Orphanet

101016. Romano-Ward syndrome.

PharmGKB

PA24799.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0666.

HOGENOM

HOG000169277.

HOVERGEN

HBG100442.

KO

K10380.

PhylomeDB

Q01484.

Enzyme and pathway databases

Reactome

REACT_111045. Developmental Biology.

Gene expression databases

ArrayExpress

Q01484.

Bgee

Q01484.

CleanEx

HS_ANK2.

Genevestigator

Q01484.

GermOnline

ENSG00000145362. Homo sapiens.

Family and domain databases

Gene3D

1.10.533.10. 1 hit.
1.25.40.20. 3 hits.

InterPro

IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR000906. ZU5.
[Graphical view]

Pfam

PF00023. Ank. 3 hits.
PF12796. Ank_2. 7 hits.
PF00531. Death. 1 hit.
PF00791. ZU5. 2 hits.
[Graphical view]

PRINTS

PR01415. ANKYRIN.

SMART

SM00248. ANK. 23 hits.
SM00005. DEATH. 1 hit.
[Graphical view]

SUPFAM

SSF48403. ANK. 2 hits.
SSF47986. DEATH_like. 1 hit.

PROSITE

PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 20 hits.
PS50017. DEATH_DOMAIN. 1 hit.
PS51145. ZU5. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

Ank2. human.

GenomeRNAi

287.

NextBio

1169.

SOURCE

Search...

Entry information

Entry name

ANK2_HUMAN

Accession

Primary (citable) accession number: Q01484
Secondary accession number(s): Q01485 , Q08AC7, Q08AC8, Q7Z3L5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	May 16, 2012
Last modified:	May 1, 2013
This is version 140 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.