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Reviewed, UniProtKB/Swiss-Prot Q01484 (ANK2_HUMAN)

Last modified February 9, 2010. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

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

Protein attributes

Sequence length3924 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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

Interacts with RHBG and SPTBN1. Ref.9 Ref.10 Ref.14

Subcellular location

Cytoplasmcytoskeleton. Membrane. CytoplasmmyofibrilsarcomereM-band By similarity. Apical cell membrane By similarity. Cell membrane. 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. Ref.14

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.14 Ref.1 Ref.7

Post-translational modification

Phosphorylated at multiple sites by different protein kinases and each phosphorylation event regulates the protein's structure and function Potential. Ref.11 Ref.12 Ref.13

Involvement in disease

Defects in ANK2 are the cause of long QT syndrome type 4 (LQT4) [MIM:600919]; also known as sick sinus syndrome with bradycardia. Long QT syndromes are heart disorders 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. LQT4 displays 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. Ref.8 Ref.16

Sequence similarities

Contains 24 ANK repeats.

Contains 1 death domain.

Contains 1 ZU5 domain.

Sequence caution

The sequence AAI25237.1 differs from that shown. Reason: Frameshift at position 1372.

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

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Long QT syndrome
   DomainANK repeat
Repeat
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processsignal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular componentM band

Inferred from electronic annotation. Source: UniProtKB-SubCell

apical plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

basolateral plasma membrane Ref.10

Inferred from direct assay. Source: UniProtKB

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein binding Ref.9

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q01484-1)

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:
     1039-1039: Q → QFLGKLHLPTAPPPLNEGESLVSRILQLGPPGTK
     1444-3528: Missing.
Isoform 3 (identifier: Q01484-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1039-1039: Q → QFLGKLHLPTAPPPLNEGESLVSRILQLGPPGTK
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
     1039-1039: Q → QFLGKLHLPTAPPPLNEGESLVSRILQLGPPGTK
     1444-3528: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q01484-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1315: Missing.
     1444-3528: Missing.
     3837-3837: K → KELTEELGELEASSDEEAMVTTRVVRRRVIIQ

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 39243924Ankyrin-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 – 1073108ZU5
Repeat1773 – 178412Repeat A
Repeat1785 – 179612Repeat A
Repeat1797 – 180812Repeat A
Repeat1809 – 182012Repeat A
Repeat1821 – 183212Repeat A
Repeat1833 – 184412Repeat A
Repeat1845 – 185612Repeat A
Repeat1857 – 186711Repeat A; approximate
Repeat1868 – 187912Repeat A
Repeat1880 – 189112Repeat A
Repeat1892 – 190211Repeat A; approximate
Repeat1903 – 191412Repeat A
Repeat1915 – 192612Repeat A
Repeat1927 – 193812Repeat A
Repeat1939 – 195012Repeat A
Domain3536 – 362085Death
Region966 – 1125160Interaction with SPTBN1
Region1773 – 1950178Repeat-rich region

Amino acid modifications

Modified residue311Phosphoserine By similarity
Modified residue341Phosphoserine By similarity
Modified residue3781Phosphotyrosine By similarity
Modified residue5311Phosphotyrosine By similarity
Modified residue8461Phosphoserine By similarity
Modified residue8981Phosphoserine By similarity
Modified residue9111Phosphoserine Ref.12
Modified residue13491Phosphotyrosine By similarity
Modified residue14281Phosphoserine By similarity
Modified residue14751Phosphoserine Ref.12
Modified residue14901Phosphothreonine Ref.12
Modified residue25501Phosphothreonine Ref.11
Modified residue30601Phosphothreonine By similarity
Modified residue32401Phosphoserine By similarity
Modified residue33291Phosphoserine By similarity
Modified residue33571Phosphoserine By similarity
Modified residue33761Phosphoserine By similarity
Modified residue33771Phosphotyrosine By similarity
Modified residue37021Phosphoserine By similarity
Modified residue37431Phosphothreonine By similarity
Modified residue37601Phosphoserine Ref.13
Modified residue37621Phosphoserine Ref.13
Modified residue37641Phosphothreonine Ref.13
Modified residue37691Phosphoserine By similarity
Modified residue37701Phosphothreonine By similarity
Modified residue37901Phosphoserine By similarity
Modified residue38111Phosphothreonine By similarity

Natural variations

Alternative sequence1 – 13151315Missing in isoform 5.
VSP_037057
Alternative sequence1 – 2727MMNED…RKRPK → MTTMLQ in isoform 4.
VSP_037058
Alternative sequence9671G → GRASPCLERDNSS in isoform 4.
VSP_037059
Alternative sequence10391Q → QFLGKLHLPTAPPPLNEGES LVSRILQLGPPGTK in isoform 2, isoform 3 and isoform 4.
VSP_000267
Alternative sequence1444 – 35282085Missing in isoform 2, isoform 4 and isoform 5.
VSP_000268
Alternative sequence38371K → KELTEELGELEASSDEEAMV TTRVVRRRVIIQ in isoform 5.
VSP_037060
Natural variant6851G → E in a breast cancer sample; somatic mutation. Ref.17
VAR_035606
Natural variant6871N → S: dbSNP rs29372.
VAR_055504
Natural variant12341G → R in a colorectal cancer sample; somatic mutation. Ref.17
VAR_035607
Natural variant14251E → G in LQT4; loss of function. Ref.8 Ref.16
VAR_022934
Natural variant23361V → A: dbSNP rs28377576.
VAR_055505
Natural variant36201T → K in a colorectal cancer sample; somatic mutation. Ref.17
VAR_035608
Natural variant37071L → I in LQT4; loss of function. Ref.16
VAR_022935
Natural variant37111T → N in LQT4; loss of function. Ref.16
VAR_022936
Natural variant38731R → W in LQT4; loss of function. Ref.16
VAR_022937
Natural variant38981E → K in LQT4; loss of function. Ref.16
VAR_022938

Experimental info

Mutagenesis975 – 9773DAR → AAA: Prevents binding to SPTBN1.
Mutagenesis10001A → P: Prevents binding to SPTBN1. Ref.9
Mutagenesis1067 – 10704ENGD → AAGA: Weak binding to SPTBN1. Ref.9
Sequence conflict2201V → I in CAD97827. Ref.4
Sequence conflict475 – 4762GQ → PE in AAA62828. Ref.7
Sequence conflict27541A → R in CAB42644. Ref.3
Sequence conflict29661Q → L in CAB42644. Ref.3
Sequence conflict3107 – 31082EE → RY in AC093879. Ref.5
Sequence conflict31521D → S in CAB42644. Ref.3
Sequence conflict36661V → A in CAD97827. Ref.4
Sequence conflict37041A → S in CAA40279. Ref.1
Sequence conflict37041A → S in CAB42644. Ref.3
Sequence conflict3922 – 39232NN → SM in AC093879. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 25, 2008. Version 3.
Checksum: C8C426698EBE2FDB

FASTA3,924430,255
        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 LGPVIVEIPH FAALRGKERE LVVLRSENGD SWKEHFCDYT 

      1090       1100       1110       1120       1130       1140 
EDELNEILNG MDEVLDSPED LEKKRICRII TRDFPQYFAV VSRIKQDSNL IGPEGGVLSS 

      1150       1160       1170       1180       1190       1200 
TVVPQVQAVF PEGALTKRIR VGLQAQPMHS ELVKKILGNK ATFSPIVTLE PRRRKFHKPI 

      1210       1220       1230       1240       1250       1260 
TMTIPVPKAS SDVMLNGFGG DAPTLRLLCS ITGGTTPAQW EDITGTTPLT FVNECVSFTT 

      1270       1280       1290       1300       1310       1320 
NVSARFWLID CRQIQESVTF ASQVYREIIC VPYMAKFVVF AKSHDPIEAR LRCFCMTDDK 

      1330       1340       1350       1360       1370       1380 
VDKTLEQQEN FAEVARSRDV EVLEGKPIYV DCFGNLVPLT KSGQHHIFSF FAFKENRLPL 

      1390       1400       1410       1420       1430       1440 
FVKVRDTTQE PCGRLSFMKE PKSTRGLVHQ AICNLNITLP IYTKESESDQ EQEEEIDMTS 

      1450       1460       1470       1480       1490       1500 
EKNDETESTE TSVLKSHLVN EVPVLASPDL LSEVSEMKQD LIKMTAILTT DVSDKAGSIK 

      1510       1520       1530       1540       1550       1560 
VKELVKAAEE EPGEPFEIVE RVKEDLEKVN EILRSGTCTR DESSVQSSRS ERGLVEEEWV 

      1570       1580       1590       1600       1610       1620 
IVSDEEIEEA RQKAPLEITE YPCVEVRIDK EIKGKVEKDS TGLVNYLTDD LNTCVPLPKE 

      1630       1640       1650       1660       1670       1680 
QLQTVQDKAG KKCEALAVGR SSEKEGKDIP PDETQSTQKQ HKPSLGIKKP VRRKLKEKQK 

      1690       1700       1710       1720       1730       1740 
QKEEGLQASA EKAELKKGSS EESLGEDPGL APEPLPTVKA TSPLIEETPI GSIKDKVKAL 

      1750       1760       1770       1780       1790       1800 
QKRVEDEQKG RSKLPIRVKG KEDVPKKTTH RPHPAASPSL KSERHAPGSP SPKTERHSTL 

      1810       1820       1830       1840       1850       1860 
SSSAKTERHP PVSPSSKTEK HSPVSPSAKT ERHSPASSSS KTEKHSPVSP STKTERHSPV 

      1870       1880       1890       1900       1910       1920 
SSTKTERHPP VSPSGKTDKR PPVSPSGRTE KHPPVSPGRT EKRLPVSPSG RTDKHQPVST 

      1930       1940       1950       1960       1970       1980 
AGKTEKHLPV SPSGKTEKQP PVSPTSKTER IEETMSVREL MKAFQSGQDP SKHKTGLFEH 

      1990       2000       2010       2020       2030       2040 
KSAKQKQPQE KGKVRVEKEK GPILTQREAQ KTENQTIKRG QRLPVTGTAE SKRGVRVSSI 

      2050       2060       2070       2080       2090       2100 
GVKKEDAAGG KEKVLSHKIP EPVQSVPEEE SHRESEVPKE KMADEQGDMD LQISPDRKTS 

      2110       2120       2130       2140       2150       2160 
TDFSEVIKQE LEDNDKYQQF RLSEETEKAQ LHLDQVLTSP FNTTFPLDYM KDEFLPALSL 

      2170       2180       2190       2200       2210       2220 
QSGALDGSSE SLKNEGVAGS PCGSLMEGTP QISSEESYKH EGLAETPETS PESLSFSPKK 

      2230       2240       2250       2260       2270       2280 
SEEQTGETKE STKTETTTEI RSEKEHPTTK DITGGSEERG ATVTEDSETS TESFQKEATL 

      2290       2300       2310       2320       2330       2340 
GSPKDTSPKR QDDCTGSCSV ALAKETPTGL TEEAACDEGQ RTFGSSAHKT QTDSEVQEST 

      2350       2360       2370       2380       2390       2400 
ATSDETKALP LPEASVKTDT GTESKPQGVI RSPQGLELAL PSRDSEVLSA VADDSLAVSH 

      2410       2420       2430       2440       2450       2460 
KDSLEASPVL EDNSSHKTPD SLEPSPLKES PCRDSLESSP VEPKMKAGIF PSHFPLPAAV 

      2470       2480       2490       2500       2510       2520 
AKTELLTEVA SVRSRLLRDP DGSAEDDSLE QTSLMESSGK SPLSPDTPSS EEVSYEVTPK 

      2530       2540       2550       2560       2570       2580 
TTDVSTPKPA VIHECAEEDD SENGEKKRFT PEEEMFKMVT KIKMFDELEQ EAKQKRDYKK 

      2590       2600       2610       2620       2630       2640 
EPKQEESSSS SDPDADCSVD VDEPKHTGSG EDESGVPVLV TSESRKVSSS SESEPELAQL 

      2650       2660       2670       2680       2690       2700 
KKGADSGLLP EPVIRVQPPS PLPSSMDSNS SPEEVQFQPV VSKQYTFKMN EDTQEEPGKS 

      2710       2720       2730       2740       2750       2760 
EEEKDSESHL AEDRHAVSTE AEDRSYDKLN RDTDQPKICD GHGCEAMSPS SSAAPVSSGL 

      2770       2780       2790       2800       2810       2820 
QSPTGDDVDE QPVIYKESLA LQGTHEKDTE GEELDVSRAE SPQADCPSES FSSSSSLPHC 

      2830       2840       2850       2860       2870       2880 
LVSEGKELDE DISATSSIQK TEVTKTDETF ENLPKDCPSQ DSSITTQTDR FSMDVPVSDL 

      2890       2900       2910       2920       2930       2940 
AENDEIYDPQ ITSPYENVPS QSFFSSEESK TQTDANHTTS FHSSEVYSVT ITSPVEDVVV 

      2950       2960       2970       2980       2990       3000 
ASSSSGTVLS KESNFEGQDI KMESQQESTL WEMQSDSVSS SFEPTMSATT TVVGEQISKV 

      3010       3020       3030       3040       3050       3060 
IITKTDVDSD SWSEIREDDE AFEARVKEEE QKIFGLMVDR QSQGTTPDTT PARTPTEEGT 

      3070       3080       3090       3100       3110       3120 
PTSEQNPFLF QEGKLFEMTR SGAIDMTKRS YADESFHFFQ IGQESREETL SEDVKEGATG 

      3130       3140       3150       3160       3170       3180 
ADPLPLETSA ESLALSESKE TVDDEADLLP DDVSEEVEEI PASDAQLNSQ MGISASTETP 

      3190       3200       3210       3220       3230       3240 
TKEAVSVGTK DLPTVQTGDI PPLSGVKQIS CPDSSEPAVQ VQLDFSTLTR SVYSDRGDDS 

      3250       3260       3270       3280       3290       3300 
PDSSPEEQKS VIEIPTAPME NVPFTESKSK IPVRTMPTST PAPPSAEYES SVSEDFLSSV 

      3310       3320       3330       3340       3350       3360 
DEENKADEAK PKSKLPVKVP LQRVEQQLSD LDTSVQKTVA PQGQDMASIA PDNRSKSESD 

      3370       3380       3390       3400       3410       3420 
ASSLDSKTKC PVKTRSYTET ETESRERAEE LELESEEGAT RPKILTSRLP VKSRSTTSSC 

      3430       3440       3450       3460       3470       3480 
RGGTSPTKES KEHFFDLYRN SIEFFEEISD EASKLVDRLT QSEREQEIVS DDESSSALEV 

      3490       3500       3510       3520       3530       3540 
SVIENLPPVE TEHSVPEDIF DTRPIWDESI ETLIERIPDE NGHDHAEDPQ DEQERIEERL 

      3550       3560       3570       3580       3590       3600 
AYIADHLGFS WTELARELDF TEEQIHQIRI ENPNSLQDQS HALLKYWLER DGKHATDTNL 

      3610       3620       3630       3640       3650       3660 
VECLTKINRM DIVHLMETNT EPLQERISHS YAEIEQTITL DHSEGFSVLQ EELCTAQHKQ 

      3670       3680       3690       3700       3710       3720 
KEEQAVSKES ETCDHPPIVS EEDISVGYST FQDGVPKTEG DSSATALFPQ THKEQVQQDF 

      3730       3740       3750       3760       3770       3780 
SGKMQDLPEE SSLEYQQEYF VTTPGTETSE TQKAMIVPSS PSKTPEEVST PAEEEKLYLQ 

      3790       3800       3810       3820       3830       3840 
TPTSSERGGS PIIQEPEEPS EHREESSPRK TSLVIVESAD NQPETCERLD EDAAFEKGDD 

      3850       3860       3870       3880       3890       3900 
MPEIPPETVT EEEYIDEHGH TVVKKVTRKI IRRYVSSEGT EKEEIMVQGM PQEPVNIEEG 

      3910       3920 
DGYSKVIKRV VLKSDTEQSE DNNE 

« Hide

Isoform 2.

Checksum: 425D5422CF5CE930
Show »

FASTA1,872205,795
Isoform 3.

Checksum: 41C1A240CC5A3B72
Show »

FASTA3,957433,715
Isoform 4.

Checksum: 4E2B2DB97E1DDC0A
Show »

FASTA1,863204,752
Isoform 5.

Checksum: C0C03881D8E0EFD9
Show »

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: 1830053] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), 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: 8253844] [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: 17974005] [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: 15815621] [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: 15489334] [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: 1833308] [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: 12571597] [Abstract]
Cited for: FUNCTION, VARIANT LQT4 GLY-1425.
[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: 15262991] [Abstract]
Cited for: INTERACTION WITH SPTBN1, MUTAGENESIS OF 975-ASP--ARG-977; ALA-1000 AND 1067-GLU--ASP-1070.
[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: 15611082] [Abstract]
Cited for: INTERACTION WITH RHBG.
[11]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2550, MASS SPECTROMETRY.
Tissue: Epithelium.
[12]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-911; SER-1475 AND THR-1490, MASS SPECTROMETRY.
[13]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3760; SER-3762 AND THR-3764, MASS SPECTROMETRY.
[14]"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: 19007774] [Abstract]
Cited for: SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[15]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[16]"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: 15178757] [Abstract]
Cited for: VARIANTS LQT4 GLY-1425; ILE-3707; ASN-3711; TRP-3873 AND LYS-3898, CHARACTERIZATION OF VARIANTS LQT4.
[17]"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: 16959974] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLU-685; ARG-1234 AND LYS-3620.
+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.
IPIIPI00007834.
IPI00074962.
IPI00305279.
IPI00384928.
IPI00895856.
PIRS37431.
RefSeqNP_001120965.1.
NP_001139.3.
NP_066187.2.
UniGeneHs.620557

3D structure databases

DisProtDP00467.
ModBaseSearch...

Protein-protein interaction databases

IntActQ01484. 6 interactions.
STRINGQ01484.

Protein family/group databases

TCDB8.A.28.1.1. ankyrin family.

PTM databases

PhosphoSiteQ01484.

Genome annotation databases

EnsemblENST00000361149; ENSP00000354873; ENSG00000145362; Homo sapiens. [Genome view]
GeneID287.
KEGGhsa:287.
UCSCuc003ibe.2. human.
uc003ibf.2. human.

Organism-specific databases

CTD287.
GeneCardsGC04P114132.
HGNCHGNC:493. ANK2.
MIM106410. gene.
600919. phenotype.
Orphanet768. Long QT syndrome, familial.
PharmGKBPA24799.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG17755.
HOVERGENQ01484.
OMAKTEKHSP.
OrthoDBEOG9VHNS3.

Gene expression databases

ArrayExpressQ01484.
BgeeQ01484.
CleanExHS_ANK2.
GenevestigatorQ01484.
GermOnlineENSG00000145362. Homo sapiens.

Family and domain databases

InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR000488. Death.
IPR011029. DEATH-like.
IPR000906. ZU5.
[Graphical view]
Gene3DG3DSA:1.25.40.20. ANK. 4 hits.
G3DSA:1.10.533.10. DEATH_like. 1 hit.
PfamPF00023. Ank. 19 hits.
PF00531. Death. 1 hit.
PF00791. ZU5. 1 hit.
[Graphical view]
SMARTSM00248. ANK. 23 hits.
SM00005. DEATH. 1 hit.
SM00218. ZU5. 1 hit.
[Graphical view]
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 20 hits.
PS50017. DEATH_DOMAIN. 1 hit.
PS51145. ZU5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

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: November 25, 2008
Last modified: February 9, 2010
This is version 105 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 4

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents