TAD2B_HUMAN
ID TAD2B_HUMAN Reviewed; 420 AA.
AC Q86TJ2; A0AUJ8; A4QMR7; B3KSN0; B3KU86; Q6MZG9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Transcriptional adapter 2-beta;
DE AltName: Full=ADA2-like protein beta;
DE Short=ADA2-beta;
GN Name=TADA2B; Synonyms=ADA2B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, and Uterus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-282 (ISOFORM 1).
RC TISSUE=PNS;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 91-420.
RC TISSUE=Small intestine;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP FUNCTION, INTERACTION WITH GCN5L2; SMARCA4; SMARCE1 AND PAX5, AND
RP IDENTIFICATION IN THE TFTC-HAT COMPLEX WITH GCN5L2; TAF5; TAF6 AND TAF10.
RX PubMed=12972612; DOI=10.1128/mcb.23.19.6944-6957.2003;
RA Barlev N.A., Emelyanov A.V., Castagnino P., Zegerman P., Bannister A.J.,
RA Sepulveda M.A., Robert F., Tora L., Kouzarides T., Birshtein B.K.,
RA Berger S.L.;
RT "A novel human Ada2 homologue functions with Gcn5 or Brg1 to coactivate
RT transcription.";
RL Mol. Cell. Biol. 23:6944-6957(2003).
RN [7]
RP IDENTIFICATION IN THE TFTC-HAT COMPLEX.
RX PubMed=17694077; DOI=10.1038/sj.onc.1210604;
RA Nagy Z., Tora L.;
RT "Distinct GCN5/PCAF-containing complexes function as co-activators and are
RT involved in transcription factor and global histone acetylation.";
RL Oncogene 26:5341-5357(2007).
RN [8]
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., Buerckstuemmer 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Coactivates PAX5-dependent transcription together with either
CC SMARCA4 or GCN5L2. {ECO:0000269|PubMed:12972612}.
CC -!- SUBUNIT: Interacts with GCN5L2, SMARCA4, SMARCE1 and PAX5. Component of
CC the TFTC-HAT complex. {ECO:0000269|PubMed:12972612,
CC ECO:0000269|PubMed:17694077}.
CC -!- INTERACTION:
CC Q86TJ2; Q9NY61: AATF; NbExp=4; IntAct=EBI-2512219, EBI-372428;
CC Q86TJ2-3; X5D778: ANKRD11; NbExp=3; IntAct=EBI-18173581, EBI-17183751;
CC Q86TJ2-3; Q8IYR0: CFAP206; NbExp=3; IntAct=EBI-18173581, EBI-749051;
CC Q86TJ2-3; P42858: HTT; NbExp=3; IntAct=EBI-18173581, EBI-466029;
CC Q86TJ2-3; O60333-2: KIF1B; NbExp=3; IntAct=EBI-18173581, EBI-10975473;
CC Q86TJ2-3; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-18173581, EBI-348259;
CC Q86TJ2-3; P07196: NEFL; NbExp=3; IntAct=EBI-18173581, EBI-475646;
CC Q86TJ2-3; O76024: WFS1; NbExp=3; IntAct=EBI-18173581, EBI-720609;
CC Q86TJ2-3; Q8N5A5-2: ZGPAT; NbExp=3; IntAct=EBI-18173581, EBI-10183064;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q86TJ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86TJ2-2; Sequence=VSP_030110;
CC Name=3;
CC IsoId=Q86TJ2-3; Sequence=VSP_030109;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH47794.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAI01338.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK093974; BAG52792.1; -; mRNA.
DR EMBL; AK096655; BAG53348.1; -; mRNA.
DR EMBL; AC097382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471131; EAW82372.1; -; Genomic_DNA.
DR EMBL; BC047794; AAH47794.1; ALT_SEQ; mRNA.
DR EMBL; BC101334; AAI01335.1; -; mRNA.
DR EMBL; BC101335; AAI01336.1; -; mRNA.
DR EMBL; BC101336; AAI01337.1; -; mRNA.
DR EMBL; BC101337; AAI01338.1; ALT_INIT; mRNA.
DR EMBL; BX641147; CAE46064.1; -; mRNA.
DR CCDS; CCDS47007.1; -. [Q86TJ2-1]
DR RefSeq; NP_689506.2; NM_152293.2. [Q86TJ2-1]
DR RefSeq; XP_011511897.1; XM_011513595.1. [Q86TJ2-3]
DR AlphaFoldDB; Q86TJ2; -.
DR SMR; Q86TJ2; -.
DR BioGRID; 125041; 72.
DR ComplexPortal; CPX-6802; SAGA complex, KAT2B variant.
DR ComplexPortal; CPX-900; SAGA complex, KAT2A variant.
DR CORUM; Q86TJ2; -.
DR IntAct; Q86TJ2; 41.
DR MINT; Q86TJ2; -.
DR STRING; 9606.ENSP00000308022; -.
DR iPTMnet; Q86TJ2; -.
DR PhosphoSitePlus; Q86TJ2; -.
DR BioMuta; TADA2B; -.
DR DMDM; 166225686; -.
DR EPD; Q86TJ2; -.
DR jPOST; Q86TJ2; -.
DR MassIVE; Q86TJ2; -.
DR MaxQB; Q86TJ2; -.
DR PaxDb; Q86TJ2; -.
DR PeptideAtlas; Q86TJ2; -.
DR PRIDE; Q86TJ2; -.
DR ProteomicsDB; 69705; -. [Q86TJ2-1]
DR ProteomicsDB; 69706; -. [Q86TJ2-2]
DR ProteomicsDB; 69707; -. [Q86TJ2-3]
DR Antibodypedia; 22702; 89 antibodies from 19 providers.
DR DNASU; 93624; -.
DR Ensembl; ENST00000310074.8; ENSP00000308022.6; ENSG00000173011.12. [Q86TJ2-1]
DR Ensembl; ENST00000512388.1; ENSP00000423947.1; ENSG00000173011.12. [Q86TJ2-2]
DR Ensembl; ENST00000515646.1; ENSP00000423181.1; ENSG00000173011.12. [Q86TJ2-3]
DR GeneID; 93624; -.
DR KEGG; hsa:93624; -.
DR MANE-Select; ENST00000310074.8; ENSP00000308022.6; NM_152293.3; NP_689506.2.
DR UCSC; uc003gjw.5; human. [Q86TJ2-1]
DR CTD; 93624; -.
DR DisGeNET; 93624; -.
DR GeneCards; TADA2B; -.
DR HGNC; HGNC:30781; TADA2B.
DR HPA; ENSG00000173011; Low tissue specificity.
DR MIM; 608790; gene.
DR neXtProt; NX_Q86TJ2; -.
DR OpenTargets; ENSG00000173011; -.
DR PharmGKB; PA165664556; -.
DR VEuPathDB; HostDB:ENSG00000173011; -.
DR eggNOG; KOG0457; Eukaryota.
DR GeneTree; ENSGT00940000157318; -.
DR HOGENOM; CLU_018273_4_2_1; -.
DR InParanoid; Q86TJ2; -.
DR OMA; IELCPDC; -.
DR OrthoDB; 812864at2759; -.
DR PhylomeDB; Q86TJ2; -.
DR TreeFam; TF313975; -.
DR PathwayCommons; Q86TJ2; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR SignaLink; Q86TJ2; -.
DR BioGRID-ORCS; 93624; 215 hits in 1127 CRISPR screens.
DR ChiTaRS; TADA2B; human.
DR GenomeRNAi; 93624; -.
DR Pharos; Q86TJ2; Tbio.
DR PRO; PR:Q86TJ2; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q86TJ2; protein.
DR Bgee; ENSG00000173011; Expressed in tibialis anterior and 190 other tissues.
DR ExpressionAtlas; Q86TJ2; baseline and differential.
DR Genevisible; Q86TJ2; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000124; C:SAGA complex; IC:ComplexPortal.
DR GO; GO:0070461; C:SAGA-type complex; IDA:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0043966; P:histone H3 acetylation; IC:ComplexPortal.
DR GO; GO:0035521; P:monoubiquitinated histone deubiquitination; IDA:ComplexPortal.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; IDA:ComplexPortal.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:0043484; P:regulation of RNA splicing; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00167; SANT; 1.
DR CDD; cd02335; ZZ_ADA2; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR041983; ADA2-like_ZZ.
DR InterPro; IPR016827; Ada2/TADA2.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR PIRSF; PIRSF025024; Transcriptional_adaptor_2; 1.
DR SMART; SM00717; SANT; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51293; SANT; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..420
FT /note="Transcriptional adapter 2-beta"
FT /id="PRO_0000313711"
FT DOMAIN 65..118
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT ZN_FING 4..59
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 305..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 12
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 23
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 26
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 45
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT VAR_SEQ 1..92
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_030109"
FT VAR_SEQ 16..90
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030110"
FT CONFLICT 251
FT /note="E -> K (in Ref. 5; CAE46064)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 420 AA; 48470 MW; 89C3365128DF5EBC CRC64;
MAELGKKYCV YCLAEVSPLR FRCTECQDIE LCPECFSAGA EIGHHRRYHG YQLVDGGRFT
LWGPEAEGGW TSREEQLLLD AIEQFGFGNW EDMAAHVGAS RTPQEVMEHY VSMYIHGNLG
KACIPDTIPN RVTDHTCPSG GPLSPSLTTP LPPLDISVAE QQQLGYMPLR DDYEIEYDQD
AETLISGLSV NYDDDDVEIE LKRAHVDMYV RKLKERQRRK NIARDYNLVP AFLGKDKKEK
EKALKRKITK EEKELRLKLR PLYQFMSCKE FDDLFENMHK EKMLRAKIRE LQRYRRNGIT
KMEESAEYEA ARHKREKRKE NKNLAGSKRG KEDGKDSEFA AIENLPGFEL LSDREKVLCS
SLNLSPARYV TVKTIIIKDH LQKRQGIPSK SRLPSYLDKV LKKRILNFLT ESGWISRDAS
