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Q02357

- ANK1_MOUSE

UniProt

Q02357 - ANK1_MOUSE

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Protein

Ankyrin-1

Gene

Ank1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP85, and to the cytoskeletal proteins fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link spectrin (beta chain) to the cytoplasmic domain of the erythrocytes anion exchange protein; they retain most or all of these binding functions. In skeletal muscle, isoform Mu7 together with obscurin may provide a molecular link between the sarcoplasmic reticulum and myofibrils.

GO - Biological processi

  1. ER to Golgi vesicle-mediated transport Source: Ensembl
  2. erythrocyte development Source: MGI
  3. iron ion homeostasis Source: MGI
  4. monovalent inorganic cation transport Source: MGI
  5. porphyrin-containing compound biosynthetic process Source: MGI
  6. positive regulation of organelle organization Source: Ensembl
  7. protein targeting to plasma membrane Source: Ensembl
  8. signal transduction Source: InterPro
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Ankyrin-1
Short name:
ANK-1
Alternative name(s):
Erythrocyte ankyrin
Gene namesi
Name:Ank1
Synonyms:Ank-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:88024. Ank1.

Subcellular locationi

Isoform Er1 : Cytoplasmcytoskeleton By similarity
Note: Probably the other erythrocyte (Er) isoforms, are located near the surface of erythrocytic plasma membrane.By similarity
Isoform Mu7 : Membrane By similarity

GO - Cellular componenti

  1. axolemma Source: Ensembl
  2. cortical cytoskeleton Source: MGI
  3. M band Source: Ensembl
  4. membrane Source: MGI
  5. nucleus Source: Ensembl
  6. postsynaptic membrane Source: Ensembl
  7. sarcolemma Source: Ensembl
  8. sarcoplasmic reticulum Source: UniProtKB-KW
  9. spectrin-associated cytoskeleton Source: MGI
  10. Z disc Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane, Sarcoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18621862Ankyrin-1PRO_0000066884Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei101 – 1011(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
Modified residuei229 – 2291(3S)-3-hydroxyasparagine; by HIF1ANBy similarity
Modified residuei427 – 4271(3S)-3-hydroxyasparagine; by HIF1ANBy similarity
Modified residuei460 – 4601(3S)-3-hydroxyasparagine; by HIF1ANBy similarity
Modified residuei625 – 6251(3S)-3-hydroxyasparagine; by HIF1ANBy similarity
Modified residuei658 – 6581(3S)-3-hydroxyasparagine; by HIF1ANBy similarity
Modified residuei691 – 6911(3S)-3-hydroxyaspartate; by HIF1ANBy similarity
Modified residuei724 – 7241(3S)-3-hydroxyasparagine; by HIF1ANBy similarity
Modified residuei757 – 7571(3S)-3-hydroxyasparagine; by HIF1ANBy similarity
Modified residuei852 – 8521Phosphoserine1 Publication
Modified residuei862 – 8621Phosphothreonine1 Publication
Modified residuei957 – 9571Phosphothreonine1 Publication
Modified residuei1069 – 10691Phosphotyrosine1 Publication
Modified residuei1388 – 13881Phosphoserine1 Publication

Post-translational modificationi

Regulated by phosphorylation.By similarity
Acylated by palmitic acid group(s).By similarity
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.By similarity

Keywords - PTMi

Hydroxylation, Lipoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ02357.
PaxDbiQ02357.
PRIDEiQ02357.

PTM databases

PhosphoSiteiQ02357.

Expressioni

Gene expression databases

BgeeiQ02357.
CleanExiMM_ANK1.
ExpressionAtlasiQ02357. baseline and differential.
GenevestigatoriQ02357.

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 (By similarity).By similarity

Protein-protein interaction databases

IntActiQ02357. 3 interactions.
MINTiMINT-255055.

Structurei

3D structure databases

ProteinModelPortaliQ02357.
SMRiQ02357. Positions 7-808, 907-1493.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati40 – 6930ANK 1Add
BLAST
Repeati73 – 10230ANK 2Add
BLAST
Repeati106 – 13530ANK 3Add
BLAST
Repeati139 – 16830ANK 4Add
BLAST
Repeati170 – 19728ANK 5Add
BLAST
Repeati201 – 23030ANK 6Add
BLAST
Repeati234 – 26330ANK 7Add
BLAST
Repeati267 – 29630ANK 8Add
BLAST
Repeati300 – 32930ANK 9Add
BLAST
Repeati333 – 36230ANK 10Add
BLAST
Repeati366 – 39530ANK 11Add
BLAST
Repeati399 – 42830ANK 12Add
BLAST
Repeati432 – 46130ANK 13Add
BLAST
Repeati465 – 49430ANK 14Add
BLAST
Repeati498 – 52730ANK 15Add
BLAST
Repeati531 – 56030ANK 16Add
BLAST
Repeati564 – 59330ANK 17Add
BLAST
Repeati597 – 62630ANK 18Add
BLAST
Repeati630 – 65930ANK 19Add
BLAST
Repeati663 – 69230ANK 20Add
BLAST
Repeati696 – 72530ANK 21Add
BLAST
Repeati729 – 75830ANK 22Add
BLAST
Repeati762 – 79130ANK 23Add
BLAST
Domaini907 – 1032126ZU5 1PROSITE-ProRule annotationAdd
BLAST
Domaini1033 – 1196164ZU5 2PROSITE-ProRule annotationAdd
BLAST
Domaini1399 – 148385DeathPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 82782789 kDa domainAdd
BLAST
Regioni1197 – 1331135UPA domainBy similarityAdd
BLAST
Regioni1387 – 186247655 kDa regulatory domainAdd
BLAST

Domaini

The 55 kDa regulatory domain is involved in regulating binding of SPTB/spectrin (beta chain) and SLC4A1/erythrocyte membrane protein band 3.By similarity
The ANK repeat region forms a spiral around a large central cavity and is involved in binding of ion transporters.By similarity
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.
HOVERGENiHBG004234.
InParanoidiQ02357.
KOiK10380.
OMAiYTIASEA.
OrthoDBiEOG7P02H2.
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. 8 hits.
PF00531. Death. 1 hit.
PF00791. ZU5. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 23 hits.
SM00005. DEATH. 1 hit.
SM00218. ZU5. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF48403. SSF48403. 2 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 20 hits.
PS50017. DEATH_DOMAIN. 1 hit.
PS51145. ZU5. 1 hit.
[Graphical view]

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative promoter usage and alternative splicing. Align

Isoform Er1 (identifier: Q02357-1) [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
MGFCKADAAT SFLRAARSGN LDKALDHLRN GVDINTCNQN GLNGLHLASK
60 70 80 90 100
EGHVKMVVEL LHKEIILETT TKKGNTALHI AALAGQDEVV RELVNYGANV
110 120 130 140 150
NAQSQKGFTP LYMAAQENHL EVVKFLLENG ANQNVATEDG FTPLAVALQQ
160 170 180 190 200
GHENVVAHLI NYGTKGKVRL PALHIAARND DTRTAAVLLQ NDPNPDVLSK
210 220 230 240 250
TGFTPLHIAA HYENLNVAQL LLNRGASVNF TPQNGITPLH IASRRGNVIM
260 270 280 290 300
VRLLLDRGAQ IETRTKDELT PLHCAARNGH VRISEILLDH GAPIQAKTKN
310 320 330 340 350
GLSPIHMAAQ GDHLDCVRLL LQYNAEIDDI TLDHLTPLHV AAHCGHHRVA
360 370 380 390 400
KVLLDKGAKP NSRALNGFTP LHIACKKNHI RVMELLLKTG ASIDAVTESG
410 420 430 440 450
LTPLHVASFM GHLPIVKNLL QRGASPNVSN VKVETPLHMA ARAGHTEVAK
460 470 480 490 500
YLLQNKAKAN AKAKDDQTPL HCAARIGHTG MVKLLLENGA SPNLATTAGH
510 520 530 540 550
TPLHTAAREG HVDTALALLE KEASQACMTK KGFTPLHVAA KYGKVRLAEL
560 570 580 590 600
LLEHDAHPNA AGKNGLTPLH VAVHHNNLDI VKLLLPRGGS PHSPAWNGYT
610 620 630 640 650
PLHIAAKQNQ IEVARSLLQY GGSANAESVQ GVTPLHLAAQ EGHTEMVALL
660 670 680 690 700
LSKQANGNLG NKSGLTPLHL VSQEGHVPVA DVLIKHGVTV DATTRMGYTP
710 720 730 740 750
LHVASHYGNI KLVKFLLQHQ ADVNAKTKLG YSPLHQAAQQ GHTDIVTLLL
760 770 780 790 800
KNGASPNEVS SNGTTPLAIA KRLGYISVTD VLKVVTDETS VVLVSDKHRM
810 820 830 840 850
SYPETVDEIL DVSEDEGDEL VGSKAERRDS RDVGEEKELL DFVPKLDQVV
860 870 880 890 900
ESPAIPRIPC VTPETVVIRS EDQEQASKEY DEDSLIPSSP ATETSDNISP
910 920 930 940 950
VASPVHTGFL VSFMVDARGG SMRGSRHNGL RVVIPPRTCA APTRITCRLV
960 970 980 990 1000
KPQKLNTPPP LAEEEGLASR IIALGPTGAQ FLSPVIVEIP HFASHGRGDR
1010 1020 1030 1040 1050
ELVVLRSENG SVWKEHKSRY GESYLDQILN GMDEELGSLE ELEKKRVCRI
1060 1070 1080 1090 1100
ITTDFPLYFV IMSRLCQDYD TIGPEGGSLR SKLVPLVQAT FPENAVTKKV
1110 1120 1130 1140 1150
KLALQAQPVP DELVTKLLGN QATFSPIVTV EPRRRKFHRP IGLRIPLPPS
1160 1170 1180 1190 1200
WTDNPRDSGE GDTTSLRLLC SVIGGTDQAQ WEDITGTTKL IYANECANFT
1210 1220 1230 1240 1250
TNVSARFWLS DCPRTAEAVH FATLLYKELT AVPYMAKFVI FAKMNDAREG
1260 1270 1280 1290 1300
RLRCYCMTDD KVDKTLEQHE NFVEVARSRD IEVLEGMPLF AELSGNLVPV
1310 1320 1330 1340 1350
KKAAQQRSFH FQSFRENRLA IPVKVRDSSR EPGGFLSFLR KTMKYEDTQH
1360 1370 1380 1390 1400
ILCHLNITMP PCTKGSGAED RRRTLTPLTL RYSILSESRL GFTSDTDRVE
1410 1420 1430 1440 1450
MRMAVIREHL GLSWAELARE LQFSVEDINR IRVENPNSLL DQSTALLTLW
1460 1470 1480 1490 1500
VDREGENAKM ENLYTALRNI DRSEIVNMLE GSGRQSRNLK PERRHGDREY
1510 1520 1530 1540 1550
SLSPSQVNGY SSLQDELLSP ASLQYALPSP LCADQYWNEV TVIDAIPLAA
1560 1570 1580 1590 1600
TEHDTMLEMS DMQVWSAGLT PSLVTAEDSS LECSKAEDSD AIPEWKLEGA
1610 1620 1630 1640 1650
HSEDTQGPEL GSQDLVEDDT VDSDATNGLA DLLGQEEGQR SEKKRQEVSG
1660 1670 1680 1690 1700
TEQDTETEVS LVSGQQRVHA RITDSPSVRQ VLDRSQARTL DWDKQGSTAV
1710 1720 1730 1740 1750
HPQEATQSSW QEEVTQGPHS FQRRITTIQG PEPGALQEYE QVLVSTREHV
1760 1770 1780 1790 1800
QRGPPETGSP KAGKEPSLWA PESAFSQEVQ GDELQNIPGE QVTEEQFTDE
1810 1820 1830 1840 1850
QGNIVTKKII RKVVRQVDSS GAIDTQQHEE VELRGSGLQP DLIEGRKGAQ
1860
IVKRASLKRG KQ

Note: Produced by alternative promoter usage.

Length:1,862
Mass (Da):204,227
Last modified:May 16, 2006 - v2
Checksum:iB5F3EBB447C3485D
GO
Isoform Br2 (identifier: Q02357-2) [UniParc]FASTAAdd to Basket

Also known as: Cb14/11

The sequence of this isoform differs from the canonical sequence as follows:
     1-5: MGFCK → MAERPRRSGSDPA
     817-817: G → GTAHISIMG
     1636-1665: Missing.

Note: Produced by alternative splicing of isoform Er1.

Show »
Length:1,848
Mass (Da):202,549
Checksum:iBF5A6FAA4DE9071A
GO
Isoform Er3 (identifier: Q02357-3) [UniParc]FASTAAdd to Basket

Also known as: Er18

The sequence of this isoform differs from the canonical sequence as follows:
     1832-1862: ELRGSGLQPDLIEGRKGAQIVKRASLKRGKQ → IVEGPLADPGDLEADIESFMKLTKDHTSTPKP

Note: Incomplete sequence. Produced by alternative splicing of isoform Er1.

Show »
Length:1,863
Mass (Da):204,290
Checksum:i54B9C9F6E47ECB68
GO
Isoform Br4 (identifier: Q02357-4) [UniParc]FASTAAdd to Basket

Also known as: Cb12

The sequence of this isoform differs from the canonical sequence as follows:
     1831-1831: V → VIVEGPLADPGDLEADIESFMKLTKV

Note: Incomplete sequence. Produced by alternative splicing of isoform Er1.

Show »
Length:1,887
Mass (Da):206,897
Checksum:i1D67DB304BEE32D5
GO
Isoform 5 (identifier: Q02357-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MGFC → MAQAAKQLKKIKDIEAQALQEQKEKEESNRKRRNRSRDRKK
     1510-1664: Missing.

Note: Produced by alternative splicing of isoform Er1.

Show »
Length:1,744
Mass (Da):192,033
Checksum:i86F90F57AF6707A4
GO
Isoform 6 (identifier: Q02357-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MGFC → MAQAAKQLKKIKDIEAQALQEQKEKEESNRKRRNRSRDRKK
     817-817: G → GTAHISIMG

Note: Produced by alternative splicing of isoform Er1.

Show »
Length:1,907
Mass (Da):209,548
Checksum:i1BFB9FEE0C5CCFAC
GO
Isoform Mu7 (identifier: Q02357-7) [UniParc]FASTAAdd to Basket

Also known as: skAnk1

The sequence of this isoform differs from the canonical sequence as follows:
     1-1707: Missing.
     1708-1780: SSWQEEVTQG...PESAFSQEVQ → MWTFITQLLV...RVVRRRVFLK

Note: Produced by alternative promoter usage.

Show »
Length:155
Mass (Da):17,539
Checksum:i304B0AC409407EA1
GO
Isoform Mu8 (identifier: Q02357-8) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1707: Missing.
     1708-1780: SSWQEEVTQG...PESAFSQEVQ → MWTFITQLLV...RVVRRRVFLK
     1832-1862: ELRGSGLQPDLIEGRKGAQIVKRASLKRGKQ → IVEGPLADPGDLEADIESFMKLTKDHTSTPKP

Note: Produced by alternative splicing of isoform Mu7.

Show »
Length:156
Mass (Da):17,602
Checksum:iC67C71179430485E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti507 – 5071A → T in BAE34375. (PubMed:9628825)Curated
Sequence conflicti678 – 6781P → L in AAA37236. (PubMed:1386265)Curated
Sequence conflicti818 – 8181D → G in BAE34375. (PubMed:9628825)Curated
Sequence conflicti1098 – 10981K → N in CAA48801. (PubMed:8486643)Curated
Sequence conflicti1481 – 14811G → V in CAA48801. (PubMed:8486643)Curated
Sequence conflicti1541 – 15411T → A in BAE27815. (PubMed:9628825)Curated
Sequence conflicti1541 – 15411T → A in BAE28015. (PubMed:9628825)Curated
Sequence conflicti1644 – 16441K → R in BAE28015. (PubMed:9628825)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 17071707Missing in isoform Mu7 and isoform Mu8. 3 PublicationsVSP_018452Add
BLAST
Alternative sequencei1 – 55MGFCK → MAERPRRSGSDPA in isoform Br2. 2 PublicationsVSP_018453
Alternative sequencei1 – 44MGFC → MAQAAKQLKKIKDIEAQALQ EQKEKEESNRKRRNRSRDRK K in isoform 5 and isoform 6. 1 PublicationVSP_018454
Alternative sequencei817 – 8171G → GTAHISIMG in isoform Br2 and isoform 6. 2 PublicationsVSP_018455
Alternative sequencei1510 – 1664155Missing in isoform 5. 1 PublicationVSP_018456Add
BLAST
Alternative sequencei1636 – 166530Missing in isoform Br2. 2 PublicationsVSP_018457Add
BLAST
Alternative sequencei1708 – 178073SSWQE…SQEVQ → MWTFITQLLVTLVLLGFFLV SCQNVMHIVKGSLCFVLKHI HQELDKELGESEGLSDDEET ISTRVVRRRVFLK in isoform Mu7 and isoform Mu8. 3 PublicationsVSP_018458Add
BLAST
Alternative sequencei1831 – 18311V → VIVEGPLADPGDLEADIESF MKLTKV in isoform Br4. 1 PublicationVSP_018459
Alternative sequencei1832 – 186231ELRGS…KRGKQ → IVEGPLADPGDLEADIESFM KLTKDHTSTPKP in isoform Er3 and isoform Mu8. 2 PublicationsVSP_018460Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M84756 mRNA. Translation: AAA37236.1.
X69063 mRNA. Translation: CAA48801.1.
X69064 mRNA. Translation: CAA48802.1.
U73972 mRNA. Translation: AAC24156.1.
AK134267 mRNA. Translation: BAE22074.1.
AK147278 mRNA. Translation: BAE27815.1.
AK147597 mRNA. Translation: BAE28015.1.
AK158131 mRNA. Translation: BAE34375.1.
BC061219 mRNA. Translation: AAH61219.1.
U76758 Genomic DNA. Translation: AAB37323.1.
U76758 Genomic DNA. Translation: AAB37324.1.
U76758 Genomic DNA. Translation: AAB37325.1.
CCDSiCCDS22187.1. [Q02357-2]
CCDS52523.1. [Q02357-6]
CCDS72099.1. [Q02357-5]
CCDS72100.1. [Q02357-1]
CCDS72101.1. [Q02357-4]
PIRiI49502.
S37771.
S37772.
RefSeqiNP_001104253.1. NM_001110783.3.
NP_001264209.1. NM_001277280.2. [Q02357-5]
NP_001264210.1. NM_001277281.2.
NP_001264215.1. NM_001277286.2.
NP_001264218.1. NM_001277289.2.
NP_112435.2. NM_031158.4.
XP_006509068.1. XM_006509005.1. [Q02357-8]
XP_006509069.1. XM_006509006.1. [Q02357-7]
UniGeneiMm.334444.

Genome annotation databases

EnsembliENSMUST00000033947; ENSMUSP00000033947; ENSMUSG00000031543. [Q02357-8]
ENSMUST00000110688; ENSMUSP00000106316; ENSMUSG00000031543. [Q02357-5]
ENSMUST00000121075; ENSMUSP00000112966; ENSMUSG00000031543. [Q02357-7]
ENSMUST00000121802; ENSMUSP00000113571; ENSMUSG00000031543.
GeneIDi11733.
KEGGimmu:11733.
UCSCiuc009lee.2. mouse. [Q02357-6]
uc009lef.2. mouse. [Q02357-5]
uc009lel.1. mouse. [Q02357-7]
uc009lem.1. mouse. [Q02357-8]

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M84756 mRNA. Translation: AAA37236.1 .
X69063 mRNA. Translation: CAA48801.1 .
X69064 mRNA. Translation: CAA48802.1 .
U73972 mRNA. Translation: AAC24156.1 .
AK134267 mRNA. Translation: BAE22074.1 .
AK147278 mRNA. Translation: BAE27815.1 .
AK147597 mRNA. Translation: BAE28015.1 .
AK158131 mRNA. Translation: BAE34375.1 .
BC061219 mRNA. Translation: AAH61219.1 .
U76758 Genomic DNA. Translation: AAB37323.1 .
U76758 Genomic DNA. Translation: AAB37324.1 .
U76758 Genomic DNA. Translation: AAB37325.1 .
CCDSi CCDS22187.1. [Q02357-2 ]
CCDS52523.1. [Q02357-6 ]
CCDS72099.1. [Q02357-5 ]
CCDS72100.1. [Q02357-1 ]
CCDS72101.1. [Q02357-4 ]
PIRi I49502.
S37771.
S37772.
RefSeqi NP_001104253.1. NM_001110783.3.
NP_001264209.1. NM_001277280.2. [Q02357-5 ]
NP_001264210.1. NM_001277281.2.
NP_001264215.1. NM_001277286.2.
NP_001264218.1. NM_001277289.2.
NP_112435.2. NM_031158.4.
XP_006509068.1. XM_006509005.1. [Q02357-8 ]
XP_006509069.1. XM_006509006.1. [Q02357-7 ]
UniGenei Mm.334444.

3D structure databases

ProteinModelPortali Q02357.
SMRi Q02357. Positions 7-808, 907-1493.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q02357. 3 interactions.
MINTi MINT-255055.

PTM databases

PhosphoSitei Q02357.

Proteomic databases

MaxQBi Q02357.
PaxDbi Q02357.
PRIDEi Q02357.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000033947 ; ENSMUSP00000033947 ; ENSMUSG00000031543 . [Q02357-8 ]
ENSMUST00000110688 ; ENSMUSP00000106316 ; ENSMUSG00000031543 . [Q02357-5 ]
ENSMUST00000121075 ; ENSMUSP00000112966 ; ENSMUSG00000031543 . [Q02357-7 ]
ENSMUST00000121802 ; ENSMUSP00000113571 ; ENSMUSG00000031543 .
GeneIDi 11733.
KEGGi mmu:11733.
UCSCi uc009lee.2. mouse. [Q02357-6 ]
uc009lef.2. mouse. [Q02357-5 ]
uc009lel.1. mouse. [Q02357-7 ]
uc009lem.1. mouse. [Q02357-8 ]

Organism-specific databases

CTDi 286.
MGIi MGI:88024. Ank1.

Phylogenomic databases

eggNOGi COG0666.
GeneTreei ENSGT00760000118950.
HOVERGENi HBG004234.
InParanoidi Q02357.
KOi K10380.
OMAi YTIASEA.
OrthoDBi EOG7P02H2.
TreeFami TF351263.

Miscellaneous databases

NextBioi 279431.
PROi Q02357.
SOURCEi Search...

Gene expression databases

Bgeei Q02357.
CleanExi MM_ANK1.
ExpressionAtlasi Q02357. baseline and differential.
Genevestigatori Q02357.

Family and domain databases

Gene3Di 1.10.533.10. 1 hit.
1.25.40.20. 3 hits.
InterProi IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR000906. ZU5_dom.
[Graphical view ]
Pfami PF00023. Ank. 3 hits.
PF12796. Ank_2. 8 hits.
PF00531. Death. 1 hit.
PF00791. ZU5. 1 hit.
[Graphical view ]
PRINTSi PR01415. ANKYRIN.
SMARTi SM00248. ANK. 23 hits.
SM00005. DEATH. 1 hit.
SM00218. ZU5. 1 hit.
[Graphical view ]
SUPFAMi SSF47986. SSF47986. 1 hit.
SSF48403. SSF48403. 2 hits.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 20 hits.
PS50017. DEATH_DOMAIN. 1 hit.
PS51145. ZU5. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Murine erythrocyte ankyrin cDNA: highly conserved regions of the regulatory domain."
    White R.A., Birkenmeier C.S., Peters L.L., Barker J.E., Lux S.E.
    Mamm. Genome 3:281-285(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ER1).
    Tissue: Erythrocyte.
  2. "Complex patterns of sequence variation and multiple 5' and 3' ends are found among transcripts of the erythroid ankyrin gene."
    Birkenmeier C.S., White R.A., Peters L.L., Hall E.J., Lux S.E., Barker J.E.
    J. Biol. Chem. 268:9533-9540(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BR2; ER3 AND BR4).
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  3. "An alternative first exon in the distal end of the erythroid ankyrin gene leads to production of a small isoform containing an NH2-terminal membrane anchor."
    Birkenmeier C.S., Sharp J.J., Gifford E.J., Deveau S.A., Barker J.E.
    Genomics 50:79-88(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MU7), TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Strain: C57BL/6J.
    Tissue: Skeletal muscle.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS BR2; 5; 6 AND MU8).
    Strain: C57BL/6J.
    Tissue: Forelimb and Inner ear.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MU7).
    Tissue: Heart and Lung.
  6. Birkenmeier C.B., Sharp J.J., Hall E.J., Deveau S.A., Barker J.E.
    Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: C57BL/6J.
  7. "Asparagine and aspartate hydroxylation of the cytoskeletal ankyrin family is catalyzed by factor-inhibiting hypoxia-inducible factor."
    Yang M., Ge W., Chowdhury R., Claridge T.D., Kramer H.B., Schmierer B., McDonough M.A., Gong L., Kessler B.M., Ratcliffe P.J., Coleman M.L., Schofield C.J.
    J. Biol. Chem. 286:7648-7660(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 95-106, HYDROXYLATION AT ASN-101.
  8. "Small, membrane-bound, alternatively spliced forms of ankyrin 1 associated with the sarcoplasmic reticulum of mammalian skeletal muscle."
    Zhou D., Birkenmeier C.S., Williams M.W., Sharp J.J., Barker J.E., Bloch R.J.
    J. Cell Biol. 136:621-631(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-852 AND THR-862, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-957 AND SER-1388, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1069, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiANK1_MOUSE
AccessioniPrimary (citable) accession number: Q02357
Secondary accession number(s): P70440
, P97446, P97941, Q3TZ35, Q3UH42, Q3UHP2, Q3UYY7, Q61302, Q61303, Q78E45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: May 16, 2006
Last modified: October 29, 2014
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3