ID KI67_MOUSE Reviewed; 3177 AA. AC E9PVX6; Q61769; Q7TSF6; DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot. DT 05-APR-2011, sequence version 1. DT 27-MAR-2024, entry version 89. DE RecName: Full=Proliferation marker protein Ki-67 {ECO:0000305}; DE AltName: Full=Antigen identified by monoclonal antibody Ki-67 homolog {ECO:0000305}; DE Short=Antigen KI-67 homolog {ECO:0000305}; DE Short=Antigen Ki67 homolog {ECO:0000305}; GN Name=Mki67 {ECO:0000312|MGI:MGI:106035}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND DEVELOPMENTAL STAGE. RC STRAIN=CBA/J; TISSUE=Testis; RX PubMed=8834799; DOI=10.1242/jcs.109.1.143; RA Starborg M., Gell K., Brundell E., Hoog C.; RT "The murine Ki-67 cell proliferation antigen accumulates in the nucleolar RT and heterochromatic regions of interphase cells and at the periphery of the RT mitotic chromosomes in a process essential for cell cycle progression."; RL J. Cell Sci. 109:143-153(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2379-3177. RC TISSUE=Limb; 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 [4] RP SUBCELLULAR LOCATION. RX PubMed=12355204; DOI=10.1007/s00412-002-0202-8; RA Traut W., Endl E., Scholzen T., Gerdes J., Winking H.; RT "The temporal and spatial distribution of the proliferation associated Ki- RT 67 protein during female and male meiosis."; RL Chromosoma 111:156-164(2002). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337; SER-373; SER-1587; RP SER-2545 AND THR-3021, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162; SER-276; SER-277; RP SER-286; SER-287; SER-503; SER-588; THR-1150; SER-1152; THR-1159; THR-1175; RP THR-1363; SER-1366; THR-1400; THR-1416; SER-1469; SER-1734; SER-1825; RP THR-1868; THR-1884; THR-1989; THR-2005; THR-2073; SER-2076; SER-2103; RP THR-2106; THR-2122; THR-2218; SER-2220; THR-2227; THR-2243; SER-2390; RP SER-2392; SER-2423; SER-2425; SER-2545; SER-2780 AND THR-3021, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Heart, Kidney, Lung, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2928, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). RN [8] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=26949251; DOI=10.7554/elife.13722; RA Sobecki M., Mrouj K., Camasses A., Parisis N., Nicolas E., Lleres D., RA Gerbe F., Prieto S., Krasinska L., David A., Eguren M., Birling M.C., RA Urbach S., Hem S., Dejardin J., Malumbres M., Jay P., Dulic V., RA Lafontaine D.L.J., Feil R., Fisher D.; RT "The cell proliferation antigen Ki-67 organises heterochromatin."; RL Elife 5:0-0(2016). RN [9] RP FUNCTION. RX PubMed=27362226; DOI=10.1038/nature18610; RA Cuylen S., Blaukopf C., Politi A.Z., Mueller-Reichert T., Neumann B., RA Poser I., Ellenberg J., Hyman A.A., Gerlich D.W.; RT "Ki-67 acts as a biological surfactant to disperse mitotic chromosomes."; RL Nature 535:308-312(2016). CC -!- FUNCTION: Required to maintain individual mitotic chromosomes dispersed CC in the cytoplasm following nuclear envelope disassembly CC (PubMed:27362226). Associates with the surface of the mitotic CC chromosome, the perichromosomal layer, and covers a substantial CC fraction of the chromosome surface (PubMed:27362226). Prevents CC chromosomes from collapsing into a single chromatin mass by forming a CC steric and electrostatic charge barrier: the protein has a high net CC electrical charge and acts as a surfactant, dispersing chromosomes and CC enabling independent chromosome motility (PubMed:27362226). Binds DNA, CC with a preference for supercoiled DNA and AT-rich DNA (By similarity). CC Does not contribute to the internal structure of mitotic chromosomes CC (PubMed:26949251). May play a role in chromatin organization CC (PubMed:26949251). It is however unclear whether it plays a direct role CC in chromatin organization or whether it is an indirect consequence of CC its function in maintaining mitotic chromosomes dispersed. CC {ECO:0000250|UniProtKB:P46013, ECO:0000269|PubMed:26949251, CC ECO:0000269|PubMed:27362226, ECO:0000305}. CC -!- SUBUNIT: Interacts with KIF15 (By similarity). Interacts (via the FHA CC domain) with NIFK (By similarity). Interacts with PPP1CC (By CC similarity). Component of a complex at least composed of ZNF335, HCFC1, CC CCAR2, EMSY, MKI67, RBBP5, ASH2L and WDR5; the complex is formed as a CC result of interactions between components of a nuclear receptor- CC mediated transcription complex and a histone methylation complex (By CC similarity). Interacts with ZNF335 (By similarity). CC {ECO:0000250|UniProtKB:P46013}. CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:12355204, CC ECO:0000269|PubMed:8834799}. Nucleus {ECO:0000269|PubMed:12355204, CC ECO:0000269|PubMed:8834799}. Nucleus, nucleolus CC {ECO:0000269|PubMed:12355204, ECO:0000269|PubMed:8834799}. CC Note=Associates with the surface of the mitotic chromosome, the CC perichromosomal layer, and covers a substantial fraction of the mitotic CC chromosome surface (PubMed:8834799, PubMed:12355204). Associates with CC satellite DNA in G1 phase (By similarity). Binds tightly to chromatin CC in interphase, chromatin-binding decreases in mitosis when it CC associates with the surface of the condensed chromosomes (By CC similarity). Predominantly localized in the G1 phase in the CC perinucleolar region, in the later phases it is also detected CC throughout the nuclear interior, being predominantly localized in the CC nuclear matrix (By similarity). {ECO:0000250|UniProtKB:P46013, CC ECO:0000269|PubMed:12355204, ECO:0000269|PubMed:8834799}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=E9PVX6-1; Sequence=Displayed; CC Name=2; CC IsoId=E9PVX6-2; Sequence=VSP_058551; CC -!- TISSUE SPECIFICITY: Mainly present in proliferating cells (at protein CC level). {ECO:0000269|PubMed:8834799}. CC -!- DEVELOPMENTAL STAGE: Accumulates during the late G1 stage in the CC nucleus and maximum expression is found during G2 phase and mitosis CC (PubMed:8834799). During male meiosis, present in nuclei of all stages CC from the spermatogonium through spermatocytes I and II up to the CC earliest spermatid stage (early round spermatids) and then fades out CC (PubMed:12355204). Not detected in later spermatid stages or sperm CC (PubMed:12355204). During female meiosis, present in prophase I oocytes CC of fetal ovaries, while it is absent in resting oocytes. Reappears in CC oocytes of growing follicles and is continuously present up to CC metaphase II (at protein level) (PubMed:12355204). CC {ECO:0000269|PubMed:12355204, ECO:0000269|PubMed:8834799}. CC -!- PTM: Phosphorylated. Hyperphosphorylated in mitosis. CC Hyperphosphorylated form does not bind DNA. CC {ECO:0000250|UniProtKB:P46013}. CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice were born at the CC expected Mendelian ratio and show no overt phenotype (PubMed:26949251). CC Cells do not show proliferation defects, but chromatin organization is CC impaired, with defects in heterochromatin compaction and long-range CC genomic interactions (PubMed:26949251). {ECO:0000269|PubMed:26949251}. CC -!- CAUTION: Was thought to play a key role in cell proliferation, and is CC commonly used as a marker of cell proliferation. However, its primary CC function is uncoupled from cell proliferation (PubMed:26949251). CC Required to maintain mitotic chromosomes dispersed by forming a steric CC and electrostatic charge barrier (PubMed:27362226). CC {ECO:0000269|PubMed:26949251, ECO:0000269|PubMed:27362226}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH53453.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=CAA58026.1; Type=Frameshift; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=The contours of heredity CC - Issue 186 of December 2016; CC URL="https://web.expasy.org/spotlight/back_issues/186/"; 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; X82786; CAA58026.1; ALT_FRAME; mRNA. DR EMBL; AC123047; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC053453; AAH53453.1; ALT_FRAME; mRNA. DR CCDS; CCDS52421.1; -. [E9PVX6-1] DR PIR; T30249; T30249. DR RefSeq; NP_001074586.2; NM_001081117.2. [E9PVX6-1] DR SMR; E9PVX6; -. DR IntAct; E9PVX6; 18. DR STRING; 10090.ENSMUSP00000033310; -. DR GlyGen; E9PVX6; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; E9PVX6; -. DR PhosphoSitePlus; E9PVX6; -. DR EPD; E9PVX6; -. DR jPOST; E9PVX6; -. DR MaxQB; E9PVX6; -. DR PaxDb; 10090-ENSMUSP00000033310; -. DR PeptideAtlas; E9PVX6; -. DR ProteomicsDB; 263442; -. [E9PVX6-1] DR ProteomicsDB; 263443; -. [E9PVX6-2] DR Pumba; E9PVX6; -. DR Antibodypedia; 741; 2754 antibodies from 60 providers. DR Ensembl; ENSMUST00000033310.9; ENSMUSP00000033310.8; ENSMUSG00000031004.9. [E9PVX6-1] DR GeneID; 17345; -. DR KEGG; mmu:17345; -. DR UCSC; uc009kem.2; mouse. [E9PVX6-1] DR AGR; MGI:106035; -. DR CTD; 4288; -. DR MGI; MGI:106035; Mki67. DR VEuPathDB; HostDB:ENSMUSG00000031004; -. DR eggNOG; ENOG502QRVV; Eukaryota. DR GeneTree; ENSGT00940000154352; -. DR HOGENOM; CLU_000534_0_0_1; -. DR InParanoid; E9PVX6; -. DR OMA; KNRAQPL; -. DR OrthoDB; 3140593at2759; -. DR PhylomeDB; E9PVX6; -. DR TreeFam; TF336000; -. DR BioGRID-ORCS; 17345; 6 hits in 78 CRISPR screens. DR ChiTaRS; Mki67; mouse. DR PRO; PR:E9PVX6; -. DR Proteomes; UP000000589; Chromosome 7. DR RNAct; E9PVX6; Protein. DR Bgee; ENSMUSG00000031004; Expressed in fetal liver hematopoietic progenitor cell and 233 other cell types or tissues. DR ExpressionAtlas; E9PVX6; baseline and differential. DR GO; GO:0005694; C:chromosome; ISO:MGI. DR GO; GO:0000775; C:chromosome, centromeric region; IDA:MGI. DR GO; GO:0000793; C:condensed chromosome; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0016604; C:nuclear body; ISO:MGI. DR GO; GO:0005730; C:nucleolus; IDA:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0008283; P:cell population proliferation; IDA:MGI. DR GO; GO:1990705; P:cholangiocyte proliferation; IDA:MGI. DR GO; GO:0050673; P:epithelial cell proliferation; IDA:MGI. DR GO; GO:0072574; P:hepatocyte proliferation; IDA:MGI. DR GO; GO:0051321; P:meiotic cell cycle; IDA:MGI. DR GO; GO:1902275; P:regulation of chromatin organization; IMP:UniProtKB. DR GO; GO:0051983; P:regulation of chromosome segregation; ISS:UniProtKB. DR GO; GO:0007088; P:regulation of mitotic nuclear division; ISS:UniProtKB. DR GO; GO:0072089; P:stem cell proliferation; IDA:MGI. DR CDD; cd22673; FHA_Ki67; 1. DR Gene3D; 2.60.200.20; -; 1. DR InterPro; IPR000253; FHA_dom. DR InterPro; IPR012568; KI67R. DR InterPro; IPR029334; PP1-bd. DR InterPro; IPR008984; SMAD_FHA_dom_sf. DR PANTHER; PTHR21603; ANTIGEN KI-67-LIKE PROTEIN; 1. DR PANTHER; PTHR21603:SF17; PROLIFERATION MARKER PROTEIN KI-67; 1. DR Pfam; PF00498; FHA; 1. DR Pfam; PF08065; KI67R; 16. DR Pfam; PF15276; PP1_bind; 1. DR SMART; SM00240; FHA; 1. DR SMART; SM01295; K167R; 16. DR SUPFAM; SSF49879; SMAD/FHA domain; 1. DR PROSITE; PS50006; FHA_DOMAIN; 1. DR Genevisible; E9PVX6; MM. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; ATP-binding; Cell cycle; Chromosome; KW DNA-binding; Isopeptide bond; Nucleotide-binding; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Ubl conjugation. FT CHAIN 1..3177 FT /note="Proliferation marker protein Ki-67" FT /id="PRO_0000437535" FT DOMAIN 27..76 FT /note="FHA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086" FT DOMAIN 462..509 FT /note="PP1-binding" FT /evidence="ECO:0000255" FT REPEAT 994..1101 FT /note="K167R 1" FT /evidence="ECO:0000255" FT REPEAT 1108..1216 FT /note="K167R 2" FT /evidence="ECO:0000255" FT REPEAT 1228..1336 FT /note="K167R 3" FT /evidence="ECO:0000255" FT REPEAT 1348..1450 FT /note="K167R 4" FT /evidence="ECO:0000255" FT REPEAT 1461..1569 FT /note="K167R 5" FT /evidence="ECO:0000255" FT REPEAT 1582..1684 FT /note="K167R 6" FT /evidence="ECO:0000255" FT REPEAT 1696..1806 FT /note="K167R 7" FT /evidence="ECO:0000255" FT REPEAT 1817..1925 FT /note="K167R 8" FT /evidence="ECO:0000255" FT REPEAT 1937..2046 FT /note="K167R 9" FT /evidence="ECO:0000255" FT REPEAT 2059..2163 FT /note="K167R 10" FT /evidence="ECO:0000255" FT REPEAT 2175..2284 FT /note="K167R 11" FT /evidence="ECO:0000255" FT REPEAT 2296..2405 FT /note="K167R 12" FT /evidence="ECO:0000255" FT REPEAT 2419..2526 FT /note="K167R 13" FT /evidence="ECO:0000255" FT REPEAT 2537..2639 FT /note="K167R 14" FT /evidence="ECO:0000255" FT REPEAT 2643..2748 FT /note="K167R 15" FT /evidence="ECO:0000255" FT REPEAT 2762..2870 FT /note="K167R 16" FT /evidence="ECO:0000255" FT REGION 98..442 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 473..572 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 614..652 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 793..815 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 835..901 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 956..989 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1109..1321 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1334..1410 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1526..1550 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1749..1797 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1925..2033 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2047..2112 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2124..2343 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2378..2447 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2538..2828 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2879..3160 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 116..139 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 163..189 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 196..228 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 229..262 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 270..286 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 302..318 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 319..341 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 635..652 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 866..892 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1110..1132 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1163..1191 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1215..1250 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1252..1269 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1270..1303 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1335..1371 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1372..1389 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1763..1780 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1938..1960 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1993..2021 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2047..2083 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2084..2099 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2162..2200 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2201..2216 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2252..2269 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2282..2321 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2392..2441 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2553..2569 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2576..2593 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2620..2639 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2646..2661 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2676..2712 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2750..2780 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2781..2801 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2802..2828 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2881..2895 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2896..2921 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2956..2995 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3004..3030 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3045..3059 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3060..3094 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3120..3160 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 2973..2980 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT MOD_RES 125 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 128 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 162 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 250 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 276 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 277 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 286 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 287 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 307 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 316 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 321 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 337 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319" FT MOD_RES 373 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319" FT MOD_RES 498 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 503 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 588 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 701 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 1062 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 1114 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 1122 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 1125 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 1150 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1152 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1159 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1175 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1189 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 1215 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 1235 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 1243 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 1279 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 1295 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 1307 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 1315 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 1335 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 1356 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 1363 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1366 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1400 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1416 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1469 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1477 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 1480 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 1513 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 1542 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 1587 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319" FT MOD_RES 1609 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 1684 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 1712 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 1734 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1766 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 1779 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 1805 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 1825 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1859 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 1868 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1884 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 1924 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 1944 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 1966 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 1989 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2005 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2025 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 2045 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 2065 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 2073 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2076 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2095 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 2103 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2106 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2122 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2162 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 2182 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 2190 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 2198 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 2218 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2220 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2227 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2243 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2283 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 2303 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 2311 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 2348 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 2390 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2392 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2405 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 2423 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2425 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2464 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 2487 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 2545 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319, FT ECO:0007744|PubMed:21183079" FT MOD_RES 2592 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 2649 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 2768 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 2780 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2928 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 2980 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT MOD_RES 3021 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19144319, FT ECO:0007744|PubMed:21183079" FT MOD_RES 3061 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P46013" FT CROSSLNK 236 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P46013" FT CROSSLNK 1013 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P46013" FT CROSSLNK 1026 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P46013" FT CROSSLNK 1082 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0000250|UniProtKB:P46013" FT CROSSLNK 1082 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P46013" FT CROSSLNK 1317 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P46013" FT CROSSLNK 1668 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P46013" FT CROSSLNK 2027 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0000250|UniProtKB:P46013" FT CROSSLNK 2027 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P46013" FT CROSSLNK 2451 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0000250|UniProtKB:P46013" FT CROSSLNK 2675 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0000250|UniProtKB:P46013" FT CROSSLNK 2675 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0000250|UniProtKB:P46013" FT CROSSLNK 2909 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P46013" FT VAR_SEQ 1150..1390 FT /note="Missing (in isoform 2)" FT /id="VSP_058551" FT CONFLICT 344 FT /note="E -> G (in Ref. 1; CAA58026)" FT /evidence="ECO:0000305" FT CONFLICT 364..365 FT /note="AA -> TP (in Ref. 1; CAA58026)" FT /evidence="ECO:0000305" FT CONFLICT 372 FT /note="A -> G (in Ref. 1; CAA58026)" FT /evidence="ECO:0000305" FT CONFLICT 384..385 FT /note="KK -> PQ (in Ref. 1; CAA58026)" FT /evidence="ECO:0000305" FT CONFLICT 401 FT /note="K -> N (in Ref. 1; CAA58026)" FT /evidence="ECO:0000305" FT CONFLICT 546 FT /note="K -> N (in Ref. 1; CAA58026)" FT /evidence="ECO:0000305" FT CONFLICT 622 FT /note="Q -> P (in Ref. 1; CAA58026)" FT /evidence="ECO:0000305" FT CONFLICT 1079 FT /note="E -> G (in Ref. 1; CAA58026)" FT /evidence="ECO:0000305" FT CONFLICT 2911 FT /note="D -> V (in Ref. 1; CAA58026)" FT /evidence="ECO:0000305" FT CONFLICT 2978 FT /note="H -> Y (in Ref. 1; CAA58026)" FT /evidence="ECO:0000305" SQ SEQUENCE 3177 AA; 350864 MW; 969A3BE300D755B0 CRC64; MASSAHLVTI KRSGDDGAHF PLSLSSCLFG RSIECDIRIQ LPVVSKRHCK IEVKEQEAIL YNFSSTNPTQ VNGVTIDEPV RLRHGDIITI IDRSFRYEDG NHEDGSKPTE FPGKSLGKEP SRRASRDSFC ADPDGEGQDT KASKMTASRR SFVYAKGLSA DSPASDGSKN SVSQDSSGHV EQHTGRNIVE PTSGDLFKKS RSTGSSYREP KSSPTQSLSN SNEKESPFEK LYQSMKEELD VKSQKSCRKS EPQPDRAAEE SRETQLLVSG RARAKSSGST PVTAASSPKV GKIWTERWRG GMVPVQTSTE TAKMKTPVRH SQQLKDEDSR VTGRRHSVNL DEGESAQAVH KTVTPGKLAT RNQAAVEAGD VASPADTPEH SSSKKRSIPA KVEAPSAETQ KRLSLTQRLV PGEKKTPKGS FSKPEKLATA AEQTCSGLPG LSSVDISNFG DSINKSEGMP MKRRRVSFGG HLRPELFDEN LPPNTPLKRG ETPTKRKSLG THSPAVLKTI IKERPQSPGK QESPGITPPR TNDQRRRSGR TSSGSKFLCE TDIPKKAGRK SGNLPAKRAS ISRSQHGILQ MICSKRRSGA SEANLIVAKS WADVVKLGVK QTQTKVAKHV PQKQTSKRQR RPSTPKKPTS NLHNQFTTGH ANSPCTIVVG RAQIEKVSVP ARPYKMLNNL MLNRKVDFSE DLSGLTEMFK TPVKEKQQQM SDTGSVLSNS ANLSERQLQV TNSGDIPEPI TTEILGEKVL SSTRNAAKQQ SDRYSASPTL RRRSIKHENT VQTPKNVHNI TDLEKKTPVS ETEPLKTASS VSKLRRSREL RHTLVETMNE KTEAVLAENT TARHLRGTFR EQKVDQQVQD NENAPQRCKE SGELSEGSEK TSARRSSARK QKPTKDLLGS QMVTQTADYA EELLSQGQGT IQNLEESMHM QNTSISEDQG ITEKKVNIIV YATKEKHSPK TPGKKAQPLE GPAGLKEHFE TPNPKDKPIT EDRTRVLCKS PQVTTENITT NTKPQTSTSG KKVDMKEESS ALTKRIHMPG ESRHNPKILK LECEDIKALK QSENEMLTST VNGSKRTLEK SKKKAQPLED LTCFQELFIS PVPTNIIKKI PSKSPHTQPV RTPASTKRLS KTGLSKVDVR QEPSTLGKRT KSPGRAPGTP APVQEENDST AFMETPKQKL DFAGNSSGSK RRSRTSKNRS QPLEDLDGFQ ELFQTPAGAS DSVTVEESAK ISLESSQAEP VKTPASTKRR SKMSLMKVDM KELSILEKQT QSRGRDAGTP APMQEGNGTT AIMETPKQKL DFTGNSTGHK RRPRTPKIRA QPLEDLDGFQ ELFQTPAGAN DSVTVEESAK MSLESSQAEP VKTPASTKRL SKTDLSKVDV REDPSILGKK TKSPGRAPGT PAPVQEENDC TAYMETPKQK LESIENLTGL RKQSRTPKDI TGFQDSFQIP DHANGPLVVV KTKKMFFNSP QPESAITRKS RERQSRASIS KIDVKEELLE SEEHLQLGEG VDTFQVSTNK VIRSSRKPAK RKLDSTAGMP NSKRMRCSSK DNTPCLEDLN GFQELFQMPG YANDSLTTGI STMLARSPQL GPVRTQINKK SLPKIILRKM DVTEEISGLW KQSLGRVHTT QEQEDNAIKA IMEIPKETLQ TAADGTRLTR QPQTPKEKVQ PLEDHSVFQE LFQTSRYCSD PLIGNKQTRM SLRSPQPGFV RTPRTSKRLA KTSVGNIAVR EKISPVSLPQ CATGEVVHIP IGPEDDTENK GVKESTPQTL DSSASRTVSK RQQGAHEERP QFSGDLFHPQ ELFQTPASGK DPVTVDETTK IALQSPQPGH IINPASMKRQ SNMSLRKDMR EFSILEKQTQ SRGRDAGTPA PMQEENGTTA IMETPKQKLD FIGNSTGHKR RPRTPKNRAQ PLEDLDGFQE LFQTPAGASD PVSVEESAKI SLASSQAEPV RTPASTKRRS KTGLSKVDVR QEPSTLGKRM KSLGRAPGTP APVQEENDST AFMETPKQKL DFTGNSSGHK RRPQTPKIRA QPLEDLDGFQ ELFQTPAGAN DSVTVEESVK MSLESSQAEP VKTPASTKRL SKTGLSKVDV REDPSILEKK TKSPGTPAPV QEENDCTAFM ETPKQKLDFT GNSSGHKRRP RTPKIRAQPL EDLDGFQELF QTPAGASDSV TVEESAKMSL ESSQAKPVKT PASTKRLSKT GLSKVDVRED PSTLGKKTKS PGRAPGTPAP VQEENDSTAF METPKQKLDF AENSSGSKRR SRTSKNRSQP LEDLDGFQEL FQTPAGASNP VSVEESAKIS LESSQAEPVR TRASTKRLSK TGLNKMDVRE GHSPLSKSSC ASQKVMQTLT LGEDHGRETK DGKVLLAQKL EPAIYVTRGK RQQRSCKKRS QSPEDLSGVQ EVFQTSGHNK DSVTVDNLAK LPSSSPPLEP TDTSVTSRRQ ARTGLRKVHV KNELSGGIMH PQISGEIVDL PREPEGEGKV IKTRKQSVKR KLDTEVNVPR SKRQRITRAE KTLEDLPGFQ ELCQAPSLVM DSVIVEKTPK MPDKSPEPVD TTSETQARRR LRRLVVTEEP IPQRKTTRVV RQTRNTQKEP ISDNQGMEEF KESSVQKQDP SVSLTGRRNQ PRTVKEKTQP LEELTSFQEE TAKRISSKSP QPEEKETLAG LKRQLRIQLI NDGVKEEPTA QRKQPSRETR NTLKEPVGDS INVEEVKKST KQKIDPVASV PVSKRPRRVP KEKAQALELA GLKGPIQTLG HTDESASDKG PTQMPCNSLQ PEQVDSFQSS PRRPRTRRGK VEADEEPSAV RKTVSTSRQT MRSRKVPEIG NNGTQVSKAS IKQTLDTVAK VTGSRRQLRT HKDGVQPLEV LGDSKEITQI SDHSEKLAHD TSILKSTQQQ KPDSVKPLRT CRRVLRASKE DPKEVLVDTR DHATLQSKSN PLLSPKRKSA RDGSIVRTRA LRSLAPKQEA TDEKPVPEKK RAASSKRHVS PEPVKMKHLK IVSNKLESVE EQVSTVMKTE EMEAKRENPV TPDQNSRYRK KTNVKQPRPK FDASAENVGI KKNEKTMKTA SQETELQNPD DGAKKSTSRG QVSGKRTCLR SRGTTEMPQP CEAEEKTSKP AAEILIKPQE EKGVSGESDV RCLRSRKTRV ALDSEPKPRV TRGTKKDAKT LKEDEDIVCT KKLRTRS //