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P16157

- ANK1_HUMAN

UniProt

P16157 - ANK1_HUMAN

Protein

Ankyrin-1

Gene

ANK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 171 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes anion exchange protein; they retain most or all of these binding functions.1 Publication
    Isoform Mu17 together with obscurin in skeletal muscle may provide a molecular link between the sarcoplasmic reticulum and myofibrils.1 Publication

    GO - Molecular functioni

    1. ATPase binding Source: BHF-UCL
    2. cytoskeletal adaptor activity Source: UniProtKB
    3. enzyme binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. spectrin binding Source: UniProtKB
    6. structural constituent of cytoskeleton Source: ProtInc
    7. structural molecule activity Source: UniProtKB

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. cytoskeleton organization Source: UniProtKB
    3. ER to Golgi vesicle-mediated transport Source: BHF-UCL
    4. erythrocyte development Source: Ensembl
    5. exocytosis Source: UniProtKB
    6. maintenance of epithelial cell apical/basal polarity Source: UniProtKB
    7. monovalent inorganic cation transport Source: Ensembl
    8. porphyrin-containing compound biosynthetic process Source: Ensembl
    9. positive regulation of organelle organization Source: Ensembl
    10. protein targeting to plasma membrane Source: BHF-UCL
    11. signal transduction Source: InterPro

    Enzyme and pathway databases

    ReactomeiREACT_22266. Interaction between L1 and Ankyrins.
    REACT_22292. CHL1 interactions.
    REACT_22312. Neurofascin interactions.
    REACT_22329. NrCAM interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ankyrin-1
    Short name:
    ANK-1
    Alternative name(s):
    Ankyrin-R
    Erythrocyte ankyrin
    Gene namesi
    Name:ANK1
    Synonyms:ANK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:492. ANK1.

    Subcellular locationi

    Isoform Er1 : Cytoplasmcytoskeleton
    Note: Probably the other erythrocyte (Er) isoforms, are located near the surface of erythrocytic plasma membrane.
    Isoform Mu17 : Membrane. CytoplasmmyofibrilsarcomereM line
    Note: Colocalizes with OBSCN isoform 3/obscurin at the M line in differentiated skeletal muscle cells.

    GO - Cellular componenti

    1. axolemma Source: Ensembl
    2. basolateral plasma membrane Source: UniProtKB
    3. cortical cytoskeleton Source: Ensembl
    4. cytoskeleton Source: UniProtKB
    5. cytosol Source: Reactome
    6. M band Source: UniProtKB-SubCell
    7. nucleus Source: Ensembl
    8. plasma membrane Source: UniProtKB
    9. postsynaptic membrane Source: Ensembl
    10. sarcolemma Source: Ensembl
    11. sarcoplasmic reticulum Source: UniProtKB-SubCell
    12. spectrin-associated cytoskeleton Source: BHF-UCL
    13. Z disc Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Membrane, Sarcoplasmic reticulum

    Pathology & Biotechi

    Involvement in diseasei

    Spherocytosis 1 (SPH1) [MIM:182900]: Spherocytosis is a hematologic disorder leading to chronic hemolytic anemia and characterized by numerous abnormally shaped erythrocytes which are generally spheroidal. SPH1 is characterized by severe hemolytic anemia. Inheritance is autosomal recessive.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti276 – 2761L → R in SPH1. 1 Publication
    VAR_054991
    Natural varianti463 – 4631V → I in SPH1. 1 Publication
    VAR_000596
    Natural varianti1054 – 10541I → T in SPH1. 1 Publication
    VAR_054992

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1824 – 18241T → P: Abolishes interaction with OBSCN (in isoform Mu17). 1 Publication
    Mutagenesisi1826 – 18261K → E: Abolishes interaction with OBSCN (in isoform Mu17). 1 Publication
    Mutagenesisi1829 – 18291R → G: Abolishes interaction with OBSCN (in isoform Mu17). 1 Publication
    Mutagenesisi1830 – 18301K → E: Abolishes interaction with OBSCN (in isoform Mu17). 1 Publication

    Keywords - Diseasei

    Disease mutation, Elliptocytosis, Hereditary hemolytic anemia

    Organism-specific databases

    MIMi182900. phenotype.
    Orphaneti251066. 8p11.2 deletion syndrome.
    822. Hereditary spherocytosis.
    PharmGKBiPA24798.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 18811881Ankyrin-1PRO_0000066883Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei105 – 1051(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
    Modified residuei233 – 2331(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
    Modified residuei431 – 4311(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
    Modified residuei464 – 4641(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
    Modified residuei629 – 6291(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
    Modified residuei662 – 6621(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
    Modified residuei695 – 6951(3S)-3-hydroxyaspartate; by HIF1AN; partial1 Publication
    Modified residuei728 – 7281(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
    Modified residuei761 – 7611(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
    Modified residuei856 – 8561PhosphoserineBy similarity
    Modified residuei961 – 9611PhosphothreonineBy similarity
    Modified residuei1073 – 10731PhosphotyrosineBy similarity
    Modified residuei1392 – 13921PhosphoserineBy similarity

    Post-translational modificationi

    Regulated by phosphorylation.
    Palmitoylated.
    Hydroxylated by HIF1AN at several asparagine and 1 aspartate residue within ANK repeat region. Hydroxylation seems to increase the conformational stability of this region and may also modulate protein-protein interactions mediated by the ANK repeat region.1 Publication

    Keywords - PTMi

    Hydroxylation, Lipoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP16157.
    PaxDbiP16157.
    PRIDEiP16157.

    PTM databases

    PhosphoSiteiP16157.

    Miscellaneous databases

    PMAP-CutDBP16157.

    Expressioni

    Tissue specificityi

    Isoform Mu17, isoform Mu18, isoform Mu19 and isoform Mu20 are expressed in skeletal muscle. Isoform Br21 is expressed in brain.1 Publication

    Gene expression databases

    ArrayExpressiP16157.
    BgeeiP16157.
    CleanExiHS_ANK1.
    GenevestigatoriP16157.

    Organism-specific databases

    HPAiCAB016057.
    HPA004842.
    HPA056953.

    Interactioni

    Subunit structurei

    Interacts with a number of integral membrane proteins and cytoskeletal proteins. Interacts (via N-terminus) with SPTB/spectrin (beta chain). Interacts (via N-terminus ANK repeats) with SLC4A1/erythrocyte membrane protein band 3 (via cytoplasmic N-terminus). Also interacts with TTN/titin. Isoform Mu17 interacts with OBSCN isoform 3/obscurin. Interacts with HIF1AN.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    OBSCNQ5VST9-38EBI-941819,EBI-941921

    Protein-protein interaction databases

    BioGridi106783. 17 interactions.
    IntActiP16157. 1 interaction.
    MINTiMINT-254860.
    STRINGi9606.ENSP00000265709.

    Structurei

    Secondary structure

    1
    1881
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi407 – 4148
    Helixi417 – 4259
    Beta strandi433 – 4353
    Helixi440 – 4478
    Helixi450 – 45910
    Helixi473 – 4808
    Helixi483 – 49210
    Helixi506 – 5138
    Helixi516 – 5249
    Helixi539 – 5457
    Helixi549 – 5579
    Helixi572 – 5787
    Helixi582 – 5887
    Helixi589 – 5913
    Helixi605 – 6117
    Helixi615 – 6239
    Helixi638 – 6447
    Helixi648 – 6558
    Turni656 – 6583
    Helixi671 – 6788
    Helixi681 – 69010
    Helixi704 – 7107
    Helixi715 – 7228
    Helixi737 – 7437
    Helixi747 – 7559
    Beta strandi765 – 7673
    Helixi770 – 7767
    Helixi780 – 78910
    Beta strandi914 – 9196
    Beta strandi924 – 9274
    Turni930 – 9323
    Beta strandi935 – 9384
    Beta strandi942 – 9454
    Beta strandi947 – 9548
    Helixi956 – 9583
    Beta strandi959 – 9613
    Beta strandi970 – 9734
    Beta strandi975 – 9806
    Beta strandi984 – 99411
    Beta strandi1000 – 10034
    Beta strandi1006 – 101510
    Beta strandi1018 – 10203
    Helixi1026 – 10283
    Helixi1029 – 10335
    Helixi1043 – 10497
    Beta strandi1051 – 10588
    Beta strandi1061 – 10677
    Beta strandi1074 – 10763
    Beta strandi1081 – 10844
    Beta strandi1092 – 10954
    Beta strandi1099 – 11024
    Beta strandi1104 – 11118
    Helixi1115 – 11228
    Beta strandi1131 – 11388
    Beta strandi1140 – 115011
    Helixi1153 – 11575
    Beta strandi1165 – 11673
    Beta strandi1169 – 11757
    Beta strandi1195 – 11973
    Beta strandi1200 – 12078
    Beta strandi1210 – 12156
    Helixi1219 – 12213
    Helixi1222 – 123211
    Turni1398 – 14025
    Helixi1403 – 141412
    Helixi1415 – 14173
    Helixi1418 – 14247
    Helixi1429 – 143810
    Helixi1443 – 145816
    Helixi1459 – 14613
    Helixi1464 – 147310
    Helixi1477 – 14837

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1N11X-ray2.70A402-827[»]
    2YQFNMR-A1394-1497[»]
    2YVIX-ray1.92A1394-1497[»]
    3F59X-ray2.00A/B/C/D911-1068[»]
    3KBTX-ray2.75C/D911-1068[»]
    3KBUX-ray2.75C/D911-1068[»]
    3UD1X-ray2.00A/B/C911-1233[»]
    3UD2X-ray2.21A/B/C911-1233[»]
    ProteinModelPortaliP16157.
    SMRiP16157. Positions 5-812, 911-1497.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP16157.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati44 – 7330ANK 1Add
    BLAST
    Repeati77 – 10630ANK 2Add
    BLAST
    Repeati110 – 13930ANK 3Add
    BLAST
    Repeati143 – 17230ANK 4Add
    BLAST
    Repeati174 – 20128ANK 5Add
    BLAST
    Repeati205 – 23430ANK 6Add
    BLAST
    Repeati238 – 26730ANK 7Add
    BLAST
    Repeati271 – 30030ANK 8Add
    BLAST
    Repeati304 – 33330ANK 9Add
    BLAST
    Repeati337 – 36630ANK 10Add
    BLAST
    Repeati370 – 39930ANK 11Add
    BLAST
    Repeati403 – 43230ANK 12Add
    BLAST
    Repeati436 – 46530ANK 13Add
    BLAST
    Repeati469 – 49830ANK 14Add
    BLAST
    Repeati502 – 53130ANK 15Add
    BLAST
    Repeati535 – 56430ANK 16Add
    BLAST
    Repeati568 – 59730ANK 17Add
    BLAST
    Repeati601 – 63030ANK 18Add
    BLAST
    Repeati634 – 66330ANK 19Add
    BLAST
    Repeati667 – 69630ANK 20Add
    BLAST
    Repeati700 – 72930ANK 21Add
    BLAST
    Repeati733 – 76230ANK 22Add
    BLAST
    Repeati766 – 79530ANK 23Add
    BLAST
    Domaini911 – 1066156ZU5 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1067 – 1233167ZU5 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1403 – 148785DeathPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 82782789 kDa domainAdd
    BLAST
    Regioni1234 – 1362129UPA domainBy similarityAdd
    BLAST
    Regioni1383 – 188149955 kDa regulatory domainAdd
    BLAST

    Domaini

    The 55 kDa regulatory domain is involved in regulating binding of SPTB/spectrin (beta chain) and SLC4A1/erythrocyte membrane protein band 3.
    The ANK repeat region forms a spiral around a large central cavity and is involved in binding of ion transporters.
    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 By similarity.By similarity

    Sequence similaritiesi

    Contains 23 ANK repeats.PROSITE-ProRule annotation
    Contains 1 death domain.PROSITE-ProRule annotation
    Contains 2 ZU5 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    ANK repeat, Repeat

    Phylogenomic databases

    eggNOGiCOG0666.
    HOVERGENiHBG004234.
    KOiK10380.
    OMAiRLCQDYD.
    OrthoDBiEOG7P02H2.
    PhylomeDBiP16157.
    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. 20 hits.
    PF00531. Death. 1 hit.
    PF00791. ZU5. 1 hit.
    [Graphical view]
    PRINTSiPR01415. ANKYRIN.
    SMARTiSM00248. ANK. 23 hits.
    SM00005. DEATH. 1 hit.
    SM00218. ZU5. 1 hit.
    [Graphical view]
    SUPFAMiSSF47986. SSF47986. 1 hit.
    SSF48403. SSF48403. 2 hits.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 20 hits.
    PS50017. DEATH_DOMAIN. 1 hit.
    PS51145. ZU5. 1 hit.
    [Graphical view]

    Sequences (23)i

    Sequence statusi: Complete.

    This entry describes 23 isoformsi produced by alternative promoter usage and alternative splicing. Align

    Isoform Er1 (identifier: P16157-1) [UniParc]FASTAAdd to Basket

    Also known as: 1, 2.1

    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.

    « Hide

    MPYSVGFREA DAATSFLRAA RSGNLDKALD HLRNGVDINT CNQNGLNGLH     50
    LASKEGHVKM VVELLHKEII LETTTKKGNT ALHIAALAGQ DEVVRELVNY 100
    GANVNAQSQK GFTPLYMAAQ ENHLEVVKFL LENGANQNVA TEDGFTPLAV 150
    ALQQGHENVV AHLINYGTKG KVRLPALHIA ARNDDTRTAA VLLQNDPNPD 200
    VLSKTGFTPL HIAAHYENLN VAQLLLNRGA SVNFTPQNGI TPLHIASRRG 250
    NVIMVRLLLD RGAQIETKTK DELTPLHCAA RNGHVRISEI LLDHGAPIQA 300
    KTKNGLSPIH MAAQGDHLDC VRLLLQYDAE IDDITLDHLT PLHVAAHCGH 350
    HRVAKVLLDK GAKPNSRALN GFTPLHIACK KNHVRVMELL LKTGASIDAV 400
    TESGLTPLHV ASFMGHLPIV KNLLQRGASP NVSNVKVETP LHMAARAGHT 450
    EVAKYLLQNK AKVNAKAKDD QTPLHCAARI GHTNMVKLLL ENNANPNLAT 500
    TAGHTPLHIA AREGHVETVL ALLEKEASQA CMTKKGFTPL HVAAKYGKVR 550
    VAELLLERDA HPNAAGKNGL TPLHVAVHHN NLDIVKLLLP RGGSPHSPAW 600
    NGYTPLHIAA KQNQVEVARS LLQYGGSANA ESVQGVTPLH LAAQEGHAEM 650
    VALLLSKQAN GNLGNKSGLT PLHLVAQEGH VPVADVLIKH GVMVDATTRM 700
    GYTPLHVASH YGNIKLVKFL LQHQADVNAK TKLGYSPLHQ AAQQGHTDIV 750
    TLLLKNGASP NEVSSDGTTP LAIAKRLGYI SVTDVLKVVT DETSFVLVSD 800
    KHRMSFPETV DEILDVSEDE GEELISFKAE RRDSRDVDEE KELLDFVPKL 850
    DQVVESPAIP RIPCAMPETV VIRSEEQEQA SKEYDEDSLI PSSPATETSD 900
    NISPVASPVH TGFLVSFMVD ARGGSMRGSR HNGLRVVIPP RTCAAPTRIT 950
    CRLVKPQKLS TPPPLAEEEG LASRIIALGP TGAQFLSPVI VEIPHFASHG 1000
    RGDRELVVLR SENGSVWKEH RSRYGESYLD QILNGMDEEL GSLEELEKKR 1050
    VCRIITTDFP LYFVIMSRLC QDYDTIGPEG GSLKSKLVPL VQATFPENAV 1100
    TKRVKLALQA QPVPDELVTK LLGNQATFSP IVTVEPRRRK FHRPIGLRIP 1150
    LPPSWTDNPR DSGEGDTTSL RLLCSVIGGT DQAQWEDITG TTKLVYANEC 1200
    ANFTTNVSAR FWLSDCPRTA EAVNFATLLY KELTAVPYMA KFVIFAKMND 1250
    PREGRLRCYC MTDDKVDKTL EQHENFVEVA RSRDIEVLEG MSLFAELSGN 1300
    LVPVKKAAQQ RSFHFQSFRE NRLAMPVKVR DSSREPGGSL SFLRKAMKYE 1350
    DTQHILCHLN ITMPPCAKGS GAEDRRRTPT PLALRYSILS ESTPGSLSGT 1400
    EQAEMKMAVI SEHLGLSWAE LARELQFSVE DINRIRVENP NSLLEQSVAL 1450
    LNLWVIREGQ NANMENLYTA LQSIDRGEIV NMLEGSGRQS RNLKPDRRHT 1500
    DRDYSLSPSQ MNGYSSLQDE LLSPASLGCA LSSPLRADQY WNEVAVLDAI 1550
    PLAATEHDTM LEMSDMQVWS AGLTPSLVTA EDSSLECSKA EDSDATGHEW 1600
    KLEGALSEEP RGPELGSLEL VEDDTVDSDA TNGLIDLLEQ EEGQRSEEKL 1650
    PGSKRQDDAT GAGQDSENEV SLVSGHQRGQ ARITHSPTVS QVTERSQDRL 1700
    QDWDADGSIV SYLQDAAQGS WQEEVTQGPH SFQGTSTMTE GLEPGGSQEY 1750
    EKVLVSVSEH TWTEQPEAES SQADRDRRQQ GQEEQVQEAK NTFTQVVQGN 1800
    EFQNIPGEQV TEEQFTDEQG NIVTKKIIRK VVRQIDLSSA DAAQEHEEVT 1850
    VEGPLEDPSE LEVDIDYFMK HSKDHTSTPN P 1881

    Note: Major erythrocyte-specific isoform. Produced by alternative promoter usage.

    Length:1,881
    Mass (Da):206,265
    Last modified:January 23, 2007 - v3
    Checksum:i49466F6F915019EC
    GO
    Isoform Er2 (identifier: P16157-4) [UniParc]FASTAAdd to Basket

    Also known as: 2, 2.2

    The sequence of this isoform differs from the canonical sequence as follows:
         1514-1675: Missing.

    Note: Predominant form of minor erythrocyte-specific isoforms. Produced by alternative splicing of isoform Er1.

    Show »
    Length:1,719
    Mass (Da):188,999
    Checksum:i407D614678AF8EE0
    GO
    Isoform Er3 (identifier: P16157-5) [UniParc]FASTAAdd to Basket

    Also known as: 3

    The sequence of this isoform differs from the canonical sequence as follows:
         1849-1873: Missing.

    Note: Produced by alternative splicing of isoform Er1.

    Show »
    Length:1,856
    Mass (Da):203,405
    Checksum:iFEC7837B2E7711B8
    GO
    Isoform Er4 (identifier: P16157-6) [UniParc]FASTAAdd to Basket

    Also known as: 4

    The sequence of this isoform differs from the canonical sequence as follows:
         1514-1675: Missing.
         1849-1873: Missing.

    Note: Produced by alternative splicing of isoform Er1.

    Show »
    Length:1,694
    Mass (Da):186,139
    Checksum:iBB17E7510AE1067A
    GO
    Isoform Er5 (identifier: P16157-3) [UniParc]FASTAAdd to Basket

    Also known as: 5

    The sequence of this isoform differs from the canonical sequence as follows:
         1850-1881: TVEGPLEDPSELEVDIDYFMKHSKDHTSTPNP → ELRGSGLQPDLIEGRKGAQIVKRASLKRGKQ

    Note: Produced by alternative splicing of isoform Er1.

    Show »
    Length:1,880
    Mass (Da):206,026
    Checksum:i3153959168D8D91D
    GO
    Isoform Er6 (identifier: P16157-7) [UniParc]FASTAAdd to Basket

    Also known as: 6

    The sequence of this isoform differs from the canonical sequence as follows:
         1514-1675: Missing.
         1850-1881: TVEGPLEDPSELEVDIDYFMKHSKDHTSTPNP → ELRGSGLQPDLIEGRKGAQIVKRASLKRGKQ

    Note: Produced by alternative splicing of isoform Er1.

    Show »
    Length:1,718
    Mass (Da):188,760
    Checksum:i9A5DBC78974FD512
    GO
    Isoform Er7 (identifier: P16157-8) [UniParc]FASTAAdd to Basket

    Also known as: 7

    The sequence of this isoform differs from the canonical sequence as follows:
         1827-1873: Missing.

    Note: Produced by alternative splicing of isoform Er1.

    Show »
    Length:1,834
    Mass (Da):200,915
    Checksum:iB3735FA102F08B3D
    GO
    Isoform Er8 (identifier: P16157-9) [UniParc]FASTAAdd to Basket

    Also known as: 8

    The sequence of this isoform differs from the canonical sequence as follows:
         1514-1675: Missing.
         1827-1873: Missing.

    Show »
    Length:1,672
    Mass (Da):183,649
    Checksum:i195930085EF487B7
    GO
    Isoform Er9 (identifier: P16157-10) [UniParc]FASTAAdd to Basket

    Also known as: 9

    The sequence of this isoform differs from the canonical sequence as follows:
         1799-1873: Missing.

    Note: Produced by alternative splicing of isoform Er1.

    Show »
    Length:1,806
    Mass (Da):197,752
    Checksum:iA50828175CF6AD01
    GO
    Isoform Er10 (identifier: P16157-11) [UniParc]FASTAAdd to Basket

    Also known as: 10

    The sequence of this isoform differs from the canonical sequence as follows:
         1514-1675: Missing.
         1799-1873: Missing.

    Note: Produced by alternative splicing of isoform Er1.

    Show »
    Length:1,644
    Mass (Da):180,487
    Checksum:i21DC6E7730722E51
    GO
    Isoform Er11 (identifier: P16157-12) [UniParc]FASTAAdd to Basket

    Also known as: 11

    The sequence of this isoform differs from the canonical sequence as follows:
         1874-1881: DHTSTPNP → VELRGSGLQPDLIEGRKGAQIVKRASLKRGKQ

    Note: Produced by alternative splicing of isoform Er1.

    Show »
    Length:1,905
    Mass (Da):208,886
    Checksum:i22CA0F47329C69FA
    GO
    Isoform Er12 (identifier: P16157-13) [UniParc]FASTAAdd to Basket

    Also known as: 12

    The sequence of this isoform differs from the canonical sequence as follows:
         1514-1675: Missing.
         1874-1881: DHTSTPNP → VELRGSGLQPDLIEGRKGAQIVKRASLKRGKQ

    Note: Produced by alternative splicing of isoform Er1.

    Show »
    Length:1,743
    Mass (Da):191,620
    Checksum:iAA2C9A6353D00A2C
    GO
    Isoform Er13 (identifier: P16157-14) [UniParc]FASTAAdd to Basket

    Also known as: 13

    The sequence of this isoform differs from the canonical sequence as follows:
         1874-1881: DHTSTPNP → VLRRPRPWGT...KRASLKRGKQ

    Note: Produced by alternative splicing of isoform Er1.

    Show »
    Length:1,983
    Mass (Da):217,479
    Checksum:i94434C72B761D98D
    GO
    Isoform Er14 (identifier: P16157-15) [UniParc]FASTAAdd to Basket

    Also known as: 14

    The sequence of this isoform differs from the canonical sequence as follows:
         1514-1675: Missing.
         1874-1881: DHTSTPNP → VLRRPRPWGT...KRASLKRGKQ

    Note: Produced by alternative splicing of isoform Er1.

    Show »
    Length:1,821
    Mass (Da):200,214
    Checksum:i748E485DAAC8FAAC
    GO
    Isoform Er15 (identifier: P16157-16) [UniParc]FASTAAdd to Basket

    Also known as: 15

    The sequence of this isoform differs from the canonical sequence as follows:
         1827-1881: IIRKVVRQID...SKDHTSTPNP → VELRGSGLQPDLIEGRKGAQIVKRASLKRGKQ

    Note: Produced by alternative splicing of isoform Er1.

    Show »
    Length:1,858
    Mass (Da):203,536
    Checksum:i1DFB26BFA488DCC4
    GO
    Isoform Er16 (identifier: P16157-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1513-1874: Missing.
         1875-1875: H → D

    Note: Produced by alternative splicing of isoform Er1.

    Show »
    Length:1,519
    Mass (Da):166,480
    Checksum:i1D71CA896F1FDD7F
    GO
    Isoform Mu17 (identifier: P16157-17) [UniParc]FASTAAdd to Basket

    Also known as: ank1.5, muscle-specific 1

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1725: Missing.
         1726-1798: TQGPHSFQGT...AKNTFTQVVQ → MWTFVTQLLV...RVVRRRVFLK
         1850-1881: TVEGPLEDPSELEVDIDYFMKHSKDHTSTPNP → ELRGSGLQPDLIEGRKGAQIVKRASLKRGKQ

    Note: Produced by alternative promoter usage.Curated

    Show »
    Length:155
    Mass (Da):17,615
    Checksum:i55C5EA3888044FFB
    GO
    Isoform Mu18 (identifier: P16157-18) [UniParc]FASTAAdd to Basket

    Also known as: ank1.6, muscle-specific 2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1725: Missing.
         1726-1798: TQGPHSFQGT...AKNTFTQVVQ → MWTFVTQLLV...RVVRRRVFLK
         1827-1881: IIRKVVRQID...SKDHTSTPNP → VELRGSGLQPDLIEGRKGAQIVKRASLKRGKQ

    Note: Produced by alternative splicing of isoform Mu17.

    Show »
    Length:133
    Mass (Da):15,125
    Checksum:iC987D8EF586B6704
    GO
    Isoform Mu19 (identifier: P16157-19) [UniParc]FASTAAdd to Basket

    Also known as: muscle-specific 3

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1725: Missing.
         1726-1798: TQGPHSFQGT...AKNTFTQVVQ → MWTFVTQLLV...RVVRRRVFLK
         1799-1873: Missing.

    Note: Produced by alternative splicing of isoform Mu17.

    Show »
    Length:81
    Mass (Da):9,342
    Checksum:i6A4EA54308E3B04B
    GO
    Isoform Mu20 (identifier: P16157-20) [UniParc]FASTAAdd to Basket

    Also known as: muscle-specific 4

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1725: Missing.
         1726-1798: TQGPHSFQGT...AKNTFTQVVQ → MWTFVTQLLV...LCFVLKHIHQ
         1799-1881: GNEFQNIPGE...SKDHTSTPNP → VELRGSGLQPDLIEGRKGAQIVKRASLKRGKQ

    Note: Produced by alternative splicing of isoform Mu17.

    Show »
    Length:74
    Mass (Da):8,374
    Checksum:iFA79EF4284FBDDEB
    GO
    Isoform Br21 (identifier: P16157-21) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-9: MPYSVGFRE → MAQAAKQLKKIKDIEAQALQEQKEKEESNRKRRNRSRDRKKK
         820-820: E → EGTAHITIM
         1849-1873: Missing.

    Note: No experimental confirmation available. Produced by alternative splicing of isoform Er1.

    Show »
    Length:1,897
    Mass (Da):208,239
    Checksum:i82682973D1A52BA2
    GO
    Isoform 22 (identifier: P16157-22) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1725: Missing.
         1726-1798: TQGPHSFQGT...AKNTFTQVVQ → MWTFVTQLLV...RVVRRRVFLK
         1826-1872: Missing.

    Note: Produced by alternative splicing.

    Show »
    Length:109
    Mass (Da):12,504
    Checksum:iCA36067BFBD7B9A4
    GO
    Isoform 23 (identifier: P16157-23) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1725: Missing.
         1726-1798: TQGPHSFQGT...AKNTFTQVVQ → MWTFVTQLLV...RVVRRRVFLK

    Show »
    Length:156
    Mass (Da):17,854
    Checksum:iCE82F91038B0C57A
    GO

    Sequence cautioni

    The sequence AAB47805.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti230 – 2301A → S in AAA51732. (PubMed:1689849)Curated
    Sequence conflicti801 – 8011K → L in AAB47805. (PubMed:9235914)Curated
    Sequence conflicti845 – 8451D → R AA sequence (PubMed:2137557)Curated
    Sequence conflicti902 – 9021I → T in AAB47805. (PubMed:9235914)Curated
    Isoform Mu17 (identifier: P16157-17)
    Sequence conflicti63 – 631T → P in AAC01950. (PubMed:9430667)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti21 – 211R → T.
    VAR_000595
    Natural varianti276 – 2761L → R in SPH1. 1 Publication
    VAR_054991
    Natural varianti332 – 3321D → H in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035605
    Natural varianti463 – 4631V → I in SPH1. 1 Publication
    VAR_000596
    Natural varianti619 – 6191R → H in Brueggen.
    Corresponds to variant rs2304877 [ dbSNP | Ensembl ].
    VAR_000597
    Natural varianti733 – 7331L → I.
    Corresponds to variant rs11778936 [ dbSNP | Ensembl ].
    VAR_028769
    Natural varianti750 – 7501V → A.1 Publication
    VAR_000598
    Natural varianti832 – 8321R → Q.
    Corresponds to variant rs34523608 [ dbSNP | Ensembl ].
    VAR_061012
    Natural varianti845 – 8451D → E.
    VAR_000599
    Natural varianti991 – 9911V → L.1 Publication
    VAR_026411
    Natural varianti1054 – 10541I → T in SPH1. 1 Publication
    VAR_054992
    Natural varianti1075 – 10751T → I.4 Publications
    Corresponds to variant rs35213384 [ dbSNP | Ensembl ].
    VAR_048263
    Natural varianti1126 – 11261A → P.
    Corresponds to variant rs504465 [ dbSNP | Ensembl ].
    VAR_028770
    Natural varianti1192 – 11921T → P.
    Corresponds to variant rs486770 [ dbSNP | Ensembl ].
    VAR_028771
    Natural varianti1286 – 12861E → D.1 Publication
    VAR_000601
    Natural varianti1325 – 13251M → V.
    Corresponds to variant rs10093583 [ dbSNP | Ensembl ].
    VAR_028772
    Natural varianti1392 – 13921S → T.
    VAR_000600
    Natural varianti1546 – 15461V → I.1 Publication
    Corresponds to variant rs1060130 [ dbSNP | Ensembl ].
    VAR_028773
    Natural varianti1592 – 15921D → N in Duesseldorf.
    VAR_000602

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 17251725Missing in isoform Mu17, isoform Mu18, isoform Mu19, isoform Mu20, isoform 22 and isoform 23. 2 PublicationsVSP_018440Add
    BLAST
    Alternative sequencei1 – 99MPYSVGFRE → MAQAAKQLKKIKDIEAQALQ EQKEKEESNRKRRNRSRDRK KK in isoform Br21. 1 PublicationVSP_018439
    Alternative sequencei820 – 8201E → EGTAHITIM in isoform Br21. 1 PublicationVSP_018441
    Alternative sequencei1513 – 1874362Missing in isoform Er16. 1 PublicationVSP_000264Add
    BLAST
    Alternative sequencei1514 – 1675162Missing in isoform Er2, isoform Er4, isoform Er6, isoform Er8, isoform Er10, isoform Er12 and isoform Er14. 1 PublicationVSP_018442Add
    BLAST
    Alternative sequencei1726 – 179873TQGPH…TQVVQ → MWTFVTQLLVTLVLLSFFLV SCQNVMHIVRGSLCFVLKHI HQELDKELGESEGLSDDEET ISTRVVRRRVFLK in isoform Mu17, isoform Mu18, isoform Mu19, isoform 22 and isoform 23. 2 PublicationsVSP_018443Add
    BLAST
    Alternative sequencei1726 – 179873TQGPH…TQVVQ → MWTFVTQLLVTLVLLSFFLV SCQNVMHIVRGSLCFVLKHI HQ in isoform Mu20. 1 PublicationVSP_018444Add
    BLAST
    Alternative sequencei1799 – 188183GNEFQ…STPNP → VELRGSGLQPDLIEGRKGAQ IVKRASLKRGKQ in isoform Mu20. 1 PublicationVSP_018446Add
    BLAST
    Alternative sequencei1799 – 187375Missing in isoform Er9, isoform Er10 and isoform Mu19. 1 PublicationVSP_018445Add
    BLAST
    Alternative sequencei1826 – 187247Missing in isoform 22. 1 PublicationVSP_045439Add
    BLAST
    Alternative sequencei1827 – 188155IIRKV…STPNP → VELRGSGLQPDLIEGRKGAQ IVKRASLKRGKQ in isoform Er15 and isoform Mu18. 1 PublicationVSP_018448Add
    BLAST
    Alternative sequencei1827 – 187347Missing in isoform Er7 and isoform Er8. CuratedVSP_018447Add
    BLAST
    Alternative sequencei1849 – 187325Missing in isoform Er3, isoform Er4 and isoform Br21. 1 PublicationVSP_018449Add
    BLAST
    Alternative sequencei1850 – 188132TVEGP…STPNP → ELRGSGLQPDLIEGRKGAQI VKRASLKRGKQ in isoform Er5, isoform Er6 and isoform Mu17. 3 PublicationsVSP_000266Add
    BLAST
    Alternative sequencei1874 – 18818DHTSTPNP → VELRGSGLQPDLIEGRKGAQ IVKRASLKRGKQ in isoform Er11 and isoform Er12. CuratedVSP_018450
    Alternative sequencei1874 – 18818DHTSTPNP → VLRRPRPWGTQRHHCCLALP GRLHDTSLHSPLYELSLQSL FSLVGSVSAPPCRSFRSSAC VLPVFAICPAFCLCCCLQVE LRGSGLQPDLIEGRKGAQIV KRASLKRGKQ in isoform Er13 and isoform Er14. CuratedVSP_018451
    Alternative sequencei1875 – 18751H → D in isoform Er16. 1 PublicationVSP_000265

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16609 mRNA. Translation: CAA34610.1.
    X16609 mRNA. Translation: CAA34611.1.
    M28880 mRNA. Translation: AAA51732.1.
    U50133
    , U50092, U50093, U50094, U50095, U50096, U50097, U50098, U50099, U50100, U50101, U50102, U50103, U50104, U50105, U50106, U50107, U50108, U50109, U50110, U50111, U50112, U50113, U50114, U50115, U50116, U50117, U50118, U50119, U50120, U50121, U50122, U50123, U50124, U50125, U50126, U50127, U50128, U50129, U50130, U50131, U50132 Genomic DNA. Translation: AAB47805.1. Sequence problems.
    AF005213 mRNA. Translation: AAC01950.1.
    AB209418 mRNA. Translation: BAD92655.1.
    AK223578 mRNA. Translation: BAD97298.1.
    AC027702 Genomic DNA. No translation available.
    AC113133 Genomic DNA. No translation available.
    CH471080 Genomic DNA. Translation: EAW63243.1.
    CH471080 Genomic DNA. Translation: EAW63244.1.
    BC030957 mRNA. Translation: AAH30957.1.
    BC117121 mRNA. Translation: AAI17122.1.
    BC014467 mRNA. No translation available.
    CCDSiCCDS47849.1. [P16157-21]
    CCDS55227.1. [P16157-23]
    CCDS6119.1. [P16157-1]
    CCDS6120.1. [P16157-22]
    CCDS6121.1. [P16157-3]
    CCDS6122.1. [P16157-17]
    PIRiA35049.
    S08275. SJHUK.
    RefSeqiNP_000028.3. NM_000037.3. [P16157-3]
    NP_001135917.1. NM_001142445.1. [P16157-23]
    NP_001135918.1. NM_001142446.1. [P16157-21]
    NP_065208.2. NM_020475.2. [P16157-5]
    NP_065209.2. NM_020476.2. [P16157-1]
    NP_065210.2. NM_020477.2. [P16157-4]
    NP_065211.2. NM_020478.4. [P16157-17]
    NP_065213.2. NM_020480.4. [P16157-22]
    UniGeneiHs.654438.
    Hs.667377.
    Hs.708861.

    Genome annotation databases

    EnsembliENST00000265709; ENSP00000265709; ENSG00000029534. [P16157-21]
    ENST00000289734; ENSP00000289734; ENSG00000029534. [P16157-3]
    ENST00000314214; ENSP00000319123; ENSG00000029534. [P16157-17]
    ENST00000347528; ENSP00000339620; ENSG00000029534. [P16157-1]
    ENST00000348036; ENSP00000297744; ENSG00000029534. [P16157-22]
    ENST00000522543; ENSP00000430368; ENSG00000029534. [P16157-23]
    GeneIDi286.
    KEGGihsa:286.
    UCSCiuc003xod.3. human.
    uc003xof.3. human.
    uc003xoi.3. human. [P16157-3]
    uc003xoj.3. human. [P16157-5]
    uc003xok.3. human. [P16157-1]
    uc003xol.3. human. [P16157-4]
    uc003xom.3. human. [P16157-21]

    Polymorphism databases

    DMDMi116241246.

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Ankyrin entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X16609 mRNA. Translation: CAA34610.1 .
    X16609 mRNA. Translation: CAA34611.1 .
    M28880 mRNA. Translation: AAA51732.1 .
    U50133
    , U50092 , U50093 , U50094 , U50095 , U50096 , U50097 , U50098 , U50099 , U50100 , U50101 , U50102 , U50103 , U50104 , U50105 , U50106 , U50107 , U50108 , U50109 , U50110 , U50111 , U50112 , U50113 , U50114 , U50115 , U50116 , U50117 , U50118 , U50119 , U50120 , U50121 , U50122 , U50123 , U50124 , U50125 , U50126 , U50127 , U50128 , U50129 , U50130 , U50131 , U50132 Genomic DNA. Translation: AAB47805.1 . Sequence problems.
    AF005213 mRNA. Translation: AAC01950.1 .
    AB209418 mRNA. Translation: BAD92655.1 .
    AK223578 mRNA. Translation: BAD97298.1 .
    AC027702 Genomic DNA. No translation available.
    AC113133 Genomic DNA. No translation available.
    CH471080 Genomic DNA. Translation: EAW63243.1 .
    CH471080 Genomic DNA. Translation: EAW63244.1 .
    BC030957 mRNA. Translation: AAH30957.1 .
    BC117121 mRNA. Translation: AAI17122.1 .
    BC014467 mRNA. No translation available.
    CCDSi CCDS47849.1. [P16157-21 ]
    CCDS55227.1. [P16157-23 ]
    CCDS6119.1. [P16157-1 ]
    CCDS6120.1. [P16157-22 ]
    CCDS6121.1. [P16157-3 ]
    CCDS6122.1. [P16157-17 ]
    PIRi A35049.
    S08275. SJHUK.
    RefSeqi NP_000028.3. NM_000037.3. [P16157-3 ]
    NP_001135917.1. NM_001142445.1. [P16157-23 ]
    NP_001135918.1. NM_001142446.1. [P16157-21 ]
    NP_065208.2. NM_020475.2. [P16157-5 ]
    NP_065209.2. NM_020476.2. [P16157-1 ]
    NP_065210.2. NM_020477.2. [P16157-4 ]
    NP_065211.2. NM_020478.4. [P16157-17 ]
    NP_065213.2. NM_020480.4. [P16157-22 ]
    UniGenei Hs.654438.
    Hs.667377.
    Hs.708861.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1N11 X-ray 2.70 A 402-827 [» ]
    2YQF NMR - A 1394-1497 [» ]
    2YVI X-ray 1.92 A 1394-1497 [» ]
    3F59 X-ray 2.00 A/B/C/D 911-1068 [» ]
    3KBT X-ray 2.75 C/D 911-1068 [» ]
    3KBU X-ray 2.75 C/D 911-1068 [» ]
    3UD1 X-ray 2.00 A/B/C 911-1233 [» ]
    3UD2 X-ray 2.21 A/B/C 911-1233 [» ]
    ProteinModelPortali P16157.
    SMRi P16157. Positions 5-812, 911-1497.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106783. 17 interactions.
    IntActi P16157. 1 interaction.
    MINTi MINT-254860.
    STRINGi 9606.ENSP00000265709.

    PTM databases

    PhosphoSitei P16157.

    Polymorphism databases

    DMDMi 116241246.

    Proteomic databases

    MaxQBi P16157.
    PaxDbi P16157.
    PRIDEi P16157.

    Protocols and materials databases

    DNASUi 286.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265709 ; ENSP00000265709 ; ENSG00000029534 . [P16157-21 ]
    ENST00000289734 ; ENSP00000289734 ; ENSG00000029534 . [P16157-3 ]
    ENST00000314214 ; ENSP00000319123 ; ENSG00000029534 . [P16157-17 ]
    ENST00000347528 ; ENSP00000339620 ; ENSG00000029534 . [P16157-1 ]
    ENST00000348036 ; ENSP00000297744 ; ENSG00000029534 . [P16157-22 ]
    ENST00000522543 ; ENSP00000430368 ; ENSG00000029534 . [P16157-23 ]
    GeneIDi 286.
    KEGGi hsa:286.
    UCSCi uc003xod.3. human.
    uc003xof.3. human.
    uc003xoi.3. human. [P16157-3 ]
    uc003xoj.3. human. [P16157-5 ]
    uc003xok.3. human. [P16157-1 ]
    uc003xol.3. human. [P16157-4 ]
    uc003xom.3. human. [P16157-21 ]

    Organism-specific databases

    CTDi 286.
    GeneCardsi GC08M041510.
    HGNCi HGNC:492. ANK1.
    HPAi CAB016057.
    HPA004842.
    HPA056953.
    MIMi 182900. phenotype.
    612641. gene.
    neXtProti NX_P16157.
    Orphaneti 251066. 8p11.2 deletion syndrome.
    822. Hereditary spherocytosis.
    PharmGKBi PA24798.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0666.
    HOVERGENi HBG004234.
    KOi K10380.
    OMAi RLCQDYD.
    OrthoDBi EOG7P02H2.
    PhylomeDBi P16157.
    TreeFami TF351263.

    Enzyme and pathway databases

    Reactomei REACT_22266. Interaction between L1 and Ankyrins.
    REACT_22292. CHL1 interactions.
    REACT_22312. Neurofascin interactions.
    REACT_22329. NrCAM interactions.

    Miscellaneous databases

    EvolutionaryTracei P16157.
    GeneWikii ANK1.
    GenomeRNAii 286.
    NextBioi 1155.
    PMAP-CutDB P16157.
    PROi P16157.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P16157.
    Bgeei P16157.
    CleanExi HS_ANK1.
    Genevestigatori P16157.

    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. 20 hits.
    PF00531. Death. 1 hit.
    PF00791. ZU5. 1 hit.
    [Graphical view ]
    PRINTSi PR01415. ANKYRIN.
    SMARTi SM00248. ANK. 23 hits.
    SM00005. DEATH. 1 hit.
    SM00218. ZU5. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47986. SSF47986. 1 hit.
    SSF48403. SSF48403. 2 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. "Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue-differentiation and cell-cycle control proteins."
      Lux S.E., John K.M., Bennett V.
      Nature 344:36-42(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ER1 AND ER2), PROTEIN SEQUENCE OF 3-30; 733-753; 828-871; 959-1003; 1106-1128; 1149-1168; 1282-1288; 1345-1367; 1383-1427; 1601-1626; 1686-1700 AND 1763-1772, VARIANTS ALA-750 AND ILE-1075.
      Tissue: Hematopoietic.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ER1; ER5 AND ER16), VARIANTS ILE-1075 AND ILE-1546.
    3. "Structure and organization of the human ankyrin-1 gene. Basis for complexity of pre-mRNA processing."
      Gallagher P.G., Tse W.T., Scarpa A.L., Lux S.E., Forget B.G.
      J. Biol. Chem. 272:19220-19228(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, VARIANTS LEU-991 AND ILE-1075.
    4. "An alternate promoter directs expression of a truncated, muscle-specific isoform of the human ankyrin 1 gene."
      Gallagher P.G., Forget B.G.
      J. Biol. Chem. 273:1339-1348(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MU17; MU18; MU19 AND MU20), TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
      Tissue: Skeletal muscle.
    5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BR21), VARIANT ILE-1075.
      Tissue: Brain.
    6. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORMS MU17; 22 AND 23).
      Tissue: B-cell and Skeletal muscle.
    9. "Mapping the binding sites of human erythrocyte ankyrin for the anion exchanger and spectrin."
      Davis L.H., Bennett V.
      J. Biol. Chem. 265:10589-10596(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 5-12; 403-422; 797-814; 862-877 AND 899-912, DOMAINS SPTB AND SLC4A1 BINDING, VARIANT ASP-1286.
    10. "Asparagine and aspartate hydroxylation of the cytoskeletal ankyrin family is catalyzed by factor-inhibiting hypoxia-inducible factor."
      Yang M., Ge W., Chowdhury R., Claridge T.D., Kramer H.B., Schmierer B., McDonough M.A., Gong L., Kessler B.M., Ratcliffe P.J., Coleman M.L., Schofield C.J.
      J. Biol. Chem. 286:7648-7660(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 99-110; 129-169 AND 233-248, INTERACTION WITH HIF1AN, HYDROXYLATION AT ASN-105; ASN-233; ASN-431; ASN-464; ASN-629; ASN-662; ASP-695; ASN-728 AND ASN-761.
    11. "The ANK repeats of erythrocyte ankyrin form two distinct but cooperative binding sites for the erythrocyte anion exchanger."
      Michaely P., Bennett V.
      J. Biol. Chem. 270:22050-22057(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLC4A1.
    12. "The hydrophilic domain of small ankyrin-1 interacts with the two N-terminal immunoglobulin domains of titin."
      Kontrogianni-Konstantopoulos A., Bloch R.J.
      J. Biol. Chem. 278:3985-3991(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TTN.
    13. "Binding of an ankyrin-1 isoform to obscurin suggests a molecular link between the sarcoplasmic reticulum and myofibrils in striated muscles."
      Bagnato P., Barone V., Giacomello E., Rossi D., Sorrentino V.
      J. Cell Biol. 160:245-253(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH OBSCN, MUTAGENESIS OF THR-1824; LYS-1826; ARG-1829 AND LYS-1830.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Crystal structure of a 12 ANK repeat stack from human ankyrinR."
      Michaely P., Tomchick D.R., Machius M., Anderson R.G.
      EMBO J. 21:6387-6396(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 402-827, FUNCTION OF ANK REPEAT DOMAIN.
    18. "Solution structure of the DEATH domain of ankyrin-1."
      RIKEN structural genomics initiative (RSGI)
      Submitted (APR-2008) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 1392-1497.
    19. "Structurally similar but functionally diverse ZU5 domains in human erythrocyte ankyrin."
      Yasunaga M., Ipsaro J.J., Mondragon A.
      J. Mol. Biol. 417:336-350(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 911-1233, DOMAINS ZU5.
    20. Cited for: VARIANT SPH1 ILE-463.
    21. "Low frequency of ankyrin mutations in hereditary spherocytosis: identification of three novel mutations."
      Leite R.C.A., Basseres D.S., Ferreira J.S., Alberto F.L., Costa F.F., Saad S.T.O.
      Hum. Mutat. 16:529-529(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SPH1 ARG-276 AND THR-1054.
    22. Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-332.

    Entry informationi

    Entry nameiANK1_HUMAN
    AccessioniPrimary (citable) accession number: P16157
    Secondary accession number(s): A0PJN8
    , A6NJ23, E5RFL7, O43400, Q13768, Q53ER1, Q59FP2, Q8N604, Q99407
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 171 of the entry and version 3 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: 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