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Q01484

- ANK2_HUMAN

UniProt

Q01484 - ANK2_HUMAN

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Protein

Ankyrin-2

Gene
ANK2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

In skeletal muscle, required for proper localization of DMD and DCTN4 and for the formation and/or stability of a special subset of microtubules associated with costameres and neuromuscular junctions By similarity. Attaches integral membrane proteins to cytoskeletal elements. Also binds to cytoskeletal proteins. Required for coordinate assembly of Na/Ca exchanger, Na/K ATPase and InsP3 receptor at sarcoplasmic reticulum sites in cardiomyocytes. Required for the coordinated expression of the Na/K ATPase, Na/Ca exchanger and beta-2-spectrin (SPTBN1) in the inner segment of rod photoreceptors. Required for expression and targeting of SPTBN1 in neonatal cardiomyocytes and for the regulation of neonatal cardiomyocyte contraction rate.1 Publication

GO - Molecular functioni

  1. ATPase binding Source: BHF-UCL
  2. enzyme binding Source: UniProtKB
  3. ion channel binding Source: BHF-UCL
  4. potassium channel regulator activity Source: Ensembl
  5. protein binding Source: UniProtKB
  6. protein binding, bridging Source: BHF-UCL
  7. protein kinase binding Source: BHF-UCL
  8. spectrin binding Source: BHF-UCL
  9. structural constituent of cytoskeleton Source: Ensembl

GO - Biological processi

  1. atrial cardiac muscle cell action potential Source: BHF-UCL
  2. atrial cardiac muscle cell to AV node cell communication Source: BHF-UCL
  3. atrial septum development Source: BHF-UCL
  4. axon guidance Source: Reactome
  5. cardiac muscle contraction Source: Ensembl
  6. cellular calcium ion homeostasis Source: BHF-UCL
  7. cellular protein localization Source: BHF-UCL
  8. membrane depolarization during SA node cell action potential Source: BHF-UCL
  9. paranodal junction assembly Source: Ensembl
  10. positive regulation of calcium ion transmembrane transporter activity Source: BHF-UCL
  11. positive regulation of calcium ion transport Source: BHF-UCL
  12. positive regulation of cation channel activity Source: BHF-UCL
  13. positive regulation of gene expression Source: BHF-UCL
  14. positive regulation of potassium ion transmembrane transporter activity Source: BHF-UCL
  15. positive regulation of potassium ion transport Source: BHF-UCL
  16. protein localization to cell surface Source: BHF-UCL
  17. protein localization to endoplasmic reticulum Source: BHF-UCL
  18. protein localization to M-band Source: BHF-UCL
  19. protein localization to organelle Source: BHF-UCL
  20. protein localization to plasma membrane Source: BHF-UCL
  21. protein localization to T-tubule Source: BHF-UCL
  22. protein stabilization Source: BHF-UCL
  23. protein targeting to plasma membrane Source: Ensembl
  24. regulation of calcium ion transmembrane transporter activity Source: BHF-UCL
  25. regulation of calcium ion transport Source: BHF-UCL
  26. regulation of cardiac muscle cell contraction Source: BHF-UCL
  27. regulation of cardiac muscle cell membrane potential Source: Ensembl
  28. regulation of cardiac muscle contraction Source: BHF-UCL
  29. regulation of cardiac muscle contraction by calcium ion signaling Source: BHF-UCL
  30. regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: BHF-UCL
  31. regulation of heart rate Source: BHF-UCL
  32. regulation of heart rate by cardiac conduction Source: BHF-UCL
  33. regulation of protein stability Source: BHF-UCL
  34. regulation of release of sequestered calcium ion into cytosol Source: BHF-UCL
  35. regulation of ventricular cardiac muscle cell membrane repolarization Source: BHF-UCL
  36. response to methylmercury Source: Ensembl
  37. SA node cell action potential Source: BHF-UCL
  38. SA node cell to atrial cardiac muscle cell communication Source: BHF-UCL
  39. sarcoplasmic reticulum calcium ion transport Source: BHF-UCL
  40. T-tubule organization Source: BHF-UCL
  41. ventricular cardiac muscle cell action potential Source: BHF-UCL
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_22266. Interaction between L1 and Ankyrins.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Ankyrin-2
Short name:
ANK-2
Alternative name(s):
Ankyrin-B
Brain ankyrin
Non-erythroid ankyrin
Gene namesi
Name:ANK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:493. ANK2.

Subcellular locationi

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.1 Publication

GO - Cellular componenti

  1. A band Source: BHF-UCL
  2. apical plasma membrane Source: UniProtKB-SubCell
  3. basolateral plasma membrane Source: UniProtKB
  4. costamere Source: BHF-UCL
  5. cytoskeleton Source: UniProtKB-SubCell
  6. cytosol Source: Reactome
  7. integral component of plasma membrane Source: Ensembl
  8. intercalated disc Source: BHF-UCL
  9. intracellular Source: BHF-UCL
  10. M band Source: BHF-UCL
  11. membrane raft Source: Ensembl
  12. neuron projection Source: Ensembl
  13. perinuclear region of cytoplasm Source: Ensembl
  14. plasma membrane Source: BHF-UCL
  15. postsynaptic membrane Source: UniProtKB-SubCell
  16. sarcolemma Source: BHF-UCL
  17. T-tubule Source: BHF-UCL
  18. Z disc Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

Long QT syndrome 4 (LQT4) [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.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1458 – 14581E → G in LQT4; loss of function. 2 Publications
Corresponds to variant rs72544141 [ dbSNP | Ensembl ].
VAR_022934
Natural varianti3740 – 37401L → I in LQT4; loss of function. 1 Publication
Corresponds to variant rs35530544 [ dbSNP | Ensembl ].
VAR_022935
Natural varianti3744 – 37441T → N in LQT4; loss of function. 1 Publication
VAR_022936
Natural varianti3906 – 39061R → W in LQT4; loss of function. 1 Publication
Corresponds to variant rs121912706 [ dbSNP | Ensembl ].
VAR_022937
Natural varianti3931 – 39311E → K in LQT4; loss of function. 1 Publication
Corresponds to variant rs45454496 [ dbSNP | Ensembl ].
VAR_022938

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi975 – 9773DAR → AAA: Prevents binding to SPTBN1. 1 Publication
Mutagenesisi1000 – 10001A → P: Prevents binding to SPTBN1. 1 Publication
Mutagenesisi1100 – 11034ENGD → AAGA: Weak binding to SPTBN1. 1 Publication

Keywords - Diseasei

Disease mutation, Long QT syndrome

Organism-specific databases

MIMi600919. phenotype.
Orphaneti101016. Romano-Ward syndrome.
PharmGKBiPA24799.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 39573957Ankyrin-2PRO_0000066885Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei378 – 3781Phosphotyrosine By similarity
Modified residuei531 – 5311Phosphotyrosine By similarity
Modified residuei1382 – 13821Phosphotyrosine By similarity
Modified residuei3776 – 37761Phosphothreonine By similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ01484.
PaxDbiQ01484.
PRIDEiQ01484.

PTM databases

PhosphoSiteiQ01484.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiQ01484.
BgeeiQ01484.
CleanExiHS_ANK2.
GenevestigatoriQ01484.

Organism-specific databases

HPAiCAB015178.
HPA007570.
HPA008007.
HPA035970.

Interactioni

Subunit structurei

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 SPTBN1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DMDP11532-52EBI-941975,EBI-1018651
GRB2P629932EBI-941975,EBI-401755

Protein-protein interaction databases

BioGridi106784. 8 interactions.
DIPiDIP-37425N.
IntActiQ01484. 16 interactions.
STRINGi9606.ENSP00000349588.

Structurei

Secondary structure

1
3957
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi969 – 9746
Beta strandi979 – 9824
Beta strandi984 – 9863
Beta strandi990 – 9934
Beta strandi1002 – 10098
Beta strandi1025 – 10284
Beta strandi1031 – 10355
Beta strandi1039 – 10424
Beta strandi1076 – 10827
Turni1088 – 10914
Beta strandi1092 – 110312
Helixi1131 – 11377
Beta strandi1139 – 11468
Beta strandi1149 – 11579
Beta strandi1159 – 11657
Beta strandi1168 – 11725
Beta strandi1174 – 11763
Beta strandi1180 – 11834
Beta strandi1192 – 11998
Helixi1203 – 12108
Beta strandi1213 – 12164
Beta strandi1219 – 12268
Beta strandi1228 – 123811
Beta strandi1258 – 12636
Helixi1277 – 12793
Beta strandi1283 – 12853
Beta strandi1288 – 12958
Beta strandi1298 – 13058
Helixi1307 – 13093
Helixi1310 – 132112
Beta strandi1325 – 133511
Beta strandi1338 – 134912
Helixi1357 – 13593
Beta strandi1365 – 13695
Beta strandi1373 – 13764
Beta strandi1380 – 139112
Beta strandi1399 – 14024
Beta strandi1410 – 14189
Beta strandi1424 – 14329
Beta strandi1445 – 14517

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4D8OX-ray2.20A966-1476[»]
DisProtiDP00467.
ProteinModelPortaliQ01484.
SMRiQ01484. Positions 432-841, 3570-3647.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati30 – 6233ANK 1Add
BLAST
Repeati63 – 9230ANK 2Add
BLAST
Repeati96 – 12530ANK 3Add
BLAST
Repeati129 – 15830ANK 4Add
BLAST
Repeati162 – 19130ANK 5Add
BLAST
Repeati193 – 22028ANK 6Add
BLAST
Repeati232 – 26130ANK 7Add
BLAST
Repeati265 – 29430ANK 8Add
BLAST
Repeati298 – 32730ANK 9Add
BLAST
Repeati331 – 36030ANK 10Add
BLAST
Repeati364 – 39330ANK 11Add
BLAST
Repeati397 – 42630ANK 12Add
BLAST
Repeati430 – 45930ANK 13Add
BLAST
Repeati463 – 49230ANK 14Add
BLAST
Repeati496 – 52530ANK 15Add
BLAST
Repeati529 – 55830ANK 16Add
BLAST
Repeati562 – 59130ANK 17Add
BLAST
Repeati595 – 62430ANK 18Add
BLAST
Repeati628 – 65730ANK 19Add
BLAST
Repeati661 – 69030ANK 20Add
BLAST
Repeati694 – 72330ANK 21Add
BLAST
Repeati727 – 75630ANK 22Add
BLAST
Repeati760 – 78930ANK 23Add
BLAST
Repeati793 – 82230ANK 24Add
BLAST
Domaini966 – 1124159ZU5 1Add
BLAST
Domaini1125 – 1288164ZU5 2Add
BLAST
Domaini1450 – 153586Death 1Add
BLAST
Repeati1806 – 181712Repeat AAdd
BLAST
Repeati1818 – 182912Repeat AAdd
BLAST
Repeati1830 – 184112Repeat AAdd
BLAST
Repeati1842 – 185312Repeat AAdd
BLAST
Repeati1854 – 186512Repeat AAdd
BLAST
Repeati1866 – 187712Repeat AAdd
BLAST
Repeati1878 – 188912Repeat AAdd
BLAST
Repeati1890 – 190011Repeat A; approximateAdd
BLAST
Repeati1901 – 191212Repeat AAdd
BLAST
Repeati1913 – 192412Repeat AAdd
BLAST
Repeati1925 – 193511Repeat A; approximateAdd
BLAST
Repeati1936 – 194712Repeat AAdd
BLAST
Repeati1948 – 195912Repeat AAdd
BLAST
Repeati1960 – 197112Repeat AAdd
BLAST
Repeati1972 – 198312Repeat AAdd
BLAST
Domaini3569 – 365385Death 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni966 – 1125160Interaction with SPTBN1Add
BLAST
Regioni1289 – 1423135UPA domainAdd
BLAST
Regioni1806 – 1983178Repeat-rich regionAdd
BLAST

Domaini

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

Sequence similaritiesi

Contains 24 ANK repeats.
Contains 2 death domains.
Contains 2 ZU5 domains.

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiCOG0666.
HOGENOMiHOG000169277.
HOVERGENiHBG100442.
KOiK10380.
OMAiYLIMASS.
PhylomeDBiQ01484.
TreeFamiTF351263.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
1.25.40.20. 3 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR000906. ZU5.
[Graphical view]
PfamiPF00023. Ank. 19 hits.
PF12796. Ank_2. 1 hit.
PF00531. Death. 1 hit.
PF00791. ZU5. 2 hits.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 23 hits.
SM00005. DEATH. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF48403. SSF48403. 3 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 20 hits.
PS50017. DEATH_DOMAIN. 1 hit.
PS51145. ZU5. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

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

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

« Hide

MMNEDAAQKS DSGEKFNGSS QRRKRPKKSD SNASFLRAAR AGNLDKVVEY     50
LKGGIDINTC NQNGLNALHL AAKEGHVGLV QELLGRGSSV DSATKKGNTA 100
LHIASLAGQA EVVKVLVKEG ANINAQSQNG FTPLYMAAQE NHIDVVKYLL 150
ENGANQSTAT EDGFTPLAVA LQQGHNQAVA ILLENDTKGK VRLPALHIAA 200
RKDDTKSAAL LLQNDHNADV QSKMMVNRTT ESGFTPLHIA AHYGNVNVAT 250
LLLNRGAAVD FTARNGITPL HVASKRGNTN MVKLLLDRGG QIDAKTRDGL 300
TPLHCAARSG HDQVVELLLE RGAPLLARTK NGLSPLHMAA QGDHVECVKH 350
LLQHKAPVDD VTLDYLTALH VAAHCGHYRV TKLLLDKRAN PNARALNGFT 400
PLHIACKKNR IKVMELLVKY GASIQAITES GLTPIHVAAF MGHLNIVLLL 450
LQNGASPDVT NIRGETALHM AARAGQVEVV RCLLRNGALV DARAREEQTP 500
LHIASRLGKT EIVQLLLQHM AHPDAATTNG YTPLHISARE GQVDVASVLL 550
EAGAAHSLAT KKGFTPLHVA AKYGSLDVAK LLLQRRAAAD SAGKNGLTPL 600
HVAAHYDNQK VALLLLEKGA SPHATAKNGY TPLHIAAKKN QMQIASTLLN 650
YGAETNIVTK QGVTPLHLAS QEGHTDMVTL LLDKGANIHM STKSGLTSLH 700
LAAQEDKVNV ADILTKHGAD QDAHTKLGYT PLIVACHYGN VKMVNFLLKQ 750
GANVNAKTKN GYTPLHQAAQ QGHTHIINVL LQHGAKPNAT TANGNTALAI 800
AKRLGYISVV DTLKVVTEEV TTTTTTITEK HKLNVPETMT EVLDVSDEEG 850
DDTMTGDGGE YLRPEDLKEL GDDSLPSSQF LDGMNYLRYS LEGGRSDSLR 900
SFSSDRSHTL SHASYLRDSA VMDDSVVIPS HQVSTLAKEA ERNSYRLSWG 950
TENLDNVALS SSPIHSGFLV SFMVDARGGA MRGCRHNGLR IIIPPRKCTA 1000
PTRVTCRLVK RHRLATMPPM VEGEGLASRL IEVGPSGAQF LGKLHLPTAP 1050
PPLNEGESLV SRILQLGPPG TKFLGPVIVE IPHFAALRGK ERELVVLRSE 1100
NGDSWKEHFC DYTEDELNEI LNGMDEVLDS PEDLEKKRIC RIITRDFPQY 1150
FAVVSRIKQD SNLIGPEGGV LSSTVVPQVQ AVFPEGALTK RIRVGLQAQP 1200
MHSELVKKIL GNKATFSPIV TLEPRRRKFH KPITMTIPVP KASSDVMLNG 1250
FGGDAPTLRL LCSITGGTTP AQWEDITGTT PLTFVNECVS FTTNVSARFW 1300
LIDCRQIQES VTFASQVYRE IICVPYMAKF VVFAKSHDPI EARLRCFCMT 1350
DDKVDKTLEQ QENFAEVARS RDVEVLEGKP IYVDCFGNLV PLTKSGQHHI 1400
FSFFAFKENR LPLFVKVRDT TQEPCGRLSF MKEPKSTRGL VHQAICNLNI 1450
TLPIYTKESE SDQEQEEEID MTSEKNDETE STETSVLKSH LVNEVPVLAS 1500
PDLLSEVSEM KQDLIKMTAI LTTDVSDKAG SIKVKELVKA AEEEPGEPFE 1550
IVERVKEDLE KVNEILRSGT CTRDESSVQS SRSERGLVEE EWVIVSDEEI 1600
EEARQKAPLE ITEYPCVEVR IDKEIKGKVE KDSTGLVNYL TDDLNTCVPL 1650
PKEQLQTVQD KAGKKCEALA VGRSSEKEGK DIPPDETQST QKQHKPSLGI 1700
KKPVRRKLKE KQKQKEEGLQ ASAEKAELKK GSSEESLGED PGLAPEPLPT 1750
VKATSPLIEE TPIGSIKDKV KALQKRVEDE QKGRSKLPIR VKGKEDVPKK 1800
TTHRPHPAAS PSLKSERHAP GSPSPKTERH STLSSSAKTE RHPPVSPSSK 1850
TEKHSPVSPS AKTERHSPAS SSSKTEKHSP VSPSTKTERH SPVSSTKTER 1900
HPPVSPSGKT DKRPPVSPSG RTEKHPPVSP GRTEKRLPVS PSGRTDKHQP 1950
VSTAGKTEKH LPVSPSGKTE KQPPVSPTSK TERIEETMSV RELMKAFQSG 2000
QDPSKHKTGL FEHKSAKQKQ PQEKGKVRVE KEKGPILTQR EAQKTENQTI 2050
KRGQRLPVTG TAESKRGVRV SSIGVKKEDA AGGKEKVLSH KIPEPVQSVP 2100
EEESHRESEV PKEKMADEQG DMDLQISPDR KTSTDFSEVI KQELEDNDKY 2150
QQFRLSEETE KAQLHLDQVL TSPFNTTFPL DYMKDEFLPA LSLQSGALDG 2200
SSESLKNEGV AGSPCGSLME GTPQISSEES YKHEGLAETP ETSPESLSFS 2250
PKKSEEQTGE TKESTKTETT TEIRSEKEHP TTKDITGGSE ERGATVTEDS 2300
ETSTESFQKE ATLGSPKDTS PKRQDDCTGS CSVALAKETP TGLTEEAACD 2350
EGQRTFGSSA HKTQTDSEVQ ESTATSDETK ALPLPEASVK TDTGTESKPQ 2400
GVIRSPQGLE LALPSRDSEV LSAVADDSLA VSHKDSLEAS PVLEDNSSHK 2450
TPDSLEPSPL KESPCRDSLE SSPVEPKMKA GIFPSHFPLP AAVAKTELLT 2500
EVASVRSRLL RDPDGSAEDD SLEQTSLMES SGKSPLSPDT PSSEEVSYEV 2550
TPKTTDVSTP KPAVIHECAE EDDSENGEKK RFTPEEEMFK MVTKIKMFDE 2600
LEQEAKQKRD YKKEPKQEES SSSSDPDADC SVDVDEPKHT GSGEDESGVP 2650
VLVTSESRKV SSSSESEPEL AQLKKGADSG LLPEPVIRVQ PPSPLPSSMD 2700
SNSSPEEVQF QPVVSKQYTF KMNEDTQEEP GKSEEEKDSE SHLAEDRHAV 2750
STEAEDRSYD KLNRDTDQPK ICDGHGCEAM SPSSSAAPVS SGLQSPTGDD 2800
VDEQPVIYKE SLALQGTHEK DTEGEELDVS RAESPQADCP SESFSSSSSL 2850
PHCLVSEGKE LDEDISATSS IQKTEVTKTD ETFENLPKDC PSQDSSITTQ 2900
TDRFSMDVPV SDLAENDEIY DPQITSPYEN VPSQSFFSSE ESKTQTDANH 2950
TTSFHSSEVY SVTITSPVED VVVASSSSGT VLSKESNFEG QDIKMESQQE 3000
STLWEMQSDS VSSSFEPTMS ATTTVVGEQI SKVIITKTDV DSDSWSEIRE 3050
DDEAFEARVK EEEQKIFGLM VDRQSQGTTP DTTPARTPTE EGTPTSEQNP 3100
FLFQEGKLFE MTRSGAIDMT KRSYADESFH FFQIGQESRE ETLSEDVKEG 3150
ATGADPLPLE TSAESLALSE SKETVDDEAD LLPDDVSEEV EEIPASDAQL 3200
NSQMGISAST ETPTKEAVSV GTKDLPTVQT GDIPPLSGVK QISCPDSSEP 3250
AVQVQLDFST LTRSVYSDRG DDSPDSSPEE QKSVIEIPTA PMENVPFTES 3300
KSKIPVRTMP TSTPAPPSAE YESSVSEDFL SSVDEENKAD EAKPKSKLPV 3350
KVPLQRVEQQ LSDLDTSVQK TVAPQGQDMA SIAPDNRSKS ESDASSLDSK 3400
TKCPVKTRSY TETETESRER AEELELESEE GATRPKILTS RLPVKSRSTT 3450
SSCRGGTSPT KESKEHFFDL YRNSIEFFEE ISDEASKLVD RLTQSEREQE 3500
IVSDDESSSA LEVSVIENLP PVETEHSVPE DIFDTRPIWD ESIETLIERI 3550
PDENGHDHAE DPQDEQERIE ERLAYIADHL GFSWTELARE LDFTEEQIHQ 3600
IRIENPNSLQ DQSHALLKYW LERDGKHATD TNLVECLTKI NRMDIVHLME 3650
TNTEPLQERI SHSYAEIEQT ITLDHSEGFS VLQEELCTAQ HKQKEEQAVS 3700
KESETCDHPP IVSEEDISVG YSTFQDGVPK TEGDSSATAL FPQTHKEQVQ 3750
QDFSGKMQDL PEESSLEYQQ EYFVTTPGTE TSETQKAMIV PSSPSKTPEE 3800
VSTPAEEEKL YLQTPTSSER GGSPIIQEPE EPSEHREESS PRKTSLVIVE 3850
SADNQPETCE RLDEDAAFEK GDDMPEIPPE TVTEEEYIDE HGHTVVKKVT 3900
RKIIRRYVSS EGTEKEEIMV QGMPQEPVNI EEGDGYSKVI KRVVLKSDTE 3950
QSEDNNE 3957
Length:3,957
Mass (Da):433,715
Last modified:May 16, 2012 - v4
Checksum:i41C1A240CC5A3B72
GO
Isoform 2 (identifier: Q01484-2) [UniParc]FASTAAdd to Basket

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

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

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

Note: No experimental confirmation available.

Show »
Length:1,863
Mass (Da):204,752
Checksum:i4E2B2DB97E1DDC0A
GO
Isoform 5 (identifier: Q01484-7) [UniParc]FASTAAdd to Basket

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

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

Sequence cautioni

The sequence CAB42644.1 differs from that shown. Reason: CDS lacks C-terminal region which is nevertheless present in the underlying cDNA.
The sequence AAI25237.1 differs from that shown. Reason: Frameshift at position 1405.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti685 – 6851G → E in a breast cancer sample; somatic mutation. 1 Publication
VAR_035606
Natural varianti687 – 6871N → S.
Corresponds to variant rs29372 [ dbSNP | Ensembl ].
VAR_055504
Natural varianti1267 – 12671G → R in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035607
Natural varianti1458 – 14581E → G in LQT4; loss of function. 2 Publications
Corresponds to variant rs72544141 [ dbSNP | Ensembl ].
VAR_022934
Natural varianti2369 – 23691V → A.
Corresponds to variant rs28377576 [ dbSNP | Ensembl ].
VAR_055505
Natural varianti3653 – 36531T → K in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035608
Natural varianti3740 – 37401L → I in LQT4; loss of function. 1 Publication
Corresponds to variant rs35530544 [ dbSNP | Ensembl ].
VAR_022935
Natural varianti3744 – 37441T → N in LQT4; loss of function. 1 Publication
VAR_022936
Natural varianti3906 – 39061R → W in LQT4; loss of function. 1 Publication
Corresponds to variant rs121912706 [ dbSNP | Ensembl ].
VAR_022937
Natural varianti3931 – 39311E → K in LQT4; loss of function. 1 Publication
Corresponds to variant rs45454496 [ dbSNP | Ensembl ].
VAR_022938

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 13481348Missing in isoform 5. VSP_037057Add
BLAST
Alternative sequencei1 – 2727MMNED…RKRPK → MTTMLQ in isoform 4. VSP_037058Add
BLAST
Alternative sequencei967 – 9671G → GRASPCLERDNSS in isoform 4. VSP_037059
Alternative sequencei1477 – 35612085Missing in isoform 2, isoform 4 and isoform 5. VSP_000268Add
BLAST
Alternative sequencei3870 – 38701K → KELTEELGELEASSDEEAMV TTRVVRRRVIIQ in isoform 5. VSP_037060

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti220 – 2201V → I in CAD97827. 1 Publication
Sequence conflicti475 – 4762GQ → PE in AAA62828. 1 Publication
Sequence conflicti2787 – 27871A → R in CAB42644. 1 Publication
Sequence conflicti2999 – 29991Q → L in CAB42644. 1 Publication
Sequence conflicti3140 – 31412EE → RY in AC093879. 1 Publication
Sequence conflicti3185 – 31851D → S in CAB42644. 1 Publication
Sequence conflicti3699 – 36991V → A in CAD97827. 1 Publication
Sequence conflicti3737 – 37371A → S in CAA40279. 1 Publication
Sequence conflicti3737 – 37371A → S in CAB42644. 1 Publication
Sequence conflicti3955 – 39562NN → SM in AC093879. 1 Publication

Sequence databases

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

Genome annotation databases

EnsembliENST00000357077; ENSP00000349588; ENSG00000145362. [Q01484-4]
ENST00000394537; ENSP00000378044; ENSG00000145362. [Q01484-2]
ENST00000506722; ENSP00000421067; ENSG00000145362. [Q01484-5]
ENST00000510275; ENSP00000421023; ENSG00000145362. [Q01484-7]
GeneIDi287.
KEGGihsa:287.
UCSCiuc003ibd.4. human. [Q01484-5]
uc003ibe.4. human. [Q01484-4]
uc003ibf.4. human. [Q01484-2]
uc003ibh.4. human. [Q01484-7]

Polymorphism databases

DMDMi387912917.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Ankyrin entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X56957 mRNA. Translation: CAA40278.1 .
X56958 mRNA. Translation: CAA40279.2 .
Z26634 mRNA. Translation: CAB42644.1 . Sequence problems.
BX537758 mRNA. Translation: CAD97827.1 .
AC004057 Genomic DNA. No translation available.
AC093617 Genomic DNA. No translation available.
AC093879 Genomic DNA. No translation available.
AC093900 Genomic DNA. No translation available.
BC125235 mRNA. Translation: AAI25236.1 .
BC125236 mRNA. Translation: AAI25237.1 . Frameshift.
M37123 Genomic DNA. Translation: AAA62828.1 .
CCDSi CCDS3702.1. [Q01484-4 ]
CCDS43261.1. [Q01484-2 ]
CCDS54796.1. [Q01484-5 ]
PIRi S37431.
RefSeqi NP_001120965.1. NM_001127493.1. [Q01484-5 ]
NP_001139.3. NM_001148.4. [Q01484-4 ]
NP_066187.2. NM_020977.3. [Q01484-2 ]
UniGenei Hs.620557.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4D8O X-ray 2.20 A 966-1476 [» ]
DisProti DP00467.
ProteinModelPortali Q01484.
SMRi Q01484. Positions 432-841, 3570-3647.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106784. 8 interactions.
DIPi DIP-37425N.
IntActi Q01484. 16 interactions.
STRINGi 9606.ENSP00000349588.

Protein family/group databases

TCDBi 8.A.28.1.1. the ankyrin (ankyrin) family.

PTM databases

PhosphoSitei Q01484.

Polymorphism databases

DMDMi 387912917.

Proteomic databases

MaxQBi Q01484.
PaxDbi Q01484.
PRIDEi Q01484.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000357077 ; ENSP00000349588 ; ENSG00000145362 . [Q01484-4 ]
ENST00000394537 ; ENSP00000378044 ; ENSG00000145362 . [Q01484-2 ]
ENST00000506722 ; ENSP00000421067 ; ENSG00000145362 . [Q01484-5 ]
ENST00000510275 ; ENSP00000421023 ; ENSG00000145362 . [Q01484-7 ]
GeneIDi 287.
KEGGi hsa:287.
UCSCi uc003ibd.4. human. [Q01484-5 ]
uc003ibe.4. human. [Q01484-4 ]
uc003ibf.4. human. [Q01484-2 ]
uc003ibh.4. human. [Q01484-7 ]

Organism-specific databases

CTDi 287.
GeneCardsi GC04P113739.
H-InvDB HIX0164018.
HGNCi HGNC:493. ANK2.
HPAi CAB015178.
HPA007570.
HPA008007.
HPA035970.
MIMi 106410. gene.
600919. phenotype.
neXtProti NX_Q01484.
Orphaneti 101016. Romano-Ward syndrome.
PharmGKBi PA24799.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0666.
HOGENOMi HOG000169277.
HOVERGENi HBG100442.
KOi K10380.
OMAi YLIMASS.
PhylomeDBi Q01484.
TreeFami TF351263.

Enzyme and pathway databases

Reactomei REACT_22266. Interaction between L1 and Ankyrins.

Miscellaneous databases

ChiTaRSi Ank2. human.
GenomeRNAii 287.
NextBioi 1169.
PROi Q01484.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q01484.
Bgeei Q01484.
CleanExi HS_ANK2.
Genevestigatori Q01484.

Family and domain databases

Gene3Di 1.10.533.10. 1 hit.
1.25.40.20. 3 hits.
InterProi IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR000906. ZU5.
[Graphical view ]
Pfami PF00023. Ank. 19 hits.
PF12796. Ank_2. 1 hit.
PF00531. Death. 1 hit.
PF00791. ZU5. 2 hits.
[Graphical view ]
PRINTSi PR01415. ANKYRIN.
SMARTi SM00248. ANK. 23 hits.
SM00005. DEATH. 1 hit.
[Graphical view ]
SUPFAMi SSF47986. SSF47986. 1 hit.
SSF48403. SSF48403. 3 hits.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 20 hits.
PS50017. DEATH_DOMAIN. 1 hit.
PS51145. ZU5. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. Cited for: VARIANTS LQT4 GLY-1458; ILE-3740; ASN-3744; TRP-3906 AND LYS-3931, CHARACTERIZATION OF VARIANTS LQT4.
  16. Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLU-685; ARG-1267 AND LYS-3653.

Entry informationi

Entry nameiANK2_HUMAN
AccessioniPrimary (citable) accession number: Q01484
Secondary accession number(s): Q01485
, Q08AC7, Q08AC8, Q7Z3L5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: May 16, 2012
Last modified: September 3, 2014
This is version 154 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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