ANR11_HUMAN
ID ANR11_HUMAN Reviewed; 2663 AA.
AC Q6UB99; Q6NTG1; Q6QMF8;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Ankyrin repeat domain-containing protein 11;
DE AltName: Full=Ankyrin repeat-containing cofactor 1;
GN Name=ANKRD11; Synonyms=ANCO1;
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], AND SUBCELLULAR LOCATION.
RA Powell J.A., Settasatian C., Lower K., Callen D.F.;
RT "ANKRD11 and ANKRD12 are novel 9kb genes encoding nuclear-located proteins
RT with ankyrin domains.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND INTERACTION WITH
RP P160.
RX PubMed=15184363; DOI=10.1074/jbc.m403997200;
RA Zhang A., Yeung P.L., Li C.-W., Tsai S.-C., Dinh G.K., Wu X., Li H.,
RA Chen J.D.;
RT "Identification of a novel family of ankyrin repeats-containing cofactors
RT for p160 nuclear receptor coactivators.";
RL J. Biol. Chem. 279:33799-33805(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-451.
RC TISSUE=Pancreas;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1509, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276; SER-408; THR-410;
RP SER-411; SER-834; THR-1120; SER-1123; THR-1419; SER-1792; SER-1847 AND
RP SER-1859, AND 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276; SER-408; THR-410 AND
RP SER-411, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276; SER-408; THR-410;
RP SER-411; SER-834 AND THR-1419, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP INVOLVEMENT IN KBGS.
RX PubMed=21782149; DOI=10.1016/j.ajhg.2011.06.007;
RA Sirmaci A., Spiliopoulos M., Brancati F., Powell E., Duman D., Abrams A.,
RA Bademci G., Agolini E., Guo S., Konuk B., Kavaz A., Blanton S.,
RA Digilio M.C., Dallapiccola B., Young J., Zuchner S., Tekin M.;
RT "Mutations in ANKRD11 cause KBG syndrome, characterized by intellectual
RT disability, skeletal malformations, and macrodontia.";
RL Am. J. Hum. Genet. 89:289-294(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408; THR-410; SER-411 AND
RP SER-834, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276; SER-834; THR-1419;
RP SER-1792 AND SER-1990, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25556659; DOI=10.1016/j.devcel.2014.11.031;
RA Gallagher D., Voronova A., Zander M.A., Cancino G.I., Bramall A.,
RA Krause M.P., Abad C., Tekin M., Neilsen P.M., Callen D.F., Scherer S.W.,
RA Keller G.M., Kaplan D.R., Walz K., Miller F.D.;
RT "Ankrd11 is a chromatin regulator involved in autism that is essential for
RT neural development.";
RL Dev. Cell 32:31-42(2015).
RN [13]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, PROTEASOMAL DEGRADATION, AND
RP VARIANT KBGS GLN-2512.
RX PubMed=25413698; DOI=10.1007/s00439-014-1509-2;
RA Walz K., Cohen D., Neilsen P.M., Foster J. II, Brancati F., Demir K.,
RA Fisher R., Moffat M., Verbeek N.E., Bjoergo K., Lo Castro A., Curatolo P.,
RA Novelli G., Abad C., Lei C., Zhang L., Diaz-Horta O., Young J.I.,
RA Callen D.F., Tekin M.;
RT "Characterization of ANKRD11 mutations in humans and mice related to KBG
RT syndrome.";
RL Hum. Genet. 134:181-190(2015).
CC -!- FUNCTION: Chromatin regulator which modulates histone acetylation and
CC gene expression in neural precursor cells (By similarity). May recruit
CC histone deacetylases (HDACs) to the p160 coactivators/nuclear receptor
CC complex to inhibit ligand-dependent transactivation (PubMed:15184363).
CC Has a role in proliferation and development of cortical neural
CC precursors (PubMed:25556659). May also regulate bone homeostasis (By
CC similarity). {ECO:0000250|UniProtKB:E9Q4F7,
CC ECO:0000269|PubMed:15184363, ECO:0000269|PubMed:25556659}.
CC -!- SUBUNIT: Interacts with the PAS region of the p160 coactivators.
CC {ECO:0000269|PubMed:15184363}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15184363,
CC ECO:0000269|PubMed:25413698, ECO:0000269|PubMed:25556659,
CC ECO:0000269|Ref.1}. Note=Localizes to chromatin during prometaphase.
CC {ECO:0000269|PubMed:25413698}.
CC -!- DEVELOPMENTAL STAGE: Expression levels are regulated during the cell
CC cycle, reaching maximal levels at M phase and then rapidly declining
CC after late M phase. {ECO:0000269|PubMed:25413698}.
CC -!- PTM: Subject to proteasomal degradation which is probably essential to
CC regulate its activity. {ECO:0000269|PubMed:25413698}.
CC -!- DISEASE: KBG syndrome (KBGS) [MIM:148050]: A syndrome characterized by
CC macrodontia of the upper central incisors, distinctive craniofacial
CC findings, short stature, skeletal anomalies, and neurologic involvement
CC that includes global developmental delay, seizures, and intellectual
CC disability. {ECO:0000269|PubMed:21782149, ECO:0000269|PubMed:25413698}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH69013.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AY373756; AAR25661.1; -; mRNA.
DR EMBL; AY533563; AAS45544.1; -; mRNA.
DR EMBL; AC137932; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069013; AAH69013.1; ALT_SEQ; mRNA.
DR CCDS; CCDS32513.1; -.
DR RefSeq; NP_001243111.1; NM_001256182.1.
DR RefSeq; NP_001243112.1; NM_001256183.1.
DR RefSeq; NP_037407.4; NM_013275.5.
DR RefSeq; XP_011521353.1; XM_011523051.2.
DR RefSeq; XP_011521355.1; XM_011523053.2.
DR RefSeq; XP_016878671.1; XM_017023182.1.
DR RefSeq; XP_016878672.1; XM_017023183.1.
DR RefSeq; XP_016878673.1; XM_017023184.1.
DR RefSeq; XP_016878674.1; XM_017023185.1.
DR RefSeq; XP_016878675.1; XM_017023186.1.
DR RefSeq; XP_016878676.1; XM_017023187.1.
DR AlphaFoldDB; Q6UB99; -.
DR SMR; Q6UB99; -.
DR BioGRID; 118888; 135.
DR CORUM; Q6UB99; -.
DR IntAct; Q6UB99; 21.
DR STRING; 9606.ENSP00000301030; -.
DR CarbonylDB; Q6UB99; -.
DR GlyGen; Q6UB99; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6UB99; -.
DR PhosphoSitePlus; Q6UB99; -.
DR BioMuta; ANKRD11; -.
DR DMDM; 296439440; -.
DR EPD; Q6UB99; -.
DR jPOST; Q6UB99; -.
DR MassIVE; Q6UB99; -.
DR MaxQB; Q6UB99; -.
DR PaxDb; Q6UB99; -.
DR PeptideAtlas; Q6UB99; -.
DR PRIDE; Q6UB99; -.
DR ProteomicsDB; 67406; -.
DR Antibodypedia; 4516; 137 antibodies from 22 providers.
DR DNASU; 29123; -.
DR Ensembl; ENST00000301030.10; ENSP00000301030.4; ENSG00000167522.17.
DR Ensembl; ENST00000378330.7; ENSP00000367581.2; ENSG00000167522.17.
DR Ensembl; ENST00000642600.1; ENSP00000495226.1; ENSG00000167522.17.
DR GeneID; 29123; -.
DR KEGG; hsa:29123; -.
DR MANE-Select; ENST00000301030.10; ENSP00000301030.4; NM_013275.6; NP_037407.4.
DR UCSC; uc002fmx.3; human.
DR CTD; 29123; -.
DR DisGeNET; 29123; -.
DR GeneCards; ANKRD11; -.
DR GeneReviews; ANKRD11; -.
DR HGNC; HGNC:21316; ANKRD11.
DR HPA; ENSG00000167522; Low tissue specificity.
DR MalaCards; ANKRD11; -.
DR MIM; 148050; phenotype.
DR MIM; 611192; gene.
DR neXtProt; NX_Q6UB99; -.
DR OpenTargets; ENSG00000167522; -.
DR Orphanet; 261250; 16q24.3 microdeletion syndrome.
DR Orphanet; 2332; KBG syndrome.
DR PharmGKB; PA134861925; -.
DR VEuPathDB; HostDB:ENSG00000167522; -.
DR eggNOG; ENOG502QQG5; Eukaryota.
DR GeneTree; ENSGT00940000155966; -.
DR HOGENOM; CLU_229338_0_0_1; -.
DR InParanoid; Q6UB99; -.
DR OMA; LNDGESC; -.
DR OrthoDB; 854133at2759; -.
DR PhylomeDB; Q6UB99; -.
DR TreeFam; TF326440; -.
DR PathwayCommons; Q6UB99; -.
DR SignaLink; Q6UB99; -.
DR SIGNOR; Q6UB99; -.
DR BioGRID-ORCS; 29123; 244 hits in 1090 CRISPR screens.
DR ChiTaRS; ANKRD11; human.
DR GenomeRNAi; 29123; -.
DR Pharos; Q6UB99; Tbio.
DR PRO; PR:Q6UB99; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q6UB99; protein.
DR Bgee; ENSG00000167522; Expressed in tendon of biceps brachii and 187 other tissues.
DR ExpressionAtlas; Q6UB99; baseline and differential.
DR Genevisible; Q6UB99; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0060325; P:face morphogenesis; IMP:MGI.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
DR GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR042636; ANKRD11.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR PANTHER; PTHR24145; PTHR24145; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
PE 1: Evidence at protein level;
KW ANK repeat; Disease variant; Dwarfism; Intellectual disability; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..2663
FT /note="Ankyrin repeat domain-containing protein 11"
FT /id="PRO_0000066907"
FT REPEAT 167..196
FT /note="ANK 1"
FT REPEAT 200..229
FT /note="ANK 2"
FT REPEAT 233..262
FT /note="ANK 3"
FT REPEAT 266..292
FT /note="ANK 4"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1059..1393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1424..1710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1814..1836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1988..2019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2131..2406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2369..2663
FT /note="Important for protein degradation"
FT /evidence="ECO:0000269|PubMed:25413698"
FT COMPBIAS 23..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..465
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..642
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1145..1305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1328..1393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1424..1446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1455..1548
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1557..1574
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1588..1602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1609..1658
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2339..2353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2370..2385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2391..2406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 410
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 834
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1079
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9Q4F7"
FT MOD_RES 1120
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1419
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1509
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 1692
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9Q4F7"
FT MOD_RES 1792
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1847
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1850
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:E9Q4F7"
FT MOD_RES 1851
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:E9Q4F7"
FT MOD_RES 1852
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9Q4F7"
FT MOD_RES 1859
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1990
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 2512
FT /note="R -> Q (in KBGS; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:25413698"
FT /id="VAR_075870"
FT CONFLICT 76
FT /note="E -> EE (in Ref. 1; AAR25661)"
FT /evidence="ECO:0000305"
FT CONFLICT 971
FT /note="A -> V (in Ref. 1; AAR25661 and 2; AAS45544)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2663 AA; 297913 MW; 845B04094AF37CFE CRC64;
MPKGGCPKAP QQEELPLSSD MVEKQTGKKD KDKVSLTKTP KLERGDGGKE VRERASKRKL
PFTAGANGEQ KDSDTEKQGP ERKRIKKEPV TRKAGLLFGM GLSGIRAGYP LSERQQVALL
MQMTAEESAN SPVDTTPKHP SQSTVCQKGT PNSASKTKDK VNKRNERGET RLHRAAIRGD
ARRIKELISE GADVNVKDFA GWTALHEACN RGYYDVAKQL LAAGAEVNTK GLDDDTPLHD
AANNGHYKVV KLLLRYGGNP QQSNRKGETP LKVANSPTMV NLLLGKGTYT SSEESSTESS
EEEDAPSFAP SSSVDGNNTD SEFEKGLKHK AKNPEPQKAT APVKDEYEFD EDDEQDRVPP
VDDKHLLKKD YRKETKSNSF ISIPKMEVKS YTKNNTIAPK KASHRILSDT SDEEDASVTV
GTGEKLRLSA HTILPGSKTR EPSNAKQQKE KNKVKKKRKK ETKGREVRFG KRSDKFCSSE
SESESSESGE DDRDSLGSSG CLKGSPLVLK DPSLFSSLSA SSTSSHGSSA AQKQNPSHTD
QHTKHWRTDN WKTISSPAWS EVSSLSDSTR TRLTSESDYS SEGSSVESLK PVRKRQEHRK
RASLSEKKSP FLSSAEGAVP KLDKEGKVVK KHKTKHKHKN KEKGQCSISQ ELKLKSFTYE
YEDSKQKSDK AILLENDLST ENKLKVLKHD RDHFKKEEKL SKMKLEEKEW LFKDEKSLKR
IKDTNKDISR SFREEKDRSN KAEKERSLKE KSPKEEKLRL YKEERKKKSK DRPSKLEKKN
DLKEDKISKE KEKIFKEDKE KLKKEKVYRE DSAFDEYCNK NQFLENEDTK FSLSDDQRDR
WFSDLSDSSF DFKGEDSWDS PVTDYRDMKS DSVAKLILET VKEDSKERRR DSRAREKRDY
REPFFRKKDR DYLDKNSEKR KEQTEKHKSV PGYLSEKDKK RRESAEAGRD RKDALESCKE
RRDGRAKPEE AHREELKECG CESGFKDKSD GDFGKGLEPW ERHHPAREKE KKDGPDKERK
EKTKPERYKE KSSDKDKSEK SILEKCQKDK EFDKCFKEKK DTKEKHKDTH GKDKERKASL
DQGKEKKEKA FPGIISEDFS EKKDDKKGKE KSWYIADIFT DESEDDRDSC MGSGFKMGEA
SDLPRTDGLQ EKEEGREAYA SDRHRKSSDK QHPERQKDKE PRDRRKDRGA ADAGRDKKEK
VFEKHKEKKD KESTEKYKDR KDRASVDSTQ DKKNKQKLPE KAEKKHAAED KAKSKHKEKS
DKEHSKERKS SRSADAEKSL LEKLEEEALH EYREDSNDKI SEVSSDSFTD RGQEPGLTAF
LEVSFTEPPG DDKPRESACL PEKLKEKERH RHSSSSSKKS HDRERAKKEK AEKKEKGEDY
KEGGSRKDSG QYEKDFLEAD AYGVSYNMKA DIEDELDKTI ELFSTEKKDK NDSEREPSKK
IEKELKPYGS SAINILKEKK KREKHREKWR DEKERHRDRH ADGLLRHHRD ELLRHHRDEQ
KPATRDKDSP PRVLKDKSRD EGPRLGDAKL KEKFKDGAEK EKGDPVKMSN GNDKVAPSKD
PGKKDARPRE KLLGDGDLMM TSFERMLSQK DLEIEERHKR HKERMKQMEK LRHRSGDPKL
KEKAKPADDG RKKGLDIPAK KPPGLDPPFK DKKLKESTPI PPAAENKLHP ASGADSKDWL
AGPHMKEVLP ASPRPDQSRP TGVPTPTSVL SCPSYEEVMH TPRTPSCSAD DYADLVFDCA
DSQHSTPVPT APTSACSPSF FDRFSVASSG LSENASQAPA RPLSTNLYRS VSVDIRRTPE
EEFSVGDKLF RQQSVPAASS YDSPMPPSME DRAPLPPVPA EKFACLSPGY YSPDYGLPSP
KVDALHCPPA AVVTVTPSPE GVFSSLQAKP SPSPRAELLV PSLEGALPPD LDTSEDQQAT
AAIIPPEPSY LEPLDEGPFS AVITEEPVEW AHPSEQALAS SLIGGTSENP VSWPVGSDLL
LKSPQRFPES PKRFCPADPL HSAAPGPFSA SEAPYPAPPA SPAPYALPVA EPGLEDVKDG
VDAVPAAIST SEAAPYAPPS GLESFFSNCK SLPEAPLDVA PEPACVAAVA QVEALGPLEN
SFLDGSRGLS HLGQVEPVPW ADAFAGPEDD LDLGPFSLPE LPLQTKDAAD GEAEPVEESL
APPEEMPPGA PGVINGGDVS TVVAEEPPAL PPDQASTRLP AELEPEPSGE PKLDVALEAA
VEAETVPEER ARGDPDSSVE PAPVPPEQRP LGSGDQGAEA EGPPAASLCA PDGPAPNTVA
QAQAADGAGP EDDTEASRAA APAEGPPGGI QPEAAEPKPT AEAPKAPRVE EIPQRMTRNR
AQMLANQSKQ GPPPSEKECA PTPAPVTRAK ARGSEDDDAQ AQHPRKRRFQ RSTQQLQQQL
NTSTQQTREV IQQTLAAIVD AIKLDAIEPY HSDRANPYFE YLQIRKKIEE KRKILCCITP
QAPQCYAEYV TYTGSYLLDG KPLSKLHIPV IAPPPSLAEP LKELFRQQEA VRGKLRLQHS
IEREKLIVSC EQEILRVHCR AARTIANQAV PFSACTMLLD SEVYNMPLES QGDENKSVRD
RFNARQFISW LQDVDDKYDR MKTCLLMRQQ HEAAALNAVQ RMEWQLKVQE LDPAGHKSLC
VNEVPSFYVP MVDVNDDFVL LPA
