ANK1_HUMAN
ID ANK1_HUMAN Reviewed; 1881 AA.
AC P16157; A0PJN8; A6NJ23; E5RFL7; O43400; Q13768; Q53ER1; Q59FP2; Q8N604;
AC Q99407;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 233.
DE RecName: Full=Ankyrin-1;
DE Short=ANK-1;
DE AltName: Full=Ankyrin-R;
DE AltName: Full=Erythrocyte ankyrin;
GN Name=ANK1; Synonyms=ANK;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ER1 AND ER2), PROTEIN SEQUENCE OF
RP 3-30; 733-753; 828-871; 959-1003; 1106-1128; 1149-1168; 1282-1288;
RP 1345-1367; 1383-1427; 1601-1626; 1686-1700 AND 1763-1772, AND VARIANTS
RP ALA-750 AND ILE-1075.
RC TISSUE=Hematopoietic;
RX PubMed=2137557; DOI=10.1038/344036a0;
RA Lux S.E., John K.M., Bennett V.;
RT "Analysis of cDNA for human erythrocyte ankyrin indicates a repeated
RT structure with homology to tissue-differentiation and cell-cycle control
RT proteins.";
RL Nature 344:36-42(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ER1; ER5 AND ER16), AND VARIANTS
RP ILE-1075 AND ILE-1546.
RX PubMed=1689849; DOI=10.1073/pnas.87.5.1730;
RA Lambert S., Yu H., Prchal J.T., Lawler J., Ruff P., Speicher D.,
RA Cheung M.C., Kan Y.W., Palek J.;
RT "cDNA sequence for human erythrocyte ankyrin.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:1730-1734(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND VARIANTS
RP LEU-991 AND ILE-1075.
RX PubMed=9235914; DOI=10.1074/jbc.272.31.19220;
RA Gallagher P.G., Tse W.T., Scarpa A.L., Lux S.E., Forget B.G.;
RT "Structure and organization of the human ankyrin-1 gene. Basis for
RT complexity of pre-mRNA processing.";
RL J. Biol. Chem. 272:19220-19228(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MU17; MU18; MU19 AND MU20), TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Skeletal muscle;
RX PubMed=9430667; DOI=10.1074/jbc.273.3.1339;
RA Gallagher P.G., Forget B.G.;
RT "An alternate promoter directs expression of a truncated, muscle-specific
RT isoform of the human ankyrin 1 gene.";
RL J. Biol. Chem. 273:1339-1348(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BR21), AND VARIANT
RP ILE-1075.
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS MU17; 22 AND 23).
RC TISSUE=B-cell, and Skeletal muscle;
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 [9]
RP PROTEIN SEQUENCE OF 5-12; 403-422; 797-814; 862-877 AND 899-912, DOMAINS
RP SPTB AND SLC4A1 BINDING, AND VARIANT ASP-1286.
RX PubMed=2141335; DOI=10.1016/s0021-9258(18)86987-3;
RA Davis L.H., Bennett V.;
RT "Mapping the binding sites of human erythrocyte ankyrin for the anion
RT exchanger and spectrin.";
RL J. Biol. Chem. 265:10589-10596(1990).
RN [10]
RP PROTEIN SEQUENCE OF 99-110; 129-169 AND 233-248, INTERACTION WITH HIF1AN,
RP AND HYDROXYLATION AT ASN-105; ASN-233; ASN-431; ASN-464; ASN-629; ASN-662;
RP ASP-695; ASN-728 AND ASN-761.
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 [11]
RP INTERACTION WITH SLC4A1.
RX PubMed=7665627; DOI=10.1074/jbc.270.37.22050;
RA Michaely P., Bennett V.;
RT "The ANK repeats of erythrocyte ankyrin form two distinct but cooperative
RT binding sites for the erythrocyte anion exchanger.";
RL J. Biol. Chem. 270:22050-22057(1995).
RN [12]
RP INTERACTION WITH TTN.
RX PubMed=12444090; DOI=10.1074/jbc.m209012200;
RA Kontrogianni-Konstantopoulos A., Bloch R.J.;
RT "The hydrophilic domain of small ankyrin-1 interacts with the two N-
RT terminal immunoglobulin domains of titin.";
RL J. Biol. Chem. 278:3985-3991(2003).
RN [13]
RP SUBCELLULAR LOCATION, INTERACTION WITH OBSCN, MUTAGENESIS OF THR-1824;
RP LYS-1826; ARG-1829 AND LYS-1830, AND FUNCTION.
RX PubMed=12527750; DOI=10.1083/jcb.200208109;
RA Bagnato P., Barone V., Giacomello E., Rossi D., Sorrentino V.;
RT "Binding of an ankyrin-1 isoform to obscurin suggests a molecular link
RT between the sarcoplasmic reticulum and myofibrils in striated muscles.";
RL J. Cell Biol. 160:245-253(2003).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429; SER-759; SER-781;
RP SER-856; THR-1378; THR-1380; SER-1396; SER-1486; SER-1666; SER-1671;
RP SER-1686; SER-1690 AND SER-1696, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-781; SER-817; SER-834;
RP SER-856; SER-1428; SER-1523 AND SER-1533, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION).
RX PubMed=29459732; DOI=10.1038/s41564-018-0111-0;
RA Thomas J.A., Tan M.S.Y., Bisson C., Borg A., Umrekar T.R., Hackett F.,
RA Hale V.L., Vizcay-Barrena G., Fleck R.A., Snijders A.P., Saibil H.R.,
RA Blackman M.J.;
RT "A protease cascade regulates release of the human malaria parasite
RT Plasmodium falciparum from host red blood cells.";
RL Nat. Microbiol. 3:447-455(2018).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 402-827, AND FUNCTION OF ANK
RP REPEAT DOMAIN.
RX PubMed=12456646; DOI=10.1093/emboj/cdf651;
RA Michaely P., Tomchick D.R., Machius M., Anderson R.G.;
RT "Crystal structure of a 12 ANK repeat stack from human ankyrinR.";
RL EMBO J. 21:6387-6396(2002).
RN [21]
RP STRUCTURE BY NMR OF 1392-1497.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the DEATH domain of ankyrin-1.";
RL Submitted (APR-2008) to the PDB data bank.
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 911-1233, AND DOMAINS ZU5.
RX PubMed=22310050; DOI=10.1016/j.jmb.2012.01.041;
RA Yasunaga M., Ipsaro J.J., Mondragon A.;
RT "Structurally similar but functionally diverse ZU5 domains in human
RT erythrocyte ankyrin.";
RL J. Mol. Biol. 417:336-350(2012).
RN [23]
RP VARIANT SPH1 ILE-463.
RX PubMed=8640229; DOI=10.1038/ng0696-214;
RA Eber S.W., Gonzalez J.M., Lux M.L., Scarpa A.L., Tse W.T., Dornwell M.,
RA Herbers J., Kugler W., Oezcan R., Pekrun A., Gallagher P.G., Schroeter W.,
RA Forget B.G., Lux S.E.;
RT "Ankyrin-1 mutations are a major cause of dominant and recessive hereditary
RT spherocytosis.";
RL Nat. Genet. 13:214-218(1996).
RN [24]
RP VARIANTS SPH1 ARG-276 AND THR-1054.
RX PubMed=11102985;
RX DOI=10.1002/1098-1004(200012)16:6<529::aid-humu13>3.0.co;2-n;
RA Leite R.C.A., Basseres D.S., Ferreira J.S., Alberto F.L., Costa F.F.,
RA Saad S.T.O.;
RT "Low frequency of ankyrin mutations in hereditary spherocytosis:
RT identification of three novel mutations.";
RL Hum. Mutat. 16:529-529(2000).
RN [25]
RP VARIANT [LARGE SCALE ANALYSIS] HIS-332.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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. {ECO:0000269|PubMed:12456646}.
CC -!- FUNCTION: [Isoform Mu17]: Together with obscurin in skeletal muscle may
CC provide a molecular link between the sarcoplasmic reticulum and
CC myofibrils. {ECO:0000269|PubMed:12527750}.
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.
CC {ECO:0000269|PubMed:12444090, ECO:0000269|PubMed:12527750,
CC ECO:0000269|PubMed:21177872, ECO:0000269|PubMed:7665627}.
CC -!- INTERACTION:
CC P16157; Q5VST9-3: OBSCN; NbExp=3; IntAct=EBI-941686, EBI-941921;
CC P16157-17; P50402: EMD; NbExp=3; IntAct=EBI-941819, EBI-489887;
CC P16157-17; P54849: EMP1; NbExp=3; IntAct=EBI-941819, EBI-4319440;
CC P16157-17; Q14802-3: FXYD3; NbExp=3; IntAct=EBI-941819, EBI-12175685;
CC P16157-17; Q8IXM6: NRM; NbExp=3; IntAct=EBI-941819, EBI-10262547;
CC P16157-17; Q5VST9-3: OBSCN; NbExp=8; IntAct=EBI-941819, EBI-941921;
CC P16157-17; Q8N0V3: RBFA; NbExp=3; IntAct=EBI-941819, EBI-3232108;
CC P16157-17; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-941819, EBI-10244780;
CC P16157-17; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-941819, EBI-10262251;
CC P16157-17; P0DN84: STRIT1; NbExp=3; IntAct=EBI-941819, EBI-12200293;
CC P16157-17; Q969S6: TMEM203; NbExp=3; IntAct=EBI-941819, EBI-12274070;
CC -!- SUBCELLULAR LOCATION: [Isoform Er1]: Cytoplasm, cytoskeleton.
CC Note=Probably the other erythrocyte (Er) isoforms, are located near the
CC surface of erythrocytic plasma membrane.
CC -!- SUBCELLULAR LOCATION: [Isoform Mu17]: Membrane. Cytoplasm, myofibril,
CC sarcomere, M line. Note=Colocalizes with OBSCN isoform 3/obscurin at
CC the M line in differentiated skeletal muscle cells.
CC -!- SUBCELLULAR LOCATION: [Isoform Mu18]: Sarcoplasmic reticulum
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform Mu19]: Sarcoplasmic reticulum
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform Mu20]: Sarcoplasmic reticulum
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=23;
CC Name=Er1; Synonyms=1, 2.1;
CC IsoId=P16157-1; Sequence=Displayed;
CC Name=Er2; Synonyms=2, 2.2;
CC IsoId=P16157-4; Sequence=VSP_018442;
CC Name=Er3; Synonyms=3;
CC IsoId=P16157-5; Sequence=VSP_018449;
CC Name=Er4; Synonyms=4;
CC IsoId=P16157-6; Sequence=VSP_018442, VSP_018449;
CC Name=Er5; Synonyms=5;
CC IsoId=P16157-3; Sequence=VSP_000266;
CC Name=Er6; Synonyms=6;
CC IsoId=P16157-7; Sequence=VSP_018442, VSP_000266;
CC Name=Er7; Synonyms=7;
CC IsoId=P16157-8; Sequence=VSP_018447;
CC Name=Er8; Synonyms=8;
CC IsoId=P16157-9; Sequence=VSP_018442, VSP_018447;
CC Name=Er9; Synonyms=9;
CC IsoId=P16157-10; Sequence=VSP_018445;
CC Name=Er10; Synonyms=10;
CC IsoId=P16157-11; Sequence=VSP_018442, VSP_018445;
CC Name=Er11; Synonyms=11;
CC IsoId=P16157-12; Sequence=VSP_018450;
CC Name=Er12; Synonyms=12;
CC IsoId=P16157-13; Sequence=VSP_018442, VSP_018450;
CC Name=Er13; Synonyms=13;
CC IsoId=P16157-14; Sequence=VSP_018451;
CC Name=Er14; Synonyms=14;
CC IsoId=P16157-15; Sequence=VSP_018442, VSP_018451;
CC Name=Er15; Synonyms=15;
CC IsoId=P16157-16; Sequence=VSP_018448;
CC Name=Er16;
CC IsoId=P16157-2; Sequence=VSP_000264, VSP_000265;
CC Name=Mu17; Synonyms=ank1.5, muscle-specific 1;
CC IsoId=P16157-17; Sequence=VSP_018440, VSP_018443, VSP_000266;
CC Name=Mu18; Synonyms=ank1.6, muscle-specific 2;
CC IsoId=P16157-18; Sequence=VSP_018440, VSP_018443, VSP_018448;
CC Name=Mu19; Synonyms=muscle-specific 3;
CC IsoId=P16157-19; Sequence=VSP_018440, VSP_018443, VSP_018445;
CC Name=Mu20; Synonyms=muscle-specific 4;
CC IsoId=P16157-20; Sequence=VSP_018440, VSP_018444, VSP_018446;
CC Name=Br21;
CC IsoId=P16157-21; Sequence=VSP_018439, VSP_018441, VSP_018449;
CC Name=22;
CC IsoId=P16157-22; Sequence=VSP_018440, VSP_018443, VSP_045439;
CC Name=23;
CC IsoId=P16157-23; Sequence=VSP_018440, VSP_018443;
CC -!- TISSUE SPECIFICITY: Isoform Mu17, isoform Mu18, isoform Mu19 and
CC isoform Mu20 are expressed in skeletal muscle. Isoform Br21 is
CC expressed in brain. {ECO:0000269|PubMed:9430667}.
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.
CC -!- DOMAIN: The ANK repeat region forms a spiral around a large central
CC cavity and is involved in binding of ion transporters.
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.
CC -!- PTM: Palmitoylated.
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.
CC {ECO:0000269|PubMed:21177872}.
CC -!- PTM: (Microbial infection) Probably cleaved by P.falciparum SERA6; the
CC cleavage probably causes the disruption of the actin cytoskeleton and
CC the rupture of the erythrocyte cell membrane releasing the merozoites.
CC {ECO:0000269|PubMed:29459732}.
CC -!- DISEASE: Spherocytosis 1 (SPH1) [MIM:182900]: A form of spherocytosis,
CC a hematologic disorder leading to chronic hemolytic anemia and
CC characterized by numerous abnormally shaped erythrocytes which are
CC generally spheroidal. SPH1 is characterized by severe hemolytic anemia.
CC Inheritance can be autosomal dominant or autosomal recessive. Patients
CC with homozygous mutations have a more severe disorder.
CC {ECO:0000269|PubMed:11102985, ECO:0000269|PubMed:8640229}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: [Isoform Er1]: Major erythrocyte-specific isoform.
CC Produced by alternative promoter usage.
CC -!- MISCELLANEOUS: [Isoform Er2]: Predominant form of minor erythrocyte-
CC specific isoforms. Produced by alternative splicing of isoform Er1.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform Er3]: Produced by alternative splicing of
CC isoform Er1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform Er4]: Produced by alternative splicing of
CC isoform Er1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform Er5]: Produced by alternative splicing of
CC isoform Er1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform Er6]: Produced by alternative splicing of
CC isoform Er1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform Er7]: Produced by alternative splicing of
CC isoform Er1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform Er9]: Produced by alternative splicing of
CC isoform Er1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform Er10]: Produced by alternative splicing of
CC isoform Er1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform Er11]: Produced by alternative splicing of
CC isoform Er1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform Er12]: Produced by alternative splicing of
CC isoform Er1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform Er13]: Produced by alternative splicing of
CC isoform Er1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform Er14]: Produced by alternative splicing of
CC isoform Er1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform Er15]: Produced by alternative splicing of
CC isoform Er1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform Er16]: Produced by alternative splicing of
CC isoform Er1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform Mu17]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform Mu18]: Produced by alternative splicing of
CC isoform Mu17. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform Mu19]: Produced by alternative splicing of
CC isoform Mu17. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform Mu20]: Produced by alternative splicing of
CC isoform Mu17. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform Br21]: Produced by alternative splicing of
CC isoform Er1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 22]: Produced by alternative splicing.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB47805.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Ankyrin entry;
CC URL="https://en.wikipedia.org/wiki/Ankyrin";
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DR EMBL; X16609; CAA34610.1; -; mRNA.
DR EMBL; X16609; CAA34611.1; -; mRNA.
DR EMBL; M28880; AAA51732.1; -; mRNA.
DR EMBL; U50133; AAB47805.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U50092; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50093; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50094; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50095; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50096; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50097; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50098; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50099; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50100; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50101; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50102; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50103; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50104; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50105; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50106; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50107; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50108; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50109; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50110; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50111; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50112; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50113; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50114; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50115; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50116; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50117; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50118; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50119; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50120; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50121; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50122; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50123; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50124; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50125; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50126; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50127; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50128; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50129; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50130; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50131; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; U50132; AAB47805.1; JOINED; Genomic_DNA.
DR EMBL; AF005213; AAC01950.1; -; mRNA.
DR EMBL; AB209418; BAD92655.1; -; mRNA.
DR EMBL; AK223578; BAD97298.1; -; mRNA.
DR EMBL; AC027702; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC113133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471080; EAW63243.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63244.1; -; Genomic_DNA.
DR EMBL; BC030957; AAH30957.1; -; mRNA.
DR EMBL; BC117121; AAI17122.1; -; mRNA.
DR EMBL; BC014467; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS47849.1; -. [P16157-21]
DR CCDS; CCDS55227.1; -. [P16157-23]
DR CCDS; CCDS6119.1; -. [P16157-1]
DR CCDS; CCDS6120.1; -. [P16157-22]
DR CCDS; CCDS6121.1; -. [P16157-3]
DR CCDS; CCDS6122.1; -. [P16157-17]
DR PIR; A35049; A35049.
DR PIR; S08275; SJHUK.
DR RefSeq; NP_000028.3; NM_000037.3. [P16157-3]
DR RefSeq; NP_001135917.1; NM_001142445.1. [P16157-23]
DR RefSeq; NP_001135918.1; NM_001142446.1. [P16157-21]
DR RefSeq; NP_065208.2; NM_020475.2. [P16157-5]
DR RefSeq; NP_065209.2; NM_020476.2. [P16157-1]
DR RefSeq; NP_065210.2; NM_020477.2. [P16157-4]
DR RefSeq; NP_065211.2; NM_020478.4. [P16157-17]
DR RefSeq; NP_065213.2; NM_020480.4. [P16157-22]
DR PDB; 1N11; X-ray; 2.70 A; A=402-827.
DR PDB; 2YQF; NMR; -; A=1394-1497.
DR PDB; 2YVI; X-ray; 1.92 A; A=1394-1497.
DR PDB; 3F59; X-ray; 2.00 A; A/B/C/D=911-1068.
DR PDB; 3KBT; X-ray; 2.75 A; C/D=911-1068.
DR PDB; 3KBU; X-ray; 2.75 A; C/D=911-1068.
DR PDB; 3UD1; X-ray; 2.00 A; A/B/C=911-1233.
DR PDB; 3UD2; X-ray; 2.21 A; A/B/C=911-1233.
DR PDBsum; 1N11; -.
DR PDBsum; 2YQF; -.
DR PDBsum; 2YVI; -.
DR PDBsum; 3F59; -.
DR PDBsum; 3KBT; -.
DR PDBsum; 3KBU; -.
DR PDBsum; 3UD1; -.
DR PDBsum; 3UD2; -.
DR AlphaFoldDB; P16157; -.
DR BMRB; P16157; -.
DR SMR; P16157; -.
DR BioGRID; 106783; 44.
DR IntAct; P16157; 20.
DR STRING; 9606.ENSP00000265709; -.
DR TCDB; 8.A.28.1.2; the ankyrin (ankyrin) family.
DR GlyConnect; 2881; 1 O-Linked glycan (4 sites).
DR GlyGen; P16157; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; P16157; -.
DR MetOSite; P16157; -.
DR PhosphoSitePlus; P16157; -.
DR BioMuta; ANK1; -.
DR DMDM; 116241246; -.
DR EPD; P16157; -.
DR jPOST; P16157; -.
DR MassIVE; P16157; -.
DR MaxQB; P16157; -.
DR PaxDb; P16157; -.
DR PeptideAtlas; P16157; -.
DR PRIDE; P16157; -.
DR ProteomicsDB; 15386; -.
DR ProteomicsDB; 53299; -. [P16157-1]
DR ProteomicsDB; 53300; -. [P16157-10]
DR ProteomicsDB; 53301; -. [P16157-11]
DR ProteomicsDB; 53302; -. [P16157-12]
DR ProteomicsDB; 53303; -. [P16157-13]
DR ProteomicsDB; 53304; -. [P16157-14]
DR ProteomicsDB; 53305; -. [P16157-15]
DR ProteomicsDB; 53306; -. [P16157-16]
DR ProteomicsDB; 53307; -. [P16157-17]
DR ProteomicsDB; 53308; -. [P16157-18]
DR ProteomicsDB; 53309; -. [P16157-19]
DR ProteomicsDB; 53310; -. [P16157-2]
DR ProteomicsDB; 53311; -. [P16157-20]
DR ProteomicsDB; 53312; -. [P16157-21]
DR ProteomicsDB; 53313; -. [P16157-3]
DR ProteomicsDB; 53314; -. [P16157-4]
DR ProteomicsDB; 53315; -. [P16157-5]
DR ProteomicsDB; 53316; -. [P16157-6]
DR ProteomicsDB; 53317; -. [P16157-7]
DR ProteomicsDB; 53318; -. [P16157-8]
DR ProteomicsDB; 53319; -. [P16157-9]
DR ProteomicsDB; 62; -.
DR ProteomicsDB; 62447; -.
DR ABCD; P16157; 3 sequenced antibodies.
DR Antibodypedia; 4229; 460 antibodies from 34 providers.
DR DNASU; 286; -.
DR Ensembl; ENST00000265709.13; ENSP00000265709.8; ENSG00000029534.21. [P16157-21]
DR Ensembl; ENST00000289734.13; ENSP00000289734.8; ENSG00000029534.21. [P16157-3]
DR Ensembl; ENST00000314214.12; ENSP00000319123.8; ENSG00000029534.21. [P16157-17]
DR Ensembl; ENST00000347528.8; ENSP00000339620.4; ENSG00000029534.21. [P16157-1]
DR Ensembl; ENST00000348036.8; ENSP00000297744.5; ENSG00000029534.21. [P16157-22]
DR Ensembl; ENST00000522543.5; ENSP00000430368.1; ENSG00000029534.21. [P16157-23]
DR GeneID; 286; -.
DR KEGG; hsa:286; -.
DR MANE-Select; ENST00000289734.13; ENSP00000289734.8; NM_000037.4; NP_000028.3. [P16157-3]
DR UCSC; uc003xoc.4; human. [P16157-1]
DR CTD; 286; -.
DR DisGeNET; 286; -.
DR GeneCards; ANK1; -.
DR HGNC; HGNC:492; ANK1.
DR HPA; ENSG00000029534; Group enriched (skeletal muscle, tongue).
DR MalaCards; ANK1; -.
DR MIM; 182900; phenotype.
DR MIM; 612641; gene.
DR neXtProt; NX_P16157; -.
DR OpenTargets; ENSG00000029534; -.
DR Orphanet; 251066; 8p11.2 deletion syndrome.
DR Orphanet; 822; Hereditary spherocytosis.
DR PharmGKB; PA24798; -.
DR VEuPathDB; HostDB:ENSG00000029534; -.
DR eggNOG; KOG4177; Eukaryota.
DR GeneTree; ENSGT00940000155760; -.
DR HOGENOM; CLU_1694857_0_0_1; -.
DR InParanoid; P16157; -.
DR OMA; AQHILCH; -.
DR OrthoDB; 1011028at2759; -.
DR PhylomeDB; P16157; -.
DR TreeFam; TF351263; -.
DR PathwayCommons; P16157; -.
DR Reactome; R-HSA-445095; Interaction between L1 and Ankyrins.
DR Reactome; R-HSA-447038; NrCAM interactions.
DR Reactome; R-HSA-447041; CHL1 interactions.
DR Reactome; R-HSA-447043; Neurofascin interactions.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR SignaLink; P16157; -.
DR SIGNOR; P16157; -.
DR BioGRID-ORCS; 286; 14 hits in 1080 CRISPR screens.
DR ChiTaRS; ANK1; human.
DR EvolutionaryTrace; P16157; -.
DR GeneWiki; ANK1; -.
DR GenomeRNAi; 286; -.
DR Pharos; P16157; Tbio.
DR PRO; PR:P16157; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P16157; protein.
DR Bgee; ENSG00000029534; Expressed in skeletal muscle tissue of rectus abdominis and 161 other tissues.
DR ExpressionAtlas; P16157; baseline and differential.
DR Genevisible; P16157; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; NAS:UniProtKB.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0005856; C:cytoskeleton; NAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0014731; C:spectrin-associated cytoskeleton; IDA:BHF-UCL.
DR GO; GO:0051117; F:ATPase binding; IPI:BHF-UCL.
DR GO; GO:0008093; F:cytoskeletal anchor activity; IDA:BHF-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:ARUK-UCL.
DR GO; GO:0030507; F:spectrin binding; IDA:ARUK-UCL.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
DR GO; GO:0005198; F:structural molecule activity; NAS:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; IBA:GO_Central.
DR GO; GO:0007010; P:cytoskeleton organization; NAS:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA:BHF-UCL.
DR GO; GO:0006887; P:exocytosis; NAS:UniProtKB.
DR GO; GO:0045199; P:maintenance of epithelial cell apical/basal polarity; TAS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:BHF-UCL.
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; PF12796; Ank_2; 9.
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 3D-structure; Alternative promoter usage; Alternative splicing; ANK repeat;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease variant;
KW Elliptocytosis; Hereditary hemolytic anemia; Hydroxylation; Lipoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Sarcoplasmic reticulum.
FT CHAIN 1..1881
FT /note="Ankyrin-1"
FT /id="PRO_0000066883"
FT REPEAT 44..73
FT /note="ANK 1"
FT REPEAT 77..106
FT /note="ANK 2"
FT REPEAT 110..139
FT /note="ANK 3"
FT REPEAT 143..172
FT /note="ANK 4"
FT REPEAT 174..201
FT /note="ANK 5"
FT REPEAT 205..234
FT /note="ANK 6"
FT REPEAT 238..267
FT /note="ANK 7"
FT REPEAT 271..300
FT /note="ANK 8"
FT REPEAT 304..333
FT /note="ANK 9"
FT REPEAT 337..366
FT /note="ANK 10"
FT REPEAT 370..399
FT /note="ANK 11"
FT REPEAT 403..432
FT /note="ANK 12"
FT REPEAT 436..465
FT /note="ANK 13"
FT REPEAT 469..498
FT /note="ANK 14"
FT REPEAT 502..531
FT /note="ANK 15"
FT REPEAT 535..564
FT /note="ANK 16"
FT REPEAT 568..597
FT /note="ANK 17"
FT REPEAT 601..630
FT /note="ANK 18"
FT REPEAT 634..663
FT /note="ANK 19"
FT REPEAT 667..696
FT /note="ANK 20"
FT REPEAT 700..729
FT /note="ANK 21"
FT REPEAT 733..762
FT /note="ANK 22"
FT REPEAT 766..795
FT /note="ANK 23"
FT DOMAIN 913..1068
FT /note="ZU5 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00485"
FT DOMAIN 1070..1216
FT /note="ZU5 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00485"
FT DOMAIN 1403..1487
FT /note="Death"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT REGION 1..827
FT /note="89 kDa domain"
FT REGION 875..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1234..1362
FT /note="UPA domain"
FT /evidence="ECO:0000250"
FT REGION 1383..1881
FT /note="55 kDa regulatory domain"
FT REGION 1486..1510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1583..1613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1637..1703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1718..1791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1840..1859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1490..1504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1585..1608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1640..1655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1663..1696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1718..1743
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1769..1784
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 105
FT /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial"
FT /evidence="ECO:0000269|PubMed:21177872"
FT MOD_RES 233
FT /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial"
FT /evidence="ECO:0000269|PubMed:21177872"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 431
FT /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial"
FT /evidence="ECO:0000269|PubMed:21177872"
FT MOD_RES 464
FT /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial"
FT /evidence="ECO:0000269|PubMed:21177872"
FT MOD_RES 629
FT /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial"
FT /evidence="ECO:0000269|PubMed:21177872"
FT MOD_RES 662
FT /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial"
FT /evidence="ECO:0000269|PubMed:21177872"
FT MOD_RES 695
FT /note="(3S)-3-hydroxyaspartate; by HIF1AN; partial"
FT /evidence="ECO:0000269|PubMed:21177872"
FT MOD_RES 728
FT /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial"
FT /evidence="ECO:0000269|PubMed:21177872"
FT MOD_RES 759
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 761
FT /note="(3S)-3-hydroxyasparagine; by HIF1AN; partial"
FT /evidence="ECO:0000269|PubMed:21177872"
FT MOD_RES 781
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 817
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 834
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 856
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 961
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q02357"
FT MOD_RES 1073
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q02357"
FT MOD_RES 1082
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02357"
FT MOD_RES 1378
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1380
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1390
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02357"
FT MOD_RES 1392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02357"
FT MOD_RES 1396
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1400
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q02357"
FT MOD_RES 1428
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1486
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1533
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1617
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q02357"
FT MOD_RES 1666
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1671
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1686
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1690
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1696
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..1725
FT /note="Missing (in isoform Mu17, isoform Mu18, isoform
FT Mu19, isoform Mu20, isoform 22 and isoform 23)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9430667"
FT /id="VSP_018440"
FT VAR_SEQ 1..9
FT /note="MPYSVGFRE -> MAQAAKQLKKIKDIEAQALQEQKEKEESNRKRRNRSRDR
FT KKK (in isoform Br21)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_018439"
FT VAR_SEQ 820
FT /note="E -> EGTAHITIM (in isoform Br21)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_018441"
FT VAR_SEQ 1513..1874
FT /note="Missing (in isoform Er16)"
FT /evidence="ECO:0000303|PubMed:1689849"
FT /id="VSP_000264"
FT VAR_SEQ 1514..1675
FT /note="Missing (in isoform Er2, isoform Er4, isoform Er6,
FT isoform Er8, isoform Er10, isoform Er12 and isoform Er14)"
FT /evidence="ECO:0000303|PubMed:2137557"
FT /id="VSP_018442"
FT VAR_SEQ 1726..1798
FT /note="TQGPHSFQGTSTMTEGLEPGGSQEYEKVLVSVSEHTWTEQPEAESSQADRDR
FT RQQGQEEQVQEAKNTFTQVVQ -> MWTFVTQLLVTLVLLSFFLVSCQNVMHIVRGSLC
FT FVLKHIHQELDKELGESEGLSDDEETISTRVVRRRVFLK (in isoform Mu17,
FT isoform Mu18, isoform Mu19, isoform 22 and isoform 23)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9430667"
FT /id="VSP_018443"
FT VAR_SEQ 1726..1798
FT /note="TQGPHSFQGTSTMTEGLEPGGSQEYEKVLVSVSEHTWTEQPEAESSQADRDR
FT RQQGQEEQVQEAKNTFTQVVQ -> MWTFVTQLLVTLVLLSFFLVSCQNVMHIVRGSLC
FT FVLKHIHQ (in isoform Mu20)"
FT /evidence="ECO:0000303|PubMed:9430667"
FT /id="VSP_018444"
FT VAR_SEQ 1799..1881
FT /note="GNEFQNIPGEQVTEEQFTDEQGNIVTKKIIRKVVRQIDLSSADAAQEHEEVT
FT VEGPLEDPSELEVDIDYFMKHSKDHTSTPNP -> VELRGSGLQPDLIEGRKGAQIVKR
FT ASLKRGKQ (in isoform Mu20)"
FT /evidence="ECO:0000303|PubMed:9430667"
FT /id="VSP_018446"
FT VAR_SEQ 1799..1873
FT /note="Missing (in isoform Er9, isoform Er10 and isoform
FT Mu19)"
FT /evidence="ECO:0000303|PubMed:9430667"
FT /id="VSP_018445"
FT VAR_SEQ 1826..1872
FT /note="Missing (in isoform 22)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045439"
FT VAR_SEQ 1827..1881
FT /note="IIRKVVRQIDLSSADAAQEHEEVTVEGPLEDPSELEVDIDYFMKHSKDHTST
FT PNP -> VELRGSGLQPDLIEGRKGAQIVKRASLKRGKQ (in isoform Er15
FT and isoform Mu18)"
FT /evidence="ECO:0000303|PubMed:9430667"
FT /id="VSP_018448"
FT VAR_SEQ 1827..1873
FT /note="Missing (in isoform Er7 and isoform Er8)"
FT /evidence="ECO:0000305"
FT /id="VSP_018447"
FT VAR_SEQ 1849..1873
FT /note="Missing (in isoform Er3, isoform Er4 and isoform
FT Br21)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_018449"
FT VAR_SEQ 1850..1881
FT /note="TVEGPLEDPSELEVDIDYFMKHSKDHTSTPNP -> ELRGSGLQPDLIEGRK
FT GAQIVKRASLKRGKQ (in isoform Er5, isoform Er6 and isoform
FT Mu17)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:1689849, ECO:0000303|PubMed:9430667"
FT /id="VSP_000266"
FT VAR_SEQ 1874..1881
FT /note="DHTSTPNP -> VELRGSGLQPDLIEGRKGAQIVKRASLKRGKQ (in
FT isoform Er11 and isoform Er12)"
FT /evidence="ECO:0000305"
FT /id="VSP_018450"
FT VAR_SEQ 1874..1881
FT /note="DHTSTPNP -> VLRRPRPWGTQRHHCCLALPGRLHDTSLHSPLYELSLQSL
FT FSLVGSVSAPPCRSFRSSACVLPVFAICPAFCLCCCLQVELRGSGLQPDLIEGRKGAQI
FT VKRASLKRGKQ (in isoform Er13 and isoform Er14)"
FT /evidence="ECO:0000305"
FT /id="VSP_018451"
FT VAR_SEQ 1875
FT /note="H -> D (in isoform Er16)"
FT /evidence="ECO:0000303|PubMed:1689849"
FT /id="VSP_000265"
FT VARIANT 21
FT /note="R -> T"
FT /id="VAR_000595"
FT VARIANT 276
FT /note="L -> R (in SPH1)"
FT /evidence="ECO:0000269|PubMed:11102985"
FT /id="VAR_054991"
FT VARIANT 332
FT /note="D -> H (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035605"
FT VARIANT 463
FT /note="V -> I (in SPH1; dbSNP:rs140085544)"
FT /evidence="ECO:0000269|PubMed:8640229"
FT /id="VAR_000596"
FT VARIANT 619
FT /note="R -> H (in Brueggen; dbSNP:rs2304877)"
FT /id="VAR_000597"
FT VARIANT 733
FT /note="L -> I (in dbSNP:rs11778936)"
FT /id="VAR_028769"
FT VARIANT 750
FT /note="V -> A"
FT /evidence="ECO:0000269|PubMed:2137557"
FT /id="VAR_000598"
FT VARIANT 832
FT /note="R -> Q (in dbSNP:rs34523608)"
FT /id="VAR_061012"
FT VARIANT 845
FT /note="D -> E"
FT /id="VAR_000599"
FT VARIANT 991
FT /note="V -> L (in dbSNP:rs758454168)"
FT /evidence="ECO:0000269|PubMed:9235914"
FT /id="VAR_026411"
FT VARIANT 1054
FT /note="I -> T (in SPH1)"
FT /evidence="ECO:0000269|PubMed:11102985"
FT /id="VAR_054992"
FT VARIANT 1075
FT /note="T -> I (in dbSNP:rs35213384)"
FT /evidence="ECO:0000269|PubMed:1689849,
FT ECO:0000269|PubMed:2137557, ECO:0000269|PubMed:9235914,
FT ECO:0000269|Ref.5"
FT /id="VAR_048263"
FT VARIANT 1126
FT /note="A -> P (in dbSNP:rs504465)"
FT /id="VAR_028770"
FT VARIANT 1192
FT /note="T -> P (in dbSNP:rs486770)"
FT /id="VAR_028771"
FT VARIANT 1286
FT /note="E -> D"
FT /evidence="ECO:0000269|PubMed:2141335"
FT /id="VAR_000601"
FT VARIANT 1325
FT /note="M -> V (in dbSNP:rs10093583)"
FT /id="VAR_028772"
FT VARIANT 1392
FT /note="S -> T"
FT /id="VAR_000600"
FT VARIANT 1546
FT /note="V -> I (in dbSNP:rs1060130)"
FT /evidence="ECO:0000269|PubMed:1689849"
FT /id="VAR_028773"
FT VARIANT 1592
FT /note="D -> N (in Duesseldorf; dbSNP:rs1457291305)"
FT /id="VAR_000602"
FT MUTAGEN 1824
FT /note="T->P: Abolishes interaction with OBSCN (in isoform
FT Mu17)."
FT /evidence="ECO:0000269|PubMed:12527750"
FT MUTAGEN 1826
FT /note="K->E: Abolishes interaction with OBSCN (in isoform
FT Mu17)."
FT /evidence="ECO:0000269|PubMed:12527750"
FT MUTAGEN 1829
FT /note="R->G: Abolishes interaction with OBSCN (in isoform
FT Mu17)."
FT /evidence="ECO:0000269|PubMed:12527750"
FT MUTAGEN 1830
FT /note="K->E: Abolishes interaction with OBSCN (in isoform
FT Mu17)."
FT /evidence="ECO:0000269|PubMed:12527750"
FT CONFLICT 230
FT /note="A -> S (in Ref. 2; AAA51732)"
FT /evidence="ECO:0000305"
FT CONFLICT 801
FT /note="K -> L (in Ref. 3; AAB47805)"
FT /evidence="ECO:0000305"
FT CONFLICT 845
FT /note="D -> R (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 902
FT /note="I -> T (in Ref. 3; AAB47805)"
FT /evidence="ECO:0000305"
FT HELIX 407..414
FT /evidence="ECO:0007829|PDB:1N11"
FT HELIX 417..425
FT /evidence="ECO:0007829|PDB:1N11"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:1N11"
FT HELIX 440..447
FT /evidence="ECO:0007829|PDB:1N11"
FT HELIX 450..459
FT /evidence="ECO:0007829|PDB:1N11"
FT HELIX 473..480
FT /evidence="ECO:0007829|PDB:1N11"
FT HELIX 483..492
FT /evidence="ECO:0007829|PDB:1N11"
FT HELIX 506..513
FT /evidence="ECO:0007829|PDB:1N11"
FT HELIX 516..524
FT /evidence="ECO:0007829|PDB:1N11"
FT HELIX 539..545
FT /evidence="ECO:0007829|PDB:1N11"
FT HELIX 549..557
FT /evidence="ECO:0007829|PDB:1N11"
FT HELIX 572..578
FT /evidence="ECO:0007829|PDB:1N11"
FT HELIX 582..588
FT /evidence="ECO:0007829|PDB:1N11"
FT HELIX 589..591
FT /evidence="ECO:0007829|PDB:1N11"
FT HELIX 605..611
FT /evidence="ECO:0007829|PDB:1N11"
FT HELIX 615..623
FT /evidence="ECO:0007829|PDB:1N11"
FT HELIX 638..644
FT /evidence="ECO:0007829|PDB:1N11"
FT HELIX 648..655
FT /evidence="ECO:0007829|PDB:1N11"
FT TURN 656..658
FT /evidence="ECO:0007829|PDB:1N11"
FT HELIX 671..678
FT /evidence="ECO:0007829|PDB:1N11"
FT HELIX 681..690
FT /evidence="ECO:0007829|PDB:1N11"
FT HELIX 704..710
FT /evidence="ECO:0007829|PDB:1N11"
FT HELIX 715..722
FT /evidence="ECO:0007829|PDB:1N11"
FT HELIX 737..743
FT /evidence="ECO:0007829|PDB:1N11"
FT HELIX 747..755
FT /evidence="ECO:0007829|PDB:1N11"
FT STRAND 765..767
FT /evidence="ECO:0007829|PDB:1N11"
FT HELIX 770..776
FT /evidence="ECO:0007829|PDB:1N11"
FT HELIX 780..789
FT /evidence="ECO:0007829|PDB:1N11"
FT STRAND 914..919
FT /evidence="ECO:0007829|PDB:3F59"
FT STRAND 924..927
FT /evidence="ECO:0007829|PDB:3F59"
FT TURN 930..932
FT /evidence="ECO:0007829|PDB:3UD1"
FT STRAND 935..938
FT /evidence="ECO:0007829|PDB:3F59"
FT STRAND 942..945
FT /evidence="ECO:0007829|PDB:3KBT"
FT STRAND 947..954
FT /evidence="ECO:0007829|PDB:3F59"
FT HELIX 956..958
FT /evidence="ECO:0007829|PDB:3F59"
FT STRAND 959..961
FT /evidence="ECO:0007829|PDB:3KBU"
FT STRAND 970..973
FT /evidence="ECO:0007829|PDB:3KBT"
FT STRAND 975..980
FT /evidence="ECO:0007829|PDB:3F59"
FT STRAND 984..994
FT /evidence="ECO:0007829|PDB:3F59"
FT STRAND 1000..1003
FT /evidence="ECO:0007829|PDB:3KBT"
FT STRAND 1006..1015
FT /evidence="ECO:0007829|PDB:3F59"
FT STRAND 1018..1020
FT /evidence="ECO:0007829|PDB:3KBT"
FT HELIX 1026..1028
FT /evidence="ECO:0007829|PDB:3F59"
FT HELIX 1029..1033
FT /evidence="ECO:0007829|PDB:3F59"
FT HELIX 1043..1049
FT /evidence="ECO:0007829|PDB:3F59"
FT STRAND 1051..1058
FT /evidence="ECO:0007829|PDB:3F59"
FT STRAND 1061..1067
FT /evidence="ECO:0007829|PDB:3F59"
FT STRAND 1074..1076
FT /evidence="ECO:0007829|PDB:3UD1"
FT STRAND 1081..1084
FT /evidence="ECO:0007829|PDB:3UD1"
FT STRAND 1092..1095
FT /evidence="ECO:0007829|PDB:3UD1"
FT STRAND 1099..1102
FT /evidence="ECO:0007829|PDB:3UD1"
FT STRAND 1104..1111
FT /evidence="ECO:0007829|PDB:3UD1"
FT HELIX 1115..1122
FT /evidence="ECO:0007829|PDB:3UD1"
FT STRAND 1131..1138
FT /evidence="ECO:0007829|PDB:3UD1"
FT STRAND 1140..1150
FT /evidence="ECO:0007829|PDB:3UD1"
FT HELIX 1153..1157
FT /evidence="ECO:0007829|PDB:3UD1"
FT STRAND 1165..1167
FT /evidence="ECO:0007829|PDB:3UD2"
FT STRAND 1169..1175
FT /evidence="ECO:0007829|PDB:3UD1"
FT STRAND 1195..1197
FT /evidence="ECO:0007829|PDB:3UD1"
FT STRAND 1200..1207
FT /evidence="ECO:0007829|PDB:3UD1"
FT STRAND 1210..1215
FT /evidence="ECO:0007829|PDB:3UD1"
FT HELIX 1219..1221
FT /evidence="ECO:0007829|PDB:3UD1"
FT HELIX 1222..1232
FT /evidence="ECO:0007829|PDB:3UD1"
FT TURN 1398..1402
FT /evidence="ECO:0007829|PDB:2YVI"
FT HELIX 1403..1414
FT /evidence="ECO:0007829|PDB:2YVI"
FT HELIX 1415..1417
FT /evidence="ECO:0007829|PDB:2YVI"
FT HELIX 1418..1424
FT /evidence="ECO:0007829|PDB:2YVI"
FT HELIX 1429..1438
FT /evidence="ECO:0007829|PDB:2YVI"
FT HELIX 1443..1458
FT /evidence="ECO:0007829|PDB:2YVI"
FT HELIX 1459..1461
FT /evidence="ECO:0007829|PDB:2YVI"
FT HELIX 1464..1473
FT /evidence="ECO:0007829|PDB:2YVI"
FT HELIX 1477..1483
FT /evidence="ECO:0007829|PDB:2YVI"
FT CONFLICT P16157-17:63
FT /note="T -> P (in Ref. 4; AAC01950)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1881 AA; 206265 MW; 49466F6F915019EC CRC64;
MPYSVGFREA DAATSFLRAA RSGNLDKALD HLRNGVDINT CNQNGLNGLH LASKEGHVKM
VVELLHKEII LETTTKKGNT ALHIAALAGQ DEVVRELVNY GANVNAQSQK GFTPLYMAAQ
ENHLEVVKFL LENGANQNVA TEDGFTPLAV ALQQGHENVV AHLINYGTKG KVRLPALHIA
ARNDDTRTAA VLLQNDPNPD VLSKTGFTPL HIAAHYENLN VAQLLLNRGA SVNFTPQNGI
TPLHIASRRG NVIMVRLLLD RGAQIETKTK DELTPLHCAA RNGHVRISEI LLDHGAPIQA
KTKNGLSPIH MAAQGDHLDC VRLLLQYDAE IDDITLDHLT PLHVAAHCGH HRVAKVLLDK
GAKPNSRALN GFTPLHIACK KNHVRVMELL LKTGASIDAV TESGLTPLHV ASFMGHLPIV
KNLLQRGASP NVSNVKVETP LHMAARAGHT EVAKYLLQNK AKVNAKAKDD QTPLHCAARI
GHTNMVKLLL ENNANPNLAT TAGHTPLHIA AREGHVETVL ALLEKEASQA CMTKKGFTPL
HVAAKYGKVR VAELLLERDA HPNAAGKNGL TPLHVAVHHN NLDIVKLLLP RGGSPHSPAW
NGYTPLHIAA KQNQVEVARS LLQYGGSANA ESVQGVTPLH LAAQEGHAEM VALLLSKQAN
GNLGNKSGLT PLHLVAQEGH VPVADVLIKH GVMVDATTRM GYTPLHVASH YGNIKLVKFL
LQHQADVNAK TKLGYSPLHQ AAQQGHTDIV TLLLKNGASP NEVSSDGTTP LAIAKRLGYI
SVTDVLKVVT DETSFVLVSD KHRMSFPETV DEILDVSEDE GEELISFKAE RRDSRDVDEE
KELLDFVPKL DQVVESPAIP RIPCAMPETV VIRSEEQEQA SKEYDEDSLI PSSPATETSD
NISPVASPVH TGFLVSFMVD ARGGSMRGSR HNGLRVVIPP RTCAAPTRIT CRLVKPQKLS
TPPPLAEEEG LASRIIALGP TGAQFLSPVI VEIPHFASHG RGDRELVVLR SENGSVWKEH
RSRYGESYLD QILNGMDEEL GSLEELEKKR VCRIITTDFP LYFVIMSRLC QDYDTIGPEG
GSLKSKLVPL VQATFPENAV TKRVKLALQA QPVPDELVTK LLGNQATFSP IVTVEPRRRK
FHRPIGLRIP LPPSWTDNPR DSGEGDTTSL RLLCSVIGGT DQAQWEDITG TTKLVYANEC
ANFTTNVSAR FWLSDCPRTA EAVNFATLLY KELTAVPYMA KFVIFAKMND PREGRLRCYC
MTDDKVDKTL EQHENFVEVA RSRDIEVLEG MSLFAELSGN LVPVKKAAQQ RSFHFQSFRE
NRLAMPVKVR DSSREPGGSL SFLRKAMKYE DTQHILCHLN ITMPPCAKGS GAEDRRRTPT
PLALRYSILS ESTPGSLSGT EQAEMKMAVI SEHLGLSWAE LARELQFSVE DINRIRVENP
NSLLEQSVAL LNLWVIREGQ NANMENLYTA LQSIDRGEIV NMLEGSGRQS RNLKPDRRHT
DRDYSLSPSQ MNGYSSLQDE LLSPASLGCA LSSPLRADQY WNEVAVLDAI PLAATEHDTM
LEMSDMQVWS AGLTPSLVTA EDSSLECSKA EDSDATGHEW KLEGALSEEP RGPELGSLEL
VEDDTVDSDA TNGLIDLLEQ EEGQRSEEKL PGSKRQDDAT GAGQDSENEV SLVSGHQRGQ
ARITHSPTVS QVTERSQDRL QDWDADGSIV SYLQDAAQGS WQEEVTQGPH SFQGTSTMTE
GLEPGGSQEY EKVLVSVSEH TWTEQPEAES SQADRDRRQQ GQEEQVQEAK NTFTQVVQGN
EFQNIPGEQV TEEQFTDEQG NIVTKKIIRK VVRQIDLSSA DAAQEHEEVT VEGPLEDPSE
LEVDIDYFMK HSKDHTSTPN P
