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Protein

Ankyrin-1

Gene

ANK1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • ATPase binding Source: BHF-UCL
  • cytoskeletal adaptor activity Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • spectrin binding Source: UniProtKB
  • structural constituent of cytoskeleton Source: ProtInc
  • structural molecule activity Source: UniProtKB

GO - Biological processi

  • cytoskeleton organization Source: UniProtKB
  • ER to Golgi vesicle-mediated transport Source: BHF-UCL
  • exocytosis Source: UniProtKB
  • maintenance of epithelial cell apical/basal polarity Source: UniProtKB
  • positive regulation of organelle organization Source: Ensembl
  • protein targeting to plasma membrane Source: BHF-UCL
  • signal transduction Source: InterPro
Complete GO annotation...

Enzyme and pathway databases

BioCyciZFISH:ENSG00000029534-MONOMER.
ReactomeiR-HSA-445095. Interaction between L1 and Ankyrins.
R-HSA-447038. NrCAM interactions.
R-HSA-447041. CHL1 interactions.
R-HSA-447043. Neurofascin interactions.
R-HSA-6807878. COPI-mediated anterograde transport.

Protein family/group databases

TCDBi8.A.28.1.2. the ankyrin (ankyrin) family.

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
Proteomesi
  • UP000005640 Componenti: 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 :

GO - Cellular componenti

  • axolemma Source: Ensembl
  • basolateral plasma membrane Source: UniProtKB
  • cytoplasm Source: GO_Central
  • cytoskeleton Source: UniProtKB
  • cytosol Source: Reactome
  • M band Source: UniProtKB-SubCell
  • nucleus Source: Ensembl
  • plasma membrane Source: UniProtKB
  • postsynaptic membrane Source: Ensembl
  • sarcolemma Source: Ensembl
  • sarcoplasmic reticulum Source: UniProtKB-SubCell
  • spectrin-associated cytoskeleton Source: BHF-UCL
  • Z disc Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane, Sarcoplasmic reticulum

Pathology & Biotechi

Involvement in diseasei

Spherocytosis 1 (SPH1)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of spherocytosis, 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 can be autosomal dominant or autosomal recessive. Patients with homozygous mutations have a more severe disorder.
See also OMIM:182900
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_054991276L → R in SPH1. 1 Publication1
Natural variantiVAR_000596463V → I in SPH1. 1 PublicationCorresponds to variant rs140085544dbSNPEnsembl.1
Natural variantiVAR_0549921054I → T in SPH1. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1824T → P: Abolishes interaction with OBSCN (in isoform Mu17). 1 Publication1
Mutagenesisi1826K → E: Abolishes interaction with OBSCN (in isoform Mu17). 1 Publication1
Mutagenesisi1829R → G: Abolishes interaction with OBSCN (in isoform Mu17). 1 Publication1
Mutagenesisi1830K → E: Abolishes interaction with OBSCN (in isoform Mu17). 1 Publication1

Keywords - Diseasei

Disease mutation, Elliptocytosis, Hereditary hemolytic anemia

Organism-specific databases

DisGeNETi286.
MalaCardsiANK1.
MIMi182900. phenotype.
OpenTargetsiENSG00000029534.
Orphaneti251066. 8p11.2 deletion syndrome.
822. Hereditary spherocytosis.
PharmGKBiPA24798.

Polymorphism and mutation databases

BioMutaiANK1.
DMDMi116241246.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000668831 – 1881Ankyrin-1Add BLAST1881

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei105(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication1
Modified residuei233(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication1
Modified residuei429PhosphoserineCombined sources1
Modified residuei431(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication1
Modified residuei464(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication1
Modified residuei629(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication1
Modified residuei662(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication1
Modified residuei695(3S)-3-hydroxyaspartate; by HIF1AN; partial1 Publication1
Modified residuei728(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication1
Modified residuei759PhosphoserineCombined sources1
Modified residuei761(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication1
Modified residuei781PhosphoserineCombined sources1
Modified residuei817PhosphoserineCombined sources1
Modified residuei834PhosphoserineCombined sources1
Modified residuei856PhosphoserineCombined sources1
Modified residuei961PhosphothreonineBy similarity1
Modified residuei1073PhosphotyrosineBy similarity1
Modified residuei1082PhosphoserineBy similarity1
Modified residuei1378PhosphothreonineCombined sources1
Modified residuei1380PhosphothreonineCombined sources1
Modified residuei1390PhosphoserineBy similarity1
Modified residuei1392PhosphoserineBy similarity1
Modified residuei1396PhosphoserineCombined sources1
Modified residuei1400PhosphothreonineBy similarity1
Modified residuei1428PhosphoserineCombined sources1
Modified residuei1486PhosphoserineCombined sources1
Modified residuei1523PhosphoserineCombined sources1
Modified residuei1533PhosphoserineCombined sources1
Modified residuei1617PhosphoserineBy similarity1
Modified residuei1666PhosphoserineCombined sources1
Modified residuei1671PhosphoserineCombined sources1
Modified residuei1686PhosphoserineCombined sources1
Modified residuei1690PhosphoserineCombined sources1
Modified residuei1696PhosphoserineCombined sources1

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.
PeptideAtlasiP16157.
PRIDEiP16157.

PTM databases

iPTMnetiP16157.
PhosphoSitePlusiP16157.

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

BgeeiENSG00000029534.
CleanExiHS_ANK1.
ExpressionAtlasiP16157. baseline and differential.
GenevisibleiP16157. HS.

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

GO - Molecular functioni

  • ATPase binding Source: BHF-UCL
  • cytoskeletal adaptor activity Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • spectrin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi106783. 22 interactors.
IntActiP16157. 3 interactors.
MINTiMINT-254860.
STRINGi9606.ENSP00000265709.

Structurei

Secondary structure

11881
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi407 – 414Combined sources8
Helixi417 – 425Combined sources9
Beta strandi433 – 435Combined sources3
Helixi440 – 447Combined sources8
Helixi450 – 459Combined sources10
Helixi473 – 480Combined sources8
Helixi483 – 492Combined sources10
Helixi506 – 513Combined sources8
Helixi516 – 524Combined sources9
Helixi539 – 545Combined sources7
Helixi549 – 557Combined sources9
Helixi572 – 578Combined sources7
Helixi582 – 588Combined sources7
Helixi589 – 591Combined sources3
Helixi605 – 611Combined sources7
Helixi615 – 623Combined sources9
Helixi638 – 644Combined sources7
Helixi648 – 655Combined sources8
Turni656 – 658Combined sources3
Helixi671 – 678Combined sources8
Helixi681 – 690Combined sources10
Helixi704 – 710Combined sources7
Helixi715 – 722Combined sources8
Helixi737 – 743Combined sources7
Helixi747 – 755Combined sources9
Beta strandi765 – 767Combined sources3
Helixi770 – 776Combined sources7
Helixi780 – 789Combined sources10
Beta strandi914 – 919Combined sources6
Beta strandi924 – 927Combined sources4
Turni930 – 932Combined sources3
Beta strandi935 – 938Combined sources4
Beta strandi942 – 945Combined sources4
Beta strandi947 – 954Combined sources8
Helixi956 – 958Combined sources3
Beta strandi959 – 961Combined sources3
Beta strandi970 – 973Combined sources4
Beta strandi975 – 980Combined sources6
Beta strandi984 – 994Combined sources11
Beta strandi1000 – 1003Combined sources4
Beta strandi1006 – 1015Combined sources10
Beta strandi1018 – 1020Combined sources3
Helixi1026 – 1028Combined sources3
Helixi1029 – 1033Combined sources5
Helixi1043 – 1049Combined sources7
Beta strandi1051 – 1058Combined sources8
Beta strandi1061 – 1067Combined sources7
Beta strandi1074 – 1076Combined sources3
Beta strandi1081 – 1084Combined sources4
Beta strandi1092 – 1095Combined sources4
Beta strandi1099 – 1102Combined sources4
Beta strandi1104 – 1111Combined sources8
Helixi1115 – 1122Combined sources8
Beta strandi1131 – 1138Combined sources8
Beta strandi1140 – 1150Combined sources11
Helixi1153 – 1157Combined sources5
Beta strandi1165 – 1167Combined sources3
Beta strandi1169 – 1175Combined sources7
Beta strandi1195 – 1197Combined sources3
Beta strandi1200 – 1207Combined sources8
Beta strandi1210 – 1215Combined sources6
Helixi1219 – 1221Combined sources3
Helixi1222 – 1232Combined sources11
Turni1398 – 1402Combined sources5
Helixi1403 – 1414Combined sources12
Helixi1415 – 1417Combined sources3
Helixi1418 – 1424Combined sources7
Helixi1429 – 1438Combined sources10
Helixi1443 – 1458Combined sources16
Helixi1459 – 1461Combined sources3
Helixi1464 – 1473Combined sources10
Helixi1477 – 1483Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16157.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati44 – 73ANK 1Add BLAST30
Repeati77 – 106ANK 2Add BLAST30
Repeati110 – 139ANK 3Add BLAST30
Repeati143 – 172ANK 4Add BLAST30
Repeati174 – 201ANK 5Add BLAST28
Repeati205 – 234ANK 6Add BLAST30
Repeati238 – 267ANK 7Add BLAST30
Repeati271 – 300ANK 8Add BLAST30
Repeati304 – 333ANK 9Add BLAST30
Repeati337 – 366ANK 10Add BLAST30
Repeati370 – 399ANK 11Add BLAST30
Repeati403 – 432ANK 12Add BLAST30
Repeati436 – 465ANK 13Add BLAST30
Repeati469 – 498ANK 14Add BLAST30
Repeati502 – 531ANK 15Add BLAST30
Repeati535 – 564ANK 16Add BLAST30
Repeati568 – 597ANK 17Add BLAST30
Repeati601 – 630ANK 18Add BLAST30
Repeati634 – 663ANK 19Add BLAST30
Repeati667 – 696ANK 20Add BLAST30
Repeati700 – 729ANK 21Add BLAST30
Repeati733 – 762ANK 22Add BLAST30
Repeati766 – 795ANK 23Add BLAST30
Domaini911 – 1066ZU5 1PROSITE-ProRule annotationAdd BLAST156
Domaini1067 – 1233ZU5 2PROSITE-ProRule annotationAdd BLAST167
Domaini1403 – 1487DeathPROSITE-ProRule annotationAdd BLAST85

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 82789 kDa domainAdd BLAST827
Regioni1234 – 1362UPA domainBy similarityAdd BLAST129
Regioni1383 – 188155 kDa regulatory domainAdd BLAST499

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

eggNOGiKOG4177. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00840000129677.
HOGENOMiHOG000237351.
HOVERGENiHBG004234.
InParanoidiP16157.
KOiK10380.
OMAiRLCQDYD.
OrthoDBiEOG091G00GN.
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_dom.
[Graphical view]
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 9 hits.
PF13606. Ank_3. 1 hit.
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. AlignAdd to basket

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

        10         20         30         40         50
MPYSVGFREA DAATSFLRAA RSGNLDKALD HLRNGVDINT CNQNGLNGLH
60 70 80 90 100
LASKEGHVKM VVELLHKEII LETTTKKGNT ALHIAALAGQ DEVVRELVNY
110 120 130 140 150
GANVNAQSQK GFTPLYMAAQ ENHLEVVKFL LENGANQNVA TEDGFTPLAV
160 170 180 190 200
ALQQGHENVV AHLINYGTKG KVRLPALHIA ARNDDTRTAA VLLQNDPNPD
210 220 230 240 250
VLSKTGFTPL HIAAHYENLN VAQLLLNRGA SVNFTPQNGI TPLHIASRRG
260 270 280 290 300
NVIMVRLLLD RGAQIETKTK DELTPLHCAA RNGHVRISEI LLDHGAPIQA
310 320 330 340 350
KTKNGLSPIH MAAQGDHLDC VRLLLQYDAE IDDITLDHLT PLHVAAHCGH
360 370 380 390 400
HRVAKVLLDK GAKPNSRALN GFTPLHIACK KNHVRVMELL LKTGASIDAV
410 420 430 440 450
TESGLTPLHV ASFMGHLPIV KNLLQRGASP NVSNVKVETP LHMAARAGHT
460 470 480 490 500
EVAKYLLQNK AKVNAKAKDD QTPLHCAARI GHTNMVKLLL ENNANPNLAT
510 520 530 540 550
TAGHTPLHIA AREGHVETVL ALLEKEASQA CMTKKGFTPL HVAAKYGKVR
560 570 580 590 600
VAELLLERDA HPNAAGKNGL TPLHVAVHHN NLDIVKLLLP RGGSPHSPAW
610 620 630 640 650
NGYTPLHIAA KQNQVEVARS LLQYGGSANA ESVQGVTPLH LAAQEGHAEM
660 670 680 690 700
VALLLSKQAN GNLGNKSGLT PLHLVAQEGH VPVADVLIKH GVMVDATTRM
710 720 730 740 750
GYTPLHVASH YGNIKLVKFL LQHQADVNAK TKLGYSPLHQ AAQQGHTDIV
760 770 780 790 800
TLLLKNGASP NEVSSDGTTP LAIAKRLGYI SVTDVLKVVT DETSFVLVSD
810 820 830 840 850
KHRMSFPETV DEILDVSEDE GEELISFKAE RRDSRDVDEE KELLDFVPKL
860 870 880 890 900
DQVVESPAIP RIPCAMPETV VIRSEEQEQA SKEYDEDSLI PSSPATETSD
910 920 930 940 950
NISPVASPVH TGFLVSFMVD ARGGSMRGSR HNGLRVVIPP RTCAAPTRIT
960 970 980 990 1000
CRLVKPQKLS TPPPLAEEEG LASRIIALGP TGAQFLSPVI VEIPHFASHG
1010 1020 1030 1040 1050
RGDRELVVLR SENGSVWKEH RSRYGESYLD QILNGMDEEL GSLEELEKKR
1060 1070 1080 1090 1100
VCRIITTDFP LYFVIMSRLC QDYDTIGPEG GSLKSKLVPL VQATFPENAV
1110 1120 1130 1140 1150
TKRVKLALQA QPVPDELVTK LLGNQATFSP IVTVEPRRRK FHRPIGLRIP
1160 1170 1180 1190 1200
LPPSWTDNPR DSGEGDTTSL RLLCSVIGGT DQAQWEDITG TTKLVYANEC
1210 1220 1230 1240 1250
ANFTTNVSAR FWLSDCPRTA EAVNFATLLY KELTAVPYMA KFVIFAKMND
1260 1270 1280 1290 1300
PREGRLRCYC MTDDKVDKTL EQHENFVEVA RSRDIEVLEG MSLFAELSGN
1310 1320 1330 1340 1350
LVPVKKAAQQ RSFHFQSFRE NRLAMPVKVR DSSREPGGSL SFLRKAMKYE
1360 1370 1380 1390 1400
DTQHILCHLN ITMPPCAKGS GAEDRRRTPT PLALRYSILS ESTPGSLSGT
1410 1420 1430 1440 1450
EQAEMKMAVI SEHLGLSWAE LARELQFSVE DINRIRVENP NSLLEQSVAL
1460 1470 1480 1490 1500
LNLWVIREGQ NANMENLYTA LQSIDRGEIV NMLEGSGRQS RNLKPDRRHT
1510 1520 1530 1540 1550
DRDYSLSPSQ MNGYSSLQDE LLSPASLGCA LSSPLRADQY WNEVAVLDAI
1560 1570 1580 1590 1600
PLAATEHDTM LEMSDMQVWS AGLTPSLVTA EDSSLECSKA EDSDATGHEW
1610 1620 1630 1640 1650
KLEGALSEEP RGPELGSLEL VEDDTVDSDA TNGLIDLLEQ EEGQRSEEKL
1660 1670 1680 1690 1700
PGSKRQDDAT GAGQDSENEV SLVSGHQRGQ ARITHSPTVS QVTERSQDRL
1710 1720 1730 1740 1750
QDWDADGSIV SYLQDAAQGS WQEEVTQGPH SFQGTSTMTE GLEPGGSQEY
1760 1770 1780 1790 1800
EKVLVSVSEH TWTEQPEAES SQADRDRRQQ GQEEQVQEAK NTFTQVVQGN
1810 1820 1830 1840 1850
EFQNIPGEQV TEEQFTDEQG NIVTKKIIRK VVRQIDLSSA DAAQEHEEVT
1860 1870 1880
VEGPLEDPSE LEVDIDYFMK HSKDHTSTPN P
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 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti230A → S in AAA51732 (PubMed:1689849).Curated1
Sequence conflicti801K → L in AAB47805 (PubMed:9235914).Curated1
Sequence conflicti845D → R AA sequence (PubMed:2137557).Curated1
Sequence conflicti902I → T in AAB47805 (PubMed:9235914).Curated1
Isoform Mu17 (identifier: P16157-17)
Sequence conflicti63T → P in AAC01950 (PubMed:9430667).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00059521R → T.1
Natural variantiVAR_054991276L → R in SPH1. 1 Publication1
Natural variantiVAR_035605332D → H in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_000596463V → I in SPH1. 1 PublicationCorresponds to variant rs140085544dbSNPEnsembl.1
Natural variantiVAR_000597619R → H in Brueggen. Corresponds to variant rs2304877dbSNPEnsembl.1
Natural variantiVAR_028769733L → I.Corresponds to variant rs11778936dbSNPEnsembl.1
Natural variantiVAR_000598750V → A.1 Publication1
Natural variantiVAR_061012832R → Q.Corresponds to variant rs34523608dbSNPEnsembl.1
Natural variantiVAR_000599845D → E.1
Natural variantiVAR_026411991V → L.1 Publication1
Natural variantiVAR_0549921054I → T in SPH1. 1 Publication1
Natural variantiVAR_0482631075T → I.4 PublicationsCorresponds to variant rs35213384dbSNPEnsembl.1
Natural variantiVAR_0287701126A → P.Corresponds to variant rs504465dbSNPEnsembl.1
Natural variantiVAR_0287711192T → P.Corresponds to variant rs486770dbSNPEnsembl.1
Natural variantiVAR_0006011286E → D.1 Publication1
Natural variantiVAR_0287721325M → V.Corresponds to variant rs10093583dbSNPEnsembl.1
Natural variantiVAR_0006001392S → T.1
Natural variantiVAR_0287731546V → I.1 PublicationCorresponds to variant rs1060130dbSNPEnsembl.1
Natural variantiVAR_0006021592D → N in Duesseldorf. 1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0184401 – 1725Missing in isoform Mu17, isoform Mu18, isoform Mu19, isoform Mu20, isoform 22 and isoform 23. 2 PublicationsAdd BLAST1725
Alternative sequenceiVSP_0184391 – 9MPYSVGFRE → MAQAAKQLKKIKDIEAQALQ EQKEKEESNRKRRNRSRDRK KK in isoform Br21. 1 Publication9
Alternative sequenceiVSP_018441820E → EGTAHITIM in isoform Br21. 1 Publication1
Alternative sequenceiVSP_0002641513 – 1874Missing in isoform Er16. 1 PublicationAdd BLAST362
Alternative sequenceiVSP_0184421514 – 1675Missing in isoform Er2, isoform Er4, isoform Er6, isoform Er8, isoform Er10, isoform Er12 and isoform Er14. 1 PublicationAdd BLAST162
Alternative sequenceiVSP_0184431726 – 1798TQGPH…TQVVQ → MWTFVTQLLVTLVLLSFFLV SCQNVMHIVRGSLCFVLKHI HQELDKELGESEGLSDDEET ISTRVVRRRVFLK in isoform Mu17, isoform Mu18, isoform Mu19, isoform 22 and isoform 23. 2 PublicationsAdd BLAST73
Alternative sequenceiVSP_0184441726 – 1798TQGPH…TQVVQ → MWTFVTQLLVTLVLLSFFLV SCQNVMHIVRGSLCFVLKHI HQ in isoform Mu20. 1 PublicationAdd BLAST73
Alternative sequenceiVSP_0184461799 – 1881GNEFQ…STPNP → VELRGSGLQPDLIEGRKGAQ IVKRASLKRGKQ in isoform Mu20. 1 PublicationAdd BLAST83
Alternative sequenceiVSP_0184451799 – 1873Missing in isoform Er9, isoform Er10 and isoform Mu19. 1 PublicationAdd BLAST75
Alternative sequenceiVSP_0454391826 – 1872Missing in isoform 22. 1 PublicationAdd BLAST47
Alternative sequenceiVSP_0184481827 – 1881IIRKV…STPNP → VELRGSGLQPDLIEGRKGAQ IVKRASLKRGKQ in isoform Er15 and isoform Mu18. 1 PublicationAdd BLAST55
Alternative sequenceiVSP_0184471827 – 1873Missing in isoform Er7 and isoform Er8. CuratedAdd BLAST47
Alternative sequenceiVSP_0184491849 – 1873Missing in isoform Er3, isoform Er4 and isoform Br21. 1 PublicationAdd BLAST25
Alternative sequenceiVSP_0002661850 – 1881TVEGP…STPNP → ELRGSGLQPDLIEGRKGAQI VKRASLKRGKQ in isoform Er5, isoform Er6 and isoform Mu17. 3 PublicationsAdd BLAST32
Alternative sequenceiVSP_0184501874 – 1881DHTSTPNP → VELRGSGLQPDLIEGRKGAQ IVKRASLKRGKQ in isoform Er11 and isoform Er12. Curated8
Alternative sequenceiVSP_0184511874 – 1881DHTSTPNP → VLRRPRPWGTQRHHCCLALP GRLHDTSLHSPLYELSLQSL FSLVGSVSAPPCRSFRSSAC VLPVFAICPAFCLCCCLQVE LRGSGLQPDLIEGRKGAQIV KRASLKRGKQ in isoform Er13 and isoform Er14. Curated8
Alternative sequenceiVSP_0002651875H → D in isoform Er16. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
UCSCiuc003xoc.4. human. [P16157-1]

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Ankyrin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106783. 22 interactors.
IntActiP16157. 3 interactors.
MINTiMINT-254860.
STRINGi9606.ENSP00000265709.

Protein family/group databases

TCDBi8.A.28.1.2. the ankyrin (ankyrin) family.

PTM databases

iPTMnetiP16157.
PhosphoSitePlusiP16157.

Polymorphism and mutation databases

BioMutaiANK1.
DMDMi116241246.

Proteomic databases

MaxQBiP16157.
PaxDbiP16157.
PeptideAtlasiP16157.
PRIDEiP16157.

Protocols and materials databases

DNASUi286.
Structural Biology KnowledgebaseSearch...

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.
UCSCiuc003xoc.4. human. [P16157-1]

Organism-specific databases

CTDi286.
DisGeNETi286.
GeneCardsiANK1.
HGNCiHGNC:492. ANK1.
HPAiCAB016057.
HPA004842.
HPA056953.
MalaCardsiANK1.
MIMi182900. phenotype.
612641. gene.
neXtProtiNX_P16157.
OpenTargetsiENSG00000029534.
Orphaneti251066. 8p11.2 deletion syndrome.
822. Hereditary spherocytosis.
PharmGKBiPA24798.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4177. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00840000129677.
HOGENOMiHOG000237351.
HOVERGENiHBG004234.
InParanoidiP16157.
KOiK10380.
OMAiRLCQDYD.
OrthoDBiEOG091G00GN.
PhylomeDBiP16157.
TreeFamiTF351263.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000029534-MONOMER.
ReactomeiR-HSA-445095. Interaction between L1 and Ankyrins.
R-HSA-447038. NrCAM interactions.
R-HSA-447041. CHL1 interactions.
R-HSA-447043. Neurofascin interactions.
R-HSA-6807878. COPI-mediated anterograde transport.

Miscellaneous databases

EvolutionaryTraceiP16157.
GeneWikiiANK1.
GenomeRNAii286.
PMAP-CutDBP16157.
PROiP16157.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000029534.
CleanExiHS_ANK1.
ExpressionAtlasiP16157. baseline and differential.
GenevisibleiP16157. HS.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
1.25.40.20. 3 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR000906. ZU5_dom.
[Graphical view]
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 9 hits.
PF13606. Ank_3. 1 hit.
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]
ProtoNetiSearch...

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: November 2, 2016
This is version 193 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.