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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
 
 
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