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Q01484

- ANK2_HUMAN

UniProt

Q01484 - ANK2_HUMAN

Protein

Ankyrin-2

Gene

ANK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 155 (01 Oct 2014)
      Sequence version 4 (16 May 2012)
      Previous versions | rss
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    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 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

    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. 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

    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.
    Mutagenesisi1000 – 10001A → P: Prevents binding to SPTBN1. 1 Publication
    Mutagenesisi1100 – 11034ENGD → AAGA: Weak binding to SPTBN1.

    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

    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.By similarity3 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.
    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.
    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.

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    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

    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. 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

    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 1, 2014
    This is version 155 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