MYO9B_HUMAN
ID MYO9B_HUMAN Reviewed; 2157 AA.
AC Q13459; O75314; Q9NUJ2; Q9UHN0;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 3.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Unconventional myosin-IXb;
DE AltName: Full=Unconventional myosin-9b;
GN Name=MYO9B; Synonyms=MYR5;
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 [MRNA] (ISOFORM LONG/SHORT), SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Liver, and Small intestine;
RX PubMed=8907710; DOI=10.1242/jcs.109.3.653;
RA Wirth J.A., Jensen K.A., Post P.L., Bement W.M., Mooseker M.S.;
RT "Human myosin-IXb, an unconventional myosin with a chimerin-like rho/rac
RT GTPase-activating protein domain in its tail.";
RL J. Cell Sci. 109:653-661(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RX PubMed=10580159; DOI=10.1016/s0378-1119(99)00459-x;
RA Grewal P.K., Jones A.-M., Maconochie M., Lemmers R.J.F., Frants R.R.,
RA Hewitt J.E.;
RT "Cloning of the murine unconventional myosin gene Myo9b and identification
RT of alternative splicing.";
RL Gene 240:389-398(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1940-2157 (ISOFORM LONG), FUNCTION,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9490638; DOI=10.1242/jcs.111.7.941;
RA Post P.L., Bokoch G.M., Mooseker M.S.;
RT "Human myosin-IXb is a mechanochemically active motor and a GAP for rho.";
RL J. Cell Sci. 111:941-950(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1828-2022 (ISOFORM SHORT).
RC TISSUE=Placenta;
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 [6]
RP ASSOCIATION WITH CELIAC DISEASE 4.
RX PubMed=16282976; DOI=10.1038/ng1680;
RA Monsuur A.J., de Bakker P.I., Alizadeh B.Z., Zhernakova A., Bevova M.R.,
RA Strengman E., Franke L., van't Slot R., van Belzen M.J., Lavrijsen I.C.,
RA Diosdado B., Daly M.J., Mulder C.J., Mearin M.L., Meijer J.W., Meijer G.A.,
RA van Oort E., Wapenaar M.C., Koeleman B.P., Wijmenga C.;
RT "Myosin IXB variant increases the risk of celiac disease and points toward
RT a primary intestinal barrier defect.";
RL Nat. Genet. 37:1341-1344(2005).
RN [7]
RP IDENTIFICATION 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 phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1290, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1267; THR-1271 AND SER-1290,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1290 AND SER-1405, AND
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 the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-716; SER-1290; SER-1354 AND
RP SER-1992, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1290 AND SER-1992, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1267; THR-1271 AND SER-1992,
RP AND IDENTIFICATION BY 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1290; SER-1323 AND THR-1346,
RP AND 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 [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1267; THR-1271; SER-1290;
RP SER-1354 AND SER-1992, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-717; SER-1114; SER-1115;
RP SER-1122; SER-1242; SER-1261; SER-1267; THR-1271; SER-1290; SER-1331;
RP THR-1346; SER-1354; SER-1405; SER-1926; SER-1972; SER-1992 AND SER-2050,
RP AND 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).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1261; SER-1267; THR-1271;
RP SER-1290; THR-1346 AND SER-1356, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
RN [21] {ECO:0007744|PDB:5C5S}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1691-1916, FUNCTION, INTERACTION
RP WITH ROBO1 AND RHOA, AND MUTAGENESIS OF ALA-1739; ASN-1741 AND ARG-1742.
RX PubMed=26529257; DOI=10.1172/jci81673;
RA Kong R., Yi F., Wen P., Liu J., Chen X., Ren J., Li X., Shang Y., Nie Y.,
RA Wu K., Fan D., Zhu L., Feng W., Wu J.Y.;
RT "Myo9b is a key player in SLIT/ROBO-mediated lung tumor suppression.";
RL J. Clin. Invest. 125:4407-4420(2015).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity.
CC Unconventional myosins serve in intracellular movements. Binds actin
CC with high affinity both in the absence and presence of ATP and its
CC mechanochemical activity is inhibited by calcium ions (PubMed:9490638).
CC Also acts as a GTPase activator for RHOA (PubMed:9490638,
CC PubMed:26529257). Plays a role in the regulation of cell migration via
CC its role as RHOA GTPase activator. This is regulated by its interaction
CC with the SLIT2 receptor ROBO1; interaction with ROBO1 impairs
CC interaction with RHOA and subsequent activation of RHOA GTPase
CC activity, and thereby leads to increased levels of active, GTP-bound
CC RHOA (PubMed:26529257). {ECO:0000269|PubMed:26529257,
CC ECO:0000269|PubMed:9490638}.
CC -!- SUBUNIT: Interacts (via IQ domains) with CALM (PubMed:9490638).
CC Interacts with RHOA (PubMed:26529257). Interacts (via Rho-GAP domain)
CC with ROBO1; this inhibits the interaction with RHOA and the stimulation
CC of RHOA GTPase activity, and thereby increases the levels of active
CC RHOA (PubMed:26529257). {ECO:0000269|PubMed:9490638}.
CC -!- INTERACTION:
CC Q13459-2; Q9Y6D6: ARFGEF1; NbExp=2; IntAct=EBI-6251250, EBI-1044254;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:8907710}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:8907710}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:8907710, ECO:0000269|PubMed:9490638}. Note=In
CC undifferentiated cells colocalizes with F-actin in the cell periphery
CC while in differentiated cells its localization is cytoplasmic with the
CC highest levels in the perinuclear region. {ECO:0000269|PubMed:8907710}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=Q13459-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q13459-2; Sequence=VSP_003361, VSP_003362;
CC -!- TISSUE SPECIFICITY: Detected in peripheral blood leukocytes (at protein
CC level) (PubMed:9490638). Expressed predominantly in peripheral blood
CC leukocytes and at lower levels, in thymus, spleen, testis, prostate,
CC ovary, brain, small intestine and lung. {ECO:0000269|PubMed:8907710,
CC ECO:0000269|PubMed:9490638}.
CC -!- DISEASE: Celiac disease 4 (CELIAC4) [MIM:609753]: A multifactorial,
CC chronic disorder of the small intestine caused by intolerance to
CC gluten. It is characterized by immune-mediated enteropathy associated
CC with failed intestinal absorption, and malnutrition. In predisposed
CC individuals, the ingestion of gluten-containing food such as wheat and
CC rye induces a flat jejunal mucosa with infiltration of lymphocytes.
CC Note=Disease susceptibility is associated with variants affecting the
CC gene represented in this entry.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: Represents an unconventional myosin. This protein should not
CC be confused with the conventional myosin-9 (MYH9). {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50402.1; Type=Miscellaneous discrepancy; Note=The C-terminal sequence from position 1917 onwards appears to be not correctly spliced.; Evidence={ECO:0000305};
CC Sequence=BAA92132.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=MYO9B entry;
CC URL="https://en.wikipedia.org/wiki/MYO9B";
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DR EMBL; U42391; AAC50402.1; ALT_SEQ; mRNA.
DR EMBL; AC020913; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC020908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF143684; AAF00119.1; -; mRNA.
DR EMBL; AF020267; AAC26597.1; -; mRNA.
DR EMBL; AK002201; BAA92132.1; ALT_INIT; mRNA.
DR CCDS; CCDS46010.1; -. [Q13459-2]
DR RefSeq; NP_004136.2; NM_004145.3. [Q13459-1]
DR PDB; 5C5S; X-ray; 2.20 A; A/B/C/D=1691-1916.
DR PDB; 5HPY; X-ray; 2.40 A; A/D=1691-1916.
DR PDBsum; 5C5S; -.
DR PDBsum; 5HPY; -.
DR AlphaFoldDB; Q13459; -.
DR SMR; Q13459; -.
DR BioGRID; 110734; 116.
DR ELM; Q13459; -.
DR IntAct; Q13459; 34.
DR MINT; Q13459; -.
DR STRING; 9606.ENSP00000471457; -.
DR iPTMnet; Q13459; -.
DR MetOSite; Q13459; -.
DR PhosphoSitePlus; Q13459; -.
DR BioMuta; MYO9B; -.
DR DMDM; 325511388; -.
DR CPTAC; CPTAC-981; -.
DR CPTAC; CPTAC-982; -.
DR EPD; Q13459; -.
DR jPOST; Q13459; -.
DR MassIVE; Q13459; -.
DR MaxQB; Q13459; -.
DR PaxDb; Q13459; -.
DR PeptideAtlas; Q13459; -.
DR PRIDE; Q13459; -.
DR ProteomicsDB; 59458; -. [Q13459-1]
DR ProteomicsDB; 59459; -. [Q13459-2]
DR Antibodypedia; 7715; 132 antibodies from 32 providers.
DR DNASU; 4650; -.
DR Ensembl; ENST00000397274.6; ENSP00000380444.2; ENSG00000099331.14. [Q13459-2]
DR Ensembl; ENST00000595618.5; ENSP00000471457.1; ENSG00000099331.14. [Q13459-2]
DR Ensembl; ENST00000682292.1; ENSP00000507803.1; ENSG00000099331.14. [Q13459-1]
DR GeneID; 4650; -.
DR KEGG; hsa:4650; -.
DR MANE-Select; ENST00000682292.1; ENSP00000507803.1; NM_004145.4; NP_004136.2.
DR UCSC; uc002nfi.3; human. [Q13459-1]
DR CTD; 4650; -.
DR DisGeNET; 4650; -.
DR GeneCards; MYO9B; -.
DR HGNC; HGNC:7609; MYO9B.
DR HPA; ENSG00000099331; Low tissue specificity.
DR MalaCards; MYO9B; -.
DR MIM; 602129; gene.
DR MIM; 609753; phenotype.
DR neXtProt; NX_Q13459; -.
DR OpenTargets; ENSG00000099331; -.
DR VEuPathDB; HostDB:ENSG00000099331; -.
DR eggNOG; KOG1453; Eukaryota.
DR eggNOG; KOG4229; Eukaryota.
DR GeneTree; ENSGT00940000156845; -.
DR HOGENOM; CLU_000192_2_2_1; -.
DR InParanoid; Q13459; -.
DR PhylomeDB; Q13459; -.
DR TreeFam; TF319651; -.
DR PathwayCommons; Q13459; -.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-8985586; SLIT2:ROBO1 increases RHOA activity.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9035034; RHOF GTPase cycle.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR SignaLink; Q13459; -.
DR SIGNOR; Q13459; -.
DR BioGRID-ORCS; 4650; 46 hits in 1095 CRISPR screens.
DR ChiTaRS; MYO9B; human.
DR GeneWiki; MYO9B; -.
DR GenomeRNAi; 4650; -.
DR Pharos; Q13459; Tbio.
DR PRO; PR:Q13459; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q13459; protein.
DR Bgee; ENSG00000099331; Expressed in granulocyte and 171 other tissues.
DR ExpressionAtlas; Q13459; baseline and differential.
DR Genevisible; Q13459; HS.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
DR GO; GO:0005884; C:actin filament; IDA:UniProtKB.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030027; C:lamellipodium; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0001726; C:ruffle; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0043531; F:ADP binding; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0043008; F:ATP-dependent protein binding; IEA:Ensembl.
DR GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0000146; F:microfilament motor activity; IDA:UniProtKB.
DR GO; GO:0048495; F:Roundabout binding; IPI:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0030048; P:actin filament-based movement; IDA:UniProtKB.
DR GO; GO:0072673; P:lamellipodium morphogenesis; IBA:GO_Central.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IMP:UniProtKB.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007266; P:Rho protein signal transduction; IC:UniProtKB.
DR GO; GO:0035385; P:Roundabout signaling pathway; IDA:UniProtKB.
DR CDD; cd00029; C1; 1.
DR CDD; cd01385; MYSc_Myo9; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 3.40.850.10; -; 2.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR028557; MYO9B.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036023; MYSc_Myo9.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR46184:SF2; PTHR46184:SF2; 1.
DR Pfam; PF00612; IQ; 4.
DR Pfam; PF00063; Myosin_head; 2.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00109; C1; 1.
DR SMART; SM00015; IQ; 4.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00314; RA; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54236; SSF54236; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS50096; IQ; 3.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50200; RA; 1.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Alternative splicing;
KW ATP-binding; Calmodulin-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW GTPase activation; Metal-binding; Motor protein; Myosin;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..2157
FT /note="Unconventional myosin-IXb"
FT /id="PRO_0000123469"
FT DOMAIN 15..114
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT DOMAIN 146..953
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 957..977
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 979..1000
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1001..1023
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1024..1053
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1703..1888
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT ZN_FING 1632..1681
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 709..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..855
FT /note="Actin-binding"
FT /evidence="ECO:0000305"
FT REGION 940..1044
FT /note="Neck or regulatory domain"
FT /evidence="ECO:0000305"
FT REGION 1045..2157
FT /note="Tail"
FT /evidence="ECO:0000305"
FT REGION 1046..1298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1320..1410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1455..1484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1739..1744
FT /note="Interaction with RHOA"
FT /evidence="ECO:0000269|PubMed:26529257"
FT REGION 1980..2157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1046..1071
FT /evidence="ECO:0000255"
FT COILED 1880..1901
FT /evidence="ECO:0000255"
FT COILED 1959..1989
FT /evidence="ECO:0000255"
FT COMPBIAS 1048..1066
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1187..1205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1207..1224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1347..1364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1464..1484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1980..1997
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2022..2043
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 239..246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 716
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 717
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1045
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63358"
FT MOD_RES 1114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1253
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63358"
FT MOD_RES 1261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1271
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1290
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1331
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1346
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1354
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1356
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1405
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1926
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1972
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1992
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1999
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63358"
FT MOD_RES 2005
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QY06"
FT MOD_RES 2050
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QY06"
FT VAR_SEQ 2021..2022
FT /note="PP -> QY (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_003361"
FT VAR_SEQ 2023..2157
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_003362"
FT MUTAGEN 1739
FT /note="A->E,N: Decreases interaction with RHOA. Strongly
FT decreases stimulation of RHOA GTPase activity."
FT /evidence="ECO:0000269|PubMed:26529257"
FT MUTAGEN 1741
FT /note="N->E: Decreases interaction with RHOA. Decreases
FT stimulation of RHOA GTPase activity."
FT /evidence="ECO:0000269|PubMed:26529257"
FT MUTAGEN 1742
FT /note="R->E: Strongly decreases interaction with RHOA.
FT Strongly decreases stimulation of RHOA GTPase activity."
FT /evidence="ECO:0000269|PubMed:26529257"
FT CONFLICT 237..238
FT /note="IS -> YP (in Ref. 1; AAC50402)"
FT /evidence="ECO:0000305"
FT CONFLICT 276
FT /note="G -> C (in Ref. 1; AAC50402)"
FT /evidence="ECO:0000305"
FT CONFLICT 1011
FT /note="S -> A (in Ref. 1; AAC50402)"
FT /evidence="ECO:0000305"
FT CONFLICT 1693
FT /note="V -> A (in Ref. 1; AAC50402)"
FT /evidence="ECO:0000305"
FT CONFLICT 1946
FT /note="L -> P (in Ref. 4; BAA92132)"
FT /evidence="ECO:0000305"
FT CONFLICT 2039..2044
FT /note="TVAAPP -> PWPPLH (in Ref. 3; AAC26597)"
FT /evidence="ECO:0000305"
FT CONFLICT 2048
FT /note="P -> L (in Ref. 3; AAC26597)"
FT /evidence="ECO:0000305"
FT CONFLICT 2066
FT /note="P -> S (in Ref. 3; AAC26597)"
FT /evidence="ECO:0000305"
FT CONFLICT 2156..2157
FT /note="NG -> MAESHS (in Ref. 3; AAC26597)"
FT /evidence="ECO:0000305"
FT STRAND 1697..1700
FT /evidence="ECO:0007829|PDB:5C5S"
FT HELIX 1702..1705
FT /evidence="ECO:0007829|PDB:5C5S"
FT HELIX 1714..1726
FT /evidence="ECO:0007829|PDB:5C5S"
FT TURN 1727..1729
FT /evidence="ECO:0007829|PDB:5C5S"
FT TURN 1731..1735
FT /evidence="ECO:0007829|PDB:5C5S"
FT HELIX 1740..1752
FT /evidence="ECO:0007829|PDB:5C5S"
FT HELIX 1759..1761
FT /evidence="ECO:0007829|PDB:5C5S"
FT HELIX 1764..1776
FT /evidence="ECO:0007829|PDB:5C5S"
FT STRAND 1778..1780
FT /evidence="ECO:0007829|PDB:5C5S"
FT HELIX 1788..1795
FT /evidence="ECO:0007829|PDB:5C5S"
FT STRAND 1797..1799
FT /evidence="ECO:0007829|PDB:5C5S"
FT HELIX 1800..1811
FT /evidence="ECO:0007829|PDB:5C5S"
FT HELIX 1816..1834
FT /evidence="ECO:0007829|PDB:5C5S"
FT HELIX 1836..1839
FT /evidence="ECO:0007829|PDB:5C5S"
FT HELIX 1843..1854
FT /evidence="ECO:0007829|PDB:5C5S"
FT HELIX 1866..1895
FT /evidence="ECO:0007829|PDB:5C5S"
SQ SEQUENCE 2157 AA; 243401 MW; A3E72CAB759CD5FD CRC64;
MSVKEAGSSG RREQAAYHLH IYPQLSTTES QASCRVTATK DSTTSDVIKD AIASLRLDGT
KCYVLVEVKE SGGEEWVLDA NDSPVHRVLL WPRRAQDEHP QEDGYYFLLQ ERNADGTIKY
VHMQLVAQAT ATRRLVERGL LPRQQADFDD LCNLPELTEG NLLKNLKHRF LQQKIYTYAG
SILVAINPFK FLPIYNPKYV KMYENQQLGK LEPHVFALAD VAYYTMLRKR VNQCIVISGE
SGSGKTQSTN FLIHCLTALS QKGYASGVER TILGAGPVLE AFGNAKTAHN NNSSRFGKFI
QVSYLESGIV RGAVVEKYLL EKSRLVSQEK DERNYHVFYY LLLGVSEEER QEFQLKQPED
YFYLNQHNLK IEDGEDLKHD FERLKQAMEM VGFLPATKKQ IFAVLSAILY LGNVTYKKRA
TGREEGLEVG PPEVLDTLSQ LLKVKREILV EVLTKRKTVT VNDKLILPYS LSEAITARDS
MAKSLYSALF DWIVLRINHA LLNKKDVEEA VSCLSIGVLD IFGFEDFERN SFEQFCINYA
NEQLQYYFNQ HIFKLEQEEY QGEGITWHNI GYTDNVGCIH LISKKPTGLF YLLDEESNFP
HATSQTLLAK FKQQHEDNKY FLGTPVMEPA FIIQHFAGKV KYQIKDFREK NMDYMRPDIV
ALLRGSDSSY VRELIGMDPV AVFRWAVLRA AIRAMAVLRE AGRLRAERAE KAAGMSSPGA
QSHPEELPRG ASTPSEKLYR DLHNQMIKSI KGLPWQGEDP RSLLQSLSRL QKPRAFILKS
KGIKQKQIIP KNLLDSKSLK LIISMTLHDR TTKSLLHLHK KKKPPSISAQ FQTSLNKLLE
ALGKAEPFFI RCIRSNAEKK ELCFDDELVL QQLRYTGMLE TVRIRRSGYS AKYTFQDFTE
QFQVLLPKDA QPCREVISTL LEKMKIDKRN YQIGKTKVFL KETERQALQE TLHREVVRKI
LLLQSWFRMV LERRHFLQMK RAAVTIQACW RSYRVRRALE RTQAAVYLQA SWRGYWQRKL
YRHQKQSIIR LQSLCRGHLQ RKSFSQMISE KQKAEEKERE ALEAARAGAE EGGQGQAAGG
QQVAEQGPEP AEDGGHLASE PEVQPSDRSP LEHSSPEKEA PSPEKTLPPQ KTVAAESHEK
VPSSREKRES RRQRGLEHVK FQNKHIQSCK EESALREPSR RVTQEQGVSL LEDKKESRED
ETLLVVETEA ENTSQKQPTE QPQAMAVGKV SEETEKTLPS GSPRPGQLER PTSLALDSRV
SPPAPGSAPE TPEDKSKPCG SPRVQEKPDS PGGSTQIQRY LDAERLASAV ELWRGKKLVA
AASPSAMLSQ SLDLSDRHRA TGAALTPTEE RRTSFSTSDV SKLLPSLAKA QPAAETTDGE
RSAKKPAVQK KKPGDASSLP DAGLSPGSQV DSKSTFKRLF LHKTKDKKYS LEGAEELENA
VSGHVVLEAT TMKKGLEAPS GQQHRHAAGE KRTKEPGGKG KKNRNVKIGK ITVSEKWRES
VFRQITNANE LKYLDEFLLN KINDLRSQKT PIESLFIEAT EKFRSNIKTM YSVPNGKIHV
GYKDLMENYQ IVVSNLATER GQKDTNLVLN LFQSLLDEFT RGYTKNDFEP VKQSKAQKKK
RKQERAVQEH NGHVFASYQV SIPQSCEQCL SYIWLMDKAL LCSVCKMTCH KKCVHKIQSH
CSYTYGRKGE PGVEPGHFGV CVDSLTSDKA SVPIVLEKLL EHVEMHGLYT EGLYRKSGAA
NRTRELRQAL QTDPAAVKLE NFPIHAITGV LKQWLRELPE PLMTFAQYGD FLRAVELPEK
QEQLAAIYAV LEHLPEANHN SLERLIFHLV KVALLEDVNR MSPGALAIIF APCLLRCPDN
SDPLTSMKDV LKITTCVEML IKEQMRKYKV KMEEISQLEA AESIAFRRLS LLRQNAPWPL
KLGFSSPYEG VLNKSPKTRD IQEEELEVLL EEEAAGGDED REKEILIERI QSIKEEKEDI
TYRLPELDPR GSDEENLDSE TSASTESLLE ERAGRGASEG PPAPALPCPG APTPSPLPTV
AAPPRRRPSS FVTVRVKTPR RTPIMPTANI KLPPGLPSHL PRWAPGAREA AAPVRRREPP
ARRPDQIHSV YITPGADLPV QGALEPLEED GQPPGAKRRY SDPPTYCLPP ASGQTNG
