ID YTHD2_HUMAN Reviewed; 579 AA. AC Q9Y5A9; A6NKG4; A8K966; B4E1G7; D3DPM8; Q5VSZ9; Q8TDH0; Q9BUJ5; DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 16-JAN-2004, sequence version 2. DT 14-MAY-2014, entry version 115. DE RecName: Full=YTH domain-containing family protein 2; DE AltName: Full=CLL-associated antigen KW-14; DE AltName: Full=High-glucose-regulated protein 8; DE AltName: Full=Renal carcinoma antigen NY-REN-2; GN Name=YTHDF2; Synonyms=HGRG8; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND IDENTIFICATION AS A RENAL RP CANCER ANTIGEN. RC TISSUE=Renal cell carcinoma; RX PubMed=10508479; RX DOI=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5; RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., RA Old L.J.; RT "Antigens recognized by autologous antibody in patients with renal- RT cell carcinoma."; RL Int. J. Cancer 83:456-464(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Roberts T.P., Wright A., Wahab N.A., Weston B.S., Mason R.M.; RT "Gene which is selectively expressed in hyperglycaemia."; RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA Krackhardt A.M., Witzens M., Harig S., Hodi F.S., Zauls A.J., RA Chessia M., Barrett P., Gribben J.G.; RT "Identification of novel tumor antigens in CLL by SEREX: assessment of RT their potential as targets for immunotherapeutic approaches."; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Ovary, and Testis; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Placenta; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP PROTEIN SEQUENCE OF 2-12; 179-205 AND 528-536, CLEAVAGE OF INITIATOR RP METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC TISSUE=Lung carcinoma, and Ovarian carcinoma; RA Bienvenut W.V., Vousden K.H., Lukashchuk N., Lilla S., RA von Kriegsheim A., Lempens A., Kolch W.; RL Submitted (DEC-2008) to UniProtKB. RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer RT cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein RT phosphorylation analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39 AND SER-359, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [15] 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., RA Buerckstuemmer T., 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, AND IDENTIFICATION RP 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., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [17] RP RNA-BINDING, AND FUNCTION. RX PubMed=22575960; DOI=10.1038/nature11112; RA Dominissini D., Moshitch-Moshkovitz S., Schwartz S., Salmon-Divon M., RA Ungar L., Osenberg S., Cesarkas K., Jacob-Hirsch J., Amariglio N., RA Kupiec M., Sorek R., Rechavi G.; RT "Topology of the human and mouse m6A RNA methylomes revealed by m6A- RT seq."; RL Nature 485:201-206(2012). RN [18] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [19] RP RNA-BINDING. RX PubMed=24206186; DOI=10.1042/BJ20130862; RA Kang H.J., Jeong S.J., Kim K.N., Baek I.J., Chang M., Kang C.M., RA Park Y.S., Yun C.W.; RT "A novel protein, Pho92, has a conserved YTH domain and regulates RT phosphate metabolism by decreasing the mRNA stability of PHO4 in RT Saccharomyces cerevisiae."; RL Biochem. J. 457:391-400(2014). RN [20] RP RNA-BINDING, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=24284625; DOI=10.1038/nature12730; RA Wang X., Lu Z., Gomez A., Hon G.C., Yue Y., Han D., Fu Y., RA Parisien M., Dai Q., Jia G., Ren B., Pan T., He C.; RT "N-methyladenosine-dependent regulation of messenger RNA stability."; RL Nature 505:117-120(2014). CC -!- FUNCTION: Specifically recognizes and binds N6-methyladenosine CC (m6A)-containing RNAs. M6A is a modification present at internal CC sites of mRNAs and some non-coding RNAs and plays a role in the CC efficiency of mRNA splicing, processing and stability. Acts as a CC regulator of mRNA stability: binding to m6A-containing mRNAs CC results in the localization of to mRNA decay sites, such as CC processing bodies (P-bodies), leading to mRNA degradation. CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9Y5A9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9Y5A9-2; Sequence=VSP_009297; CC Note=May be due to intron retention. No experimental CC confirmation available; CC -!- SIMILARITY: Contains 1 YTH domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAD42861.1; Type=Frameshift; Positions=565; CC Sequence=AAF08813.1; Type=Frameshift; Positions=565; CC Sequence=AAL99921.1; Type=Miscellaneous discrepancy; 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; AF155095; AAD42861.1; ALT_FRAME; mRNA. DR EMBL; AF192968; AAF08813.1; ALT_FRAME; mRNA. DR EMBL; AF432214; AAL99921.1; ALT_SEQ; mRNA. DR EMBL; AK292581; BAF85270.1; -; mRNA. DR EMBL; AK303833; BAG64779.1; -; mRNA. DR EMBL; AL645729; CAH72429.1; -; Genomic_DNA. DR EMBL; AL356786; CAH72429.1; JOINED; Genomic_DNA. DR EMBL; AL356786; CAI21658.1; -; Genomic_DNA. DR EMBL; AL645729; CAI21658.1; JOINED; Genomic_DNA. DR EMBL; CH471059; EAX07673.1; -; Genomic_DNA. DR EMBL; CH471059; EAX07675.1; -; Genomic_DNA. DR EMBL; CH471059; EAX07674.1; -; Genomic_DNA. DR EMBL; BC002559; AAH02559.1; -; mRNA. DR RefSeq; NP_001166299.1; NM_001172828.1. [Q9Y5A9-2] DR RefSeq; NP_001166599.1; NM_001173128.1. [Q9Y5A9-1] DR RefSeq; NP_057342.2; NM_016258.2. [Q9Y5A9-1] DR UniGene; Hs.532286; -. DR ProteinModelPortal; Q9Y5A9; -. DR SMR; Q9Y5A9; 411-543. DR BioGrid; 119543; 20. DR IntAct; Q9Y5A9; 7. DR STRING; 9606.ENSP00000362918; -. DR PhosphoSite; Q9Y5A9; -. DR DMDM; 41019527; -. DR MaxQB; Q9Y5A9; -. DR PaxDb; Q9Y5A9; -. DR PRIDE; Q9Y5A9; -. DR DNASU; 51441; -. DR Ensembl; ENST00000373812; ENSP00000362918; ENSG00000198492. [Q9Y5A9-1] DR Ensembl; ENST00000541996; ENSP00000439394; ENSG00000198492. [Q9Y5A9-2] DR Ensembl; ENST00000542507; ENSP00000444660; ENSG00000198492. [Q9Y5A9-1] DR GeneID; 51441; -. DR KEGG; hsa:51441; -. DR UCSC; uc001brc.3; human. [Q9Y5A9-1] DR CTD; 51441; -. DR GeneCards; GC01P029063; -. DR HGNC; HGNC:31675; YTHDF2. DR HPA; HPA059621; -. DR MIM; 610640; gene. DR neXtProt; NX_Q9Y5A9; -. DR PharmGKB; PA134964518; -. DR eggNOG; NOG276347; -. DR HOVERGEN; HBG060315; -. DR InParanoid; Q9Y5A9; -. DR OMA; KDFDWNP; -. DR OrthoDB; EOG71VSSM; -. DR PhylomeDB; Q9Y5A9; -. DR TreeFam; TF323736; -. DR GenomeRNAi; 51441; -. DR NextBio; 55027; -. DR PMAP-CutDB; Q9Y5A9; -. DR PRO; PR:Q9Y5A9; -. DR Bgee; Q9Y5A9; -. DR CleanEx; HS_YTHDF2; -. DR Genevestigator; Q9Y5A9; -. DR GO; GO:0000932; C:cytoplasmic mRNA processing body; IDA:UniProtKB. DR GO; GO:1990247; F:N6-methyladenosine-containing RNA binding; IDA:UniProtKB. DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB. DR GO; GO:0006959; P:humoral immune response; TAS:ProtInc. DR GO; GO:0043488; P:regulation of mRNA stability; IMP:UniProtKB. DR InterPro; IPR007275; YTH_domain. DR Pfam; PF04146; YTH; 1. DR PROSITE; PS50882; YTH; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm; KW Direct protein sequencing; Phosphoprotein; Polymorphism; KW Reference proteome; RNA-binding. FT INIT_MET 1 1 Removed. FT CHAIN 2 579 YTH domain-containing family protein 2. FT /FTId=PRO_0000223075. FT DOMAIN 410 544 YTH. FT REGION 2 384 Localization to mRNA processing bodies FT (P-bodies). FT REGION 385 579 Interaction with m6A-containing mRNAs. FT MOD_RES 2 2 N-acetylserine. FT MOD_RES 39 39 Phosphoserine. FT MOD_RES 359 359 Phosphoserine. FT MOD_RES 394 394 Phosphoserine. FT VAR_SEQ 1 50 Missing (in isoform 2). FT /FTId=VSP_009297. FT VARIANT 217 217 T -> S (in dbSNP:rs16838382). FT /FTId=VAR_053744. FT VARIANT 454 454 P -> S (in dbSNP:rs35288745). FT /FTId=VAR_053745. SQ SEQUENCE 579 AA; 62334 MW; BF3959B5561A464E CRC64; MSASSLLEQR PKGQGNKVQN GSVHQKDGLN DDDFEPYLSP QARPNNAYTA MSDSYLPSYY SPSIGFSYSL GEAAWSTGGD TAMPYLTSYG QLSNGEPHFL PDAMFGQPGA LGSTPFLGQH GFNFFPSGID FSAWGNNSSQ GQSTQSSGYS SNYAYAPSSL GGAMIDGQSA FANETLNKAP GMNTIDQGMA ALKLGSTEVA SNVPKVVGSA VGSGSITSNI VASNSLPPAT IAPPKPASWA DIASKPAKQQ PKLKTKNGIA GSSLPPPPIK HNMDIGTWDN KGPVAKAPSQ ALVQNIGQPT QGSPQPVGQQ ANNSPPVAQA SVGQQTQPLP PPPPQPAQLS VQQQAAQPTR WVAPRNRGSG FGHNGVDGNG VGQSQAGSGS TPSEPHPVLE KLRSINNYNP KDFDWNLKHG RVFIIKSYSE DDIHRSIKYN IWCSTEHGNK RLDAAYRSMN GKGPVYLLFS VNGSGHFCGV AEMKSAVDYN TCAGVWSQDK WKGRFDVRWI FVKDVPNSQL RHIRLENNEN KPVTNSRDTQ EVPLEKAKQV LKIIASYKHT TSIFDDFSHY EKRQEEEESV KKERQGRGK //