ID A0A2R8Y7Q1_HUMAN Unreviewed; 3002 AA.
AC A0A2R8Y7Q1;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 2.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Bromodomain PHD finger transcription factor {ECO:0000313|Ensembl:ENSP00000496182.2};
DE Flags: Fragment;
GN Name=BPTF {ECO:0000313|Ensembl:ENSP00000496182.2};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000496182.2, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0007829|PubMed:17081983}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [2] {ECO:0000313|Ensembl:ENSP00000496182.2, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3] {ECO:0007829|PubMed:17525332}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R., Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [4] {ECO:0007829|PubMed:18669648}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [5] {ECO:0007829|PubMed:19413330}
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., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6] {ECO:0007829|PubMed:19690332}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [7] {ECO:0007829|PubMed:19608861}
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., Walther T.C.,
RA 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 [8] {ECO:0007829|PubMed:20068231}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9] {ECO:0007829|PubMed:21269460}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10] {ECO:0007829|PubMed:21406692}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11] {ECO:0007829|PubMed:23186163}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=23186163;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12] {ECO:0007829|PubMed:24129315}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=24129315;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [13] {ECO:0007829|PubMed:25218447}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447;
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 [14] {ECO:0007829|PubMed:25772364}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [15] {ECO:0007829|PubMed:25755297}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.O114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurethsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [16] {ECO:0007829|PubMed:28112733}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [17] {ECO:0000313|Ensembl:ENSP00000496182.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AC006534; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107377; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC134407; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KC877674; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR MassIVE; A0A2R8Y7Q1; -.
DR PeptideAtlas; A0A2R8Y7Q1; -.
DR Antibodypedia; 19216; 130 antibodies from 27 providers.
DR Ensembl; ENST00000644067.1; ENSP00000496182.2; ENSG00000171634.19.
DR HGNC; HGNC:3581; BPTF.
DR VEuPathDB; HostDB:ENSG00000171634; -.
DR GeneTree; ENSGT00940000154830; -.
DR ChiTaRS; BPTF; human.
DR Proteomes; UP000005640; Chromosome 17.
DR Bgee; ENSG00000171634; Expressed in sural nerve and 204 other cell types or tissues.
DR ExpressionAtlas; A0A2R8Y7Q1; baseline and differential.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0016589; C:NURF complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd05509; Bromo_gcn5_like; 1.
DR CDD; cd15559; PHD1_BPTF; 1.
DR CDD; cd15560; PHD2_3_BPTF; 2.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR InterPro; IPR038028; BPTF.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR018501; DDT_dom.
DR InterPro; IPR028941; WHIM2_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45975; NUCLEOSOME-REMODELING FACTOR SUBUNIT BPTF; 1.
DR PANTHER; PTHR45975:SF2; NUCLEOSOME-REMODELING FACTOR SUBUNIT BPTF; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF02791; DDT; 1.
DR Pfam; PF00628; PHD; 3.
DR Pfam; PF15613; WSD; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00571; DDT; 1.
DR SMART; SM00249; PHD; 3.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 3.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50827; DDT; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 3.
PE 1: Evidence at protein level;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Proteomics identification {ECO:0007829|EPD:A0A2R8Y7Q1,
KW ECO:0007829|MaxQB:A0A2R8Y7Q1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 138..198
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 288..335
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 2765..2816
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 2823..2874
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 2900..2970
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1113..1236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1269..1346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1363..1434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1506..1599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1873..1901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2131..2168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2250..2447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2693..2756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1921..1948
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2518..2548
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 27..85
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..524
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..639
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..1004
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1051
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1115..1136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1142..1181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1207..1222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1269..1291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1305..1341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1383..1424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1506..1558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1565..1598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2250..2304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2311..2447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2694..2719
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2732..2756
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|Ensembl:ENSP00000496182.2"
SQ SEQUENCE 3002 AA; 334805 MW; B3E7136DFFDCA44A CRC64;
XGGGGGGHLA RTTAARRAVN KVVYDDHESE EEEEEEDMVS EEEEEEDGDA EETQDSEDDE
EDEMEEDDDD SDYPEEMEDD DDDASYCTES SFRSHSTYSS TPGRRKPRVH RPRSPILEEK
DIPPLEFPKS SEDLMVPNEH IMNVIAIYEV LRNFGTVLRL SPFRFEDFCA ALVSQEQCTL
MAEMHVVLLK AVLREEDTSN TTFGPADLKD SVNSTLYFID GMTWPEVLRV YCESDKEYHH
VLPYQEAEDY PYGPVENKIK VLQFLVDQFL TTNIAREELM SEGVIQYDDH CRVCHKLGDL
LCCETCSAVY HLECVKPPLE EVPEDEWQCE VCVAHKVPGV TDCVAEIQKN KPYIRHEPIG
YDRSRRKYWF LNRRLIIEED TENENEKKIW YYSTKVQLAE LIDCLDKDYW EAELCKILEE
MREEIHRHMD ITEDLTNKAR GSNKSFLAAA NEEILESIRA KKGDIDNVKS PEETEKDKNE
TENDSKDAEK NREEFEDQSL EKDSDDKTPD DDPEQGKSEE PTEVGDKGNS VSANLGDNTT
NATSEETSPS EGRSPVGCLS ETPDSSNMAE KKVASELPQD VPEEPNKTCE SSNTSATTTS
IQPNLENSNS SSELNSSQSE SAKAADDPEN GERESHTPVS IQEEIVGDFK SEKSNGELSE
SPGAGKGASG STRIITRLRN PDSKLSQLKS QQVAAAAHEA NKLFKEGKEV LVVNSQGEIS
RLSTKKEVIM KGNINNYFKL GQEGKYRVYH NQYSTNSFAL NKHQHREDHD KRRHLAHKFC
LTPAGEFKWN GSVHGSKVLT ISTLRLTITQ LENNIPSSFL HPNWASHRAN WIKAVQMCSK
PREFALALAI LECAVKPVVM LPIWRESLGH TRLHRMTSIE REEKEKVKKK EKKQEEEETM
QQATWVKYTF PVKHQVWKQK GEEYRVTGYG GWSWISKTHV YRFVPKLPGN TNVNYRKSLE
GTKNNMDENM DESDKRKCSR SPKKIKIEPD SEKDEVKGSD AAKGADQNEM DISKITEKKD
QDVKELLDSD SDKPCKEEPM EVDDDMKTES HVNCQESSQV DVVNVSEGFH LRTSYKKKTK
SSKLDGLLER RIKQFTLEEK QRLEKIKLEG GIKGIGKTST NSSKNLSESP VITKAKEGCQ
SDSMRQEQSP NANNDQPEDL IQGCSESDSS VLRMSDPSHT TNKLYPKDRV LDDVSIRSPE
TKCPKQNSIE NDIEEKVSDL ASRGQEPSKS KTKGNDFFID DSKLASADDI GTLICKNKKP
LIQEESDTIV SSSKSALHSS VPKSTNDRDA TPLSRAMDFE GKLGCDSESN STLENSSDTV
SIQDSSEEDM IVQNSNESIS EQFRTREQDV EVLEPLKCEL VSGESTGNCE DRLPVKGTEA
NGKKPSQQKK LEERPVNKCS DQIKLKNTTD KKNNENRESE KKGQRTSTFQ INGKDNKPKI
YLKGECLKEI SESRVVSGNV EPKVNNINKI IPENDIKSLT VKESAIRPFI NGDVIMEDFN
ERNSSETKSH LLSSSDAEGN YRDSLETLPS TKESDSTQTT TPSASCPESN SVNQVEDMEI
ETSEVKKVTS SPITSEEESN LSNDFIDENG LPINKNENVN GESKRKTVIT EVTTMTSTVA
TESKTVIKVE KGDKQTVVSS TENCAKSTVT TTTTTVTKLS TPSTGGSVDI ISVKEQSKTV
VTTTVTDSLT TTGGTLVTSM TVSKEYSTRD KVKLMKFSRP KKTRSGTALP SYRKFVTKSS
KKSIFVLPND DLKKLARKGG IREVPYFNYN AKPALDIWPY PSPRPTFGIT WRYRLQTVKS
LAGVSLMLRL LWASLRWDDM AAKAPPGGGT TRTETSETEI TTTEIIKRRD VGPYGIRSEY
CIRKIICPIG VPETPKETPT PQRKGLRSSA LRPKRPETPK QTGPVIIETW VAEEELELWE
IRAFAERVEK EKAQAVEQQA KKRLEQQKPT VIATSTTSPT SSTTSTISPA QKVMVAPISG
SVTTGTKMVL TTKVGSPATV TFQQNKNFHQ TFATWVKQGQ SNSGVVQVQQ KVLGIIPSST
GTSQQTFTSF QPRTATVTIR PNTSGSGGTT SNSQVITGPQ IRPGMTVIRT PLQQSTLGKA
IIRTPVMVQP GAPQQVMTQI IRGQPVSTAV SAPNTVSSTP GQKSLTSATS TSNIQSSASQ
PPRPQQGQVK LTMAQLTQLT QGHGGNQGLT VVIQGQGQTT GQLQLIPQGV TVLPGPGQQL
MQAAMPNGTV QRFLFTPLAT TATTASTTTT TVSTTAAGTG EQRQSKLSPQ MQVHQDKTLP
PAQSSSVGPA EAQPQTAQPS AQPQPQTQPQ SPAQPEVQTQ PEVQTQTTVS SHVPSEAQPT
HAQSSKPQVA AQSQPQSNVQ GQSPVRVQSP SQTRIRPSTP SQLSPGQQSQ VQTTTSQPIP
IQPHTSLQIP SQGQPQSQPQ VQSSTQTLSS GQTLNQVTVS SPSRPQLQIQ QPQPQVIAVP
QLQQQVQVLS QIQSQVVAQI QAQQSGVPQQ IKLQLPIQIQ QSSAVQTHQI QNVVTVQAAS
VQEQLQRVQQ LRDQQQKKKQ QQIEIKREHT LQASNQSEII QKQVVMKHNA VIEHLKQKKS
MTPAEREENQ RMIVCNQVMK YILDKIDKEE KQAAKKRKRE ESVEQKRSKQ NATKLSALLF
KHKEQLRAEI LKKRALLDKD LQIEVQEELK RDLKIKKEKD LMQLAQATAV AAPCPPVTPA
PPAPPAPPPS PPPPPAVQHT GLLSTPTLPA ASQKRKREEE KDSSSKSKKK KMISTTSKET
KKDTKLYCIC KTPYDESKFY IGCDLCTNWY HGECVGITEK EAKKMDVYIC NDCKRAQEGS
SEELYCICRT PYDESQFYIG CDRCQNWYHG RCVGILQSEA ELIDEYVCPQ CQSTEDAMTV
LTPLTEKDYE GLKRVLRSLQ AHKMAWPFLE PVDPNDAPDY YGVIKEPMDL ATMEERVQRR
YYEKLTEFVA DMTKIFDNCR YYNPSDSPFY QCAEVLESFF VQKLKGFKAS RSHNNKLQST
AS
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