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Protein

Ankyrin-3

Gene

ANK3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

In skeletal muscle, required for costamere localization of DMD and betaDAG1 (By similarity). Membrane-cytoskeleton linker. May participate in the maintenance/targeting of ion channels and cell adhesion molecules at the nodes of Ranvier and axonal initial segments. Regulates KCNA1 channel activity in function of dietary Mg2+ levels, and thereby contributes to the regulation of renal Mg2+ reabsorption (PubMed:23903368).By similarity1 Publication
Isoform 5: May be part of a Golgi-specific membrane cytoskeleton in association with beta-spectrin.1 Publication

GO - Molecular functioni

  • cadherin binding Source: BHF-UCL
  • cytoskeletal protein binding Source: BHF-UCL
  • ion channel binding Source: BHF-UCL
  • protein binding, bridging Source: BHF-UCL
  • spectrin binding Source: BHF-UCL
  • structural constituent of cytoskeleton Source: BHF-UCL

GO - Biological processi

  • axon guidance Source: Ensembl
  • axonogenesis Source: BHF-UCL
  • cellular response to magnesium ion Source: UniProtKB
  • cytoskeletal anchoring at plasma membrane Source: ProtInc
  • establishment of protein localization Source: UniProtKB
  • Golgi to plasma membrane protein transport Source: BHF-UCL
  • magnesium ion homeostasis Source: UniProtKB
  • maintenance of protein location in plasma membrane Source: BHF-UCL
  • membrane assembly Source: BHF-UCL
  • mitotic cytokinesis Source: BHF-UCL
  • negative regulation of delayed rectifier potassium channel activity Source: UniProtKB
  • neuromuscular junction development Source: Ensembl
  • neuronal action potential Source: BHF-UCL
  • plasma membrane organization Source: BHF-UCL
  • positive regulation of cell communication by electrical coupling Source: Ensembl
  • positive regulation of gene expression Source: BHF-UCL
  • positive regulation of homotypic cell-cell adhesion Source: Ensembl
  • positive regulation of membrane depolarization during cardiac muscle cell action potential Source: BHF-UCL
  • positive regulation of membrane potential Source: BHF-UCL
  • positive regulation of protein targeting to membrane Source: Ensembl
  • positive regulation of sodium ion transmembrane transporter activity Source: BHF-UCL
  • positive regulation of sodium ion transport Source: BHF-UCL
  • protein localization to plasma membrane Source: BHF-UCL
  • protein targeting to plasma membrane Source: BHF-UCL
  • regulation of potassium ion transport Source: BHF-UCL
  • signal transduction Source: InterPro
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_22266. Interaction between L1 and Ankyrins.

Names & Taxonomyi

Protein namesi
Recommended name:
Ankyrin-3
Short name:
ANK-3
Alternative name(s):
Ankyrin-G
Gene namesi
Name:ANK3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:494. ANK3.

Subcellular locationi

Isoform 5 :

GO - Cellular componenti

  • axon initial segment Source: BHF-UCL
  • basolateral plasma membrane Source: UniProtKB
  • cell surface Source: BHF-UCL
  • costamere Source: BHF-UCL
  • dendrite Source: Ensembl
  • endoplasmic reticulum Source: ProtInc
  • Golgi apparatus Source: ProtInc
  • intercalated disc Source: BHF-UCL
  • lateral plasma membrane Source: BHF-UCL
  • lysosome Source: UniProtKB-SubCell
  • neuromuscular junction Source: Ensembl
  • node of Ranvier Source: BHF-UCL
  • paranode region of axon Source: Ensembl
  • plasma membrane Source: BHF-UCL
  • postsynaptic membrane Source: UniProtKB-SubCell
  • sarcolemma Source: BHF-UCL
  • sarcoplasmic reticulum Source: Ensembl
  • spectrin-associated cytoskeleton Source: BHF-UCL
  • T-tubule Source: BHF-UCL
  • Z disc Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Golgi apparatus, Lysosome, Membrane, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Involvement in diseasei

Genetic variations in ANK3 may be associated with autism spectrum disorders susceptibility.

Mental retardation, autosomal recessive 37 (MRT37)

The disease is caused by mutations affecting the gene represented in this entry. A homozygous deletion in ANK3 predicted to result in frameshift and premature truncation, has been shown to be the cause of moderate intellectual disability, an ADHD-like phenotype and behavioral problems in a consanguineous family (PubMed:23390136).

Disease descriptionA disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period. MRT37 patients manifest delayed global development with speech delay, hypotonia, spasticity, and a sleep disorder. Severe behavioral abnormalities include aggression, hyperactivity, and grinding of the teeth.

See also OMIM:615493

Keywords - Diseasei

Autism spectrum disorder, Mental retardation

Organism-specific databases

MIMi615493. phenotype.
Orphaneti356996. Intellectual disability - hypotonia - spasticity - sleep disorder.
3140. Schizophrenia.
PharmGKBiPA24800.

Polymorphism and mutation databases

BioMutaiANK3.
DMDMi257051061.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 43774377Ankyrin-3PRO_0000066886Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei39 – 391Phosphoserine1 Publication
Modified residuei847 – 8471Phosphoserine1 Publication
Modified residuei1445 – 14451Phosphoserine1 Publication
Modified residuei4229 – 42291Phosphoserine1 Publication
Modified residuei4290 – 42901Phosphoserine1 Publication
Modified residuei4298 – 42981Phosphoserine2 Publications
Cross-linki4338 – 4338Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ12955.
PaxDbiQ12955.
PRIDEiQ12955.

PTM databases

PhosphoSiteiQ12955.

Expressioni

Tissue specificityi

Expressed in brain, neurons, muscles and other tissues.2 Publications

Developmental stagei

Up-regulated during muscle cell differentiation.1 Publication

Gene expression databases

BgeeiQ12955.
CleanExiHS_ANK3.
ExpressionAtlasiQ12955. baseline and differential.
GenevisibleiQ12955. HS.

Organism-specific databases

HPAiCAB013249.
CAB015179.
HPA055643.

Interactioni

Subunit structurei

Directly interacts with DMD and betaDAG1. This interaction does not interfere with binding between DMD and betaDAG1. It is also required for DMD and betaDAG1 retention at costameres (By similarity). Interacts (via N-terminal ANK repeats) with SCHIP1 isoform 5 (via C-terminus); this interaction is required for the localization at axon initial segments (AISs) and nodes of Ranvier (NRs) (By similarity). May be a constituent of a neurofascin/NRCAM/ankyrin G complex. Interacts with RHBG (PubMed:15611082). Interacts with PLEC and FLNC (PubMed:21223964). Interacts with KCNA1; this inhibits channel activity (PubMed:23903368).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SMAD2Q157962EBI-2691178,EBI-1040141

Protein-protein interaction databases

BioGridi106785. 15 interactions.
DIPiDIP-49017N.
IntActiQ12955. 5 interactions.
STRINGi9606.ENSP00000280772.

Structurei

Secondary structure

1
4377
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4089 – 410113Combined sources
Helixi4102 – 41043Combined sources
Helixi4105 – 41117Combined sources
Helixi4116 – 412510Combined sources
Helixi4130 – 414516Combined sources
Helixi4146 – 41483Combined sources
Helixi4151 – 416010Combined sources
Helixi4164 – 41718Combined sources
Helixi4173 – 41786Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4O6XX-ray2.10A/B4088-4199[»]
ProteinModelPortaliQ12955.
SMRiQ12955. Positions 35-818, 982-1442, 4088-4187.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati73 – 10230ANK 1Add
BLAST
Repeati106 – 13530ANK 2Add
BLAST
Repeati139 – 16830ANK 3Add
BLAST
Repeati172 – 20130ANK 4Add
BLAST
Repeati203 – 23028ANK 5Add
BLAST
Repeati234 – 26330ANK 6Add
BLAST
Repeati267 – 29630ANK 7Add
BLAST
Repeati300 – 32930ANK 8Add
BLAST
Repeati333 – 36230ANK 9Add
BLAST
Repeati366 – 39530ANK 10Add
BLAST
Repeati399 – 42830ANK 11Add
BLAST
Repeati432 – 46130ANK 12Add
BLAST
Repeati465 – 49430ANK 13Add
BLAST
Repeati498 – 52730ANK 14Add
BLAST
Repeati531 – 56030ANK 15Add
BLAST
Repeati564 – 59330ANK 16Add
BLAST
Repeati597 – 62630ANK 17Add
BLAST
Repeati630 – 65930ANK 18Add
BLAST
Repeati663 – 69230ANK 19Add
BLAST
Repeati696 – 72530ANK 20Add
BLAST
Repeati729 – 75830ANK 21Add
BLAST
Repeati762 – 79130ANK 22Add
BLAST
Repeati795 – 82531ANK 23Add
BLAST
Domaini982 – 1107126ZU5 1PROSITE-ProRule annotationAdd
BLAST
Domaini1108 – 1272165ZU5 2PROSITE-ProRule annotationAdd
BLAST
Domaini4090 – 417485DeathPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1273 – 1407135UPA domainBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1519 – 1898380Ser-richAdd
BLAST
Compositional biasi2247 – 22504Poly-Thr
Compositional biasi2393 – 23964Poly-Glu
Compositional biasi3205 – 32117Poly-Glu
Compositional biasi3255 – 32595Poly-Pro
Compositional biasi3482 – 34876Poly-Ser
Compositional biasi3785 – 37917Poly-Asn
Compositional biasi3957 – 398125Thr-richAdd
BLAST

Domaini

The tandem configuration of the two ZU5 and the UPA domains forms a structural supramodule termed ZZU. ZU5-1 mediates interaction with beta-spectrin, and the ZU5-1/UPA interface is required for ankyrin's function other than binding to spectrin (By similarity).By similarity

Sequence similaritiesi

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

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00760000118950.
HOGENOMiHOG000008707.
HOVERGENiHBG024337.
InParanoidiQ12955.
KOiK10380.
OMAiDQSITEC.
OrthoDBiEOG7P02H2.
PhylomeDBiQ12955.
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. 3 hits.
PF12796. Ank_2. 6 hits.
PF00531. Death. 1 hit.
PF00791. ZU5. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 22 hits.
SM00005. DEATH. 1 hit.
SM00218. ZU5. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF48403. SSF48403. 3 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 21 hits.
PS50017. DEATH_DOMAIN. 1 hit.
PS51145. ZU5. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q12955-3) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAHAASQLKK NRDLEINAEE EPEKKRKHRK RSRDRKKKSD ANASYLRAAR
60 70 80 90 100
AGHLEKALDY IKNGVDINIC NQNGLNALHL ASKEGHVEVV SELLQREANV
110 120 130 140 150
DAATKKGNTA LHIASLAGQA EVVKVLVTNG ANVNAQSQNG FTPLYMAAQE
160 170 180 190 200
NHLEVVKFLL DNGASQSLAT EDGFTPLAVA LQQGHDQVVS LLLENDTKGK
210 220 230 240 250
VRLPALHIAA RKDDTKAAAL LLQNDNNADV ESKSGFTPLH IAAHYGNINV
260 270 280 290 300
ATLLLNRAAA VDFTARNDIT PLHVASKRGN ANMVKLLLDR GAKIDAKTRD
310 320 330 340 350
GLTPLHCGAR SGHEQVVEML LDRAAPILSK TKNGLSPLHM ATQGDHLNCV
360 370 380 390 400
QLLLQHNVPV DDVTNDYLTA LHVAAHCGHY KVAKVLLDKK ANPNAKALNG
410 420 430 440 450
FTPLHIACKK NRIKVMELLL KHGASIQAVT ESGLTPIHVA AFMGHVNIVS
460 470 480 490 500
QLMHHGASPN TTNVRGETAL HMAARSGQAE VVRYLVQDGA QVEAKAKDDQ
510 520 530 540 550
TPLHISARLG KADIVQQLLQ QGASPNAATT SGYTPLHLSA REGHEDVAAF
560 570 580 590 600
LLDHGASLSI TTKKGFTPLH VAAKYGKLEV ANLLLQKSAS PDAAGKSGLT
610 620 630 640 650
PLHVAAHYDN QKVALLLLDQ GASPHAAAKN GYTPLHIAAK KNQMDIATTL
660 670 680 690 700
LEYGADANAV TRQGIASVHL AAQEGHVDMV SLLLGRNANV NLSNKSGLTP
710 720 730 740 750
LHLAAQEDRV NVAEVLVNQG AHVDAQTKMG YTPLHVGCHY GNIKIVNFLL
760 770 780 790 800
QHSAKVNAKT KNGYTPLHQA AQQGHTHIIN VLLQNNASPN ELTVNGNTAL
810 820 830 840 850
GIARRLGYIS VVDTLKIVTE ETMTTTTVTE KHKMNVPETM NEVLDMSDDE
860 870 880 890 900
VRKANAPEML SDGEYISDVE EGEDAMTGDT DKYLGPQDLK ELGDDSLPAE
910 920 930 940 950
GYMGFSLGAR SASLRSFSSD RSYTLNRSSY ARDSMMIEEL LVPSKEQHLT
960 970 980 990 1000
FTREFDSDSL RHYSWAADTL DNVNLVSSPI HSGFLVSFMV DARGGSMRGS
1010 1020 1030 1040 1050
RHHGMRIIIP PRKCTAPTRI TCRLVKRHKL ANPPPMVEGE GLASRLVEMG
1060 1070 1080 1090 1100
PAGAQFLGPV IVEIPHFGSM RGKERELIVL RSENGETWKE HQFDSKNEDL
1110 1120 1130 1140 1150
TELLNGMDEE LDSPEELGKK RICRIITKDF PQYFAVVSRI KQESNQIGPE
1160 1170 1180 1190 1200
GGILSSTTVP LVQASFPEGA LTKRIRVGLQ AQPVPDEIVK KILGNKATFS
1210 1220 1230 1240 1250
PIVTVEPRRR KFHKPITMTI PVPPPSGEGV SNGYKGDTTP NLRLLCSITG
1260 1270 1280 1290 1300
GTSPAQWEDI TGTTPLTFIK DCVSFTTNVS ARFWLADCHQ VLETVGLATQ
1310 1320 1330 1340 1350
LYRELICVPY MAKFVVFAKM NDPVESSLRC FCMTDDKVDK TLEQQENFEE
1360 1370 1380 1390 1400
VARSKDIEVL EGKPIYVDCY GNLAPLTKGG QQLVFNFYSF KENRLPFSIK
1410 1420 1430 1440 1450
IRDTSQEPCG RLSFLKEPKT TKGLPQTAVC NLNITLPAHK KETESDQDDE
1460 1470 1480 1490 1500
IEKTDRRQSF ASLALRKRYS YLTEPGMIER STGATRSLPT TYSYKPFFST
1510 1520 1530 1540 1550
RPYQSWTTAP ITVPGPAKSG FTSLSSSSSN TPSASPLKSI WSVSTPSPIK
1560 1570 1580 1590 1600
STLGASTTSS VKSISDVASP IRSFRTMSSP IKTVVSQSPY NIQVSSGTLA
1610 1620 1630 1640 1650
RAPAVTEATP LKGLASNSTF SSRTSPVTTA GSLLERSSIT MTPPASPKSN
1660 1670 1680 1690 1700
INMYSSSLPF KSIITSAAPL ISSPLKSVVS PVKSAVDVIS SAKITMASSL
1710 1720 1730 1740 1750
SSPVKQMPGH AEVALVNGSI SPLKYPSSST LINGCKATAT LQEKISSATN
1760 1770 1780 1790 1800
SVSSVVSAAT DTVEKVFSTT TAMPFSPLRS YVSAAPSAFQ SLRTPSASAL
1810 1820 1830 1840 1850
YTSLGSSISA TTSSVTSSII TVPVYSVVNV LPEPALKKLP DSNSFTKSAA
1860 1870 1880 1890 1900
ALLSPIKTLT TETHPQPHFS RTSSPVKSSL FLAPSALKLS TPSSLSSSQE
1910 1920 1930 1940 1950
ILKDVAEMKE DLMRMTAILQ TDVPEEKPFQ PELPKEGRID DEEPFKIVEK
1960 1970 1980 1990 2000
VKEDLVKVSE ILKKDVCVDN KGSPKSPKSD KGHSPEDDWI EFSSEEIREA
2010 2020 2030 2040 2050
RQQAAASQSP SLPERVQVKA KAASEKDYNL TKVIDYLTND IGSSSLTNLK
2060 2070 2080 2090 2100
YKFEDAKKDG EERQKRVLKP AIALQEHKLK MPPASMRTST SEKELCKMAD
2110 2120 2130 2140 2150
SFFGTDTILE SPDDFSQHDQ DKSPLSDSGF ETRSEKTPSA PQSAESTGPK
2160 2170 2180 2190 2200
PLFHEVPIPP VITETRTEVV HVIRSYDPSA GDVPQTQPEE PVSPKPSPTF
2210 2220 2230 2240 2250
MELEPKPTTS SIKEKVKAFQ MKASSEEDDH NRVLSKGMRV KEETHITTTT
2260 2270 2280 2290 2300
RMVYHSPPGG EGASERIEET MSVHDIMKAF QSGRDPSKEL AGLFEHKSAV
2310 2320 2330 2340 2350
SPDVHKSAAE TSAQHAEKDN QMKPKLERII EVHIEKGNQA EPTEVIIRET
2360 2370 2380 2390 2400
KKHPEKEMYV YQKDLSRGDI NLKDFLPEKH DAFPCSEEQG QQEEEELTAE
2410 2420 2430 2440 2450
ESLPSYLESS RVNTPVSQEE DSRPSSAQLI SDDSYKTLKL LSQHSIEYHD
2460 2470 2480 2490 2500
DELSELRGES YRFAEKMLLS EKLDVSHSDT EESVTDHAGP PSSELQGSDK
2510 2520 2530 2540 2550
RSREKIATAP KKEILSKIYK DVSENGVGKV SKDEHFDKVT VLHYSGNVSS
2560 2570 2580 2590 2600
PKHAMWMRFT EDRLDRGREK LIYEDRVDRT VKEAEEKLTE VSQFFRDKTE
2610 2620 2630 2640 2650
KLNDELQSPE KKARPKNGKE YSSQSPTSSS PEKVLLTELL ASNDEWVKAR
2660 2670 2680 2690 2700
QHGPDGQGFP KAEEKAPSLP SSPEKMVLSQ QTEDSKSTVE AKGSISQSKA
2710 2720 2730 2740 2750
PDGPQSGFQL KQSKLSSIRL KFEQGTHAKS KDMSQEDRKS DGQSRIPVKK
2760 2770 2780 2790 2800
IQESKLPVYQ VFAREKQQKA IDLPDESVSV QKDFMVLKTK DEHAQSNEIV
2810 2820 2830 2840 2850
VNDSGSDNVK KQRTEMSSKA MPDSFSEQQA KDLACHITSD LATRGPWDKK
2860 2870 2880 2890 2900
VFRTWESSGA TNNKSQKEKL SHVLVHDVRE NHIGHPESKS VDQKNEFMSV
2910 2920 2930 2940 2950
TERERKLLTN GSLSEIKEMT VKSPSKKVLY REYVVKEGDH PGGLLDQPSR
2960 2970 2980 2990 3000
RSESSAVSHI PVRVADERRM LSSNIPDGFC EQSAFPKHEL SQKLSQSSMS
3010 3020 3030 3040 3050
KETVETQHFN SIEDEKVTYS EISKVSKHQS YVGLCPPLEE TETSPTKSPD
3060 3070 3080 3090 3100
SLEFSPGKES PSSDVFDHSP IDGLEKLAPL AQTEGGKEIK TLPVYVSFVQ
3110 3120 3130 3140 3150
VGKQYEKEIQ QGGVKKIISQ ECKTVQETRG TFYTTRQQKQ PPSPQGSPED
3160 3170 3180 3190 3200
DTLEQVSFLD SSGKSPLTPE TPSSEEVSYE FTSKTPDSLI AYIPGKPSPI
3210 3220 3230 3240 3250
PEVSEESEEE EQAKSTSLKQ TTVEETAVER EMPNDVSKDS NQRPKNNRVA
3260 3270 3280 3290 3300
YIEFPPPPPL DADQIESDKK HHYLPEKEVD MIEVNLQDEH DKYQLAEPVI
3310 3320 3330 3340 3350
RVQPPSPVPP GADVSDSSDD ESIYQPVPVK KYTFKLKEVD DEQKEKPKAS
3360 3370 3380 3390 3400
AEKASNQKEL ESNGSGKDNE FGLGLDSPQN EIAQNGNNDQ SITECSIATT
3410 3420 3430 3440 3450
AEFSHDTDAT EIDSLDGYDL QDEDDGLTES DSKLPIQAME IKKDIWNTEG
3460 3470 3480 3490 3500
ILKPADRSFS QSKLEVIEEE GKVGPDEDKP PSKSSSSEKT PDKTDQKSGA
3510 3520 3530 3540 3550
QFFTLEGRHP DRSVFPDTYF SYKVDEEFAT PFKTVATKGL DFDPWSNNRG
3560 3570 3580 3590 3600
DDEVFDSKSR EDETKPFGLA VEDRSPATTP DTTPARTPTD ESTPTSEPNP
3610 3620 3630 3640 3650
FPFHEGKMFE MTRSGAIDMS KRDFVEERLQ FFQIGEHTSE GKSGDQGEGD
3660 3670 3680 3690 3700
KSMVTATPQP QSGDTTVETN LERNVETPTV EPNPSIPTSG ECQEGTSSSG
3710 3720 3730 3740 3750
SLEKSAAATN TSKVDPKLRT PIKMGISAST MTMKKEGPGE ITDKIEAVMT
3760 3770 3780 3790 3800
SCQGLENETI TMISNTANSQ MGVRPHEKHD FQKDNFNNNN NLDSSTIQTD
3810 3820 3830 3840 3850
NIMSNIVLTE HSAPTCTTEK DNPVKVSSGK KTGVLQGHCV RDKQKVLGEQ
3860 3870 3880 3890 3900
QKTKELIGIR QKSKLPIKAT SPKDTFPPNH MSNTKASKMK QVSQSEKTKA
3910 3920 3930 3940 3950
LTTSSCVDVK SRIPVKNTHR DNIIAVRKAC ATQKQGQPEK GKAKQLPSKL
3960 3970 3980 3990 4000
PVKVRSTCVT TTTTTATTTT TTTTTTTTSC TVKVRKSQLK EVCKHSIEYF
4010 4020 4030 4040 4050
KGISGETLKL VDRLSEEEKK MQSELSDEEE STSRNTSLSE TSRGGQPSVT
4060 4070 4080 4090 4100
TKSARDKKTE AAPLKSKSEK AGSEKRSSRR TGPQSPCERT DIRMAIVADH
4110 4120 4130 4140 4150
LGLSWTELAR ELNFSVDEIN QIRVENPNSL ISQSFMLLKK WVTRDGKNAT
4160 4170 4180 4190 4200
TDALTSVLTK INRIDIVTLL EGPIFDYGNI SGTRSFADEN NVFHDPVDGW
4210 4220 4230 4240 4250
QNETSSGNLE SCAQARRVTG GLLDRLDDSP DQCRDSITSY LKGEAGKFEA
4260 4270 4280 4290 4300
NGSHTEITPE AKTKSYFPES QNDVGKQSTK ETLKPKIHGS GHVEEPASPL
4310 4320 4330 4340 4350
AAYQKSLEET SKLIIEETKP CVPVSMKKMS RTSPADGKPR LSLHEEEGSS
4360 4370
GSEQKQGEGF KVKTKKEIRH VEKKSHS
Length:4,377
Mass (Da):480,410
Last modified:September 1, 2009 - v3
Checksum:iF6F9FABD09F15C13
GO
Isoform 2 (identifier: Q12955-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: MAHAASQLKKNRDLEINAEEEPEKKRKHRKRSRDRK → MSEEPKEKNAKPAHRKRKG
     872-872: G → GNRCTWYKIPKVQEFTVKS
     1442-1450: Missing.
     1478-4081: Missing.
     4082-4082: G → S
     4199-4199: G → GYPSLQVELE...ESQLENVCLS

Note: Contains a phosphoserine at position 1632. Contains a phosphoserine at position 1658.1 Publication
Show »
Length:1,868
Mass (Da):204,142
Checksum:iC02C08780B3918ED
GO
Isoform 3 (identifier: Q12955-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-37: MAHAASQLKKNRDLEINAEEEPEKKRKHRKRSRDRKK → MASSASSSPAGTEDSAPAQGGFGSDYSRSSR
     1442-1450: Missing.
     1478-4081: Missing.
     4082-4082: G → S
     4199-4199: G → GYPSLQVELE...ESQLENVCLS

Note: Contains a phosphoserine at position 1625. Contains a phosphoserine at position 1651.1 Publication
Show »
Length:1,861
Mass (Da):202,592
Checksum:i06C904B8371BB406
GO
Isoform 4 (identifier: Q12955-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-866: Missing.
     867-872: SDVEEG → MALPQS
     1442-1450: Missing.
     1478-4081: Missing.
     4082-4082: G → S
     4199-4199: G → GYPSLQVELE...ESQLENVCLS

Note: Ref.3 (CAB66645) sequence(s) differ(s) from that shown due to (a) frameshift(s) in position(s) 810. Contains a phosphoserine at position 765. Contains a phosphoserine at position 791.1 Publication
Show »
Length:1,001
Mass (Da):111,099
Checksum:iEF695AFF21999D1E
GO
Isoform 5 (identifier: Q12955-7) [UniParc]FASTAAdd to basket

Also known as: AnkG119, Golgi ankyrin

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MAHAAS → MNLRCD
     7-385: Missing.
     850-870: Missing.
     913-918: Missing.
     1036-1043: MVEGEGLA → HGERRGIS
     1442-1450: Missing.
     1478-1880: IERSTGATRS...RTSSPVKSSL → TSCTVKVRKS...IRHVEKKSHS
     1881-4377: Missing.

Note: Avidly binds beta spectrin. Contains a phosphoserine at position 468.1 Publication
Show »
Length:1,465
Mass (Da):160,947
Checksum:i7B43551F7DB9691D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti197 – 1971T → A in CAI56716 (PubMed:17974005).Curated
Sequence conflicti222 – 2221L → P in CAD97900 (PubMed:17974005).Curated
Sequence conflicti327 – 3271I → V in CAD97900 (PubMed:17974005).Curated
Sequence conflicti338 – 3381L → W in BAG58523 (PubMed:14702039).Curated
Sequence conflicti523 – 5231A → T in CAD97900 (PubMed:17974005).Curated
Sequence conflicti578 – 5781L → P in CAI56716 (PubMed:17974005).Curated
Sequence conflicti921 – 9211R → G in CAB66645 (PubMed:11230166).Curated
Sequence conflicti977 – 9771S → P in CAB66645 (PubMed:11230166).Curated
Sequence conflicti1237 – 12371D → G in CAI56716 (PubMed:17974005).Curated
Sequence conflicti1418 – 14181P → R in AAA64834 (PubMed:7836469).Curated
Sequence conflicti1455 – 14551D → E in BAG58523 (PubMed:14702039).Curated
Sequence conflicti1574 – 15741F → L in AAA64834 (PubMed:7836469).Curated
Sequence conflicti1685 – 16851A → R in AAA64834 (PubMed:7836469).Curated
Sequence conflicti1726 – 17261P → A in AAA64834 (PubMed:7836469).Curated
Sequence conflicti2062 – 20632ER → GG in AAA64834 (PubMed:7836469).Curated
Sequence conflicti2146 – 21461S → T in AAA64834 (PubMed:7836469).Curated
Sequence conflicti3919 – 39191H → P in AAA64834 (PubMed:7836469).Curated
Sequence conflicti4137 – 41371L → F in CAB66645 (PubMed:11230166).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1569 – 15691S → A Found in a patient with autism; unknown pathological significance. 1 Publication
VAR_068702
Natural varianti2318 – 23181K → R.
Corresponds to variant rs59021407 [ dbSNP | Ensembl ].
VAR_061013
Natural varianti2885 – 28851H → Q.
Corresponds to variant rs11599164 [ dbSNP | Ensembl ].
VAR_059115
Natural varianti2996 – 29961Q → H.
Corresponds to variant rs41274672 [ dbSNP | Ensembl ].
VAR_061014
Natural varianti3117 – 31171I → V.
Corresponds to variant rs28932171 [ dbSNP | Ensembl ].
VAR_059116
Natural varianti3123 – 31231K → R.
Corresponds to variant rs10821668 [ dbSNP | Ensembl ].
VAR_059117
Natural varianti3720 – 37201T → M Found in a patient with autism; unknown pathological significance. 1 Publication
VAR_068703
Natural varianti4255 – 42551T → P Found in a patient with autism; unknown pathological significance. 1 Publication
VAR_068704
Natural varianti4257 – 42571I → V.
Corresponds to variant rs12261793 [ dbSNP | Ensembl ].
VAR_054333

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 866866Missing in isoform 4. 1 PublicationVSP_046885Add
BLAST
Alternative sequencei1 – 3737MAHAA…RDRKK → MASSASSSPAGTEDSAPAQG GFGSDYSRSSR in isoform 3. 1 PublicationVSP_044348Add
BLAST
Alternative sequencei1 – 3636MAHAA…SRDRK → MSEEPKEKNAKPAHRKRKG in isoform 2. 1 PublicationVSP_044349Add
BLAST
Alternative sequencei1 – 66MAHAAS → MNLRCD in isoform 5. 1 PublicationVSP_053753
Alternative sequencei7 – 385379Missing in isoform 5. 1 PublicationVSP_053754Add
BLAST
Alternative sequencei850 – 87021Missing in isoform 5. 1 PublicationVSP_053755Add
BLAST
Alternative sequencei867 – 8726SDVEEG → MALPQS in isoform 4. 1 PublicationVSP_046886
Alternative sequencei872 – 8721G → GNRCTWYKIPKVQEFTVKS in isoform 2. 1 PublicationVSP_044350
Alternative sequencei913 – 9186Missing in isoform 5. 1 PublicationVSP_053756
Alternative sequencei1036 – 10438MVEGEGLA → HGERRGIS in isoform 5. 1 PublicationVSP_053757
Alternative sequencei1442 – 14509Missing in isoform 2, isoform 3, isoform 4 and isoform 5. 4 PublicationsVSP_044351
Alternative sequencei1478 – 40812604Missing in isoform 2, isoform 3 and isoform 4. 3 PublicationsVSP_044352Add
BLAST
Alternative sequencei1478 – 1880403IERST…VKSSL → TSCTVKVRKSQLKEVCKHSI EYFKGISGETLKLVDRLSEE EKKMQSELSDEEESTSRNTS LSETSRGGQPSVTTKSARDK KTEAAPLKSKSEKAGSEKRS SRRTGPQSPCERTDIRMAIV ADHLGLSWTELARELNFSVD EINQIRVENPNSLISQSFML LKKWVTRDGKNATTDALTSV LTKINRIDIVTLLEGPIFDY GNISGTRSFADENNVFHDPV DGWQNETSSGNLESCAQARR VTGGLLDRLDDSPDQCRDSI TSYLKGEAGKFEANGSHTEI TPEAKTKSYFPESQNDVGKQ STKETLKPKIHGSGHVEEPA SPLAAYQKSLEETSKLSKLI IEETKPCVPVSMKKMSRTSP ADGKPRLSLHEEEGSSGSEQ KQGEGFKVKTKKEIRHVEKK SHS in isoform 5. 1 PublicationVSP_053758Add
BLAST
Alternative sequencei1881 – 43772497Missing in isoform 5. 1 PublicationVSP_053759Add
BLAST
Alternative sequencei4082 – 40821G → S in isoform 2, isoform 3 and isoform 4. 3 PublicationsVSP_044353
Alternative sequencei4199 – 41991G → GYPSLQVELETPTGLHYTPP TPFQQDDYFSDISSIESPLR TPSRLSDGLVPSQGNIEHSA DGPPVVTAEDASLEDSKLED SVPLTEMPEAVDVDESQLEN VCLS in isoform 2, isoform 3 and isoform 4. 3 PublicationsVSP_044354

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13616 mRNA. Translation: AAA64834.1.
U43965 mRNA. Translation: AAB08437.1.
AL136710 mRNA. Translation: CAB66645.1. Frameshift.
AK295661 mRNA. Translation: BAG58523.1.
BX537917 mRNA. Translation: CAD97900.2.
BX648574 mRNA. Translation: CAI56716.1.
AC022390 Genomic DNA. No translation available.
AC023904 Genomic DNA. No translation available.
AL359267 Genomic DNA. No translation available.
AL359377 Genomic DNA. No translation available.
AL391707 Genomic DNA. No translation available.
AL592430 Genomic DNA. No translation available.
AL607065 Genomic DNA. No translation available.
CCDSiCCDS55711.1. [Q12955-4]
CCDS55712.1. [Q12955-5]
CCDS7258.1. [Q12955-3]
CCDS7259.1. [Q12955-6]
PIRiA55575.
RefSeqiNP_001140.2. NM_001149.3. [Q12955-6]
NP_001191332.1. NM_001204403.1. [Q12955-5]
NP_001191333.1. NM_001204404.1. [Q12955-4]
NP_066267.2. NM_020987.3. [Q12955-3]
UniGeneiHs.499725.

Genome annotation databases

EnsembliENST00000280772; ENSP00000280772; ENSG00000151150. [Q12955-3]
ENST00000355288; ENSP00000347436; ENSG00000151150. [Q12955-6]
ENST00000373827; ENSP00000362933; ENSG00000151150. [Q12955-5]
ENST00000503366; ENSP00000425236; ENSG00000151150. [Q12955-4]
GeneIDi288.
KEGGihsa:288.
UCSCiuc001jky.3. human. [Q12955-3]
uc001jkz.4. human. [Q12955-5]
uc010qih.2. human. [Q12955-4]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Ankyrin entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13616 mRNA. Translation: AAA64834.1.
U43965 mRNA. Translation: AAB08437.1.
AL136710 mRNA. Translation: CAB66645.1. Frameshift.
AK295661 mRNA. Translation: BAG58523.1.
BX537917 mRNA. Translation: CAD97900.2.
BX648574 mRNA. Translation: CAI56716.1.
AC022390 Genomic DNA. No translation available.
AC023904 Genomic DNA. No translation available.
AL359267 Genomic DNA. No translation available.
AL359377 Genomic DNA. No translation available.
AL391707 Genomic DNA. No translation available.
AL592430 Genomic DNA. No translation available.
AL607065 Genomic DNA. No translation available.
CCDSiCCDS55711.1. [Q12955-4]
CCDS55712.1. [Q12955-5]
CCDS7258.1. [Q12955-3]
CCDS7259.1. [Q12955-6]
PIRiA55575.
RefSeqiNP_001140.2. NM_001149.3. [Q12955-6]
NP_001191332.1. NM_001204403.1. [Q12955-5]
NP_001191333.1. NM_001204404.1. [Q12955-4]
NP_066267.2. NM_020987.3. [Q12955-3]
UniGeneiHs.499725.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4O6XX-ray2.10A/B4088-4199[»]
ProteinModelPortaliQ12955.
SMRiQ12955. Positions 35-818, 982-1442, 4088-4187.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106785. 15 interactions.
DIPiDIP-49017N.
IntActiQ12955. 5 interactions.
STRINGi9606.ENSP00000280772.

PTM databases

PhosphoSiteiQ12955.

Polymorphism and mutation databases

BioMutaiANK3.
DMDMi257051061.

Proteomic databases

MaxQBiQ12955.
PaxDbiQ12955.
PRIDEiQ12955.

Protocols and materials databases

DNASUi288.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000280772; ENSP00000280772; ENSG00000151150. [Q12955-3]
ENST00000355288; ENSP00000347436; ENSG00000151150. [Q12955-6]
ENST00000373827; ENSP00000362933; ENSG00000151150. [Q12955-5]
ENST00000503366; ENSP00000425236; ENSG00000151150. [Q12955-4]
GeneIDi288.
KEGGihsa:288.
UCSCiuc001jky.3. human. [Q12955-3]
uc001jkz.4. human. [Q12955-5]
uc010qih.2. human. [Q12955-4]

Organism-specific databases

CTDi288.
GeneCardsiGC10M061788.
H-InvDBHIX0008849.
HGNCiHGNC:494. ANK3.
HPAiCAB013249.
CAB015179.
HPA055643.
MIMi600465. gene.
615493. phenotype.
neXtProtiNX_Q12955.
Orphaneti356996. Intellectual disability - hypotonia - spasticity - sleep disorder.
3140. Schizophrenia.
PharmGKBiPA24800.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0666.
GeneTreeiENSGT00760000118950.
HOGENOMiHOG000008707.
HOVERGENiHBG024337.
InParanoidiQ12955.
KOiK10380.
OMAiDQSITEC.
OrthoDBiEOG7P02H2.
PhylomeDBiQ12955.
TreeFamiTF351263.

Enzyme and pathway databases

ReactomeiREACT_22266. Interaction between L1 and Ankyrins.

Miscellaneous databases

ChiTaRSiANK3. human.
GeneWikiiANK3.
GenomeRNAii288.
NextBioi1175.
PROiQ12955.
SOURCEiSearch...

Gene expression databases

BgeeiQ12955.
CleanExiHS_ANK3.
ExpressionAtlasiQ12955. baseline and differential.
GenevisibleiQ12955. 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. 3 hits.
PF12796. Ank_2. 6 hits.
PF00531. Death. 1 hit.
PF00791. ZU5. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 22 hits.
SM00005. DEATH. 1 hit.
SM00218. ZU5. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF48403. SSF48403. 3 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 21 hits.
PS50017. DEATH_DOMAIN. 1 hit.
PS51145. ZU5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "AnkyrinG. A new ankyrin gene with neural-specific isoforms localized at the axonal initial segment and node of Ranvier."
    Kordeli E., Lambert S., Bennett V.
    J. Biol. Chem. 270:2352-2359(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Brain stem.
  2. "Identification of a small cytoplasmic ankyrin (AnkG119) in the kidney and muscle that binds beta I sigma spectrin and associates with the Golgi apparatus."
    Devarajan P., Stabach P.R., Mann A.S., Ardito T., Kashgarian M., Morrow J.S.
    J. Cell Biol. 133:819-830(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION (ISOFORM 5), SUBCELLULAR LOCATION (ISOFORM 5).
    Tissue: Kidney.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
    Tissue: Kidney.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Hippocampus.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Cervix and Fetal kidney.
  6. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The ammonium transporter RhBG: requirement of a tyrosine-based signal and ankyrin-G for basolateral targeting and membrane anchorage in polarized kidney epithelial cells."
    Lopez C., Metral S., Eladari D., Drevensek S., Gane P., Chambrey R., Bennett V., Cartron J.-P., Le Van Kim C., Colin Y.
    J. Biol. Chem. 280:8221-8228(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RHBG.
  8. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
    Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
    Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-4338.
    Tissue: Mammary cancer.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Novel interactions of ankyrins-G at the costameres: the muscle-specific Obscurin/Titin-Binding-related Domain (OTBD) binds plectin and filamin C."
    Maiweilidan Y., Klauza I., Kordeli E.
    Exp. Cell Res. 317:724-736(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLEC AND FLNC, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  11. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-847; SER-1445 AND SER-4298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4229; SER-4290 AND SER-4298, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1632 AND SER-1658 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1625 AND SER-1651 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-765 AND SER-791 (ISOFORM 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468 (ISOFORM 5), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. "Ankyrin-3 is a novel binding partner of the voltage-gated potassium channel Kv1.1 implicated in renal magnesium handling."
    San-Cristobal P., Lainez S., Dimke H., de Graaf M.J., Hoenderop J.G., Bindels R.J.
    Kidney Int. 85:94-102(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KCNA1.
  14. "Mutations of ANK3 identified by exome sequencing are associated with autism susceptibility."
    Bi C., Wu J., Jiang T., Liu Q., Cai W., Yu P., Cai T., Zhao M., Jiang Y.H., Sun Z.S.
    Hum. Mutat. 33:1635-1638(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ALA-1569; MET-3720 AND PRO-4255, POSSIBLE INVOLVEMENT IN SUSCEPTIBILITY TO AUTISM.
  15. Cited for: INVOLMENT IN MRT37.

Entry informationi

Entry nameiANK3_HUMAN
AccessioniPrimary (citable) accession number: Q12955
Secondary accession number(s): B1AQT2
, B4DIL1, E9PE32, Q13484, Q5CZH9, Q5VXD5, Q7Z3G4, Q9H0P5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: September 1, 2009
Last modified: June 24, 2015
This is version 149 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, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: 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

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 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.