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P16157

- ANK1_HUMAN

UniProt

P16157 - ANK1_HUMAN

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Protein
Ankyrin-1
Gene
ANK1, ANK
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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. ER to Golgi vesicle-mediated transport Source: BHF-UCL
  2. axon guidance Source: Reactome
  3. cytoskeleton organization Source: UniProtKB
  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
Complete GO annotation...

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.2 Publications
Isoform Mu17 : Membrane. CytoplasmmyofibrilsarcomereM line
Note: Colocalizes with OBSCN isoform 3/obscurin at the M line in differentiated skeletal muscle cells.2 Publications
Isoform Mu18 : Sarcoplasmic reticulum Inferred 2 Publications
Isoform Mu19 : Sarcoplasmic reticulum Inferred 2 Publications
Isoform Mu20 : Sarcoplasmic reticulum Inferred 2 Publications

GO - Cellular componenti

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

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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-1
PRO_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; partial
Modified residuei728 – 7281(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
Modified residuei761 – 7611(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
Modified residuei856 – 8561Phosphoserine By similarity
Modified residuei961 – 9611Phosphothreonine By similarity
Modified residuei1073 – 10731Phosphotyrosine By similarity
Modified residuei1392 – 13921Phosphoserine By 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.

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

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.

Miscellaneous databases

EvolutionaryTraceiP16157.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 82782789 kDa domain
Add
BLAST
Regioni1234 – 1362129UPA domain By similarity
Add
BLAST
Regioni1383 – 188149955 kDa regulatory domain
Add
BLAST

Domaini

The 55 kDa regulatory domain is involved in regulating binding of SPTB/spectrin (beta chain) and SLC4A1/erythrocyte membrane protein band 3.3 Publications
The ANK repeat region forms a spiral around a large central cavity and is involved in binding of ion transporters.3 Publications
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.3 Publications

Sequence similaritiesi

Contains 23 ANK repeats.
Contains 1 death domain.
Contains 2 ZU5 domains.

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.

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.

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.
VSP_018440Add
BLAST
Alternative sequencei1 – 99MPYSVGFRE → MAQAAKQLKKIKDIEAQALQ EQKEKEESNRKRRNRSRDRK KK in isoform Br21.
VSP_018439
Alternative sequencei820 – 8201E → EGTAHITIM in isoform Br21.
VSP_018441
Alternative sequencei1513 – 1874362Missing in isoform Er16.
VSP_000264Add
BLAST
Alternative sequencei1514 – 1675162Missing in isoform Er2, isoform Er4, isoform Er6, isoform Er8, isoform Er10, isoform Er12 and isoform Er14.
VSP_018442Add
BLAST
Alternative sequencei1726 – 179873TQGPH…TQVVQ → MWTFVTQLLVTLVLLSFFLV SCQNVMHIVRGSLCFVLKHI HQELDKELGESEGLSDDEET ISTRVVRRRVFLK in isoform Mu17, isoform Mu18, isoform Mu19, isoform 22 and isoform 23.
VSP_018443Add
BLAST
Alternative sequencei1726 – 179873TQGPH…TQVVQ → MWTFVTQLLVTLVLLSFFLV SCQNVMHIVRGSLCFVLKHI HQ in isoform Mu20.
VSP_018444Add
BLAST
Alternative sequencei1799 – 188183GNEFQ…STPNP → VELRGSGLQPDLIEGRKGAQ IVKRASLKRGKQ in isoform Mu20.
VSP_018446Add
BLAST
Alternative sequencei1799 – 187375Missing in isoform Er9, isoform Er10 and isoform Mu19.
VSP_018445Add
BLAST
Alternative sequencei1826 – 187247Missing in isoform 22.
VSP_045439Add
BLAST
Alternative sequencei1827 – 188155IIRKV…STPNP → VELRGSGLQPDLIEGRKGAQ IVKRASLKRGKQ in isoform Er15 and isoform Mu18.
VSP_018448Add
BLAST
Alternative sequencei1827 – 187347Missing in isoform Er7 and isoform Er8.
VSP_018447Add
BLAST
Alternative sequencei1849 – 187325Missing in isoform Er3, isoform Er4 and isoform Br21.
VSP_018449Add
BLAST
Alternative sequencei1850 – 188132TVEGP…STPNP → ELRGSGLQPDLIEGRKGAQI VKRASLKRGKQ in isoform Er5, isoform Er6 and isoform Mu17.
VSP_000266Add
BLAST
Alternative sequencei1874 – 18818DHTSTPNP → VELRGSGLQPDLIEGRKGAQ IVKRASLKRGKQ in isoform Er11 and isoform Er12.
VSP_018450
Alternative sequencei1874 – 18818DHTSTPNP → VLRRPRPWGTQRHHCCLALP GRLHDTSLHSPLYELSLQSL FSLVGSVSAPPCRSFRSSAC VLPVFAICPAFCLCCCLQVE LRGSGLQPDLIEGRKGAQIV KRASLKRGKQ in isoform Er13 and isoform Er14.
VSP_018451
Alternative sequencei1875 – 18751H → D in isoform Er16.
VSP_000265

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti230 – 2301A → S in AAA51732. 1 Publication
Sequence conflicti801 – 8011K → L in AAB47805. 1 Publication
Sequence conflicti845 – 8451D → R AA sequence 1 Publication
Sequence conflicti902 – 9021I → T in AAB47805. 1 Publication
Isoform Mu17 (identifier: P16157-17)
Sequence conflicti63 – 631T → P in AAC01950. 1 Publication

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]
ENST00000352337; ENSP00000309131; ENSG00000029534. [P16157-16]
ENST00000379758; ENSP00000369082; ENSG00000029534. [P16157-8]
ENST00000396942; ENSP00000380147; ENSG00000029534. [P16157-12]
ENST00000396945; ENSP00000380149; ENSG00000029534. [P16157-10]
ENST00000457297; ENSP00000403589; 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 ]
ENST00000352337 ; ENSP00000309131 ; ENSG00000029534 . [P16157-16 ]
ENST00000379758 ; ENSP00000369082 ; ENSG00000029534 . [P16157-8 ]
ENST00000396942 ; ENSP00000380147 ; ENSG00000029534 . [P16157-12 ]
ENST00000396945 ; ENSP00000380149 ; ENSG00000029534 . [P16157-10 ]
ENST00000457297 ; ENSP00000403589 ; 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 170 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

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