KI67_MOUSE
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 03-AUG-2022, entry version 80.
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/";
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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 iPTMnet; E9PVX6; -.
DR PhosphoSitePlus; E9PVX6; -.
DR EPD; E9PVX6; -.
DR jPOST; E9PVX6; -.
DR MaxQB; E9PVX6; -.
DR PaxDb; E9PVX6; -.
DR PeptideAtlas; E9PVX6; -.
DR PRIDE; E9PVX6; -.
DR ProteomicsDB; 263442; -. [E9PVX6-1]
DR ProteomicsDB; 263443; -. [E9PVX6-2]
DR Antibodypedia; 741; 2260 antibodies from 60 providers.
DR Ensembl; ENSMUST00000033310; ENSMUSP00000033310; ENSMUSG00000031004. [E9PVX6-1]
DR GeneID; 17345; -.
DR KEGG; mmu:17345; -.
DR UCSC; uc009kem.2; mouse. [E9PVX6-1]
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; GNSTGHK; -.
DR OrthoDB; 290017at2759; -.
DR PhylomeDB; E9PVX6; -.
DR TreeFam; TF336000; -.
DR BioGRID-ORCS; 17345; 5 hits in 73 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 229 other tissues.
DR ExpressionAtlas; E9PVX6; baseline and differential.
DR Genevisible; E9PVX6; MM.
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:0008022; F:protein C-terminus binding; ISO:MGI.
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; cd00060; FHA; 1.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR012568; KI67R.
DR InterPro; IPR029334; PP1-bd.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
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; SSF49879; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
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
