ID   TAF9B_HUMAN             Reviewed;         251 AA.
AC   Q9HBM6; B2RUZ9; Q9Y2S3;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 189.
DE   RecName: Full=Transcription initiation factor TFIID subunit 9B;
DE   AltName: Full=Neuronal cell death-related protein 7;
DE            Short=DN-7;
DE   AltName: Full=Transcription initiation factor TFIID subunit 9-like;
DE   AltName: Full=Transcription-associated factor TAFII31L;
GN   Name=TAF9B; Synonyms=TAF9L;
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] {ECO:0000312|EMBL:AAD27786.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary {ECO:0000312|EMBL:AAD27786.1};
RA   Peng Y., Song H., Zhou J., Huang Q., Dai M., Mao Y., Yu Y., Xu X., Luo B.,
RA   Chen J., Hu R.;
RT   "Human neuronal cell death related gene in neuron-7 (DN-7).";
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000312|EMBL:AAD27786.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Villard L.;
RT   "Characterization of a new TAFII31 gene located in Xq13.3.";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000305, ECO:0000312|EMBL:AL049589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [4] {ECO:0000312|EMBL:AAD27786.1}
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   [5] {ECO:0000312|EMBL:AAH09566.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain {ECO:0000312|EMBL:AAH10350.1}, and Urinary bladder
RC   {ECO:0000312|EMBL:AAH09566.1};
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   [6] {ECO:0000305}
RP   FUNCTION, IDENTIFICATION IN THE TFTC-HAT COMPLEX, AND INTERACTION WITH TAF5
RP   AND TAF6.
RX   PubMed=15899866; DOI=10.1128/mcb.25.11.4638-4649.2005;
RA   Frontini M., Soutoglou E., Argentini M., Bole-Feysot C., Jost B.,
RA   Scheer E., Tora L.;
RT   "TAF9b (formerly TAF9L) is a bona fide TAF that has unique and overlapping
RT   roles with TAF9.";
RL   Mol. Cell. Biol. 25:4638-4649(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-159, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-174 AND SER-177, 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., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [9]
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   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   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., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147 AND THR-174, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
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).
CC   -!- FUNCTION: Essential for cell viability. TAF9 and TAF9B are involved in
CC       transcriptional activation as well as repression of distinct but
CC       overlapping sets of genes. May have a role in gene regulation
CC       associated with apoptosis. TAFs are components of the transcription
CC       factor IID (TFIID) complex, the TBP-free TAFII complex (TFTC), the PCAF
CC       histone acetylase complex and the STAGA transcription coactivator-HAT
CC       complex. TFIID or TFTC are essential for the regulation of RNA
CC       polymerase II-mediated transcription. {ECO:0000269|PubMed:15899866}.
CC   -!- SUBUNIT: Binds TAF5 and TAF6. Component of TFIID and the TATA-binding
CC       protein-free TAF complex (TFTC). TFIID is composed of TATA binding
CC       protein (TBP) and a number of TBP-associated factors (TAFs). Binds N-
CC       terminal domain of p53/TP53 which is essential for transcription.
CC       {ECO:0000269|PubMed:15899866}.
CC   -!- INTERACTION:
CC       Q9HBM6; Q14919: DRAP1; NbExp=7; IntAct=EBI-751601, EBI-712941;
CC       Q9HBM6; Q9Y6J9: TAF6L; NbExp=10; IntAct=EBI-751601, EBI-743984;
CC       Q9HBM6; P04637: TP53; NbExp=2; IntAct=EBI-751601, EBI-366083;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TAF9 family. {ECO:0000255}.
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DR   EMBL; AF077053; AAD27786.1; -; mRNA.
DR   EMBL; AF220509; AAG09711.1; -; mRNA.
DR   EMBL; AL049589; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471104; EAW98601.1; -; Genomic_DNA.
DR   EMBL; BC009566; AAH09566.1; -; mRNA.
DR   EMBL; BC010350; AAH10350.1; -; mRNA.
DR   EMBL; BC071649; AAH71649.1; -; mRNA.
DR   EMBL; BC146952; AAI46953.1; -; mRNA.
DR   EMBL; BC146960; AAI46961.1; -; mRNA.
DR   CCDS; CCDS35340.1; -.
DR   RefSeq; NP_057059.2; NM_015975.4.
DR   PDB; 7KTR; EM; 2.93 A; E=1-251.
DR   PDB; 7KTS; EM; 19.09 A; E=1-251.
DR   PDBsum; 7KTR; -.
DR   PDBsum; 7KTS; -.
DR   AlphaFoldDB; Q9HBM6; -.
DR   EMDB; EMD-23027; -.
DR   EMDB; EMD-23028; -.
DR   SMR; Q9HBM6; -.
DR   BioGRID; 119639; 114.
DR   CORUM; Q9HBM6; -.
DR   IntAct; Q9HBM6; 33.
DR   MINT; Q9HBM6; -.
DR   STRING; 9606.ENSP00000339917; -.
DR   GlyCosmos; Q9HBM6; 7 sites, 2 glycans.
DR   GlyGen; Q9HBM6; 10 sites, 2 O-linked glycans (10 sites).
DR   iPTMnet; Q9HBM6; -.
DR   PhosphoSitePlus; Q9HBM6; -.
DR   BioMuta; TAF9B; -.
DR   DMDM; 74752778; -.
DR   EPD; Q9HBM6; -.
DR   jPOST; Q9HBM6; -.
DR   MassIVE; Q9HBM6; -.
DR   MaxQB; Q9HBM6; -.
DR   PaxDb; 9606-ENSP00000339917; -.
DR   PeptideAtlas; Q9HBM6; -.
DR   ProteomicsDB; 81578; -.
DR   Pumba; Q9HBM6; -.
DR   Antibodypedia; 28250; 150 antibodies from 24 providers.
DR   DNASU; 51616; -.
DR   Ensembl; ENST00000341864.6; ENSP00000339917.5; ENSG00000187325.5.
DR   GeneID; 51616; -.
DR   KEGG; hsa:51616; -.
DR   MANE-Select; ENST00000341864.6; ENSP00000339917.5; NM_015975.5; NP_057059.2.
DR   UCSC; uc004eda.4; human.
DR   AGR; HGNC:17306; -.
DR   CTD; 51616; -.
DR   GeneCards; TAF9B; -.
DR   HGNC; HGNC:17306; TAF9B.
DR   HPA; ENSG00000187325; Low tissue specificity.
DR   MIM; 300754; gene.
DR   neXtProt; NX_Q9HBM6; -.
DR   OpenTargets; ENSG00000187325; -.
DR   PharmGKB; PA38225; -.
DR   VEuPathDB; HostDB:ENSG00000187325; -.
DR   eggNOG; KOG3334; Eukaryota.
DR   GeneTree; ENSGT00940000161697; -.
DR   HOGENOM; CLU_068315_2_0_1; -.
DR   InParanoid; Q9HBM6; -.
DR   OMA; DDNDTMI; -.
DR   OrthoDB; 10695at2759; -.
DR   PhylomeDB; Q9HBM6; -.
DR   TreeFam; TF351417; -.
DR   PathwayCommons; Q9HBM6; -.
DR   Reactome; R-HSA-167161; HIV Transcription Initiation.
DR   Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape.
DR   Reactome; R-HSA-167172; Transcription of the HIV genome.
DR   Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR   Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR   Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR   Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape.
DR   Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR   Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation.
DR   Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR   SignaLink; Q9HBM6; -.
DR   BioGRID-ORCS; 51616; 29 hits in 780 CRISPR screens.
DR   ChiTaRS; TAF9B; human.
DR   GeneWiki; TAF9B; -.
DR   GenomeRNAi; 51616; -.
DR   Pharos; Q9HBM6; Tbio.
DR   PRO; PR:Q9HBM6; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q9HBM6; Protein.
DR   Bgee; ENSG00000187325; Expressed in primordial germ cell in gonad and 191 other cell types or tissues.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB.
DR   GO; GO:0033276; C:transcription factor TFTC complex; IDA:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IC:ARUK-UCL.
DR   GO; GO:0003714; F:transcription corepressor activity; IC:BHF-UCL.
DR   GO; GO:0006352; P:DNA-templated transcription initiation; IEA:InterPro.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:BHF-UCL.
DR   GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IC:BHF-UCL.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR   GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; IDA:BHF-UCL.
DR   CDD; cd07979; TAF9; 1.
DR   Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR003162; TFIID-31.
DR   PANTHER; PTHR48068; TAF9 RNA POLYMERASE II, TATA BOX-BINDING PROTEIN (TBP)-ASSOCIATED FACTOR; 1.
DR   PANTHER; PTHR48068:SF5; TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 9B; 1.
DR   Pfam; PF02291; TFIID-31kDa; 1.
DR   SUPFAM; SSF47113; Histone-fold; 1.
DR   Genevisible; Q9HBM6; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..251
FT                   /note="Transcription initiation factor TFIID subunit 9B"
FT                   /id="PRO_0000118891"
FT   REGION          229..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..251
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         147
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         159
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         174
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         177
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   CONFLICT        3
FT                   /note="S -> L (in Ref. 1; AAD27786)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        209
FT                   /note="I -> D (in Ref. 1; AAD27786)"
FT                   /evidence="ECO:0000305"
FT   HELIX           14..26
FT                   /evidence="ECO:0007829|PDB:7KTR"
FT   HELIX           35..60
FT                   /evidence="ECO:0007829|PDB:7KTR"
FT   HELIX           68..79
FT                   /evidence="ECO:0007829|PDB:7KTR"
FT   HELIX           89..100
FT                   /evidence="ECO:0007829|PDB:7KTR"
FT   HELIX           118..120
FT                   /evidence="ECO:0007829|PDB:7KTR"
FT   STRAND          127..131
FT                   /evidence="ECO:0007829|PDB:7KTR"
SQ   SEQUENCE   251 AA;  27622 MW;  EB3A1116F7E8BCA0 CRC64;
     MESGKMAPPK NAPRDALVMA QILKDMGITE YEPRVINQML EFAFRYVTTI LDDAKIYSSH
     AKKPNVDADD VRLAIQCRAD QSFTSPPPRD FLLDIARQKN QTPLPLIKPY AGPRLPPDRY
     CLTAPNYRLK SLIKKGPNQG RLVPRLSVGA VSSKPTTPTI ATPQTVSVPN KVATPMSVTS
     QRFTVQIPPS QSTPVKPVPA TTAVQNVLIN PSMIGPKNIL ITTNMVSSQN TANEANPLKR
     KHEDDDDNDI M
//