ID KI67_HUMAN Reviewed; 3256 AA. AC P46013; Q5VWH2; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2006, sequence version 2. DT 09-DEC-2015, entry version 161. DE RecName: Full=Antigen KI-67; GN Name=MKI67; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SHORT AND LONG), AND VARIANTS RP VAL-872; TRP-1470; LEU-1622; ALA-1849 AND ASP-3097. RX PubMed=8227122; DOI=10.1083/jcb.123.3.513; RA Schlueter C., Duchrow M., Wohlenberg C., Becker M.H.G., Key G., RA Flad H.-D., Gerdes J.; RT "The cell proliferation-associated antigen of antibody Ki-67: a very RT large, ubiquitous nuclear protein with numerous repeated elements, RT representing a new kind of cell cycle-maintaining proteins."; RL J. Cell Biol. 123:513-522(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31. RA Gerdes J.; RT "Sequence of the human Ki-67 protein gene 5' and promoter region."; RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP INTERACTION WITH KIF15. RX PubMed=10878014; DOI=10.1074/jbc.M003879200; RA Sueishi M., Takagi M., Yoneda Y.; RT "The forkhead-associated domain of Ki-67 antigen interacts with the RT novel kinesin-like protein Hklp2."; RL J. Biol. Chem. 275:28888-28892(2000). RN [5] RP INTERACTION WITH NIFK. RX PubMed=11342549; DOI=10.1074/jbc.M102227200; RA Takagi M., Sueishi M., Saiwaki T., Kametaka A., Yoneda Y.; RT "A novel nucleolar protein, NIFK, interacts with the forkhead RT associated domain of Ki-67 antigen in mitosis."; RL J. Biol. Chem. 276:25386-25391(2001). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2406 AND SER-2708, AND RP IDENTIFICATION BY 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., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-328; SER-357; SER-579; RP SER-584; SER-1131; THR-1327; THR-1569; THR-1801; THR-1923 AND RP THR-2406, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein RT phosphorylation analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1233; THR-1355; SER-1679 RP AND THR-1764, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa RT cells and high confident phosphopeptide identification by cross- RT validation of MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357; SER-579; SER-584 RP AND SER-1861, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., RA Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for RT efficient phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308; SER-357; SER-579; RP SER-648 AND SER-1679, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-264; SER-308; RP THR-328; THR-347; SER-357; THR-401; SER-579; SER-584; SER-648; RP THR-761; SER-859; THR-1017; SER-1071; THR-1091; SER-1098; THR-1111; RP SER-1131; THR-1139; SER-1142; SER-1207; SER-1253; SER-1256; THR-1261; RP THR-1298; THR-1315; THR-1327; SER-1329; THR-1335; THR-1355; SER-1376; RP THR-1383; THR-1503; SER-1506; THR-1540; TYR-1552; THR-1557; THR-1569; RP SER-1571; SER-1679; SER-1689; THR-1719; SER-1721; SER-1740; THR-1747; RP THR-1784; THR-1801; THR-1841; SER-1861; SER-1864; THR-1869; THR-1923; RP THR-2065; SER-2072; THR-2085; SER-2105; THR-2113; THR-2203; SER-2223; RP THR-2231; SER-2239; THR-2285; THR-2325; THR-2328; THR-2333; SER-2344; RP THR-2352; THR-2389; SER-2395; THR-2406; SER-2528; SER-2588; SER-2708; RP SER-2827; SER-2828 AND SER-3041, AND IDENTIFICATION BY MASS RP 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 [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP IDENTIFICATION IN A COMPLEX WITH ASCL2; C11ORF30; HCFC1; HSPA8; CCAR2; RP MATR3; RBBP5; TUBB2A; WDR5 AND ZNF335. RX PubMed=19131338; DOI=10.1074/jbc.M805872200; RA Garapaty S., Xu C.F., Trojer P., Mahajan M.A., Neubert T.A., RA Samuels H.H.; RT "Identification and characterization of a novel nuclear protein RT complex involved in nuclear hormone receptor-mediated gene RT regulation."; RL J. Biol. Chem. 284:7542-7552(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-648; SER-1131; THR-1335; RP THR-1557; THR-1764; SER-1937; THR-2406 AND SER-2420, AND RP 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 [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1639 AND LYS-2005, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308; SER-357; SER-579; RP SER-584; SER-648; THR-1091; SER-1098; SER-1131; THR-1167; THR-1193; RP SER-1207; THR-1233; THR-1315; THR-1327; SER-1329; THR-1335; THR-1355; RP THR-1557; THR-1569; SER-1571; SER-1679; THR-1747; THR-1801; SER-1815; RP SER-1861; THR-1897; THR-1923; SER-1937; THR-1963; SER-1983; THR-2065; RP SER-2072; THR-2085; SER-2105; SER-2135; SER-2223; THR-2231; THR-2233; RP SER-2239; THR-2268; THR-2285; THR-2325; SER-2344; THR-2389; SER-2395; RP THR-2406; SER-2420; THR-2446; SER-2528; SER-2588; SER-2708 AND RP SER-3128, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308; SER-352; SER-357; RP SER-1098; SER-1131; SER-1496; SER-1861; SER-1983; SER-2072; SER-2105; RP SER-2344; SER-2528; SER-2588 AND SER-2708, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [19] RP INTERACTION WITH ZNF335. RX PubMed=23178126; DOI=10.1016/j.cell.2012.10.043; RA Yang Y.J., Baltus A.E., Mathew R.S., Murphy E.A., Evrony G.D., RA Gonzalez D.M., Wang E.P., Marshall-Walker C.A., Barry B.J., Murn J., RA Tatarakis A., Mahajan M.A., Samuels H.H., Shi Y., Golden J.A., RA Mahajnah M., Shenhav R., Walsh C.A.; RT "Microcephaly gene links trithorax and REST/NRSF to control neural RT stem cell proliferation and differentiation."; RL Cell 151:1097-1112(2012). RN [20] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=22002106; DOI=10.1074/mcp.M111.013680; RA Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.; RT "Systematic analysis of protein pools, isoforms, and modifications RT affecting turnover and subcellular localization."; RL Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012). RN [21] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1035; LYS-1643; LYS-2613; RP LYS-2734 AND LYS-2852, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [22] RP STRUCTURE BY NMR OF 1-120 IN COMPLEX WITH NIFK. RX PubMed=14659764; DOI=10.1016/j.jmb.2003.10.032; RA Li H., Byeon I.-J., Ju Y., Tsai M.-D.; RT "Structure of human Ki67 FHA domain and its binding to a RT phosphoprotein fragment from hNIFK reveal unique recognition sites and RT new views to the structural basis of FHA domain functions."; RL J. Mol. Biol. 335:371-381(2004). RN [23] RP STRUCTURE BY NMR OF 1-120 IN COMPLEX WITH NIFK. RX PubMed=16244663; DOI=10.1038/nsmb1008; RA Byeon I.-J., Li H., Song H., Gronenborn A.M., Tsai M.-D.; RT "Sequential phosphorylation and multisite interactions characterize RT specific target recognition by the FHA domain of Ki67."; RL Nat. Struct. Mol. Biol. 12:987-993(2005). CC -!- FUNCTION: Thought to be required for maintaining cell CC proliferation. CC -!- SUBUNIT: Interacts with KIF15. Binds through the FHA domain to CC NIFK. Part of a complex composed at least of ASCL2, C11orf30/EMSY, CC HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; CC this complex may have a histone H3-specific methyltransferase CC activity. {ECO:0000269|PubMed:10878014, CC ECO:0000269|PubMed:11342549, ECO:0000269|PubMed:14659764, CC ECO:0000269|PubMed:16244663, ECO:0000269|PubMed:19131338, CC ECO:0000269|PubMed:23178126}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22002106}. CC Nucleus, nucleolus {ECO:0000269|PubMed:22002106}. Chromosome CC {ECO:0000269|PubMed:22002106}. Note=Predominantly localized in the CC G1 phase in the perinucleolar region, in the later phases it is CC also detected throughout the nuclear interior, being predominantly CC localized in the nuclear matrix. In mitosis, it is present on all CC chromosomes. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P46013-1; Sequence=Displayed; CC Name=Short; CC IsoId=P46013-2; Sequence=VSP_004298; CC -!- DEVELOPMENTAL STAGE: Expression of this antigen occurs CC preferentially during late G1, S, G2 and M phases of the cell CC cycle, while in cells in G0 phase the antigen cannot be detected. CC -!- SIMILARITY: Contains 1 FHA domain. {ECO:0000255|PROSITE- CC ProRule:PRU00086}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Ki-67 entry; CC URL="https://en.wikipedia.org/wiki/Ki-67_%28Biology%29"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X65550; CAA46519.1; -; mRNA. DR EMBL; X65551; CAA46520.1; -; mRNA. DR EMBL; AL390236; CAH73169.1; -; Genomic_DNA. DR EMBL; AL355529; CAH73169.1; JOINED; Genomic_DNA. DR EMBL; X94762; CAA64388.1; -; Genomic_DNA. DR CCDS; CCDS53588.1; -. [P46013-2] DR CCDS; CCDS7659.1; -. [P46013-1] DR PIR; A48666; A48666. DR RefSeq; NP_001139438.1; NM_001145966.1. [P46013-2] DR RefSeq; NP_002408.3; NM_002417.4. [P46013-1] DR UniGene; Hs.689823; -. DR UniGene; Hs.80976; -. DR PDB; 1R21; NMR; -; A=1-120. DR PDB; 2AFF; NMR; -; A=1-120. DR PDBsum; 1R21; -. DR PDBsum; 2AFF; -. DR ProteinModelPortal; P46013; -. DR SMR; P46013; 1-100. DR BioGrid; 110434; 35. DR DIP; DIP-28132N; -. DR IntAct; P46013; 33. DR MINT; MINT-137995; -. DR STRING; 9606.ENSP00000357643; -. DR PhosphoSite; P46013; -. DR BioMuta; MKI67; -. DR DMDM; 118572663; -. DR MaxQB; P46013; -. DR PaxDb; P46013; -. DR PRIDE; P46013; -. DR Ensembl; ENST00000368653; ENSP00000357642; ENSG00000148773. [P46013-2] DR Ensembl; ENST00000368654; ENSP00000357643; ENSG00000148773. [P46013-1] DR GeneID; 4288; -. DR KEGG; hsa:4288; -. DR UCSC; uc001lke.3; human. [P46013-1] DR UCSC; uc001lkf.3; human. [P46013-2] DR CTD; 4288; -. DR GeneCards; MKI67; -. DR HGNC; HGNC:7107; MKI67. DR HPA; CAB000058; -. DR HPA; CAB068198; -. DR HPA; HPA000451; -. DR HPA; HPA001164; -. DR MIM; 176741; gene. DR neXtProt; NX_P46013; -. DR PharmGKB; PA30825; -. DR eggNOG; ENOG410JR7C; Eukaryota. DR eggNOG; ENOG410ZXYW; LUCA. DR GeneTree; ENSGT00530000064425; -. DR HOGENOM; HOG000113223; -. DR HOVERGEN; HBG006213; -. DR InParanoid; P46013; -. DR KO; K17582; -. DR OMA; QTPKEKA; -. DR OrthoDB; EOG76QFGJ; -. DR PhylomeDB; P46013; -. DR TreeFam; TF336000; -. DR ChiTaRS; MKI67; human. DR EvolutionaryTrace; P46013; -. DR GeneWiki; Ki-67_(protein); -. DR GenomeRNAi; 4288; -. DR NextBio; 16881; -. DR PRO; PR:P46013; -. DR Proteomes; UP000005640; Chromosome 10. DR Bgee; P46013; -. DR CleanEx; HS_MKI67; -. DR ExpressionAtlas; P46013; baseline and differential. DR Genevisible; P46013; HS. DR GO; GO:0000775; C:chromosome, centromeric region; IEA:Ensembl. DR GO; GO:0000793; C:condensed chromosome; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB. DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB. DR GO; GO:0008283; P:cell proliferation; TAS:UniProtKB. DR GO; GO:0034605; P:cellular response to heat; IEA:Ensembl. DR GO; GO:1990705; P:cholangiocyte proliferation; IEA:Ensembl. DR GO; GO:0006259; P:DNA metabolic process; IEA:Ensembl. DR GO; GO:0072574; P:hepatocyte proliferation; IEA:Ensembl. DR GO; GO:0030212; P:hyaluronan metabolic process; IEA:Ensembl. DR GO; GO:0007126; P:meiotic nuclear division; IEA:Ensembl. DR GO; GO:0031100; P:organ regeneration; IEA:Ensembl. DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl. DR Gene3D; 2.60.200.20; -; 1. DR InterPro; IPR000253; FHA_dom. DR InterPro; IPR012568; K167R. DR InterPro; IPR029334; PP1-bd. DR InterPro; IPR008984; SMAD_FHA_domain. DR Pfam; PF00498; FHA; 1. DR Pfam; PF08065; K167R; 16. DR Pfam; PF15276; PP1_bind; 1. DR SMART; SM00240; FHA; 1. DR SUPFAM; SSF49879; SSF49879; 1. DR PROSITE; PS50006; FHA_DOMAIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; KW Cell cycle; Chromosome; Complete proteome; Isopeptide bond; KW Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; KW Reference proteome; Repeat; Ubl conjugation. FT CHAIN 1 3256 Antigen KI-67. FT /FTId=PRO_0000084301. FT DOMAIN 27 76 FHA. {ECO:0000255|PROSITE- FT ProRule:PRU00086}. FT REPEAT 1000 1112 1. FT REPEAT 1122 1234 2. FT REPEAT 1244 1356 3. FT REPEAT 1366 1477 4. FT REPEAT 1487 1598 5. FT REPEAT 1608 1720 6. FT REPEAT 1730 1842 7. FT REPEAT 1851 1964 8. FT REPEAT 1974 2086 9. FT REPEAT 2096 2204 10. FT REPEAT 2214 2326 11. FT REPEAT 2335 2447 12. FT REPEAT 2457 2569 13. FT REPEAT 2579 2689 14. FT REPEAT 2699 2808 15. FT REPEAT 2818 2928 16. FT NP_BIND 3034 3041 ATP. {ECO:0000255}. FT REGION 1000 2928 16 X 122 AA approximate repeats. FT MOD_RES 125 125 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 264 264 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 308 308 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:18691976, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692}. FT MOD_RES 328 328 Phosphothreonine. FT {ECO:0000244|PubMed:16964243, FT ECO:0000244|PubMed:18669648}. FT MOD_RES 347 347 Phosphothreonine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 352 352 Phosphoserine. FT {ECO:0000244|PubMed:21406692}. FT MOD_RES 357 357 Phosphoserine. FT {ECO:0000244|PubMed:16964243, FT ECO:0000244|PubMed:18220336, FT ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:18691976, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692}. FT MOD_RES 401 401 Phosphothreonine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 579 579 Phosphoserine. FT {ECO:0000244|PubMed:16964243, FT ECO:0000244|PubMed:18220336, FT ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:18691976, FT ECO:0000244|PubMed:19369195, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 584 584 Phosphoserine. FT {ECO:0000244|PubMed:16964243, FT ECO:0000244|PubMed:18220336, FT ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 648 648 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:18691976, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 761 761 Phosphothreonine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 859 859 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1017 1017 Phosphothreonine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1071 1071 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1091 1091 Phosphothreonine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 1098 1098 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692}. FT MOD_RES 1111 1111 Phosphothreonine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1131 1131 Phosphoserine. FT {ECO:0000244|PubMed:16964243, FT ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692}. FT MOD_RES 1139 1139 Phosphothreonine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1142 1142 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1167 1167 Phosphothreonine. FT {ECO:0000244|PubMed:20068231}. FT MOD_RES 1193 1193 Phosphothreonine. FT {ECO:0000244|PubMed:20068231}. FT MOD_RES 1207 1207 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 1233 1233 Phosphothreonine. FT {ECO:0000244|PubMed:17924679, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 1253 1253 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1256 1256 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1261 1261 Phosphothreonine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1298 1298 Phosphothreonine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1315 1315 Phosphothreonine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 1327 1327 Phosphothreonine. FT {ECO:0000244|PubMed:16964243, FT ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 1329 1329 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 1335 1335 Phosphothreonine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 1355 1355 Phosphothreonine. FT {ECO:0000244|PubMed:17924679, FT ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 1376 1376 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1383 1383 Phosphothreonine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1496 1496 Phosphoserine. FT {ECO:0000244|PubMed:21406692}. FT MOD_RES 1503 1503 Phosphothreonine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1506 1506 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1540 1540 Phosphothreonine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1552 1552 Phosphotyrosine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1557 1557 Phosphothreonine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 1569 1569 Phosphothreonine. FT {ECO:0000244|PubMed:16964243, FT ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 1571 1571 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 1639 1639 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 1679 1679 Phosphoserine. FT {ECO:0000244|PubMed:17924679, FT ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:18691976, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 1689 1689 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1719 1719 Phosphothreonine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1721 1721 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1740 1740 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1747 1747 Phosphothreonine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 1764 1764 Phosphothreonine. FT {ECO:0000244|PubMed:17924679, FT ECO:0000244|PubMed:19690332}. FT MOD_RES 1784 1784 Phosphothreonine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1801 1801 Phosphothreonine. FT {ECO:0000244|PubMed:16964243, FT ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 1815 1815 Phosphoserine. FT {ECO:0000244|PubMed:20068231}. FT MOD_RES 1841 1841 Phosphothreonine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1861 1861 Phosphoserine. FT {ECO:0000244|PubMed:18220336, FT ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692}. FT MOD_RES 1864 1864 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1869 1869 Phosphothreonine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1897 1897 Phosphothreonine. FT {ECO:0000244|PubMed:20068231}. FT MOD_RES 1923 1923 Phosphothreonine. FT {ECO:0000244|PubMed:16964243, FT ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 1937 1937 Phosphoserine. FT {ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 1963 1963 Phosphothreonine. FT {ECO:0000244|PubMed:20068231}. FT MOD_RES 1983 1983 Phosphoserine. FT {ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692}. FT MOD_RES 2005 2005 N6-acetyllysine. FT {ECO:0000244|PubMed:19608861}. FT MOD_RES 2065 2065 Phosphothreonine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 2072 2072 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692}. FT MOD_RES 2085 2085 Phosphothreonine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 2105 2105 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692}. FT MOD_RES 2113 2113 Phosphothreonine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 2135 2135 Phosphoserine. FT {ECO:0000244|PubMed:20068231}. FT MOD_RES 2203 2203 Phosphothreonine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 2223 2223 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 2231 2231 Phosphothreonine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 2233 2233 Phosphothreonine. FT {ECO:0000244|PubMed:20068231}. FT MOD_RES 2239 2239 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 2268 2268 Phosphothreonine. FT {ECO:0000244|PubMed:20068231}. FT MOD_RES 2285 2285 Phosphothreonine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 2325 2325 Phosphothreonine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 2328 2328 Phosphothreonine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 2333 2333 Phosphothreonine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 2344 2344 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692}. FT MOD_RES 2352 2352 Phosphothreonine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 2389 2389 Phosphothreonine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 2395 2395 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 2406 2406 Phosphothreonine. FT {ECO:0000244|PubMed:16964243, FT ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 2420 2420 Phosphoserine. FT {ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 2446 2446 Phosphothreonine. FT {ECO:0000244|PubMed:20068231}. FT MOD_RES 2528 2528 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692}. FT MOD_RES 2588 2588 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692}. FT MOD_RES 2708 2708 Phosphoserine. FT {ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692}. FT MOD_RES 2827 2827 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 2828 2828 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 3041 3041 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 3128 3128 Phosphoserine. FT {ECO:0000244|PubMed:20068231}. FT CROSSLNK 1035 1035 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447}. FT CROSSLNK 1643 1643 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447}. FT CROSSLNK 2613 2613 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447}. FT CROSSLNK 2734 2734 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447}. FT CROSSLNK 2852 2852 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SUMO2). FT {ECO:0000244|PubMed:25218447}. FT VAR_SEQ 136 495 Missing (in isoform Short). FT {ECO:0000303|PubMed:8227122}. FT /FTId=VSP_004298. FT VARIANT 104 104 N -> S (in dbSNP:rs2071498). FT /FTId=VAR_029055. FT VARIANT 238 238 W -> R (in dbSNP:rs7095325). FT /FTId=VAR_029056. FT VARIANT 497 497 E -> D (in dbSNP:rs11016076). FT /FTId=VAR_029057. FT VARIANT 574 574 Q -> P (in dbSNP:rs4471342). FT /FTId=VAR_029058. FT VARIANT 631 631 I -> L (in dbSNP:rs997983). FT /FTId=VAR_024161. FT VARIANT 832 832 R -> W (in dbSNP:rs34916904). FT /FTId=VAR_033995. FT VARIANT 854 854 L -> V (in dbSNP:rs2240). FT /FTId=VAR_024162. FT VARIANT 872 872 A -> V (in dbSNP:rs2853344). FT {ECO:0000269|PubMed:8227122}. FT /FTId=VAR_029059. FT VARIANT 1042 1042 G -> S (in dbSNP:rs2152143). FT /FTId=VAR_024163. FT VARIANT 1120 1120 T -> S (in dbSNP:rs11016074). FT /FTId=VAR_029060. FT VARIANT 1247 1247 T -> I (in dbSNP:rs4750685). FT /FTId=VAR_021838. FT VARIANT 1403 1403 E -> V (in dbSNP:rs3740423). FT /FTId=VAR_020047. FT VARIANT 1470 1470 L -> W (in dbSNP:rs2853345). FT {ECO:0000269|PubMed:8227122}. FT /FTId=VAR_029061. FT VARIANT 1559 1559 V -> M (in dbSNP:rs7918199). FT /FTId=VAR_029062. FT VARIANT 1622 1622 P -> L (in dbSNP:rs2782871). FT {ECO:0000269|PubMed:8227122}. FT /FTId=VAR_029063. FT VARIANT 1849 1849 T -> A (in dbSNP:rs2782872). FT {ECO:0000269|PubMed:8227122}. FT /FTId=VAR_029064. FT VARIANT 1876 1876 R -> Q (in dbSNP:rs11591817). FT /FTId=VAR_029065. FT VARIANT 1951 1951 L -> I (in dbSNP:rs34116632). FT /FTId=VAR_033996. FT VARIANT 2101 2101 I -> T (in dbSNP:rs11016073). FT /FTId=VAR_029066. FT VARIANT 2337 2337 T -> N (in dbSNP:rs7083622). FT /FTId=VAR_024164. FT VARIANT 2363 2363 N -> S (in dbSNP:rs7071768). FT /FTId=VAR_029067. FT VARIANT 2607 2607 R -> H (in dbSNP:rs34688192). FT /FTId=VAR_061671. FT VARIANT 2608 2608 P -> L (in dbSNP:rs1063535). FT /FTId=VAR_024165. FT VARIANT 2649 2649 R -> H (in dbSNP:rs12777740). FT /FTId=VAR_029068. FT VARIANT 2720 2720 T -> P (in dbSNP:rs1050767). FT /FTId=VAR_024166. FT VARIANT 2760 2760 D -> G (in dbSNP:rs10082391). FT /FTId=VAR_029069. FT VARIANT 2786 2786 R -> Q (in dbSNP:rs10764749). FT /FTId=VAR_029070. FT VARIANT 2793 2793 S -> N (in dbSNP:rs10082533). FT /FTId=VAR_029071. FT VARIANT 2845 2845 R -> H (in dbSNP:rs11016072). FT /FTId=VAR_029072. FT VARIANT 2868 2868 T -> S (in dbSNP:rs2071496). FT /FTId=VAR_024167. FT VARIANT 2904 2904 Q -> R (in dbSNP:rs11016071). FT /FTId=VAR_029073. FT VARIANT 3097 3097 N -> D (in dbSNP:rs2798669). FT {ECO:0000269|PubMed:8227122}. FT /FTId=VAR_029074. FT VARIANT 3102 3102 E -> G (in dbSNP:rs34750407). FT /FTId=VAR_033997. FT VARIANT 3150 3150 T -> S (in dbSNP:rs11106). FT /FTId=VAR_014858. FT VARIANT 3217 3217 K -> E (in dbSNP:rs8473). FT /FTId=VAR_014859. FT CONFLICT 619 626 RKSGNLPS -> ERVATCLQ (in Ref. 1; FT CAA46519/CAA46520). {ECO:0000305}. FT CONFLICT 2205 2205 I -> V (in Ref. 1; CAA46519/CAA46520). FT {ECO:0000305}. FT CONFLICT 2892 2893 KL -> NV (in Ref. 1; CAA46519/CAA46520). FT {ECO:0000305}. FT CONFLICT 3246 3246 R -> T (in Ref. 1; CAA46519/CAA46520). FT {ECO:0000305}. FT STRAND 5 12 {ECO:0000244|PDB:1R21}. FT STRAND 15 21 {ECO:0000244|PDB:1R21}. FT STRAND 24 32 {ECO:0000244|PDB:1R21}. FT STRAND 35 38 {ECO:0000244|PDB:1R21}. FT STRAND 49 53 {ECO:0000244|PDB:1R21}. FT STRAND 58 60 {ECO:0000244|PDB:1R21}. FT STRAND 65 67 {ECO:0000244|PDB:1R21}. FT STRAND 80 82 {ECO:0000244|PDB:2AFF}. FT STRAND 86 89 {ECO:0000244|PDB:1R21}. FT STRAND 94 99 {ECO:0000244|PDB:1R21}. SQ SEQUENCE 3256 AA; 358694 MW; 1332BC6C799AD64D CRC64; MWPTRRLVTI KRSGVDGPHF PLSLSTCLFG RGIECDIRIQ LPVVSKQHCK IEIHEQEAIL HNFSSTNPTQ VNGSVIDEPV RLKHGDVITI IDRSFRYENE SLQNGRKSTE FPRKIREQEP ARRVSRSSFS SDPDEKAQDS KAYSKITEGK VSGNPQVHIK NVKEDSTADD SKDSVAQGTT NVHSSEHAGR NGRNAADPIS GDFKEISSVK LVSRYGELKS VPTTQCLDNS KKNESPFWKL YESVKKELDV KSQKENVLQY CRKSGLQTDY ATEKESADGL QGETQLLVSR KSRPKSGGSG HAVAEPASPE QELDQNKGKG RDVESVQTPS KAVGASFPLY EPAKMKTPVQ YSQQQNSPQK HKNKDLYTTG RRESVNLGKS EGFKAGDKTL TPRKLSTRNR TPAKVEDAAD SATKPENLSS KTRGSIPTDV EVLPTETEIH NEPFLTLWLT QVERKIQKDS LSKPEKLGTT AGQMCSGLPG LSSVDINNFG DSINESEGIP LKRRRVSFGG HLRPELFDEN LPPNTPLKRG EAPTKRKSLV MHTPPVLKKI IKEQPQPSGK QESGSEIHVE VKAQSLVISP PAPSPRKTPV ASDQRRRSCK TAPASSSKSQ TEVPKRGGRK SGNLPSKRVS ISRSQHDILQ MICSKRRSGA SEANLIVAKS WADVVKLGAK QTQTKVIKHG PQRSMNKRQR RPATPKKPVG EVHSQFSTGH ANSPCTIIIG KAHTEKVHVP ARPYRVLNNF ISNQKMDFKE DLSGIAEMFK TPVKEQPQLT STCHIAISNS ENLLGKQFQG TDSGEEPLLP TSESFGGNVF FSAQNAAKQP SDKCSASPPL RRQCIRENGN VAKTPRNTYK MTSLETKTSD TETEPSKTVS TANRSGRSTE FRNIQKLPVE SKSEETNTEI VECILKRGQK ATLLQQRREG EMKEIERPFE TYKENIELKE NDEKMKAMKR SRTWGQKCAP MSDLTDLKSL PDTELMKDTA RGQNLLQTQD HAKAPKSEKG KITKMPCQSL QPEPINTPTH TKQQLKASLG KVGVKEELLA VGKFTRTSGE TTHTHREPAG DGKSIRTFKE SPKQILDPAA RVTGMKKWPR TPKEEAQSLE DLAGFKELFQ TPGPSEESMT DEKTTKIACK SPPPESVDTP TSTKQWPKRS LRKADVEEEF LALRKLTPSA GKAMLTPKPA GGDEKDIKAF MGTPVQKLDL AGTLPGSKRQ LQTPKEKAQA LEDLAGFKEL FQTPGHTEEL VAAGKTTKIP CDSPQSDPVD TPTSTKQRPK RSIRKADVEG ELLACRNLMP SAGKAMHTPK PSVGEEKDII IFVGTPVQKL DLTENLTGSK RRPQTPKEEA QALEDLTGFK ELFQTPGHTE EAVAAGKTTK MPCESSPPES ADTPTSTRRQ PKTPLEKRDV QKELSALKKL TQTSGETTHT DKVPGGEDKS INAFRETAKQ KLDPAASVTG SKRHPKTKEK AQPLEDLAGL KELFQTPVCT DKPTTHEKTT KIACRSQPDP VDTPTSSKPQ SKRSLRKVDV EEEFFALRKR TPSAGKAMHT PKPAVSGEKN IYAFMGTPVQ KLDLTENLTG SKRRLQTPKE KAQALEDLAG FKELFQTRGH TEESMTNDKT AKVACKSSQP DPDKNPASSK RRLKTSLGKV GVKEELLAVG KLTQTSGETT HTHTEPTGDG KSMKAFMESP KQILDSAASL TGSKRQLRTP KGKSEVPEDL AGFIELFQTP SHTKESMTNE KTTKVSYRAS QPDLVDTPTS SKPQPKRSLR KADTEEEFLA FRKQTPSAGK AMHTPKPAVG EEKDINTFLG TPVQKLDQPG NLPGSNRRLQ TRKEKAQALE ELTGFRELFQ TPCTDNPTTD EKTTKKILCK SPQSDPADTP TNTKQRPKRS LKKADVEEEF LAFRKLTPSA GKAMHTPKAA VGEEKDINTF VGTPVEKLDL LGNLPGSKRR PQTPKEKAKA LEDLAGFKEL FQTPGHTEES MTDDKITEVS CKSPQPDPVK TPTSSKQRLK ISLGKVGVKE EVLPVGKLTQ TSGKTTQTHR ETAGDGKSIK AFKESAKQML DPANYGTGME RWPRTPKEEA QSLEDLAGFK ELFQTPDHTE ESTTDDKTTK IACKSPPPES MDTPTSTRRR PKTPLGKRDI VEELSALKQL TQTTHTDKVP GDEDKGINVF RETAKQKLDP AASVTGSKRQ PRTPKGKAQP LEDLAGLKEL FQTPICTDKP TTHEKTTKIA CRSPQPDPVG TPTIFKPQSK RSLRKADVEE ESLALRKRTP SVGKAMDTPK PAGGDEKDMK AFMGTPVQKL DLPGNLPGSK RWPQTPKEKA QALEDLAGFK ELFQTPGTDK PTTDEKTTKI ACKSPQPDPV DTPASTKQRP KRNLRKADVE EEFLALRKRT PSAGKAMDTP KPAVSDEKNI NTFVETPVQK LDLLGNLPGS KRQPQTPKEK AEALEDLVGF KELFQTPGHT EESMTDDKIT EVSCKSPQPE SFKTSRSSKQ RLKIPLVKVD MKEEPLAVSK LTRTSGETTQ THTEPTGDSK SIKAFKESPK QILDPAASVT GSRRQLRTRK EKARALEDLV DFKELFSAPG HTEESMTIDK NTKIPCKSPP PELTDTATST KRCPKTRPRK EVKEELSAVE RLTQTSGQST HTHKEPASGD EGIKVLKQRA KKKPNPVEEE PSRRRPRAPK EKAQPLEDLA GFTELSETSG HTQESLTAGK ATKIPCESPP LEVVDTTAST KRHLRTRVQK VQVKEEPSAV KFTQTSGETT DADKEPAGED KGIKALKESA KQTPAPAASV TGSRRRPRAP RESAQAIEDL AGFKDPAAGH TEESMTDDKT TKIPCKSSPE LEDTATSSKR RPRTRAQKVE VKEELLAVGK LTQTSGETTH TDKEPVGEGK GTKAFKQPAK RKLDAEDVIG SRRQPRAPKE KAQPLEDLAS FQELSQTPGH TEELANGAAD SFTSAPKQTP DSGKPLKISR RVLRAPKVEP VGDVVSTRDP VKSQSKSNTS LPPLPFKRGG GKDGSVTGTK RLRCMPAPEE IVEELPASKK QRVAPRARGK SSEPVVIMKR SLRTSAKRIE PAEELNSNDM KTNKEEHKLQ DSVPENKGIS LRSRRQNKTE AEQQITEVFV LAERIEINRN EKKPMKTSPE MDIQNPDDGA RKPIPRDKVT ENKRCLRSAR QNESSQPKVA EESGGQKSAK VLMQNQKGKG EAGNSDSMCL RSRKTKSQPA ASTLESKSVQ RVTRSVKRCA ENPKKAEDNV CVKKIRTRSH RDSEDI //