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P16157 (ANK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 169. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ankyrin-1

Short name=ANK-1
Alternative name(s):
Ankyrin-R
Erythrocyte ankyrin
Gene names
Name:ANK1
Synonyms:ANK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1881 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.17

Isoform Mu17 together with obscurin in skeletal muscle may provide a molecular link between the sarcoplasmic reticulum and myofibrils. Ref.17

Subunit structure

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. Ref.10 Ref.11 Ref.12 Ref.13

Subcellular location

Isoform Er1: Cytoplasmcytoskeleton. Note: Probably the other erythrocyte (Er) isoforms, are located near the surface of erythrocytic plasma membrane. Ref.4 Ref.13

Isoform Mu17: Membrane. CytoplasmmyofibrilsarcomereM line. Note: Colocalizes with OBSCN isoform 3/obscurinat the M line in differentiated skeletal muscle cells. Ref.4 Ref.13

Isoform Mu18: Sarcoplasmic reticulum Probable Ref.4 Ref.13.

Isoform Mu19: Sarcoplasmic reticulum Probable Ref.4 Ref.13.

Isoform Mu20: Sarcoplasmic reticulum Probable Ref.4 Ref.13.

Tissue specificity

Isoform Mu17, isoform Mu18, isoform Mu19 and isoform Mu20 are expressed in skeletal muscle. Isoform Br21 is expressed in brain. Ref.4

Domain

The 55 kDa regulatory domain is involved in regulating binding of SPTB/spectrin (beta chain) and SLC4A1/erythrocyte membrane protein band 3. Ref.9 Ref.17 Ref.19

The ANK repeat region forms a spiral around a large central cavity and is involved in binding of ion transporters. Ref.9 Ref.17 Ref.19

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. Ref.9 Ref.17 Ref.19

Post-translational modification

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.

Involvement in disease

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. Ref.20 Ref.21

Sequence similarities

Contains 23 ANK repeats.

Contains 1 death domain.

Contains 2 ZU5 domains.

Sequence caution

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

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Membrane
Sarcoplasmic reticulum
   Coding sequence diversityAlternative promoter usage
Alternative splicing
Polymorphism
   DiseaseDisease mutation
Elliptocytosis
Hereditary hemolytic anemia
   DomainANK repeat
Repeat
   PTMHydroxylation
Lipoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processER to Golgi vesicle-mediated transport

Inferred from direct assay PubMed 18768923. Source: BHF-UCL

axon guidance

Traceable author statement. Source: Reactome

cytoskeleton organization

Non-traceable author statement Ref.4. Source: UniProtKB

erythrocyte development

Inferred from electronic annotation. Source: Ensembl

exocytosis

Non-traceable author statement PubMed 1833445. Source: UniProtKB

maintenance of epithelial cell apical/basal polarity

Traceable author statement PubMed 11427698. Source: UniProtKB

monovalent inorganic cation transport

Inferred from electronic annotation. Source: Ensembl

porphyrin-containing compound biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of organelle organization

Inferred from electronic annotation. Source: Ensembl

protein targeting to plasma membrane

Inferred from mutant phenotype PubMed 18768923. Source: BHF-UCL

signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentM band

Inferred from electronic annotation. Source: UniProtKB-SubCell

Z disc

Inferred from electronic annotation. Source: Ensembl

axolemma

Inferred from electronic annotation. Source: Ensembl

basolateral plasma membrane

Non-traceable author statement PubMed 12409278. Source: UniProtKB

cortical cytoskeleton

Inferred from electronic annotation. Source: Ensembl

cytoskeleton

Non-traceable author statement PubMed 1833445. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Non-traceable author statement Ref.4. Source: UniProtKB

postsynaptic membrane

Inferred from electronic annotation. Source: Ensembl

sarcolemma

Inferred from electronic annotation. Source: Ensembl

sarcoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

spectrin-associated cytoskeleton

Inferred from direct assay PubMed 379653. Source: BHF-UCL

   Molecular_functionATPase binding

Inferred from physical interaction PubMed 8159688. Source: BHF-UCL

cytoskeletal adaptor activity

Traceable author statement PubMed 11427698. Source: UniProtKB

enzyme binding

Inferred from physical interaction Ref.10. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 12719424PubMed 16580865. Source: UniProtKB

spectrin binding

Non-traceable author statement Ref.20. Source: UniProtKB

structural constituent of cytoskeleton

Traceable author statement Ref.20. Source: ProtInc

structural molecule activity

Non-traceable author statement Ref.4. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

OBSCNQ5VST9-38EBI-941819,EBI-941921

Alternative products

This entry describes 23 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]
Isoform Er1 (identifier: P16157-1)

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.
Note: Major erythrocyte-specific isoform. Produced by alternative promoter usage.
Isoform Er2 (identifier: P16157-4)

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.
Isoform Er3 (identifier: P16157-5)

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.
Isoform Er4 (identifier: P16157-6)

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.
Isoform Er5 (identifier: P16157-3)

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.
Isoform Er6 (identifier: P16157-7)

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.
Isoform Er7 (identifier: P16157-8)

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.
Isoform Er8 (identifier: P16157-9)

Also known as: 8;

The sequence of this isoform differs from the canonical sequence as follows:
     1514-1675: Missing.
     1827-1873: Missing.
Isoform Er9 (identifier: P16157-10)

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.
Isoform Er10 (identifier: P16157-11)

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.
Isoform Er11 (identifier: P16157-12)

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.
Isoform Er12 (identifier: P16157-13)

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.
Isoform Er13 (identifier: P16157-14)

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.
Isoform Er14 (identifier: P16157-15)

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.
Isoform Er15 (identifier: P16157-16)

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.
Isoform Er16 (identifier: P16157-2)

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.
Isoform Mu17 (identifier: P16157-17)

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.
Isoform Mu18 (identifier: P16157-18)

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.
Isoform Mu19 (identifier: P16157-19)

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.
Isoform Mu20 (identifier: P16157-20)

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.
Isoform Br21 (identifier: P16157-21)

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.
Isoform 22 (identifier: P16157-22)

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.
Isoform 23 (identifier: P16157-23)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18811881Ankyrin-1
PRO_0000066883

Regions

Repeat44 – 7330ANK 1
Repeat77 – 10630ANK 2
Repeat110 – 13930ANK 3
Repeat143 – 17230ANK 4
Repeat174 – 20128ANK 5
Repeat205 – 23430ANK 6
Repeat238 – 26730ANK 7
Repeat271 – 30030ANK 8
Repeat304 – 33330ANK 9
Repeat337 – 36630ANK 10
Repeat370 – 39930ANK 11
Repeat403 – 43230ANK 12
Repeat436 – 46530ANK 13
Repeat469 – 49830ANK 14
Repeat502 – 53130ANK 15
Repeat535 – 56430ANK 16
Repeat568 – 59730ANK 17
Repeat601 – 63030ANK 18
Repeat634 – 66330ANK 19
Repeat667 – 69630ANK 20
Repeat700 – 72930ANK 21
Repeat733 – 76230ANK 22
Repeat766 – 79530ANK 23
Domain911 – 1066156ZU5 1
Domain1067 – 1233167ZU5 2
Domain1403 – 148785Death
Region1 – 82782789 kDa domain
Region1234 – 1362129UPA domain By similarity
Region1383 – 188149955 kDa regulatory domain

Amino acid modifications

Modified residue1051(3S)-3-hydroxyasparagine; by HIF1AN; partial Ref.10
Modified residue2331(3S)-3-hydroxyasparagine; by HIF1AN; partial Ref.10
Modified residue4311(3S)-3-hydroxyasparagine; by HIF1AN; partial Ref.10
Modified residue4641(3S)-3-hydroxyasparagine; by HIF1AN; partial Ref.10
Modified residue6291(3S)-3-hydroxyasparagine; by HIF1AN; partial Ref.10
Modified residue6621(3S)-3-hydroxyasparagine; by HIF1AN; partial Ref.10
Modified residue6951(3S)-3-hydroxyaspartate; by HIF1AN; partial
Modified residue7281(3S)-3-hydroxyasparagine; by HIF1AN; partial Ref.10
Modified residue7611(3S)-3-hydroxyasparagine; by HIF1AN; partial Ref.10
Modified residue8561Phosphoserine By similarity
Modified residue9611Phosphothreonine By similarity
Modified residue10731Phosphotyrosine By similarity
Modified residue13921Phosphoserine By similarity

Natural variations

Alternative sequence1 – 17251725Missing in isoform Mu17, isoform Mu18, isoform Mu19, isoform Mu20, isoform 22 and isoform 23.
VSP_018440
Alternative sequence1 – 99MPYSVGFRE → MAQAAKQLKKIKDIEAQALQ EQKEKEESNRKRRNRSRDRK KK in isoform Br21.
VSP_018439
Alternative sequence8201E → EGTAHITIM in isoform Br21.
VSP_018441
Alternative sequence1513 – 1874362Missing in isoform Er16.
VSP_000264
Alternative sequence1514 – 1675162Missing in isoform Er2, isoform Er4, isoform Er6, isoform Er8, isoform Er10, isoform Er12 and isoform Er14.
VSP_018442
Alternative sequence1726 – 179873TQGPH…TQVVQ → MWTFVTQLLVTLVLLSFFLV SCQNVMHIVRGSLCFVLKHI HQELDKELGESEGLSDDEET ISTRVVRRRVFLK in isoform Mu17, isoform Mu18, isoform Mu19, isoform 22 and isoform 23.
VSP_018443
Alternative sequence1726 – 179873TQGPH…TQVVQ → MWTFVTQLLVTLVLLSFFLV SCQNVMHIVRGSLCFVLKHI HQ in isoform Mu20.
VSP_018444
Alternative sequence1799 – 188183GNEFQ…STPNP → VELRGSGLQPDLIEGRKGAQ IVKRASLKRGKQ in isoform Mu20.
VSP_018446
Alternative sequence1799 – 187375Missing in isoform Er9, isoform Er10 and isoform Mu19.
VSP_018445
Alternative sequence1826 – 187247Missing in isoform 22.
VSP_045439
Alternative sequence1827 – 188155IIRKV…STPNP → VELRGSGLQPDLIEGRKGAQ IVKRASLKRGKQ in isoform Er15 and isoform Mu18.
VSP_018448
Alternative sequence1827 – 187347Missing in isoform Er7 and isoform Er8.
VSP_018447
Alternative sequence1849 – 187325Missing in isoform Er3, isoform Er4 and isoform Br21.
VSP_018449
Alternative sequence1850 – 188132TVEGP…STPNP → ELRGSGLQPDLIEGRKGAQI VKRASLKRGKQ in isoform Er5, isoform Er6 and isoform Mu17.
VSP_000266
Alternative sequence1874 – 18818DHTSTPNP → VELRGSGLQPDLIEGRKGAQ IVKRASLKRGKQ in isoform Er11 and isoform Er12.
VSP_018450
Alternative sequence1874 – 18818DHTSTPNP → VLRRPRPWGTQRHHCCLALP GRLHDTSLHSPLYELSLQSL FSLVGSVSAPPCRSFRSSAC VLPVFAICPAFCLCCCLQVE LRGSGLQPDLIEGRKGAQIV KRASLKRGKQ in isoform Er13 and isoform Er14.
VSP_018451
Alternative sequence18751H → D in isoform Er16.
VSP_000265
Natural variant211R → T.
VAR_000595
Natural variant2761L → R in SPH1. Ref.21
VAR_054991
Natural variant3321D → H in a breast cancer sample; somatic mutation. Ref.22
VAR_035605
Natural variant4631V → I in SPH1. Ref.20
VAR_000596
Natural variant6191R → H in Brueggen.
Corresponds to variant rs2304877 [ dbSNP | Ensembl ].
VAR_000597
Natural variant7331L → I.
Corresponds to variant rs11778936 [ dbSNP | Ensembl ].
VAR_028769
Natural variant7501V → A. Ref.1
VAR_000598
Natural variant8321R → Q.
Corresponds to variant rs34523608 [ dbSNP | Ensembl ].
VAR_061012
Natural variant8451D → E.
VAR_000599
Natural variant9911V → L. Ref.3
VAR_026411
Natural variant10541I → T in SPH1. Ref.21
VAR_054992
Natural variant10751T → I. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs35213384 [ dbSNP | Ensembl ].
VAR_048263
Natural variant11261A → P.
Corresponds to variant rs504465 [ dbSNP | Ensembl ].
VAR_028770
Natural variant11921T → P.
Corresponds to variant rs486770 [ dbSNP | Ensembl ].
VAR_028771
Natural variant12861E → D. Ref.9
VAR_000601
Natural variant13251M → V.
Corresponds to variant rs10093583 [ dbSNP | Ensembl ].
VAR_028772
Natural variant13921S → T.
VAR_000600
Natural variant15461V → I. Ref.2
Corresponds to variant rs1060130 [ dbSNP | Ensembl ].
VAR_028773
Natural variant15921D → N in Duesseldorf.
VAR_000602

Experimental info

Mutagenesis18241T → P: Abolishes interaction with OBSCN (in isoform Mu17). Ref.13
Mutagenesis18261K → E: Abolishes interaction with OBSCN (in isoform Mu17). Ref.13
Mutagenesis18291R → G: Abolishes interaction with OBSCN (in isoform Mu17). Ref.13
Mutagenesis18301K → E: Abolishes interaction with OBSCN (in isoform Mu17). Ref.13
Sequence conflict2301A → S in AAA51732. Ref.2
Sequence conflict8011K → L in AAB47805. Ref.3
Sequence conflict8451D → R AA sequence Ref.1
Sequence conflict9021I → T in AAB47805. Ref.3
Isoform Mu17:
Sequence conflict631T → P in AAC01950. Ref.4

Secondary structure

........................................................................................................................................ 1881
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Er1 (1) (2.1) [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 49466F6F915019EC

FASTA1,881206,265
        10         20         30         40         50         60 
MPYSVGFREA DAATSFLRAA RSGNLDKALD HLRNGVDINT CNQNGLNGLH LASKEGHVKM 

        70         80         90        100        110        120 
VVELLHKEII LETTTKKGNT ALHIAALAGQ DEVVRELVNY GANVNAQSQK GFTPLYMAAQ 

       130        140        150        160        170        180 
ENHLEVVKFL LENGANQNVA TEDGFTPLAV ALQQGHENVV AHLINYGTKG KVRLPALHIA 

       190        200        210        220        230        240 
ARNDDTRTAA VLLQNDPNPD VLSKTGFTPL HIAAHYENLN VAQLLLNRGA SVNFTPQNGI 

       250        260        270        280        290        300 
TPLHIASRRG NVIMVRLLLD RGAQIETKTK DELTPLHCAA RNGHVRISEI LLDHGAPIQA 

       310        320        330        340        350        360 
KTKNGLSPIH MAAQGDHLDC VRLLLQYDAE IDDITLDHLT PLHVAAHCGH HRVAKVLLDK 

       370        380        390        400        410        420 
GAKPNSRALN GFTPLHIACK KNHVRVMELL LKTGASIDAV TESGLTPLHV ASFMGHLPIV 

       430        440        450        460        470        480 
KNLLQRGASP NVSNVKVETP LHMAARAGHT EVAKYLLQNK AKVNAKAKDD QTPLHCAARI 

       490        500        510        520        530        540 
GHTNMVKLLL ENNANPNLAT TAGHTPLHIA AREGHVETVL ALLEKEASQA CMTKKGFTPL 

       550        560        570        580        590        600 
HVAAKYGKVR VAELLLERDA HPNAAGKNGL TPLHVAVHHN NLDIVKLLLP RGGSPHSPAW 

       610        620        630        640        650        660 
NGYTPLHIAA KQNQVEVARS LLQYGGSANA ESVQGVTPLH LAAQEGHAEM VALLLSKQAN 

       670        680        690        700        710        720 
GNLGNKSGLT PLHLVAQEGH VPVADVLIKH GVMVDATTRM GYTPLHVASH YGNIKLVKFL 

       730        740        750        760        770        780 
LQHQADVNAK TKLGYSPLHQ AAQQGHTDIV TLLLKNGASP NEVSSDGTTP LAIAKRLGYI 

       790        800        810        820        830        840 
SVTDVLKVVT DETSFVLVSD KHRMSFPETV DEILDVSEDE GEELISFKAE RRDSRDVDEE 

       850        860        870        880        890        900 
KELLDFVPKL DQVVESPAIP RIPCAMPETV VIRSEEQEQA SKEYDEDSLI PSSPATETSD 

       910        920        930        940        950        960 
NISPVASPVH TGFLVSFMVD ARGGSMRGSR HNGLRVVIPP RTCAAPTRIT CRLVKPQKLS 

       970        980        990       1000       1010       1020 
TPPPLAEEEG LASRIIALGP TGAQFLSPVI VEIPHFASHG RGDRELVVLR SENGSVWKEH 

      1030       1040       1050       1060       1070       1080 
RSRYGESYLD QILNGMDEEL GSLEELEKKR VCRIITTDFP LYFVIMSRLC QDYDTIGPEG 

      1090       1100       1110       1120       1130       1140 
GSLKSKLVPL VQATFPENAV TKRVKLALQA QPVPDELVTK LLGNQATFSP IVTVEPRRRK 

      1150       1160       1170       1180       1190       1200 
FHRPIGLRIP LPPSWTDNPR DSGEGDTTSL RLLCSVIGGT DQAQWEDITG TTKLVYANEC 

      1210       1220       1230       1240       1250       1260 
ANFTTNVSAR FWLSDCPRTA EAVNFATLLY KELTAVPYMA KFVIFAKMND PREGRLRCYC 

      1270       1280       1290       1300       1310       1320 
MTDDKVDKTL EQHENFVEVA RSRDIEVLEG MSLFAELSGN LVPVKKAAQQ RSFHFQSFRE 

      1330       1340       1350       1360       1370       1380 
NRLAMPVKVR DSSREPGGSL SFLRKAMKYE DTQHILCHLN ITMPPCAKGS GAEDRRRTPT 

      1390       1400       1410       1420       1430       1440 
PLALRYSILS ESTPGSLSGT EQAEMKMAVI SEHLGLSWAE LARELQFSVE DINRIRVENP 

      1450       1460       1470       1480       1490       1500 
NSLLEQSVAL LNLWVIREGQ NANMENLYTA LQSIDRGEIV NMLEGSGRQS RNLKPDRRHT 

      1510       1520       1530       1540       1550       1560 
DRDYSLSPSQ MNGYSSLQDE LLSPASLGCA LSSPLRADQY WNEVAVLDAI PLAATEHDTM 

      1570       1580       1590       1600       1610       1620 
LEMSDMQVWS AGLTPSLVTA EDSSLECSKA EDSDATGHEW KLEGALSEEP RGPELGSLEL 

      1630       1640       1650       1660       1670       1680 
VEDDTVDSDA TNGLIDLLEQ EEGQRSEEKL PGSKRQDDAT GAGQDSENEV SLVSGHQRGQ 

      1690       1700       1710       1720       1730       1740 
ARITHSPTVS QVTERSQDRL QDWDADGSIV SYLQDAAQGS WQEEVTQGPH SFQGTSTMTE 

      1750       1760       1770       1780       1790       1800 
GLEPGGSQEY EKVLVSVSEH TWTEQPEAES SQADRDRRQQ GQEEQVQEAK NTFTQVVQGN 

      1810       1820       1830       1840       1850       1860 
EFQNIPGEQV TEEQFTDEQG NIVTKKIIRK VVRQIDLSSA DAAQEHEEVT VEGPLEDPSE 

      1870       1880 
LEVDIDYFMK HSKDHTSTPN P 

« Hide

Isoform Er2 (2) (2.2) [UniParc].

Checksum: 407D614678AF8EE0
Show »

FASTA1,719188,999
Isoform Er3 (3) [UniParc].

Checksum: FEC7837B2E7711B8
Show »

FASTA1,856203,405
Isoform Er4 (4) [UniParc].

Checksum: BB17E7510AE1067A
Show »

FASTA1,694186,139
Isoform Er5 (5) [UniParc].

Checksum: 3153959168D8D91D
Show »

FASTA1,880206,026
Isoform Er6 (6) [UniParc].

Checksum: 9A5DBC78974FD512
Show »

FASTA1,718188,760
Isoform Er7 (7) [UniParc].

Checksum: B3735FA102F08B3D
Show »

FASTA1,834200,915
Isoform Er8 (8) [UniParc].

Checksum: 195930085EF487B7
Show »

FASTA1,672183,649
Isoform Er9 (9) [UniParc].

Checksum: A50828175CF6AD01
Show »

FASTA1,806197,752
Isoform Er10 (10) [UniParc].

Checksum: 21DC6E7730722E51
Show »

FASTA1,644180,487
Isoform Er11 (11) [UniParc].

Checksum: 22CA0F47329C69FA
Show »

FASTA1,905208,886
Isoform Er12 (12) [UniParc].

Checksum: AA2C9A6353D00A2C
Show »

FASTA1,743191,620
Isoform Er13 (13) [UniParc].

Checksum: 94434C72B761D98D
Show »

FASTA1,983217,479
Isoform Er14 (14) [UniParc].

Checksum: 748E485DAAC8FAAC
Show »

FASTA1,821200,214
Isoform Er15 (15) [UniParc].

Checksum: 1DFB26BFA488DCC4
Show »

FASTA1,858203,536
Isoform Er16 [UniParc].

Checksum: 1D71CA896F1FDD7F
Show »

FASTA1,519166,480
Isoform Mu17 (ank1.5) (muscle-specific 1) [UniParc].

Checksum: 55C5EA3888044FFB
Show »

FASTA15517,615
Isoform Mu18 (ank1.6) (muscle-specific 2) [UniParc].

Checksum: C987D8EF586B6704
Show »

FASTA13315,125
Isoform Mu19 (muscle-specific 3) [UniParc].

Checksum: 6A4EA54308E3B04B
Show »

FASTA819,342
Isoform Mu20 (muscle-specific 4) [UniParc].

Checksum: FA79EF4284FBDDEB
Show »

FASTA748,374
Isoform Br21 [UniParc].

Checksum: 82682973D1A52BA2
Show »

FASTA1,897208,239
Isoform 22 [UniParc].

Checksum: CA36067BFBD7B9A4
Show »

FASTA10912,504
Isoform 23 [UniParc].

Checksum: CE82F91038B0C57A
Show »

FASTA15617,854

References

« Hide 'large scale' references
[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]"cDNA sequence for human erythrocyte ankyrin."
Lambert S., Yu H., Prchal J.T., Lawler J., Ruff P., Speicher D., Cheung M.C., Kan Y.W., Palek J.
Proc. Natl. Acad. Sci. U.S.A. 87:1730-1734(1990) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"Ankyrin-1 mutations are a major cause of dominant and recessive hereditary spherocytosis."
Eber S.W., Gonzalez J.M., Lux M.L., Scarpa A.L., Tse W.T., Dornwell M., Herbers J., Kugler W., Oezcan R., Pekrun A., Gallagher P.G., Schroeter W., Forget B.G., Lux S.E.
Nat. Genet. 13:214-218(1996) [PubMed] [Europe PMC] [Abstract]
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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-332.
+Additional computationally mapped references.

Web resources

Wikipedia

Ankyrin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X16609 mRNA. Translation: CAA34610.1.
X16609 mRNA. Translation: CAA34611.1.
M28880 mRNA. Translation: AAA51732.1.
U50133 expand/collapse EMBL AC list , 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.
CCDSCCDS47849.1. [P16157-21]
CCDS55227.1. [P16157-23]
CCDS6119.1. [P16157-1]
CCDS6120.1. [P16157-22]
CCDS6121.1. [P16157-3]
CCDS6122.1. [P16157-17]
PIRA35049.
SJHUK. S08275.
RefSeqNP_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]
UniGeneHs.654438.
Hs.667377.
Hs.708861.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP16157.
SMRP16157. Positions 5-812, 911-1497.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106783. 16 interactions.
IntActP16157. 1 interaction.
MINTMINT-254860.
STRING9606.ENSP00000265709.

PTM databases

PhosphoSiteP16157.

Polymorphism databases

DMDM116241246.

Proteomic databases

MaxQBP16157.
PaxDbP16157.
PRIDEP16157.

Protocols and materials databases

DNASU286.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265709; 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]
GeneID286.
KEGGhsa:286.
UCSCuc003xod.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

CTD286.
GeneCardsGC08M041510.
HGNCHGNC:492. ANK1.
HPACAB016057.
HPA004842.
HPA056953.
MIM182900. phenotype.
612641. gene.
neXtProtNX_P16157.
Orphanet251066. 8p11.2 deletion syndrome.
822. Hereditary spherocytosis.
PharmGKBPA24798.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0666.
HOVERGENHBG004234.
KOK10380.
OMARLCQDYD.
OrthoDBEOG7P02H2.
PhylomeDBP16157.
TreeFamTF351263.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.

Gene expression databases

ArrayExpressP16157.
BgeeP16157.
CleanExHS_ANK1.
GenevestigatorP16157.

Family and domain databases

Gene3D1.10.533.10. 1 hit.
1.25.40.20. 3 hits.
InterProIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR000906. ZU5.
[Graphical view]
PfamPF00023. Ank. 20 hits.
PF00531. Death. 1 hit.
PF00791. ZU5. 1 hit.
[Graphical view]
PRINTSPR01415. ANKYRIN.
SMARTSM00248. ANK. 23 hits.
SM00005. DEATH. 1 hit.
SM00218. ZU5. 1 hit.
[Graphical view]
SUPFAMSSF47986. SSF47986. 1 hit.
SSF48403. SSF48403. 2 hits.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 20 hits.
PS50017. DEATH_DOMAIN. 1 hit.
PS51145. ZU5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP16157.
GeneWikiANK1.
GenomeRNAi286.
NextBio1155.
PMAP-CutDBP16157.
PROP16157.
SOURCESearch...

Entry information

Entry nameANK1_HUMAN
AccessionPrimary (citable) accession number: P16157
Secondary accession number(s): A0PJN8 expand/collapse secondary AC list , A6NJ23, E5RFL7, O43400, Q13768, Q53ER1, Q59FP2, Q8N604, Q99407
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 169 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM