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Q12955 (ANK3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ankyrin-3

Short name=ANK-3
Alternative name(s):
Ankyrin-G
Gene names
Name:ANK3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length4377 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2

Isoform AnkG119:May be part of a Golgi-specific membrane cytoskeleton in association with beta-spectrin. Ref.2

Subunit structure

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. Ref.7

Subcellular location

Cytoplasmcytoskeleton. Cell junctionsynapsepostsynaptic cell membrane By similarity. Lysosome By similarity. Note: In skeletal muscle, localized at costameres and neuromuscular junctions By similarity. In macrophages, associated with lysosomes By similarity. Ref.2

Isoform AnkG119: Cytoplasmcytoskeleton. Golgi apparatus Ref.2.

Tissue specificity

Expressed in brain, neurons and other tissues. Ref.1

Domain

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.

Involvement in disease

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

Mental retardation, autosomal recessive 37 (MRT37) [MIM:615493]: A 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.
Note: 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 (Ref.12). Ref.12

Sequence similarities

Contains 23 ANK repeats.

Contains 1 death domain.

Contains 2 ZU5 domains.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Golgi apparatus
Lysosome
Membrane
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseMental retardation
   DomainANK repeat
Repeat
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi to plasma membrane protein transport

Inferred from mutant phenotype PubMed 17620337. Source: BHF-UCL

axon guidance

Inferred from electronic annotation. Source: Ensembl

axonogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

cytoskeletal anchoring at plasma membrane

Traceable author statement Ref.1. Source: ProtInc

establishment of protein localization

Inferred from mutant phenotype Ref.7. Source: UniProtKB

maintenance of protein location in plasma membrane

Inferred from genetic interaction PubMed 17620337. Source: BHF-UCL

membrane assembly

Inferred from mutant phenotype PubMed 14757759PubMed 17620337. Source: BHF-UCL

mitotic cytokinesis

Inferred from mutant phenotype PubMed 14757759PubMed 17620337. Source: BHF-UCL

neuromuscular junction development

Inferred from electronic annotation. Source: Ensembl

neuronal action potential

Inferred from sequence or structural similarity. Source: BHF-UCL

plasma membrane organization

Inferred from mutant phenotype PubMed 17620337. Source: BHF-UCL

positive regulation of cell communication by electrical coupling

Inferred from electronic annotation. Source: Ensembl

positive regulation of gene expression

Inferred from sequence or structural similarity PubMed 18180363. Source: BHF-UCL

positive regulation of homotypic cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

positive regulation of membrane depolarization during cardiac muscle cell action potential

Inferred from sequence or structural similarity PubMed 18180363. Source: BHF-UCL

positive regulation of membrane potential

Inferred from sequence or structural similarity PubMed 18180363. Source: BHF-UCL

positive regulation of protein targeting to membrane

Inferred from electronic annotation. Source: Ensembl

positive regulation of sodium ion transmembrane transporter activity

Inferred from sequence or structural similarity PubMed 18180363. Source: BHF-UCL

positive regulation of sodium ion transport

Inferred from sequence or structural similarity PubMed 18180363. Source: BHF-UCL

protein localization to plasma membrane

Inferred from mutant phenotype PubMed 14757759. Source: BHF-UCL

protein targeting to plasma membrane

Inferred from mutant phenotype PubMed 17620337. Source: BHF-UCL

regulation of potassium ion transport

Inferred from sequence or structural similarity. Source: BHF-UCL

signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentGolgi apparatus

Traceable author statement Ref.2. Source: ProtInc

T-tubule

Inferred from sequence or structural similarity. Source: BHF-UCL

Z disc

Inferred from electronic annotation. Source: Ensembl

axon initial segment

Inferred from sequence or structural similarity. Source: BHF-UCL

basolateral plasma membrane

Inferred from direct assay Ref.7. Source: UniProtKB

cell surface

Inferred from sequence or structural similarity PubMed 21223964. Source: BHF-UCL

costamere

Traceable author statement PubMed 21223964. Source: BHF-UCL

dendrite

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Traceable author statement Ref.2. Source: ProtInc

intercalated disc

Inferred from sequence or structural similarity. Source: BHF-UCL

lateral plasma membrane

Inferred from direct assay PubMed 14757759. Source: BHF-UCL

lysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuromuscular junction

Inferred from electronic annotation. Source: Ensembl

node of Ranvier

Inferred from sequence or structural similarity. Source: BHF-UCL

paranode region of axon

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from sequence or structural similarity. Source: BHF-UCL

postsynaptic membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

sarcolemma

Inferred from direct assay PubMed 21223964. Source: BHF-UCL

sarcoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

spectrin-associated cytoskeleton

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular_functioncadherin binding

Inferred from sequence or structural similarity. Source: BHF-UCL

cytoskeletal protein binding

Inferred from sequence or structural similarity PubMed 21223964. Source: BHF-UCL

ion channel binding

Inferred from sequence or structural similarity. Source: BHF-UCL

protein binding, bridging

Inferred from sequence or structural similarity. Source: BHF-UCL

spectrin binding

Inferred from sequence or structural similarity. Source: BHF-UCL

structural constituent of cytoskeleton

Inferred from mutant phenotype PubMed 17620337. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q12955-3)

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.
Isoform 2 (identifier: Q12955-4)

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
Isoform 3 (identifier: Q12955-5)

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
Isoform 4 (identifier: Q12955-6)

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.
Isoform AnkG119 (identifier: Q12955-7)

Also known as: 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 43774377Ankyrin-3
PRO_0000066886

Regions

Repeat73 – 10230ANK 1
Repeat106 – 13530ANK 2
Repeat139 – 16830ANK 3
Repeat172 – 20130ANK 4
Repeat203 – 23028ANK 5
Repeat234 – 26330ANK 6
Repeat267 – 29630ANK 7
Repeat300 – 32930ANK 8
Repeat333 – 36230ANK 9
Repeat366 – 39530ANK 10
Repeat399 – 42830ANK 11
Repeat432 – 46130ANK 12
Repeat465 – 49430ANK 13
Repeat498 – 52730ANK 14
Repeat531 – 56030ANK 15
Repeat564 – 59330ANK 16
Repeat597 – 62630ANK 17
Repeat630 – 65930ANK 18
Repeat663 – 69230ANK 19
Repeat696 – 72530ANK 20
Repeat729 – 75830ANK 21
Repeat762 – 79130ANK 22
Repeat795 – 82531ANK 23
Domain982 – 1107126ZU5 1
Domain1108 – 1272165ZU5 2
Domain4090 – 417485Death
Region1273 – 1407135UPA domain By similarity
Compositional bias1519 – 1898380Ser-rich
Compositional bias2247 – 22504Poly-Thr
Compositional bias2393 – 23964Poly-Glu
Compositional bias3205 – 32117Poly-Glu
Compositional bias3255 – 32595Poly-Pro
Compositional bias3482 – 34876Poly-Ser
Compositional bias3785 – 37917Poly-Asn
Compositional bias3957 – 398125Thr-rich

Amino acid modifications

Modified residue391Phosphoserine Ref.10
Modified residue8471Phosphoserine Ref.10
Modified residue14451Phosphoserine Ref.10
Modified residue42981Phosphoserine Ref.10
Cross-link4338Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.8

Natural variations

Alternative sequence1 – 866866Missing in isoform 4.
VSP_046885
Alternative sequence1 – 3737MAHAA…RDRKK → MASSASSSPAGTEDSAPAQG GFGSDYSRSSR in isoform 3.
VSP_044348
Alternative sequence1 – 3636MAHAA…SRDRK → MSEEPKEKNAKPAHRKRKG in isoform 2.
VSP_044349
Alternative sequence1 – 66MAHAAS → MNLRCD in isoform AnkG119.
VSP_053753
Alternative sequence7 – 385379Missing in isoform AnkG119.
VSP_053754
Alternative sequence850 – 87021Missing in isoform AnkG119.
VSP_053755
Alternative sequence867 – 8726SDVEEG → MALPQS in isoform 4.
VSP_046886
Alternative sequence8721G → GNRCTWYKIPKVQEFTVKS in isoform 2.
VSP_044350
Alternative sequence913 – 9186Missing in isoform AnkG119.
VSP_053756
Alternative sequence1036 – 10438MVEGEGLA → HGERRGIS in isoform AnkG119.
VSP_053757
Alternative sequence1442 – 14509Missing in isoform 2, isoform 3, isoform 4 and isoform AnkG119.
VSP_044351
Alternative sequence1478 – 40812604Missing in isoform 2, isoform 3 and isoform 4.
VSP_044352
Alternative sequence1478 – 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 AnkG119.
VSP_053758
Alternative sequence1881 – 43772497Missing in isoform AnkG119.
VSP_053759
Alternative sequence40821G → S in isoform 2, isoform 3 and isoform 4.
VSP_044353
Alternative sequence41991G → GYPSLQVELETPTGLHYTPP TPFQQDDYFSDISSIESPLR TPSRLSDGLVPSQGNIEHSA DGPPVVTAEDASLEDSKLED SVPLTEMPEAVDVDESQLEN VCLS in isoform 2, isoform 3 and isoform 4.
VSP_044354
Natural variant15691S → A Found in a patient with autism; unknown pathological significance. Ref.11
VAR_068702
Natural variant23181K → R.
Corresponds to variant rs59021407 [ dbSNP | Ensembl ].
VAR_061013
Natural variant28851H → Q.
Corresponds to variant rs11599164 [ dbSNP | Ensembl ].
VAR_059115
Natural variant29961Q → H.
Corresponds to variant rs41274672 [ dbSNP | Ensembl ].
VAR_061014
Natural variant31171I → V.
Corresponds to variant rs28932171 [ dbSNP | Ensembl ].
VAR_059116
Natural variant31231K → R.
Corresponds to variant rs10821668 [ dbSNP | Ensembl ].
VAR_059117
Natural variant37201T → M Found in a patient with autism; unknown pathological significance. Ref.11
VAR_068703
Natural variant42551T → P Found in a patient with autism; unknown pathological significance. Ref.11
VAR_068704
Natural variant42571I → V.
Corresponds to variant rs12261793 [ dbSNP | Ensembl ].
VAR_054333

Experimental info

Sequence conflict1971T → A in CAI56716. Ref.5
Sequence conflict2221L → P in CAD97900. Ref.5
Sequence conflict3271I → V in CAD97900. Ref.5
Sequence conflict3381L → W in BAG58523. Ref.4
Sequence conflict5231A → T in CAD97900. Ref.5
Sequence conflict5781L → P in CAI56716. Ref.5
Sequence conflict9211R → G in CAB66645. Ref.3
Sequence conflict9771S → P in CAB66645. Ref.3
Sequence conflict12371D → G in CAI56716. Ref.5
Sequence conflict14181P → R in AAA64834. Ref.1
Sequence conflict14551D → E in BAG58523. Ref.4
Sequence conflict15741F → L in AAA64834. Ref.1
Sequence conflict16851A → R in AAA64834. Ref.1
Sequence conflict17261P → A in AAA64834. Ref.1
Sequence conflict2062 – 20632ER → GG in AAA64834. Ref.1
Sequence conflict21461S → T in AAA64834. Ref.1
Sequence conflict39191H → P in AAA64834. Ref.1
Sequence conflict41371L → F in CAB66645. Ref.3

Sequences

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

Last modified September 1, 2009. Version 3.
Checksum: F6F9FABD09F15C13

FASTA4,377480,410
        10         20         30         40         50         60 
MAHAASQLKK NRDLEINAEE EPEKKRKHRK RSRDRKKKSD ANASYLRAAR AGHLEKALDY 

        70         80         90        100        110        120 
IKNGVDINIC NQNGLNALHL ASKEGHVEVV SELLQREANV DAATKKGNTA LHIASLAGQA 

       130        140        150        160        170        180 
EVVKVLVTNG ANVNAQSQNG FTPLYMAAQE NHLEVVKFLL DNGASQSLAT EDGFTPLAVA 

       190        200        210        220        230        240 
LQQGHDQVVS LLLENDTKGK VRLPALHIAA RKDDTKAAAL LLQNDNNADV ESKSGFTPLH 

       250        260        270        280        290        300 
IAAHYGNINV ATLLLNRAAA VDFTARNDIT PLHVASKRGN ANMVKLLLDR GAKIDAKTRD 

       310        320        330        340        350        360 
GLTPLHCGAR SGHEQVVEML LDRAAPILSK TKNGLSPLHM ATQGDHLNCV QLLLQHNVPV 

       370        380        390        400        410        420 
DDVTNDYLTA LHVAAHCGHY KVAKVLLDKK ANPNAKALNG FTPLHIACKK NRIKVMELLL 

       430        440        450        460        470        480 
KHGASIQAVT ESGLTPIHVA AFMGHVNIVS QLMHHGASPN TTNVRGETAL HMAARSGQAE 

       490        500        510        520        530        540 
VVRYLVQDGA QVEAKAKDDQ TPLHISARLG KADIVQQLLQ QGASPNAATT SGYTPLHLSA 

       550        560        570        580        590        600 
REGHEDVAAF LLDHGASLSI TTKKGFTPLH VAAKYGKLEV ANLLLQKSAS PDAAGKSGLT 

       610        620        630        640        650        660 
PLHVAAHYDN QKVALLLLDQ GASPHAAAKN GYTPLHIAAK KNQMDIATTL LEYGADANAV 

       670        680        690        700        710        720 
TRQGIASVHL AAQEGHVDMV SLLLGRNANV NLSNKSGLTP LHLAAQEDRV NVAEVLVNQG 

       730        740        750        760        770        780 
AHVDAQTKMG YTPLHVGCHY GNIKIVNFLL QHSAKVNAKT KNGYTPLHQA AQQGHTHIIN 

       790        800        810        820        830        840 
VLLQNNASPN ELTVNGNTAL GIARRLGYIS VVDTLKIVTE ETMTTTTVTE KHKMNVPETM 

       850        860        870        880        890        900 
NEVLDMSDDE VRKANAPEML SDGEYISDVE EGEDAMTGDT DKYLGPQDLK ELGDDSLPAE 

       910        920        930        940        950        960 
GYMGFSLGAR SASLRSFSSD RSYTLNRSSY ARDSMMIEEL LVPSKEQHLT FTREFDSDSL 

       970        980        990       1000       1010       1020 
RHYSWAADTL DNVNLVSSPI HSGFLVSFMV DARGGSMRGS RHHGMRIIIP PRKCTAPTRI 

      1030       1040       1050       1060       1070       1080 
TCRLVKRHKL ANPPPMVEGE GLASRLVEMG PAGAQFLGPV IVEIPHFGSM RGKERELIVL 

      1090       1100       1110       1120       1130       1140 
RSENGETWKE HQFDSKNEDL TELLNGMDEE LDSPEELGKK RICRIITKDF PQYFAVVSRI 

      1150       1160       1170       1180       1190       1200 
KQESNQIGPE GGILSSTTVP LVQASFPEGA LTKRIRVGLQ AQPVPDEIVK KILGNKATFS 

      1210       1220       1230       1240       1250       1260 
PIVTVEPRRR KFHKPITMTI PVPPPSGEGV SNGYKGDTTP NLRLLCSITG GTSPAQWEDI 

      1270       1280       1290       1300       1310       1320 
TGTTPLTFIK DCVSFTTNVS ARFWLADCHQ VLETVGLATQ LYRELICVPY MAKFVVFAKM 

      1330       1340       1350       1360       1370       1380 
NDPVESSLRC FCMTDDKVDK TLEQQENFEE VARSKDIEVL EGKPIYVDCY GNLAPLTKGG 

      1390       1400       1410       1420       1430       1440 
QQLVFNFYSF KENRLPFSIK IRDTSQEPCG RLSFLKEPKT TKGLPQTAVC NLNITLPAHK 

      1450       1460       1470       1480       1490       1500 
KETESDQDDE IEKTDRRQSF ASLALRKRYS YLTEPGMIER STGATRSLPT TYSYKPFFST 

      1510       1520       1530       1540       1550       1560 
RPYQSWTTAP ITVPGPAKSG FTSLSSSSSN TPSASPLKSI WSVSTPSPIK STLGASTTSS 

      1570       1580       1590       1600       1610       1620 
VKSISDVASP IRSFRTMSSP IKTVVSQSPY NIQVSSGTLA RAPAVTEATP LKGLASNSTF 

      1630       1640       1650       1660       1670       1680 
SSRTSPVTTA GSLLERSSIT MTPPASPKSN INMYSSSLPF KSIITSAAPL ISSPLKSVVS 

      1690       1700       1710       1720       1730       1740 
PVKSAVDVIS SAKITMASSL SSPVKQMPGH AEVALVNGSI SPLKYPSSST LINGCKATAT 

      1750       1760       1770       1780       1790       1800 
LQEKISSATN SVSSVVSAAT DTVEKVFSTT TAMPFSPLRS YVSAAPSAFQ SLRTPSASAL 

      1810       1820       1830       1840       1850       1860 
YTSLGSSISA TTSSVTSSII TVPVYSVVNV LPEPALKKLP DSNSFTKSAA ALLSPIKTLT 

      1870       1880       1890       1900       1910       1920 
TETHPQPHFS RTSSPVKSSL FLAPSALKLS TPSSLSSSQE ILKDVAEMKE DLMRMTAILQ 

      1930       1940       1950       1960       1970       1980 
TDVPEEKPFQ PELPKEGRID DEEPFKIVEK VKEDLVKVSE ILKKDVCVDN KGSPKSPKSD 

      1990       2000       2010       2020       2030       2040 
KGHSPEDDWI EFSSEEIREA RQQAAASQSP SLPERVQVKA KAASEKDYNL TKVIDYLTND 

      2050       2060       2070       2080       2090       2100 
IGSSSLTNLK YKFEDAKKDG EERQKRVLKP AIALQEHKLK MPPASMRTST SEKELCKMAD 

      2110       2120       2130       2140       2150       2160 
SFFGTDTILE SPDDFSQHDQ DKSPLSDSGF ETRSEKTPSA PQSAESTGPK PLFHEVPIPP 

      2170       2180       2190       2200       2210       2220 
VITETRTEVV HVIRSYDPSA GDVPQTQPEE PVSPKPSPTF MELEPKPTTS SIKEKVKAFQ 

      2230       2240       2250       2260       2270       2280 
MKASSEEDDH NRVLSKGMRV KEETHITTTT RMVYHSPPGG EGASERIEET MSVHDIMKAF 

      2290       2300       2310       2320       2330       2340 
QSGRDPSKEL AGLFEHKSAV SPDVHKSAAE TSAQHAEKDN QMKPKLERII EVHIEKGNQA 

      2350       2360       2370       2380       2390       2400 
EPTEVIIRET KKHPEKEMYV YQKDLSRGDI NLKDFLPEKH DAFPCSEEQG QQEEEELTAE 

      2410       2420       2430       2440       2450       2460 
ESLPSYLESS RVNTPVSQEE DSRPSSAQLI SDDSYKTLKL LSQHSIEYHD DELSELRGES 

      2470       2480       2490       2500       2510       2520 
YRFAEKMLLS EKLDVSHSDT EESVTDHAGP PSSELQGSDK RSREKIATAP KKEILSKIYK 

      2530       2540       2550       2560       2570       2580 
DVSENGVGKV SKDEHFDKVT VLHYSGNVSS PKHAMWMRFT EDRLDRGREK LIYEDRVDRT 

      2590       2600       2610       2620       2630       2640 
VKEAEEKLTE VSQFFRDKTE KLNDELQSPE KKARPKNGKE YSSQSPTSSS PEKVLLTELL 

      2650       2660       2670       2680       2690       2700 
ASNDEWVKAR QHGPDGQGFP KAEEKAPSLP SSPEKMVLSQ QTEDSKSTVE AKGSISQSKA 

      2710       2720       2730       2740       2750       2760 
PDGPQSGFQL KQSKLSSIRL KFEQGTHAKS KDMSQEDRKS DGQSRIPVKK IQESKLPVYQ 

      2770       2780       2790       2800       2810       2820 
VFAREKQQKA IDLPDESVSV QKDFMVLKTK DEHAQSNEIV VNDSGSDNVK KQRTEMSSKA 

      2830       2840       2850       2860       2870       2880 
MPDSFSEQQA KDLACHITSD LATRGPWDKK VFRTWESSGA TNNKSQKEKL SHVLVHDVRE 

      2890       2900       2910       2920       2930       2940 
NHIGHPESKS VDQKNEFMSV TERERKLLTN GSLSEIKEMT VKSPSKKVLY REYVVKEGDH 

      2950       2960       2970       2980       2990       3000 
PGGLLDQPSR RSESSAVSHI PVRVADERRM LSSNIPDGFC EQSAFPKHEL SQKLSQSSMS 

      3010       3020       3030       3040       3050       3060 
KETVETQHFN SIEDEKVTYS EISKVSKHQS YVGLCPPLEE TETSPTKSPD SLEFSPGKES 

      3070       3080       3090       3100       3110       3120 
PSSDVFDHSP IDGLEKLAPL AQTEGGKEIK TLPVYVSFVQ VGKQYEKEIQ QGGVKKIISQ 

      3130       3140       3150       3160       3170       3180 
ECKTVQETRG TFYTTRQQKQ PPSPQGSPED DTLEQVSFLD SSGKSPLTPE TPSSEEVSYE 

      3190       3200       3210       3220       3230       3240 
FTSKTPDSLI AYIPGKPSPI PEVSEESEEE EQAKSTSLKQ TTVEETAVER EMPNDVSKDS 

      3250       3260       3270       3280       3290       3300 
NQRPKNNRVA YIEFPPPPPL DADQIESDKK HHYLPEKEVD MIEVNLQDEH DKYQLAEPVI 

      3310       3320       3330       3340       3350       3360 
RVQPPSPVPP GADVSDSSDD ESIYQPVPVK KYTFKLKEVD DEQKEKPKAS AEKASNQKEL 

      3370       3380       3390       3400       3410       3420 
ESNGSGKDNE FGLGLDSPQN EIAQNGNNDQ SITECSIATT AEFSHDTDAT EIDSLDGYDL 

      3430       3440       3450       3460       3470       3480 
QDEDDGLTES DSKLPIQAME IKKDIWNTEG ILKPADRSFS QSKLEVIEEE GKVGPDEDKP 

      3490       3500       3510       3520       3530       3540 
PSKSSSSEKT PDKTDQKSGA QFFTLEGRHP DRSVFPDTYF SYKVDEEFAT PFKTVATKGL 

      3550       3560       3570       3580       3590       3600 
DFDPWSNNRG DDEVFDSKSR EDETKPFGLA VEDRSPATTP DTTPARTPTD ESTPTSEPNP 

      3610       3620       3630       3640       3650       3660 
FPFHEGKMFE MTRSGAIDMS KRDFVEERLQ FFQIGEHTSE GKSGDQGEGD KSMVTATPQP 

      3670       3680       3690       3700       3710       3720 
QSGDTTVETN LERNVETPTV EPNPSIPTSG ECQEGTSSSG SLEKSAAATN TSKVDPKLRT 

      3730       3740       3750       3760       3770       3780 
PIKMGISAST MTMKKEGPGE ITDKIEAVMT SCQGLENETI TMISNTANSQ MGVRPHEKHD 

      3790       3800       3810       3820       3830       3840 
FQKDNFNNNN NLDSSTIQTD NIMSNIVLTE HSAPTCTTEK DNPVKVSSGK KTGVLQGHCV 

      3850       3860       3870       3880       3890       3900 
RDKQKVLGEQ QKTKELIGIR QKSKLPIKAT SPKDTFPPNH MSNTKASKMK QVSQSEKTKA 

      3910       3920       3930       3940       3950       3960 
LTTSSCVDVK SRIPVKNTHR DNIIAVRKAC ATQKQGQPEK GKAKQLPSKL PVKVRSTCVT 

      3970       3980       3990       4000       4010       4020 
TTTTTATTTT TTTTTTTTSC TVKVRKSQLK EVCKHSIEYF KGISGETLKL VDRLSEEEKK 

      4030       4040       4050       4060       4070       4080 
MQSELSDEEE STSRNTSLSE TSRGGQPSVT TKSARDKKTE AAPLKSKSEK AGSEKRSSRR 

      4090       4100       4110       4120       4130       4140 
TGPQSPCERT DIRMAIVADH LGLSWTELAR ELNFSVDEIN QIRVENPNSL ISQSFMLLKK 

      4150       4160       4170       4180       4190       4200 
WVTRDGKNAT TDALTSVLTK INRIDIVTLL EGPIFDYGNI SGTRSFADEN NVFHDPVDGW 

      4210       4220       4230       4240       4250       4260 
QNETSSGNLE SCAQARRVTG GLLDRLDDSP DQCRDSITSY LKGEAGKFEA NGSHTEITPE 

      4270       4280       4290       4300       4310       4320 
AKTKSYFPES QNDVGKQSTK ETLKPKIHGS GHVEEPASPL AAYQKSLEET SKLIIEETKP 

      4330       4340       4350       4360       4370 
CVPVSMKKMS RTSPADGKPR LSLHEEEGSS GSEQKQGEGF KVKTKKEIRH VEKKSHS 

« Hide

Isoform 2 [UniParc].

Checksum: C02C08780B3918ED
Show »

FASTA1,868204,142
Isoform 3 [UniParc].

Checksum: 06C904B8371BB406
Show »

FASTA1,861202,592
Isoform 4 [UniParc].

Checksum: EF695AFF21999D1E
Show »

FASTA1,001111,099
Isoform AnkG119 (Golgi ankyrin) [UniParc].

Checksum: 7B43551F7DB9691D
Show »

FASTA1,465160,947

References

« Hide 'large scale' references
[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 ANKG119), FUNCTION (ISOFORM ANKG119), SUBCELLULAR LOCATION (ISOFORM ANKG119).
Tissue: Kidney.
[3]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"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].
[10]"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].
[11]"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 INVOLMENT IN SUSCEPTIBILITY TO AUTISM.
[12]"Homozygous and heterozygous disruptions of ANK3: at the crossroads of neurodevelopmental and psychiatric disorders."
Iqbal Z., Vandeweyer G., van der Voet M., Waryah A.M., Zahoor M.Y., Besseling J.A., Roca L.T., Vulto-van Silfhout A.T., Nijhof B., Kramer J.M., Van der Aa N., Ansar M., Peeters H., Helsmoortel C., Gilissen C., Vissers L.E., Veltman J.A., de Brouwer A.P. expand/collapse author list , Frank Kooy R., Riazuddin S., Schenck A., van Bokhoven H., Rooms L.
Hum. Mol. Genet. 22:1960-1970(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLMENT IN MRT37.
+Additional computationally mapped references.

Web resources

Wikipedia

Ankyrin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA55575.
RefSeqNP_001140.2. NM_001149.3.
NP_001191332.1. NM_001204403.1.
NP_001191333.1. NM_001204404.1.
NP_066267.2. NM_020987.3.
UniGeneHs.499725.

3D structure databases

ProteinModelPortalQ12955.
SMRQ12955. Positions 14-871, 982-1442, 4090-4167.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106785. 10 interactions.
DIPDIP-49017N.
IntActQ12955. 2 interactions.
STRING9606.ENSP00000280772.

PTM databases

PhosphoSiteQ12955.

Polymorphism databases

DMDM257051061.

Proteomic databases

PaxDbQ12955.
PRIDEQ12955.
ProMEXQ12955.

Protocols and materials databases

DNASU288.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000280772; ENSP00000280772; ENSG00000151150. [Q12955-3]
ENST00000355288; ENSP00000347436; ENSG00000151150. [Q12955-6]
ENST00000373827; ENSP00000362933; ENSG00000151150. [Q12955-5]
ENST00000503366; ENSP00000425236; ENSG00000151150. [Q12955-4]
GeneID288.
KEGGhsa:288.
UCSCuc001jky.3. human. [Q12955-3]
uc001jkz.4. human. [Q12955-5]
uc010qih.2. human. [Q12955-4]

Organism-specific databases

CTD288.
GeneCardsGC10M061788.
H-InvDBHIX0008849.
HGNCHGNC:494. ANK3.
HPACAB013249.
CAB015179.
HPA055643.
MIM600465. gene.
615493. phenotype.
neXtProtNX_Q12955.
Orphanet356996. Intellectual deficiency - hypotonia - spasticity - sleep disorder.
3140. Schizophrenia.
PharmGKBPA24800.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0666.
HOGENOMHOG000012873.
HOVERGENHBG024337.
InParanoidQ12955.
KOK10380.
OMAQNGNNDQ.
OrthoDBEOG7P02H2.
PhylomeDBQ12955.
TreeFamTF351263.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.

Gene expression databases

ArrayExpressQ12955.
BgeeQ12955.
CleanExHS_ANK3.
GenevestigatorQ12955.

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. 3 hits.
PF12796. Ank_2. 6 hits.
PF00531. Death. 1 hit.
PF00791. ZU5. 1 hit.
[Graphical view]
PRINTSPR01415. ANKYRIN.
SMARTSM00248. ANK. 22 hits.
SM00005. DEATH. 1 hit.
SM00218. ZU5. 1 hit.
[Graphical view]
SUPFAMSSF47986. SSF47986. 1 hit.
SSF48403. SSF48403. 3 hits.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 21 hits.
PS50017. DEATH_DOMAIN. 1 hit.
PS51145. ZU5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSANK3. human.
GeneWikiANK3.
GenomeRNAi288.
NextBio1175.
PROQ12955.
SOURCESearch...

Entry information

Entry nameANK3_HUMAN
AccessionPrimary (citable) accession number: Q12955
Secondary accession number(s): B1AQT2 expand/collapse secondary AC list , B4DIL1, E9PE32, Q13484, Q5CZH9, Q5VXD5, Q7Z3G4, Q9H0P5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: September 1, 2009
Last modified: April 16, 2014
This is version 135 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

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 10

Human chromosome 10: entries, gene names and cross-references to MIM