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 24-JAN-2024, entry version 220. 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"; 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; 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 CCDS; CCDS92551.1; -. [Q13459-1] 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; 140. DR ELM; Q13459; -. DR IntAct; Q13459; 33. DR MINT; Q13459; -. DR STRING; 9606.ENSP00000471457; -. DR GlyGen; Q13459; 1 site, 1 O-linked glycan (1 site). 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; 9606-ENSP00000471457; -. DR PeptideAtlas; Q13459; -. DR ProteomicsDB; 59458; -. [Q13459-1] DR ProteomicsDB; 59459; -. [Q13459-2] DR Pumba; Q13459; -. DR Antibodypedia; 7715; 150 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 AGR; HGNC:7609; -. DR CTD; 4650; -. DR DisGeNET; 4650; -. DR GeneCards; MYO9B; -. DR HGNC; HGNC:7609; MYO9B. DR HPA; ENSG00000099331; Tissue enhanced (lymphoid). 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 OrthoDB; 1094820at2759; -. 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; 48 hits in 1172 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 173 other cell types or tissues. DR ExpressionAtlas; Q13459; baseline and differential. 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:0005516; F:calmodulin binding; IDA:UniProtKB. DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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: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; cd20884; C1_Myosin-IXb; 1. DR CDD; cd01385; MYSc_Myo9; 1. DR CDD; cd17217; RA_Myosin-IXb; 1. DR CDD; cd04407; RhoGAP_myosin_IXB; 1. DR Gene3D; 1.10.10.820; -; 1. DR Gene3D; 1.20.5.190; -; 2. DR Gene3D; 1.20.58.530; -; 2. DR Gene3D; 3.30.60.20; -; 1. DR Gene3D; 6.20.240.20; -; 1. DR Gene3D; 3.40.850.10; Kinesin motor domain; 2. DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1. DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1. DR InterPro; IPR046349; C1-like_sf. DR InterPro; IPR000048; IQ_motif_EF-hand-BS. DR InterPro; IPR036961; Kinesin_motor_dom_sf. DR InterPro; IPR046987; Myo9. 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; IPR046989; RA_Myosin-IXb. DR InterPro; IPR008936; Rho_GTPase_activation_prot. DR InterPro; IPR000198; RhoGAP_dom. DR InterPro; IPR028557; RhoGAP_myosin_IXB. DR InterPro; IPR029071; Ubiquitin-like_domsf. DR PANTHER; PTHR46184:SF2; UNCONVENTIONAL MYOSIN-IXB; 1. DR PANTHER; PTHR46184; UNCONVENTIONAL MYOSIN-IXB-LIKE PROTEIN; 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; SSF57889; Cysteine-rich domain; 1. DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR SUPFAM; SSF54236; Ubiquitin-like; 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. DR Genevisible; Q13459; HS. 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 RHOAGTPase activity." FT /evidence="ECO:0000269|PubMed:26529257" FT MUTAGEN 1741 FT /note="N->E: Decreases interaction with RHOA. Decreases FT stimulation of RHOAGTPase activity." FT /evidence="ECO:0000269|PubMed:26529257" FT MUTAGEN 1742 FT /note="R->E: Strongly decreases interaction with RHOA. FT Strongly decreases stimulation of RHOAGTPase 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 //