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Q02357 (ANK1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ankyrin-1

Short name=ANK-1
Alternative name(s):
Erythrocyte ankyrin
Gene names
Name:Ank1
Synonyms:Ank-1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1862 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Interacts with a number of integral membrane proteins and cytoskeletal proteins. Interacts (via N-terminus) with SPTB/spectrin (beta chain). Interacts (via N-terminus ANK repeats) with SLC4A1/erythrocyte membrane protein band 3 (via cytoplasmic N-terminus). Also interacts with TTN/titin. Isoform Mu17interacts with OBSCN isoform 3/obscurin Interacts with HIF1AN By similarity.

Subcellular location

Isoform Er1: Cytoplasmcytoskeleton By similarity. Note: Probably the other erythrocyte (Er) isoforms, are located near the surface of erythrocytic plasma membrane By similarity. Ref.3 Ref.8

Isoform Mu7: Membrane By similarity Ref.3 Ref.8.

Isoform Mu8: Sarcoplasmic reticulum By similarity Ref.3 Ref.8.

Domain

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.

Post-translational modification

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.

Sequence similarities

Contains 23 ANK repeats.

Contains 1 death domain.

Contains 2 ZU5 domains.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Membrane
Sarcoplasmic reticulum
   Coding sequence diversityAlternative promoter usage
Alternative splicing
   DomainANK repeat
Repeat
   PTMHydroxylation
Lipoprotein
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processER to Golgi vesicle-mediated transport

Inferred from electronic annotation. Source: Ensembl

erythrocyte development

Inferred from mutant phenotype PubMed 2139228. Source: MGI

monovalent inorganic cation transport

Inferred from mutant phenotype PubMed 7492791. Source: MGI

porphyrin-containing compound biosynthetic process

Inferred from mutant phenotype PubMed 658175. Source: MGI

positive regulation of organelle organization

Inferred from electronic annotation. Source: Ensembl

protein targeting to plasma membrane

Inferred from electronic annotation. Source: Ensembl

signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentM band

Inferred from electronic annotation. Source: Ensembl

Z disc

Inferred from electronic annotation. Source: Ensembl

axolemma

Inferred from electronic annotation. Source: Ensembl

cortical cytoskeleton

Inferred from direct assay PubMed 18723693. Source: MGI

membrane

Inferred from direct assay PubMed 18723693. Source: MGI

nucleus

Inferred from electronic annotation. Source: Ensembl

postsynaptic membrane

Inferred from electronic annotation. Source: Ensembl

sarcolemma

Inferred from electronic annotation. Source: Ensembl

sarcoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

spectrin-associated cytoskeleton

Inferred from mutant phenotype PubMed 6234993. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 8 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]
Isoform Er1 (identifier: Q02357-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Produced by alternative promoter usage.
Isoform Br2 (identifier: Q02357-2)

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.
Isoform Er3 (identifier: Q02357-3)

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.
Isoform Br4 (identifier: Q02357-4)

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.
Isoform 5 (identifier: Q02357-5)

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.
Isoform 6 (identifier: Q02357-6)

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.
Isoform Mu7 (identifier: Q02357-7)

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.
Isoform Mu8 (identifier: Q02357-8)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18621862Ankyrin-1
PRO_0000066884

Regions

Repeat40 – 6930ANK 1
Repeat73 – 10230ANK 2
Repeat106 – 13530ANK 3
Repeat139 – 16830ANK 4
Repeat170 – 19728ANK 5
Repeat201 – 23030ANK 6
Repeat234 – 26330ANK 7
Repeat267 – 29630ANK 8
Repeat300 – 32930ANK 9
Repeat333 – 36230ANK 10
Repeat366 – 39530ANK 11
Repeat399 – 42830ANK 12
Repeat432 – 46130ANK 13
Repeat465 – 49430ANK 14
Repeat498 – 52730ANK 15
Repeat531 – 56030ANK 16
Repeat564 – 59330ANK 17
Repeat597 – 62630ANK 18
Repeat630 – 65930ANK 19
Repeat663 – 69230ANK 20
Repeat696 – 72530ANK 21
Repeat729 – 75830ANK 22
Repeat762 – 79130ANK 23
Domain907 – 1032126ZU5 1
Domain1033 – 1196164ZU5 2
Domain1399 – 148385Death
Region1 – 82782789 kDa domain
Region1197 – 1331135UPA domain By similarity
Region1387 – 186247655 kDa regulatory domain

Amino acid modifications

Modified residue1011(3S)-3-hydroxyasparagine; by HIF1AN; partial Ref.7
Modified residue2291(3S)-3-hydroxyasparagine; by HIF1AN By similarity
Modified residue4271(3S)-3-hydroxyasparagine; by HIF1AN By similarity
Modified residue4601(3S)-3-hydroxyasparagine; by HIF1AN By similarity
Modified residue6251(3S)-3-hydroxyasparagine; by HIF1AN By similarity
Modified residue6581(3S)-3-hydroxyasparagine; by HIF1AN By similarity
Modified residue6911(3S)-3-hydroxyaspartate; by HIF1AN By similarity
Modified residue7241(3S)-3-hydroxyasparagine; by HIF1AN By similarity
Modified residue7571(3S)-3-hydroxyasparagine; by HIF1AN By similarity
Modified residue8521Phosphoserine Ref.9
Modified residue8621Phosphothreonine Ref.9
Modified residue9571Phosphothreonine Ref.10
Modified residue10691Phosphotyrosine Ref.11
Modified residue13881Phosphoserine Ref.10

Natural variations

Alternative sequence1 – 17071707Missing in isoform Mu7 and isoform Mu8.
VSP_018452
Alternative sequence1 – 55MGFCK → MAERPRRSGSDPA in isoform Br2.
VSP_018453
Alternative sequence1 – 44MGFC → MAQAAKQLKKIKDIEAQALQ EQKEKEESNRKRRNRSRDRK K in isoform 5 and isoform 6.
VSP_018454
Alternative sequence8171G → GTAHISIMG in isoform Br2 and isoform 6.
VSP_018455
Alternative sequence1510 – 1664155Missing in isoform 5.
VSP_018456
Alternative sequence1636 – 166530Missing in isoform Br2.
VSP_018457
Alternative sequence1708 – 178073SSWQE…SQEVQ → MWTFITQLLVTLVLLGFFLV SCQNVMHIVKGSLCFVLKHI HQELDKELGESEGLSDDEET ISTRVVRRRVFLK in isoform Mu7 and isoform Mu8.
VSP_018458
Alternative sequence18311V → VIVEGPLADPGDLEADIESF MKLTKV in isoform Br4.
VSP_018459
Alternative sequence1832 – 186231ELRGS…KRGKQ → IVEGPLADPGDLEADIESFM KLTKDHTSTPKP in isoform Er3 and isoform Mu8.
VSP_018460

Experimental info

Sequence conflict5071A → T in BAE34375. Ref.3
Sequence conflict6781P → L in AAA37236. Ref.1
Sequence conflict8181D → G in BAE34375. Ref.3
Sequence conflict10981K → N in CAA48801. Ref.2
Sequence conflict14811G → V in CAA48801. Ref.2
Sequence conflict15411T → A in BAE27815. Ref.3
Sequence conflict15411T → A in BAE28015. Ref.3
Sequence conflict16441K → R in BAE28015. Ref.3

Sequences

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

Last modified May 16, 2006. Version 2.
Checksum: B5F3EBB447C3485D

FASTA1,862204,227
        10         20         30         40         50         60 
MGFCKADAAT SFLRAARSGN LDKALDHLRN GVDINTCNQN GLNGLHLASK EGHVKMVVEL 

        70         80         90        100        110        120 
LHKEIILETT TKKGNTALHI AALAGQDEVV RELVNYGANV NAQSQKGFTP LYMAAQENHL 

       130        140        150        160        170        180 
EVVKFLLENG ANQNVATEDG FTPLAVALQQ GHENVVAHLI NYGTKGKVRL PALHIAARND 

       190        200        210        220        230        240 
DTRTAAVLLQ NDPNPDVLSK TGFTPLHIAA HYENLNVAQL LLNRGASVNF TPQNGITPLH 

       250        260        270        280        290        300 
IASRRGNVIM VRLLLDRGAQ IETRTKDELT PLHCAARNGH VRISEILLDH GAPIQAKTKN 

       310        320        330        340        350        360 
GLSPIHMAAQ GDHLDCVRLL LQYNAEIDDI TLDHLTPLHV AAHCGHHRVA KVLLDKGAKP 

       370        380        390        400        410        420 
NSRALNGFTP LHIACKKNHI RVMELLLKTG ASIDAVTESG LTPLHVASFM GHLPIVKNLL 

       430        440        450        460        470        480 
QRGASPNVSN VKVETPLHMA ARAGHTEVAK YLLQNKAKAN AKAKDDQTPL HCAARIGHTG 

       490        500        510        520        530        540 
MVKLLLENGA SPNLATTAGH TPLHTAAREG HVDTALALLE KEASQACMTK KGFTPLHVAA 

       550        560        570        580        590        600 
KYGKVRLAEL LLEHDAHPNA AGKNGLTPLH VAVHHNNLDI VKLLLPRGGS PHSPAWNGYT 

       610        620        630        640        650        660 
PLHIAAKQNQ IEVARSLLQY GGSANAESVQ GVTPLHLAAQ EGHTEMVALL LSKQANGNLG 

       670        680        690        700        710        720 
NKSGLTPLHL VSQEGHVPVA DVLIKHGVTV DATTRMGYTP LHVASHYGNI KLVKFLLQHQ 

       730        740        750        760        770        780 
ADVNAKTKLG YSPLHQAAQQ GHTDIVTLLL KNGASPNEVS SNGTTPLAIA KRLGYISVTD 

       790        800        810        820        830        840 
VLKVVTDETS VVLVSDKHRM SYPETVDEIL DVSEDEGDEL VGSKAERRDS RDVGEEKELL 

       850        860        870        880        890        900 
DFVPKLDQVV ESPAIPRIPC VTPETVVIRS EDQEQASKEY DEDSLIPSSP ATETSDNISP 

       910        920        930        940        950        960 
VASPVHTGFL VSFMVDARGG SMRGSRHNGL RVVIPPRTCA APTRITCRLV KPQKLNTPPP 

       970        980        990       1000       1010       1020 
LAEEEGLASR IIALGPTGAQ FLSPVIVEIP HFASHGRGDR ELVVLRSENG SVWKEHKSRY 

      1030       1040       1050       1060       1070       1080 
GESYLDQILN GMDEELGSLE ELEKKRVCRI ITTDFPLYFV IMSRLCQDYD TIGPEGGSLR 

      1090       1100       1110       1120       1130       1140 
SKLVPLVQAT FPENAVTKKV KLALQAQPVP DELVTKLLGN QATFSPIVTV EPRRRKFHRP 

      1150       1160       1170       1180       1190       1200 
IGLRIPLPPS WTDNPRDSGE GDTTSLRLLC SVIGGTDQAQ WEDITGTTKL IYANECANFT 

      1210       1220       1230       1240       1250       1260 
TNVSARFWLS DCPRTAEAVH FATLLYKELT AVPYMAKFVI FAKMNDAREG RLRCYCMTDD 

      1270       1280       1290       1300       1310       1320 
KVDKTLEQHE NFVEVARSRD IEVLEGMPLF AELSGNLVPV KKAAQQRSFH FQSFRENRLA 

      1330       1340       1350       1360       1370       1380 
IPVKVRDSSR EPGGFLSFLR KTMKYEDTQH ILCHLNITMP PCTKGSGAED RRRTLTPLTL 

      1390       1400       1410       1420       1430       1440 
RYSILSESRL GFTSDTDRVE MRMAVIREHL GLSWAELARE LQFSVEDINR IRVENPNSLL 

      1450       1460       1470       1480       1490       1500 
DQSTALLTLW VDREGENAKM ENLYTALRNI DRSEIVNMLE GSGRQSRNLK PERRHGDREY 

      1510       1520       1530       1540       1550       1560 
SLSPSQVNGY SSLQDELLSP ASLQYALPSP LCADQYWNEV TVIDAIPLAA TEHDTMLEMS 

      1570       1580       1590       1600       1610       1620 
DMQVWSAGLT PSLVTAEDSS LECSKAEDSD AIPEWKLEGA HSEDTQGPEL GSQDLVEDDT 

      1630       1640       1650       1660       1670       1680 
VDSDATNGLA DLLGQEEGQR SEKKRQEVSG TEQDTETEVS LVSGQQRVHA RITDSPSVRQ 

      1690       1700       1710       1720       1730       1740 
VLDRSQARTL DWDKQGSTAV HPQEATQSSW QEEVTQGPHS FQRRITTIQG PEPGALQEYE 

      1750       1760       1770       1780       1790       1800 
QVLVSTREHV QRGPPETGSP KAGKEPSLWA PESAFSQEVQ GDELQNIPGE QVTEEQFTDE 

      1810       1820       1830       1840       1850       1860 
QGNIVTKKII RKVVRQVDSS GAIDTQQHEE VELRGSGLQP DLIEGRKGAQ IVKRASLKRG 


KQ 

« Hide

Isoform Br2 (Cb14/11) [UniParc].

Checksum: BF5A6FAA4DE9071A
Show »

FASTA1,848202,549
Isoform Er3 (Er18) [UniParc].

Checksum: 54B9C9F6E47ECB68
Show »

FASTA1,863204,290
Isoform Br4 (Cb12) [UniParc].

Checksum: 1D67DB304BEE32D5
Show »

FASTA1,887206,897
Isoform 5 [UniParc].

Checksum: 86F90F57AF6707A4
Show »

FASTA1,744192,033
Isoform 6 [UniParc].

Checksum: 1BFB9FEE0C5CCFAC
Show »

FASTA1,907209,548
Isoform Mu7 (skAnk1) [UniParc].

Checksum: 304B0AC409407EA1
Show »

FASTA15517,539
Isoform Mu8 [UniParc].

Checksum: C67C71179430485E
Show »

FASTA15617,602

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS22187.1. [Q02357-2]
CCDS52523.1. [Q02357-6]
CCDS72099.1. [Q02357-5]
CCDS72100.1. [Q02357-1]
CCDS72101.1. [Q02357-4]
PIRI49502.
S37771.
S37772.
RefSeqNP_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]
UniGeneMm.334444.

3D structure databases

ProteinModelPortalQ02357.
SMRQ02357. Positions 7-808, 907-1493.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ02357. 3 interactions.
MINTMINT-255055.

PTM databases

PhosphoSiteQ02357.

Proteomic databases

MaxQBQ02357.
PaxDbQ02357.
PRIDEQ02357.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033947; ENSMUSP00000033947; ENSMUSG00000031543. [Q02357-8]
ENSMUST00000110688; ENSMUSP00000106316; ENSMUSG00000031543. [Q02357-5]
ENSMUST00000121075; ENSMUSP00000112966; ENSMUSG00000031543. [Q02357-7]
ENSMUST00000121802; ENSMUSP00000113571; ENSMUSG00000031543.
GeneID11733.
KEGGmmu:11733.
UCSCuc009lee.2. mouse. [Q02357-6]
uc009lef.2. mouse. [Q02357-5]
uc009lel.1. mouse. [Q02357-7]
uc009lem.1. mouse. [Q02357-8]

Organism-specific databases

CTD286.
MGIMGI:88024. Ank1.

Phylogenomic databases

eggNOGCOG0666.
GeneTreeENSGT00720000108655.
HOVERGENHBG004234.
KOK10380.
OMAYTIASEA.
OrthoDBEOG7P02H2.
TreeFamTF351263.

Gene expression databases

ArrayExpressQ02357.
BgeeQ02357.
CleanExMM_ANK1.
GenevestigatorQ02357.

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. 8 hits.
PF00531. Death. 1 hit.
PF00791. ZU5. 1 hit.
[Graphical view]
PRINTSPR01415. ANKYRIN.
SMARTSM00248. ANK. 23 hits.
SM00005. DEATH. 1 hit.
SM00218. ZU5. 1 hit.
[Graphical view]
SUPFAMSSF47986. SSF47986. 1 hit.
SSF48403. SSF48403. 2 hits.
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 20 hits.
PS50017. DEATH_DOMAIN. 1 hit.
PS51145. ZU5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio279431.
PROQ02357.
SOURCESearch...

Entry information

Entry nameANK1_MOUSE
AccessionPrimary (citable) accession number: Q02357
Secondary accession number(s): P70440 expand/collapse secondary AC list , P97446, P97941, Q3TZ35, Q3UH42, Q3UHP2, Q3UYY7, Q61302, Q61303, Q78E45
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: May 16, 2006
Last modified: July 9, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot