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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.By similarity1 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, bridging Source: BHF-UCL
  6. protein kinase binding Source: BHF-UCL
  7. spectrin binding Source: BHF-UCL
  8. 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 1 Publication. Membrane 1 Publication. CytoplasmmyofibrilsarcomereM line By similarity. Apical cell membrane By similarity. Cell membrane 1 Publication. 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.By similarity

GO - Cellular componenti

  1. A band Source: BHF-UCL
  2. basolateral plasma membrane Source: UniProtKB
  3. costamere Source: BHF-UCL
  4. cytoskeleton Source: UniProtKB-KW
  5. cytosol Source: Reactome
  6. integral component of plasma membrane Source: Ensembl
  7. intercalated disc Source: BHF-UCL
  8. intracellular Source: BHF-UCL
  9. M band Source: BHF-UCL
  10. membrane raft Source: Ensembl
  11. neuron projection Source: Ensembl
  12. perinuclear region of cytoplasm Source: Ensembl
  13. plasma membrane Source: BHF-UCL
  14. postsynaptic membrane Source: UniProtKB-KW
  15. sarcolemma Source: BHF-UCL
  16. T-tubule Source: BHF-UCL
  17. 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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
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 – 3781PhosphotyrosineBy similarity
Modified residuei531 – 5311PhosphotyrosineBy similarity
Modified residuei1382 – 13821PhosphotyrosineBy similarity
Modified residuei3776 – 37761PhosphothreonineBy similarity

Post-translational modificationi

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

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

BgeeiQ01484.
CleanExiHS_ANK2.
ExpressionAtlasiQ01484. baseline and differential.
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.By similarity3 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi106784. 14 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.
ModBaseiSearch...
MobiDBiSearch...

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 1PROSITE-ProRule annotationAdd
BLAST
Domaini1125 – 1288164ZU5 2PROSITE-ProRule annotationAdd
BLAST
Domaini1450 – 153586Death 1PROSITE-ProRule annotationAdd
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 2PROSITE-ProRule annotationAdd
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.PROSITE-ProRule annotation
Contains 2 death domains.PROSITE-ProRule annotation
Contains 2 ZU5 domains.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00760000118950.
HOGENOMiHOG000169277.
HOVERGENiHBG100442.
InParanoidiQ01484.
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_dom.
[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

        10         20         30         40         50
MMNEDAAQKS DSGEKFNGSS QRRKRPKKSD SNASFLRAAR AGNLDKVVEY
60 70 80 90 100
LKGGIDINTC NQNGLNALHL AAKEGHVGLV QELLGRGSSV DSATKKGNTA
110 120 130 140 150
LHIASLAGQA EVVKVLVKEG ANINAQSQNG FTPLYMAAQE NHIDVVKYLL
160 170 180 190 200
ENGANQSTAT EDGFTPLAVA LQQGHNQAVA ILLENDTKGK VRLPALHIAA
210 220 230 240 250
RKDDTKSAAL LLQNDHNADV QSKMMVNRTT ESGFTPLHIA AHYGNVNVAT
260 270 280 290 300
LLLNRGAAVD FTARNGITPL HVASKRGNTN MVKLLLDRGG QIDAKTRDGL
310 320 330 340 350
TPLHCAARSG HDQVVELLLE RGAPLLARTK NGLSPLHMAA QGDHVECVKH
360 370 380 390 400
LLQHKAPVDD VTLDYLTALH VAAHCGHYRV TKLLLDKRAN PNARALNGFT
410 420 430 440 450
PLHIACKKNR IKVMELLVKY GASIQAITES GLTPIHVAAF MGHLNIVLLL
460 470 480 490 500
LQNGASPDVT NIRGETALHM AARAGQVEVV RCLLRNGALV DARAREEQTP
510 520 530 540 550
LHIASRLGKT EIVQLLLQHM AHPDAATTNG YTPLHISARE GQVDVASVLL
560 570 580 590 600
EAGAAHSLAT KKGFTPLHVA AKYGSLDVAK LLLQRRAAAD SAGKNGLTPL
610 620 630 640 650
HVAAHYDNQK VALLLLEKGA SPHATAKNGY TPLHIAAKKN QMQIASTLLN
660 670 680 690 700
YGAETNIVTK QGVTPLHLAS QEGHTDMVTL LLDKGANIHM STKSGLTSLH
710 720 730 740 750
LAAQEDKVNV ADILTKHGAD QDAHTKLGYT PLIVACHYGN VKMVNFLLKQ
760 770 780 790 800
GANVNAKTKN GYTPLHQAAQ QGHTHIINVL LQHGAKPNAT TANGNTALAI
810 820 830 840 850
AKRLGYISVV DTLKVVTEEV TTTTTTITEK HKLNVPETMT EVLDVSDEEG
860 870 880 890 900
DDTMTGDGGE YLRPEDLKEL GDDSLPSSQF LDGMNYLRYS LEGGRSDSLR
910 920 930 940 950
SFSSDRSHTL SHASYLRDSA VMDDSVVIPS HQVSTLAKEA ERNSYRLSWG
960 970 980 990 1000
TENLDNVALS SSPIHSGFLV SFMVDARGGA MRGCRHNGLR IIIPPRKCTA
1010 1020 1030 1040 1050
PTRVTCRLVK RHRLATMPPM VEGEGLASRL IEVGPSGAQF LGKLHLPTAP
1060 1070 1080 1090 1100
PPLNEGESLV SRILQLGPPG TKFLGPVIVE IPHFAALRGK ERELVVLRSE
1110 1120 1130 1140 1150
NGDSWKEHFC DYTEDELNEI LNGMDEVLDS PEDLEKKRIC RIITRDFPQY
1160 1170 1180 1190 1200
FAVVSRIKQD SNLIGPEGGV LSSTVVPQVQ AVFPEGALTK RIRVGLQAQP
1210 1220 1230 1240 1250
MHSELVKKIL GNKATFSPIV TLEPRRRKFH KPITMTIPVP KASSDVMLNG
1260 1270 1280 1290 1300
FGGDAPTLRL LCSITGGTTP AQWEDITGTT PLTFVNECVS FTTNVSARFW
1310 1320 1330 1340 1350
LIDCRQIQES VTFASQVYRE IICVPYMAKF VVFAKSHDPI EARLRCFCMT
1360 1370 1380 1390 1400
DDKVDKTLEQ QENFAEVARS RDVEVLEGKP IYVDCFGNLV PLTKSGQHHI
1410 1420 1430 1440 1450
FSFFAFKENR LPLFVKVRDT TQEPCGRLSF MKEPKSTRGL VHQAICNLNI
1460 1470 1480 1490 1500
TLPIYTKESE SDQEQEEEID MTSEKNDETE STETSVLKSH LVNEVPVLAS
1510 1520 1530 1540 1550
PDLLSEVSEM KQDLIKMTAI LTTDVSDKAG SIKVKELVKA AEEEPGEPFE
1560 1570 1580 1590 1600
IVERVKEDLE KVNEILRSGT CTRDESSVQS SRSERGLVEE EWVIVSDEEI
1610 1620 1630 1640 1650
EEARQKAPLE ITEYPCVEVR IDKEIKGKVE KDSTGLVNYL TDDLNTCVPL
1660 1670 1680 1690 1700
PKEQLQTVQD KAGKKCEALA VGRSSEKEGK DIPPDETQST QKQHKPSLGI
1710 1720 1730 1740 1750
KKPVRRKLKE KQKQKEEGLQ ASAEKAELKK GSSEESLGED PGLAPEPLPT
1760 1770 1780 1790 1800
VKATSPLIEE TPIGSIKDKV KALQKRVEDE QKGRSKLPIR VKGKEDVPKK
1810 1820 1830 1840 1850
TTHRPHPAAS PSLKSERHAP GSPSPKTERH STLSSSAKTE RHPPVSPSSK
1860 1870 1880 1890 1900
TEKHSPVSPS AKTERHSPAS SSSKTEKHSP VSPSTKTERH SPVSSTKTER
1910 1920 1930 1940 1950
HPPVSPSGKT DKRPPVSPSG RTEKHPPVSP GRTEKRLPVS PSGRTDKHQP
1960 1970 1980 1990 2000
VSTAGKTEKH LPVSPSGKTE KQPPVSPTSK TERIEETMSV RELMKAFQSG
2010 2020 2030 2040 2050
QDPSKHKTGL FEHKSAKQKQ PQEKGKVRVE KEKGPILTQR EAQKTENQTI
2060 2070 2080 2090 2100
KRGQRLPVTG TAESKRGVRV SSIGVKKEDA AGGKEKVLSH KIPEPVQSVP
2110 2120 2130 2140 2150
EEESHRESEV PKEKMADEQG DMDLQISPDR KTSTDFSEVI KQELEDNDKY
2160 2170 2180 2190 2200
QQFRLSEETE KAQLHLDQVL TSPFNTTFPL DYMKDEFLPA LSLQSGALDG
2210 2220 2230 2240 2250
SSESLKNEGV AGSPCGSLME GTPQISSEES YKHEGLAETP ETSPESLSFS
2260 2270 2280 2290 2300
PKKSEEQTGE TKESTKTETT TEIRSEKEHP TTKDITGGSE ERGATVTEDS
2310 2320 2330 2340 2350
ETSTESFQKE ATLGSPKDTS PKRQDDCTGS CSVALAKETP TGLTEEAACD
2360 2370 2380 2390 2400
EGQRTFGSSA HKTQTDSEVQ ESTATSDETK ALPLPEASVK TDTGTESKPQ
2410 2420 2430 2440 2450
GVIRSPQGLE LALPSRDSEV LSAVADDSLA VSHKDSLEAS PVLEDNSSHK
2460 2470 2480 2490 2500
TPDSLEPSPL KESPCRDSLE SSPVEPKMKA GIFPSHFPLP AAVAKTELLT
2510 2520 2530 2540 2550
EVASVRSRLL RDPDGSAEDD SLEQTSLMES SGKSPLSPDT PSSEEVSYEV
2560 2570 2580 2590 2600
TPKTTDVSTP KPAVIHECAE EDDSENGEKK RFTPEEEMFK MVTKIKMFDE
2610 2620 2630 2640 2650
LEQEAKQKRD YKKEPKQEES SSSSDPDADC SVDVDEPKHT GSGEDESGVP
2660 2670 2680 2690 2700
VLVTSESRKV SSSSESEPEL AQLKKGADSG LLPEPVIRVQ PPSPLPSSMD
2710 2720 2730 2740 2750
SNSSPEEVQF QPVVSKQYTF KMNEDTQEEP GKSEEEKDSE SHLAEDRHAV
2760 2770 2780 2790 2800
STEAEDRSYD KLNRDTDQPK ICDGHGCEAM SPSSSAAPVS SGLQSPTGDD
2810 2820 2830 2840 2850
VDEQPVIYKE SLALQGTHEK DTEGEELDVS RAESPQADCP SESFSSSSSL
2860 2870 2880 2890 2900
PHCLVSEGKE LDEDISATSS IQKTEVTKTD ETFENLPKDC PSQDSSITTQ
2910 2920 2930 2940 2950
TDRFSMDVPV SDLAENDEIY DPQITSPYEN VPSQSFFSSE ESKTQTDANH
2960 2970 2980 2990 3000
TTSFHSSEVY SVTITSPVED VVVASSSSGT VLSKESNFEG QDIKMESQQE
3010 3020 3030 3040 3050
STLWEMQSDS VSSSFEPTMS ATTTVVGEQI SKVIITKTDV DSDSWSEIRE
3060 3070 3080 3090 3100
DDEAFEARVK EEEQKIFGLM VDRQSQGTTP DTTPARTPTE EGTPTSEQNP
3110 3120 3130 3140 3150
FLFQEGKLFE MTRSGAIDMT KRSYADESFH FFQIGQESRE ETLSEDVKEG
3160 3170 3180 3190 3200
ATGADPLPLE TSAESLALSE SKETVDDEAD LLPDDVSEEV EEIPASDAQL
3210 3220 3230 3240 3250
NSQMGISAST ETPTKEAVSV GTKDLPTVQT GDIPPLSGVK QISCPDSSEP
3260 3270 3280 3290 3300
AVQVQLDFST LTRSVYSDRG DDSPDSSPEE QKSVIEIPTA PMENVPFTES
3310 3320 3330 3340 3350
KSKIPVRTMP TSTPAPPSAE YESSVSEDFL SSVDEENKAD EAKPKSKLPV
3360 3370 3380 3390 3400
KVPLQRVEQQ LSDLDTSVQK TVAPQGQDMA SIAPDNRSKS ESDASSLDSK
3410 3420 3430 3440 3450
TKCPVKTRSY TETETESRER AEELELESEE GATRPKILTS RLPVKSRSTT
3460 3470 3480 3490 3500
SSCRGGTSPT KESKEHFFDL YRNSIEFFEE ISDEASKLVD RLTQSEREQE
3510 3520 3530 3540 3550
IVSDDESSSA LEVSVIENLP PVETEHSVPE DIFDTRPIWD ESIETLIERI
3560 3570 3580 3590 3600
PDENGHDHAE DPQDEQERIE ERLAYIADHL GFSWTELARE LDFTEEQIHQ
3610 3620 3630 3640 3650
IRIENPNSLQ DQSHALLKYW LERDGKHATD TNLVECLTKI NRMDIVHLME
3660 3670 3680 3690 3700
TNTEPLQERI SHSYAEIEQT ITLDHSEGFS VLQEELCTAQ HKQKEEQAVS
3710 3720 3730 3740 3750
KESETCDHPP IVSEEDISVG YSTFQDGVPK TEGDSSATAL FPQTHKEQVQ
3760 3770 3780 3790 3800
QDFSGKMQDL PEESSLEYQQ EYFVTTPGTE TSETQKAMIV PSSPSKTPEE
3810 3820 3830 3840 3850
VSTPAEEEKL YLQTPTSSER GGSPIIQEPE EPSEHREESS PRKTSLVIVE
3860 3870 3880 3890 3900
SADNQPETCE RLDEDAAFEK GDDMPEIPPE TVTEEEYIDE HGHTVVKKVT
3910 3920 3930 3940 3950
RKIIRRYVSS EGTEKEEIMV QGMPQEPVNI EEGDGYSKVI KRVVLKSDTE

QSEDNNE
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

Show »
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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti220 – 2201V → I in CAD97827. (PubMed:17974005)Curated
Sequence conflicti475 – 4762GQ → PE in AAA62828. (PubMed:1833308)Curated
Sequence conflicti2787 – 27871A → R in CAB42644. (PubMed:8253844)Curated
Sequence conflicti2999 – 29991Q → L in CAB42644. (PubMed:8253844)Curated
Sequence conflicti3140 – 31412EE → RY in AC093879. (PubMed:15815621)Curated
Sequence conflicti3185 – 31851D → S in CAB42644. (PubMed:8253844)Curated
Sequence conflicti3699 – 36991V → A in CAD97827. (PubMed:17974005)Curated
Sequence conflicti3737 – 37371A → S in CAA40279. (PubMed:1830053)Curated
Sequence conflicti3737 – 37371A → S in CAB42644. (PubMed:8253844)Curated
Sequence conflicti3955 – 39562NN → SM in AC093879. (PubMed:15815621)Curated

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. 1 PublicationVSP_037057Add
BLAST
Alternative sequencei1 – 2727MMNED…RKRPK → MTTMLQ in isoform 4. 1 PublicationVSP_037058Add
BLAST
Alternative sequencei967 – 9671G → GRASPCLERDNSS in isoform 4. 1 PublicationVSP_037059
Alternative sequencei1477 – 35612085Missing in isoform 2, isoform 4 and isoform 5. 3 PublicationsVSP_000268Add
BLAST
Alternative sequencei3870 – 38701K → KELTEELGELEASSDEEAMV TTRVVRRRVIIQ in isoform 5. 1 PublicationVSP_037060

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. 14 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.
GeneTreei ENSGT00760000118950.
HOGENOMi HOG000169277.
HOVERGENi HBG100442.
InParanoidi Q01484.
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

Bgeei Q01484.
CleanExi HS_ANK2.
ExpressionAtlasi Q01484. baseline and differential.
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_dom.
[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: October 29, 2014
This is version 156 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