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ANK1_MOUSE
ID   ANK1_MOUSE              Reviewed;        1862 AA.
AC   Q02357; P70440; P97446; P97941; Q3TZ35; Q3UH42; Q3UHP2; Q3UYY7; Q61302;
AC   Q61303; Q78E45;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   03-AUG-2022, entry version 185.
DE   RecName: Full=Ankyrin-1;
DE            Short=ANK-1;
DE   AltName: Full=Erythrocyte ankyrin;
GN   Name=Ank1; Synonyms=Ank-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ER1).
RC   TISSUE=Erythrocyte;
RX   PubMed=1386265; DOI=10.1007/bf00292156;
RA   White R.A., Birkenmeier C.S., Peters L.L., Barker J.E., Lux S.E.;
RT   "Murine erythrocyte ankyrin cDNA: highly conserved regions of the
RT   regulatory domain.";
RL   Mamm. Genome 3:281-285(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BR2; ER3 AND BR4).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=8486643; DOI=10.1016/s0021-9258(18)98384-5;
RA   Birkenmeier C.S., White R.A., Peters L.L., Hall E.J., Lux S.E.,
RA   Barker J.E.;
RT   "Complex patterns of sequence variation and multiple 5' and 3' ends are
RT   found among transcripts of the erythroid ankyrin gene.";
RL   J. Biol. Chem. 268:9533-9540(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MU7), TISSUE SPECIFICITY, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=C57BL/6J; TISSUE=Skeletal muscle;
RX   PubMed=9628825; DOI=10.1006/geno.1998.5305;
RA   Birkenmeier C.S., Sharp J.J., Gifford E.J., Deveau S.A., Barker J.E.;
RT   "An alternative first exon in the distal end of the erythroid ankyrin gene
RT   leads to production of a small isoform containing an NH2-terminal membrane
RT   anchor.";
RL   Genomics 50:79-88(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS BR2; 5; 6 AND MU8).
RC   STRAIN=C57BL/6J; TISSUE=Forelimb, and Inner ear;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MU7).
RC   TISSUE=Heart, and Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RA   Birkenmeier C.B., Sharp J.J., Hall E.J., Deveau S.A., Barker J.E.;
RL   Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   PROTEIN SEQUENCE OF 95-106, AND HYDROXYLATION AT ASN-101.
RX   PubMed=21177872; DOI=10.1074/jbc.m110.193540;
RA   Yang M., Ge W., Chowdhury R., Claridge T.D., Kramer H.B., Schmierer B.,
RA   McDonough M.A., Gong L., Kessler B.M., Ratcliffe P.J., Coleman M.L.,
RA   Schofield C.J.;
RT   "Asparagine and aspartate hydroxylation of the cytoskeletal ankyrin family
RT   is catalyzed by factor-inhibiting hypoxia-inducible factor.";
RL   J. Biol. Chem. 286:7648-7660(2011).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=9024692; DOI=10.1083/jcb.136.3.621;
RA   Zhou D., Birkenmeier C.S., Williams M.W., Sharp J.J., Barker J.E.,
RA   Bloch R.J.;
RT   "Small, membrane-bound, alternatively spliced forms of ankyrin 1 associated
RT   with the sarcoplasmic reticulum of mammalian skeletal muscle.";
RL   J. Cell Biol. 136:621-631(1997).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-852 AND THR-862, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-957 AND SER-1388, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1069, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-777; SER-813; SER-852;
RP   THR-862; THR-957; SER-1078; SER-1386; SER-1388; THR-1396; SER-1424;
RP   SER-1473; SER-1482 AND SER-1612, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP   SER-55 (ISOFORMS MU7 AND MU8), AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Attaches integral membrane proteins to cytoskeletal elements;
CC       binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to
CC       the lymphocyte membrane protein GP85, and to the cytoskeletal proteins
CC       fodrin, tubulin, vimentin and desmin. Erythrocyte ankyrins also link
CC       spectrin (beta chain) to the cytoplasmic domain of the erythrocytes
CC       anion exchange protein; they retain most or all of these binding
CC       functions. In skeletal muscle, isoform Mu7 together with obscurin may
CC       provide a molecular link between the sarcoplasmic reticulum and
CC       myofibrils.
CC   -!- SUBUNIT: Interacts with a number of integral membrane proteins and
CC       cytoskeletal proteins. Interacts (via N-terminus) with SPTB/spectrin
CC       (beta chain). Interacts (via N-terminus ANK repeats) with
CC       SLC4A1/erythrocyte membrane protein band 3 (via cytoplasmic N-
CC       terminus). Also interacts with TTN/titin. Isoform Mu17 interacts with
CC       OBSCN isoform 3/obscurin. Interacts with HIF1AN (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Isoform Er1]: Cytoplasm, cytoskeleton
CC       {ECO:0000250}. Note=Probably the other erythrocyte (Er) isoforms, are
CC       located near the surface of erythrocytic plasma membrane.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Isoform Mu7]: Membrane {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Isoform Mu8]: Sarcoplasmic reticulum
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage, Alternative splicing; Named isoforms=8;
CC       Name=Er1;
CC         IsoId=Q02357-1; Sequence=Displayed;
CC       Name=Br2; Synonyms=Cb14/11;
CC         IsoId=Q02357-2; Sequence=VSP_018453, VSP_018455, VSP_018457;
CC       Name=Er3; Synonyms=Er18;
CC         IsoId=Q02357-3; Sequence=VSP_018460;
CC       Name=Br4; Synonyms=Cb12;
CC         IsoId=Q02357-4; Sequence=VSP_018459;
CC       Name=5;
CC         IsoId=Q02357-5; Sequence=VSP_018454, VSP_018456;
CC       Name=6;
CC         IsoId=Q02357-6; Sequence=VSP_018454, VSP_018455;
CC       Name=Mu7; Synonyms=skAnk1;
CC         IsoId=Q02357-7; Sequence=VSP_018452, VSP_018458;
CC       Name=Mu8;
CC         IsoId=Q02357-8; Sequence=VSP_018452, VSP_018458, VSP_018460;
CC   -!- DOMAIN: The 55 kDa regulatory domain is involved in regulating binding
CC       of SPTB/spectrin (beta chain) and SLC4A1/erythrocyte membrane protein
CC       band 3. {ECO:0000250}.
CC   -!- DOMAIN: The ANK repeat region forms a spiral around a large central
CC       cavity and is involved in binding of ion transporters. {ECO:0000250}.
CC   -!- DOMAIN: The tandem configuration of the two ZU5 and the UPA domains
CC       forms a structural supramodule termed ZZU. ZU5-1 mediates interaction
CC       with beta-spectrin, and the ZU5-1/UPA interface is required for
CC       ankyrin's function other than binding to spectrin (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Regulated by phosphorylation. {ECO:0000250}.
CC   -!- PTM: Acylated by palmitic acid group(s). {ECO:0000250}.
CC   -!- PTM: Hydroxylated by HIF1AN at several asparagine and 1 aspartate
CC       residue within ANK repeat region; hydroxylation seems to increase the
CC       conformational stability of this region and may also modulate protein-
CC       protein interactions mediated by the ANK repeat region. {ECO:0000250}.
CC   -!- MISCELLANEOUS: [Isoform Er1]: Produced by alternative promoter usage.
CC   -!- MISCELLANEOUS: [Isoform Br2]: Produced by alternative splicing of
CC       isoform Er1. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform Er3]: Incomplete sequence. Produced by
CC       alternative splicing of isoform Er1. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform Br4]: Incomplete sequence. Produced by
CC       alternative splicing of isoform Er1. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 5]: Produced by alternative splicing of isoform
CC       Er1. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform 6]: Produced by alternative splicing of isoform
CC       Er1. {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform Mu7]: Produced by alternative promoter usage.
CC       {ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform Mu8]: Produced by alternative splicing of
CC       isoform Mu7. {ECO:0000305}.
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DR   EMBL; M84756; AAA37236.1; -; mRNA.
DR   EMBL; X69063; CAA48801.1; -; mRNA.
DR   EMBL; X69064; CAA48802.1; -; mRNA.
DR   EMBL; U73972; AAC24156.1; -; mRNA.
DR   EMBL; AK134267; BAE22074.1; -; mRNA.
DR   EMBL; AK147278; BAE27815.1; -; mRNA.
DR   EMBL; AK147597; BAE28015.1; -; mRNA.
DR   EMBL; AK158131; BAE34375.1; -; mRNA.
DR   EMBL; BC061219; AAH61219.1; -; mRNA.
DR   EMBL; U76758; AAB37323.1; -; Genomic_DNA.
DR   EMBL; U76758; AAB37324.1; -; Genomic_DNA.
DR   EMBL; U76758; AAB37325.1; -; Genomic_DNA.
DR   CCDS; CCDS22187.1; -. [Q02357-2]
DR   CCDS; CCDS52523.1; -. [Q02357-6]
DR   CCDS; CCDS72099.1; -. [Q02357-5]
DR   CCDS; CCDS72100.1; -. [Q02357-1]
DR   CCDS; CCDS72101.1; -. [Q02357-4]
DR   CCDS; CCDS80864.1; -. [Q02357-7]
DR   CCDS; CCDS80865.1; -. [Q02357-8]
DR   PIR; I49502; I49502.
DR   PIR; S37771; S37771.
DR   PIR; S37772; S37772.
DR   RefSeq; NP_001104253.1; NM_001110783.3.
DR   RefSeq; NP_001264209.1; NM_001277280.2. [Q02357-5]
DR   RefSeq; NP_001264210.1; NM_001277281.2.
DR   RefSeq; NP_001264215.1; NM_001277286.2.
DR   RefSeq; NP_001264218.1; NM_001277289.2.
DR   RefSeq; NP_001297365.1; NM_001310436.1. [Q02357-8]
DR   RefSeq; NP_001297366.1; NM_001310437.1. [Q02357-7]
DR   RefSeq; NP_112435.2; NM_031158.4.
DR   AlphaFoldDB; Q02357; -.
DR   SMR; Q02357; -.
DR   BioGRID; 198101; 1.
DR   IntAct; Q02357; 3.
DR   MINT; Q02357; -.
DR   STRING; 10090.ENSMUSP00000113571; -.
DR   iPTMnet; Q02357; -.
DR   PhosphoSitePlus; Q02357; -.
DR   SwissPalm; Q02357; -.
DR   jPOST; Q02357; -.
DR   MaxQB; Q02357; -.
DR   PaxDb; Q02357; -.
DR   PeptideAtlas; Q02357; -.
DR   PRIDE; Q02357; -.
DR   ProteomicsDB; 296294; -. [Q02357-1]
DR   ProteomicsDB; 296295; -. [Q02357-2]
DR   ProteomicsDB; 296296; -. [Q02357-3]
DR   ProteomicsDB; 296297; -. [Q02357-4]
DR   ProteomicsDB; 296298; -. [Q02357-5]
DR   ProteomicsDB; 296299; -. [Q02357-6]
DR   ProteomicsDB; 296300; -. [Q02357-7]
DR   ProteomicsDB; 296301; -. [Q02357-8]
DR   ABCD; Q02357; 3 sequenced antibodies.
DR   Antibodypedia; 4229; 460 antibodies from 34 providers.
DR   DNASU; 11733; -.
DR   Ensembl; ENSMUST00000033947; ENSMUSP00000033947; ENSMUSG00000031543. [Q02357-8]
DR   Ensembl; ENSMUST00000110688; ENSMUSP00000106316; ENSMUSG00000031543. [Q02357-5]
DR   Ensembl; ENSMUST00000121075; ENSMUSP00000112966; ENSMUSG00000031543. [Q02357-7]
DR   GeneID; 11733; -.
DR   KEGG; mmu:11733; -.
DR   UCSC; uc009lee.3; mouse. [Q02357-6]
DR   UCSC; uc009lef.3; mouse. [Q02357-5]
DR   UCSC; uc009lel.2; mouse. [Q02357-7]
DR   UCSC; uc009lem.2; mouse. [Q02357-8]
DR   CTD; 286; -.
DR   MGI; MGI:88024; Ank1.
DR   VEuPathDB; HostDB:ENSMUSG00000031543; -.
DR   eggNOG; KOG4177; Eukaryota.
DR   GeneTree; ENSGT00940000155760; -.
DR   HOGENOM; CLU_000134_7_3_1; -.
DR   InParanoid; Q02357; -.
DR   OrthoDB; 1011028at2759; -.
DR   TreeFam; TF351263; -.
DR   Reactome; R-MMU-445095; Interaction between L1 and Ankyrins.
DR   Reactome; R-MMU-447043; Neurofascin interactions.
DR   Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR   BioGRID-ORCS; 11733; 2 hits in 74 CRISPR screens.
DR   ChiTaRS; Ank1; mouse.
DR   PRO; PR:Q02357; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q02357; protein.
DR   Bgee; ENSMUSG00000031543; Expressed in fetal liver hematopoietic progenitor cell and 182 other tissues.
DR   ExpressionAtlas; Q02357; baseline and differential.
DR   Genevisible; Q02357; MM.
DR   GO; GO:0031672; C:A band; ISO:MGI.
DR   GO; GO:0030673; C:axolemma; ISO:MGI.
DR   GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
DR   GO; GO:0031430; C:M band; ISO:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0043005; C:neuron projection; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR   GO; GO:0042383; C:sarcolemma; ISO:MGI.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; ISO:MGI.
DR   GO; GO:0014731; C:spectrin-associated cytoskeleton; IMP:MGI.
DR   GO; GO:0030018; C:Z disc; ISO:MGI.
DR   GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR   GO; GO:0008093; F:cytoskeletal anchor activity; ISO:MGI.
DR   GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR   GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR   GO; GO:0030507; F:spectrin binding; ISO:MGI.
DR   GO; GO:0044325; F:transmembrane transporter binding; IBA:GO_Central.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISO:MGI.
DR   GO; GO:0048821; P:erythrocyte development; IMP:MGI.
DR   GO; GO:0098662; P:inorganic cation transmembrane transport; IMP:MGI.
DR   GO; GO:0055072; P:iron ion homeostasis; IMP:MGI.
DR   GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IMP:MGI.
DR   GO; GO:0010638; P:positive regulation of organelle organization; ISO:MGI.
DR   GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 1.10.533.10; -; 1.
DR   Gene3D; 1.25.40.20; -; 3.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR040745; Ankyrin_UPA.
DR   InterPro; IPR011029; DEATH-like_dom_sf.
DR   InterPro; IPR000488; Death_domain.
DR   InterPro; IPR000906; ZU5_dom.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 8.
DR   Pfam; PF13637; Ank_4; 2.
DR   Pfam; PF00531; Death; 1.
DR   Pfam; PF17809; UPA_2; 1.
DR   Pfam; PF00791; ZU5; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 23.
DR   SMART; SM00005; DEATH; 1.
DR   SMART; SM00218; ZU5; 1.
DR   SUPFAM; SSF47986; SSF47986; 1.
DR   SUPFAM; SSF48403; SSF48403; 2.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 20.
DR   PROSITE; PS50017; DEATH_DOMAIN; 1.
DR   PROSITE; PS51145; ZU5; 2.
PE   1: Evidence at protein level;
KW   Alternative promoter usage; Alternative splicing; ANK repeat; Cytoplasm;
KW   Cytoskeleton; Direct protein sequencing; Hydroxylation; Lipoprotein;
KW   Membrane; Phosphoprotein; Reference proteome; Repeat;
KW   Sarcoplasmic reticulum.
FT   CHAIN           1..1862
FT                   /note="Ankyrin-1"
FT                   /id="PRO_0000066884"
FT   REPEAT          40..69
FT                   /note="ANK 1"
FT   REPEAT          73..102
FT                   /note="ANK 2"
FT   REPEAT          106..135
FT                   /note="ANK 3"
FT   REPEAT          139..168
FT                   /note="ANK 4"
FT   REPEAT          170..197
FT                   /note="ANK 5"
FT   REPEAT          201..230
FT                   /note="ANK 6"
FT   REPEAT          234..263
FT                   /note="ANK 7"
FT   REPEAT          267..296
FT                   /note="ANK 8"
FT   REPEAT          300..329
FT                   /note="ANK 9"
FT   REPEAT          333..362
FT                   /note="ANK 10"
FT   REPEAT          366..395
FT                   /note="ANK 11"
FT   REPEAT          399..428
FT                   /note="ANK 12"
FT   REPEAT          432..461
FT                   /note="ANK 13"
FT   REPEAT          465..494
FT                   /note="ANK 14"
FT   REPEAT          498..527
FT                   /note="ANK 15"
FT   REPEAT          531..560
FT                   /note="ANK 16"
FT   REPEAT          564..593
FT                   /note="ANK 17"
FT   REPEAT          597..626
FT                   /note="ANK 18"
FT   REPEAT          630..659
FT                   /note="ANK 19"
FT   REPEAT          663..692
FT                   /note="ANK 20"
FT   REPEAT          696..725
FT                   /note="ANK 21"
FT   REPEAT          729..758
FT                   /note="ANK 22"
FT   REPEAT          762..791
FT                   /note="ANK 23"
FT   DOMAIN          909..1064
FT                   /note="ZU5 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00485"
FT   DOMAIN          1066..1212
FT                   /note="ZU5 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00485"
FT   DOMAIN          1399..1483
FT                   /note="Death"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT   REGION          1..827
FT                   /note="89 kDa domain"
FT   REGION          812..834
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          872..900
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1197..1331
FT                   /note="UPA domain"
FT                   /evidence="ECO:0000250"
FT   REGION          1387..1862
FT                   /note="55 kDa regulatory domain"
FT   REGION          1481..1506
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1598..1720
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1744..1767
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        817..834
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1486..1500
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1636..1652
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1653..1684
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1699..1720
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         101
FT                   /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial"
FT                   /evidence="ECO:0000269|PubMed:21177872"
FT   MOD_RES         229
FT                   /note="(3S)-3-hydroxyasparagine; by HIF1AN"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         425
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P16157"
FT   MOD_RES         427
FT                   /note="(3S)-3-hydroxyasparagine; by HIF1AN"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         460
FT                   /note="(3S)-3-hydroxyasparagine; by HIF1AN"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         625
FT                   /note="(3S)-3-hydroxyasparagine; by HIF1AN"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         658
FT                   /note="(3S)-3-hydroxyasparagine; by HIF1AN"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         691
FT                   /note="(3S)-3-hydroxyaspartate; by HIF1AN"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         724
FT                   /note="(3S)-3-hydroxyasparagine; by HIF1AN"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         755
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P16157"
FT   MOD_RES         757
FT                   /note="(3S)-3-hydroxyasparagine; by HIF1AN"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         777
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         813
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         830
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P16157"
FT   MOD_RES         852
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16452087,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         862
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:16452087,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         957
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         1069
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:18034455"
FT   MOD_RES         1078
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1374
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P16157"
FT   MOD_RES         1376
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P16157"
FT   MOD_RES         1386
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1388
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         1396
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1424
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1473
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1482
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1519
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P16157"
FT   MOD_RES         1529
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P16157"
FT   MOD_RES         1612
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         1660
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P16157"
FT   MOD_RES         1675
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P16157"
FT   MOD_RES         1685
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P16157"
FT   VAR_SEQ         1..1707
FT                   /note="Missing (in isoform Mu7 and isoform Mu8)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:9628825"
FT                   /id="VSP_018452"
FT   VAR_SEQ         1..5
FT                   /note="MGFCK -> MAERPRRSGSDPA (in isoform Br2)"
FT                   /evidence="ECO:0000303|PubMed:16141072,
FT                   ECO:0000303|PubMed:8486643"
FT                   /id="VSP_018453"
FT   VAR_SEQ         1..4
FT                   /note="MGFC -> MAQAAKQLKKIKDIEAQALQEQKEKEESNRKRRNRSRDRKK
FT                   (in isoform 5 and isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_018454"
FT   VAR_SEQ         817
FT                   /note="G -> GTAHISIMG (in isoform Br2 and isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:16141072,
FT                   ECO:0000303|PubMed:8486643"
FT                   /id="VSP_018455"
FT   VAR_SEQ         1510..1664
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_018456"
FT   VAR_SEQ         1636..1665
FT                   /note="Missing (in isoform Br2)"
FT                   /evidence="ECO:0000303|PubMed:16141072,
FT                   ECO:0000303|PubMed:8486643"
FT                   /id="VSP_018457"
FT   VAR_SEQ         1708..1780
FT                   /note="SSWQEEVTQGPHSFQRRITTIQGPEPGALQEYEQVLVSTREHVQRGPPETGS
FT                   PKAGKEPSLWAPESAFSQEVQ -> MWTFITQLLVTLVLLGFFLVSCQNVMHIVKGSLC
FT                   FVLKHIHQELDKELGESEGLSDDEETISTRVVRRRVFLK (in isoform Mu7 and
FT                   isoform Mu8)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:9628825"
FT                   /id="VSP_018458"
FT   VAR_SEQ         1831
FT                   /note="V -> VIVEGPLADPGDLEADIESFMKLTKV (in isoform Br4)"
FT                   /evidence="ECO:0000303|PubMed:8486643"
FT                   /id="VSP_018459"
FT   VAR_SEQ         1832..1862
FT                   /note="ELRGSGLQPDLIEGRKGAQIVKRASLKRGKQ -> IVEGPLADPGDLEADIE
FT                   SFMKLTKDHTSTPKP (in isoform Er3 and isoform Mu8)"
FT                   /evidence="ECO:0000303|PubMed:16141072,
FT                   ECO:0000303|PubMed:8486643"
FT                   /id="VSP_018460"
FT   CONFLICT        507
FT                   /note="A -> T (in Ref. 3; BAE34375)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        678
FT                   /note="P -> L (in Ref. 1; AAA37236)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        818
FT                   /note="D -> G (in Ref. 3; BAE34375)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1098
FT                   /note="K -> N (in Ref. 2; CAA48801)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1481
FT                   /note="G -> V (in Ref. 2; CAA48801)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1541
FT                   /note="T -> A (in Ref. 3; BAE27815/BAE28015)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1644
FT                   /note="K -> R (in Ref. 3; BAE28015)"
FT                   /evidence="ECO:0000305"
FT   MOD_RES         Q02357-7:55
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         Q02357-8:55
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   1862 AA;  204227 MW;  B5F3EBB447C3485D CRC64;
     MGFCKADAAT SFLRAARSGN LDKALDHLRN GVDINTCNQN GLNGLHLASK EGHVKMVVEL
     LHKEIILETT TKKGNTALHI AALAGQDEVV RELVNYGANV NAQSQKGFTP LYMAAQENHL
     EVVKFLLENG ANQNVATEDG FTPLAVALQQ GHENVVAHLI NYGTKGKVRL PALHIAARND
     DTRTAAVLLQ NDPNPDVLSK TGFTPLHIAA HYENLNVAQL LLNRGASVNF TPQNGITPLH
     IASRRGNVIM VRLLLDRGAQ IETRTKDELT PLHCAARNGH VRISEILLDH GAPIQAKTKN
     GLSPIHMAAQ GDHLDCVRLL LQYNAEIDDI TLDHLTPLHV AAHCGHHRVA KVLLDKGAKP
     NSRALNGFTP LHIACKKNHI RVMELLLKTG ASIDAVTESG LTPLHVASFM GHLPIVKNLL
     QRGASPNVSN VKVETPLHMA ARAGHTEVAK YLLQNKAKAN AKAKDDQTPL HCAARIGHTG
     MVKLLLENGA SPNLATTAGH TPLHTAAREG HVDTALALLE KEASQACMTK KGFTPLHVAA
     KYGKVRLAEL LLEHDAHPNA AGKNGLTPLH VAVHHNNLDI VKLLLPRGGS PHSPAWNGYT
     PLHIAAKQNQ IEVARSLLQY GGSANAESVQ GVTPLHLAAQ EGHTEMVALL LSKQANGNLG
     NKSGLTPLHL VSQEGHVPVA DVLIKHGVTV DATTRMGYTP LHVASHYGNI KLVKFLLQHQ
     ADVNAKTKLG YSPLHQAAQQ GHTDIVTLLL KNGASPNEVS SNGTTPLAIA KRLGYISVTD
     VLKVVTDETS VVLVSDKHRM SYPETVDEIL DVSEDEGDEL VGSKAERRDS RDVGEEKELL
     DFVPKLDQVV ESPAIPRIPC VTPETVVIRS EDQEQASKEY DEDSLIPSSP ATETSDNISP
     VASPVHTGFL VSFMVDARGG SMRGSRHNGL RVVIPPRTCA APTRITCRLV KPQKLNTPPP
     LAEEEGLASR IIALGPTGAQ FLSPVIVEIP HFASHGRGDR ELVVLRSENG SVWKEHKSRY
     GESYLDQILN GMDEELGSLE ELEKKRVCRI ITTDFPLYFV IMSRLCQDYD TIGPEGGSLR
     SKLVPLVQAT FPENAVTKKV KLALQAQPVP DELVTKLLGN QATFSPIVTV EPRRRKFHRP
     IGLRIPLPPS WTDNPRDSGE GDTTSLRLLC SVIGGTDQAQ WEDITGTTKL IYANECANFT
     TNVSARFWLS DCPRTAEAVH FATLLYKELT AVPYMAKFVI FAKMNDAREG RLRCYCMTDD
     KVDKTLEQHE NFVEVARSRD IEVLEGMPLF AELSGNLVPV KKAAQQRSFH FQSFRENRLA
     IPVKVRDSSR EPGGFLSFLR KTMKYEDTQH ILCHLNITMP PCTKGSGAED RRRTLTPLTL
     RYSILSESRL GFTSDTDRVE MRMAVIREHL GLSWAELARE LQFSVEDINR IRVENPNSLL
     DQSTALLTLW VDREGENAKM ENLYTALRNI DRSEIVNMLE GSGRQSRNLK PERRHGDREY
     SLSPSQVNGY SSLQDELLSP ASLQYALPSP LCADQYWNEV TVIDAIPLAA TEHDTMLEMS
     DMQVWSAGLT PSLVTAEDSS LECSKAEDSD AIPEWKLEGA HSEDTQGPEL GSQDLVEDDT
     VDSDATNGLA DLLGQEEGQR SEKKRQEVSG TEQDTETEVS LVSGQQRVHA RITDSPSVRQ
     VLDRSQARTL DWDKQGSTAV HPQEATQSSW QEEVTQGPHS FQRRITTIQG PEPGALQEYE
     QVLVSTREHV QRGPPETGSP KAGKEPSLWA PESAFSQEVQ GDELQNIPGE QVTEEQFTDE
     QGNIVTKKII RKVVRQVDSS GAIDTQQHEE VELRGSGLQP DLIEGRKGAQ IVKRASLKRG
     KQ
 
 
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