SEPT9_HUMAN
ID SEPT9_HUMAN Reviewed; 586 AA.
AC Q9UHD8; A8K2V3; B3KPM0; B4DTL9; B4E0N2; B4E274; B7Z654; Q96QF3; Q96QF4;
AC Q96QF5; Q9HA04; Q9UG40; Q9Y5W4;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Septin-9;
DE AltName: Full=MLL septin-like fusion protein MSF-A;
DE Short=MLL septin-like fusion protein;
DE AltName: Full=Ovarian/Breast septin;
DE Short=Ov/Br septin;
DE AltName: Full=Septin D1;
GN Name=SEPTIN9 {ECO:0000312|HGNC:HGNC:7323}; Synonyms=KIAA0991, MSF, SEPT9;
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 2), VARIANT VAL-576, TISSUE
RP SPECIFICITY, DISEASE, AND CHROMOSOMAL TRANSLOCATION.
RX PubMed=10339604; DOI=10.1073/pnas.96.11.6428;
RA Osaka M., Rowley J.D., Zeleznik-Le N.J.;
RT "MSF (MLL septin-like fusion), a fusion partner gene of MLL, in a therapy-
RT related acute myeloid leukemia with a t(11;17)(q23;q25).";
RL Proc. Natl. Acad. Sci. U.S.A. 96:6428-6433(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5), AND VARIANTS CYS-76;
RP LEU-145 AND VAL-576.
RX PubMed=10987277;
RA Russell S.E.H., McIlhatton M.A., Burrows J.F., Donaghy P.G., Chanduloy S.,
RA Petty E.M., Kalikin L.M., Church S.W., McIlroy S., Harkin D.P.,
RA Keilty G.W., Cranston A.N., Weissenbach J., Hickey I., Johnston P.G.;
RT "Isolation and mapping of a human septin gene to a region on chromosome
RT 17q, commonly deleted in sporadic epithelial ovarian tumors.";
RL Cancer Res. 60:4729-4734(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), VARIANT VAL-576, TISSUE
RP SPECIFICITY, AND ALTERNATIVE SPLICING.
RX PubMed=10673329; DOI=10.1006/geno.1999.6077;
RA Kalikin L.M., Sims H.L., Petty E.M.;
RT "Genomic and expression analyses of alternatively spliced transcripts of
RT the MLL septin-like fusion gene (MSF) that map to a 17q25 region of loss in
RT breast and ovarian tumors.";
RL Genomics 63:165-172(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT VAL-576.
RA Zhang W., He L., Wan T., Yuan Z., Zhu X., Cao X.;
RT "Novel human cell division control protein septin D1.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4; 5; 7; 8 AND 9), AND
RP VARIANTS LEU-145 AND VAL-576.
RC TISSUE=Fetal brain, Mammary gland, Placenta, Teratocarcinoma, Thymus,
RC Tongue, and Trachea;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT VAL-576.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-576.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP VAL-576.
RC TISSUE=Eye, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 26-586, AND VARIANT VAL-576.
RC TISSUE=Brain;
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 353-586, AND VARIANT VAL-576.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [11]
RP TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING.
RX PubMed=11593400; DOI=10.1038/sj.onc.1204752;
RA McIlhatton M.A., Burrows J.F., Donaghy P.G., Chanduloy S., Johnston P.G.,
RA Russell S.E.;
RT "Genomic organization, complex splicing pattern and expression of a human
RT septin gene on chromosome 17q25.3.";
RL Oncogene 20:5930-5939(2001).
RN [12]
RP INTERACTION WITH SEPTIN7 AND SEPTIN11.
RX PubMed=15485874; DOI=10.1074/jbc.m406153200;
RA Nagata K., Asano T., Nozawa Y., Inagaki M.;
RT "Biochemical and cell biological analyses of a mammalian septin complex,
RT Sept7/9b/11.";
RL J. Biol. Chem. 279:55895-55904(2004).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=15915442; DOI=10.1002/path.1789;
RA Hall P.A., Jung K., Hillan K.J., Russell S.E.H.;
RT "Expression profiling the human septin gene family.";
RL J. Pathol. 206:269-278(2005).
RN [14]
RP INTERACTION WITH ARHGEF18.
RX PubMed=15558029; DOI=10.1038/sj.onc.1208101;
RA Nagata K., Inagaki M.;
RT "Cytoskeletal modification of Rho guanine nucleotide exchange factor
RT activity: identification of a Rho guanine nucleotide exchange factor as a
RT binding partner for Sept9b, a mammalian septin.";
RL Oncogene 24:65-76(2005).
RN [15]
RP INTERACTION WITH RTKN.
RX PubMed=16007136; DOI=10.1038/sj.onc.1208862;
RA Ito H., Iwamoto I., Morishita R., Nozawa Y., Narumiya S., Asano T.,
RA Nagata K.;
RT "Possible role of Rho/Rhotekin signaling in mammalian septin
RT organization.";
RL Oncogene 24:7064-7072(2005).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 AND THR-42, AND
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 [18]
RP SUBCELLULAR LOCATION, INTERACTION WITH SEPTIN4, AND VARIANTS HNA TRP-106
RP AND PHE-111.
RX PubMed=17546647; DOI=10.1002/humu.20554;
RA Sudo K., Ito H., Iwamoto I., Morishita R., Asano T., Nagata K.;
RT "SEPT9 sequence alternations causing hereditary neuralgic amyotrophy are
RT associated with altered interactions with SEPT4/SEPT11 and resistance to
RT Rho/Rhotekin-signaling.";
RL Hum. Mutat. 28:1005-1013(2007).
RN [19]
RP INTERACTION WITH SEPTIN14, AND SUBCELLULAR LOCATION.
RX PubMed=17922164; DOI=10.1007/s00335-007-9065-x;
RA Peterson E.A., Kalikin L.M., Steels J.D., Estey M.P., Trimble W.S.,
RA Petty E.M.;
RT "Characterization of a SEPT9 interacting protein, SEPT14, a novel testis-
RT specific septin.";
RL Mamm. Genome 18:796-807(2007).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; THR-38 AND THR-42, AND
RP 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 [22]
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 [23]
RP INTERACTION WITH SEPTIN2; SEPTIN6; SEPTIN7 AND SEPTIN11, AND ASSOCIATION
RP WITH ACTIN FILAMENTS AND MICROTUBULES.
RX PubMed=19145258; DOI=10.1371/journal.pone.0004196;
RA Mostowy S., Nam Tham T., Danckaert A., Guadagnini S., Boisson-Dupuis S.,
RA Pizarro-Cerda J., Cossart P.;
RT "Septins regulate bacterial entry into host cells.";
RL PLoS ONE 4:E4196-E4196(2009).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 AND TYR-278, AND
RP 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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-82; SER-85; SER-96
RP AND THR-142, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [26]
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 [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-85 AND SER-327, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., 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 [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, ACETYLATION [LARGE SCALE
RP ANALYSIS] AT MET-1 (ISOFORM 3), 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 [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-30; THR-42; THR-49;
RP SER-85; SER-89; THR-142 AND SER-332, AND IDENTIFICATION BY MASS
RP 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 [30]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [32]
RP VARIANTS HNA TRP-106 AND PHE-111.
RX PubMed=16186812; DOI=10.1038/ng1649;
RA Kuhlenbaeumer G., Hannibal M.C., Nelis E., Schirmacher A., Verpoorten N.,
RA Meuleman J., Watts G.D.J., De Vriendt E., Young P., Stoegbauer F.,
RA Halfter H., Irobi J., Goossens D., Del-Favero J., Betz B.G., Hor H.,
RA Kurlemann G., Bird T.D., Airaksinen E., Mononen T., Serradell A.P.,
RA Prats J.M., Van Broeckhoven C., De Jonghe P., Timmerman V.,
RA Ringelstein E.B., Chance P.F.;
RT "Mutations in SEPT9 cause hereditary neuralgic amyotrophy.";
RL Nat. Genet. 37:1044-1046(2005).
RN [33]
RP VARIANT HNA TRP-106.
RX PubMed=18492087; DOI=10.1111/j.1399-0004.2008.01022.x;
RA Laccone F., Hannibal M.C., Neesen J., Grisold W., Chance P.F., Rehder H.;
RT "Dysmorphic syndrome of hereditary neuralgic amyotrophy associated with a
RT SEPT9 gene mutation -- a family study.";
RL Clin. Genet. 74:279-283(2008).
RN [34]
RP VARIANTS HNA TRP-106 AND PHE-111, AND VARIANT LEU-145.
RX PubMed=19451530; DOI=10.1212/wnl.0b013e3181a609e3;
RA Hannibal M.C., Ruzzo E.K., Miller L.R., Betz B., Buchan J.G., Knutzen D.M.,
RA Barnett K., Landsverk M.L., Brice A., LeGuern E., Bedford H.M.,
RA Worrall B.B., Lovitt S., Appel S.H., Andermann E., Bird T.D., Chance P.F.;
RT "SEPT9 gene sequencing analysis reveals recurrent mutations in hereditary
RT neuralgic amyotrophy.";
RL Neurology 72:1755-1759(2009).
CC -!- FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May
CC play a role in cytokinesis (Potential). May play a role in the
CC internalization of 2 intracellular microbial pathogens, Listeria
CC monocytogenes and Shigella flexneri. {ECO:0000250, ECO:0000305}.
CC -!- SUBUNIT: Septins polymerize into heterooligomeric protein complexes
CC that form filaments, and associate with cellular membranes, actin
CC filaments, and microtubules. GTPase activity is required for filament
CC formation. Interacts with SEPTIN2, SEPTIN6, SEPTIN7, SEPTIN11 and
CC SEPTIN14. Interacts with RTKN and ARHGEF18. In a mesenchymal cell line,
CC Rho/RTKN signals cause disruption of wild-type septin filaments, but
CC not of those containing isoform 2 variants HNA Trp-106 and Phe-111. In
CC a mesenchymal cell line, isoform 2 variants HNA Trp-106 and Phe-111,
CC but not wild type, form filaments with SEPTIN4.
CC {ECO:0000269|PubMed:15485874, ECO:0000269|PubMed:15558029,
CC ECO:0000269|PubMed:16007136, ECO:0000269|PubMed:17546647,
CC ECO:0000269|PubMed:17922164, ECO:0000269|PubMed:19145258}.
CC -!- INTERACTION:
CC Q9UHD8; Q14141: SEPTIN6; NbExp=4; IntAct=EBI-851542, EBI-745901;
CC Q9UHD8-1; Q16665: HIF1A; NbExp=4; IntAct=EBI-851558, EBI-447269;
CC Q9UHD8-1; Q6ZU15: SEPTIN14; NbExp=3; IntAct=EBI-851558, EBI-2009297;
CC Q9UHD8-2; O75031: HSF2BP; NbExp=3; IntAct=EBI-851564, EBI-7116203;
CC Q9UHD8-3; Q6ZU15: SEPTIN14; NbExp=3; IntAct=EBI-851569, EBI-2009297;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:17546647, ECO:0000269|PubMed:17922164}. Note=In an
CC epithelial cell line, concentrates at cell-cell contact areas. After
CC TGF-beta1 treatment and induction of epithelial to mesenchymal
CC transition, colocalizes partly with actin stress fibers. During
CC bacterial infection, displays a collar shape structure next to actin at
CC the pole of invading bacteria.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Comment=There are potentially 18 isoforms.;
CC Name=1; Synonyms=Epsilon, MSF-A;
CC IsoId=Q9UHD8-1; Sequence=Displayed;
CC Name=2; Synonyms=Alpha;
CC IsoId=Q9UHD8-2; Sequence=VSP_012337;
CC Name=3; Synonyms=Beta, MSF-B;
CC IsoId=Q9UHD8-3; Sequence=VSP_012336;
CC Name=4; Synonyms=Delta;
CC IsoId=Q9UHD8-4; Sequence=VSP_012335;
CC Name=5; Synonyms=Gamma;
CC IsoId=Q9UHD8-5; Sequence=VSP_012338;
CC Name=7;
CC IsoId=Q9UHD8-7; Sequence=VSP_038317;
CC Name=8;
CC IsoId=Q9UHD8-8; Sequence=VSP_038316, VSP_038318;
CC Name=9;
CC IsoId=Q9UHD8-9; Sequence=VSP_038315, VSP_038319;
CC -!- TISSUE SPECIFICITY: Widely expressed. Isoforms are differentially
CC expressed in testes, kidney, liver heart, spleen, brain, peripheral
CC blood leukocytes, skeletal muscle and kidney. Specific isoforms appear
CC to demonstrate tissue specificity. Isoform 5 is the most highly
CC expressed in fetal tissue. Isoform 1 is detected in all tissues except
CC the brain and thymus, while isoform 2, isoform 3, and isoform 4 are
CC detected at low levels in approximately half of the fetal tissues.
CC {ECO:0000269|PubMed:10339604, ECO:0000269|PubMed:10673329,
CC ECO:0000269|PubMed:11593400, ECO:0000269|PubMed:15915442}.
CC -!- DISEASE: Note=A chromosomal aberration involving SEPTIN9/MSF is found
CC in therapy-related acute myeloid leukemia (t-AML). Translocation
CC t(11;17)(q23;q25) with KMT2A/MLL1. {ECO:0000269|PubMed:10339604}.
CC -!- DISEASE: Hereditary neuralgic amyotrophy (HNA) [MIM:162100]: Autosomal
CC dominant form of recurrent focal neuropathy characterized clinically by
CC acute, recurrent episodes of brachial plexus neuropathy with muscle
CC weakness and atrophy preceded by severe pain in the affected arm. HNA
CC is triggered by environmental factors such as infection or parturition.
CC {ECO:0000269|PubMed:16186812, ECO:0000269|PubMed:17546647,
CC ECO:0000269|PubMed:18492087, ECO:0000269|PubMed:19451530}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01056}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14057.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MSFID208.html";
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DR EMBL; AF123052; AAD39749.1; -; mRNA.
DR EMBL; AJ312319; CAC42221.1; -; mRNA.
DR EMBL; AJ312320; CAC42222.1; -; mRNA.
DR EMBL; AJ312321; CAC42223.1; -; mRNA.
DR EMBL; AJ312322; CAC42224.1; -; mRNA.
DR EMBL; AF189712; AAF23373.1; -; mRNA.
DR EMBL; AF189713; AAF23374.1; -; mRNA.
DR EMBL; AF142408; AAG27919.1; -; mRNA.
DR EMBL; AK022493; BAB14057.1; ALT_SEQ; mRNA.
DR EMBL; AK290368; BAF83057.1; -; mRNA.
DR EMBL; AK056495; BAG51732.1; -; mRNA.
DR EMBL; AK300270; BAG62031.1; -; mRNA.
DR EMBL; AK303449; BAG64494.1; -; mRNA.
DR EMBL; AK304143; BAG65036.1; -; mRNA.
DR EMBL; AK299828; BAH13140.1; -; mRNA.
DR EMBL; AK316473; BAH14844.1; -; mRNA.
DR EMBL; BT007215; AAP35879.1; -; mRNA.
DR EMBL; CH471099; EAW89462.1; -; Genomic_DNA.
DR EMBL; CH471099; EAW89463.1; -; Genomic_DNA.
DR EMBL; CH471099; EAW89468.1; -; Genomic_DNA.
DR EMBL; BC021192; AAH21192.1; -; mRNA.
DR EMBL; BC054004; AAH54004.1; -; mRNA.
DR EMBL; AB023208; BAA76835.2; -; mRNA.
DR EMBL; AL080131; CAB45728.1; -; mRNA.
DR CCDS; CCDS45790.1; -. [Q9UHD8-1]
DR CCDS; CCDS45791.1; -. [Q9UHD8-2]
DR CCDS; CCDS45792.1; -. [Q9UHD8-5]
DR CCDS; CCDS45793.1; -. [Q9UHD8-3]
DR CCDS; CCDS45794.1; -. [Q9UHD8-4]
DR CCDS; CCDS45795.1; -. [Q9UHD8-4]
DR CCDS; CCDS74166.1; -. [Q9UHD8-9]
DR CCDS; CCDS77122.1; -. [Q9UHD8-7]
DR PIR; T12519; T12519.
DR RefSeq; NP_001106963.1; NM_001113491.1. [Q9UHD8-1]
DR RefSeq; NP_001106964.1; NM_001113492.1. [Q9UHD8-3]
DR RefSeq; NP_001106965.1; NM_001113493.1. [Q9UHD8-5]
DR RefSeq; NP_001106966.1; NM_001113494.1. [Q9UHD8-3]
DR RefSeq; NP_001106967.1; NM_001113495.1. [Q9UHD8-4]
DR RefSeq; NP_001106968.1; NM_001113496.1. [Q9UHD8-4]
DR RefSeq; NP_001280624.1; NM_001293695.1. [Q9UHD8-7]
DR RefSeq; NP_001280625.1; NM_001293696.1. [Q9UHD8-9]
DR RefSeq; NP_001280626.1; NM_001293697.1. [Q9UHD8-4]
DR RefSeq; NP_001280627.1; NM_001293698.1. [Q9UHD8-4]
DR RefSeq; NP_006631.2; NM_006640.4. [Q9UHD8-2]
DR RefSeq; XP_005257019.1; XM_005256962.1.
DR RefSeq; XP_006721706.1; XM_006721643.2.
DR RefSeq; XP_006721707.1; XM_006721644.1.
DR RefSeq; XP_011522509.1; XM_011524207.1.
DR RefSeq; XP_011522510.1; XM_011524208.2.
DR RefSeq; XP_016879520.1; XM_017024031.1.
DR RefSeq; XP_016879521.1; XM_017024032.1.
DR PDB; 4YQF; X-ray; 2.73 A; A/B=296-565.
DR PDB; 5CYO; X-ray; 2.04 A; A/B=295-568.
DR PDB; 5CYP; X-ray; 2.89 A; A/B/C/D=293-566.
DR PDBsum; 4YQF; -.
DR PDBsum; 5CYO; -.
DR PDBsum; 5CYP; -.
DR AlphaFoldDB; Q9UHD8; -.
DR SMR; Q9UHD8; -.
DR BioGRID; 116015; 180.
DR CORUM; Q9UHD8; -.
DR DIP; DIP-36697N; -.
DR IntAct; Q9UHD8; 54.
DR MINT; Q9UHD8; -.
DR STRING; 9606.ENSP00000391249; -.
DR ChEMBL; CHEMBL4105891; -.
DR CarbonylDB; Q9UHD8; -.
DR GlyGen; Q9UHD8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UHD8; -.
DR MetOSite; Q9UHD8; -.
DR PhosphoSitePlus; Q9UHD8; -.
DR SwissPalm; Q9UHD8; -.
DR BioMuta; SEPT9; -.
DR DMDM; 93141311; -.
DR EPD; Q9UHD8; -.
DR jPOST; Q9UHD8; -.
DR MassIVE; Q9UHD8; -.
DR MaxQB; Q9UHD8; -.
DR PaxDb; Q9UHD8; -.
DR PeptideAtlas; Q9UHD8; -.
DR PRIDE; Q9UHD8; -.
DR ProteomicsDB; 84325; -. [Q9UHD8-1]
DR ProteomicsDB; 84326; -. [Q9UHD8-2]
DR ProteomicsDB; 84327; -. [Q9UHD8-3]
DR ProteomicsDB; 84328; -. [Q9UHD8-4]
DR ProteomicsDB; 84329; -. [Q9UHD8-5]
DR ProteomicsDB; 84330; -. [Q9UHD8-7]
DR ProteomicsDB; 84331; -. [Q9UHD8-8]
DR ProteomicsDB; 84332; -. [Q9UHD8-9]
DR Antibodypedia; 32488; 234 antibodies from 31 providers.
DR DNASU; 10801; -.
DR Ensembl; ENST00000329047.13; ENSP00000329161.8; ENSG00000184640.20. [Q9UHD8-2]
DR Ensembl; ENST00000423034.6; ENSP00000405877.1; ENSG00000184640.20. [Q9UHD8-5]
DR Ensembl; ENST00000427177.6; ENSP00000391249.1; ENSG00000184640.20. [Q9UHD8-1]
DR Ensembl; ENST00000427180.5; ENSP00000504196.1; ENSG00000184640.20. [Q9UHD8-4]
DR Ensembl; ENST00000427674.6; ENSP00000403194.1; ENSG00000184640.20. [Q9UHD8-3]
DR Ensembl; ENST00000431235.6; ENSP00000406987.2; ENSG00000184640.20. [Q9UHD8-3]
DR Ensembl; ENST00000449803.6; ENSP00000400181.2; ENSG00000184640.20. [Q9UHD8-3]
DR Ensembl; ENST00000541152.6; ENSP00000438089.2; ENSG00000184640.20. [Q9UHD8-4]
DR Ensembl; ENST00000585930.5; ENSP00000468120.1; ENSG00000184640.20. [Q9UHD8-9]
DR Ensembl; ENST00000588690.6; ENSP00000468668.1; ENSG00000184640.20. [Q9UHD8-3]
DR Ensembl; ENST00000591088.5; ENSP00000466247.1; ENSG00000184640.20. [Q9UHD8-4]
DR Ensembl; ENST00000591198.5; ENSP00000468406.1; ENSG00000184640.20. [Q9UHD8-7]
DR Ensembl; ENST00000592951.5; ENSP00000466648.1; ENSG00000184640.20. [Q9UHD8-4]
DR GeneID; 10801; -.
DR KEGG; hsa:10801; -.
DR MANE-Select; ENST00000427177.6; ENSP00000391249.1; NM_001113491.2; NP_001106963.1.
DR UCSC; uc002jts.5; human. [Q9UHD8-1]
DR CTD; 10801; -.
DR DisGeNET; 10801; -.
DR GeneCards; SEPTIN9; -.
DR HGNC; HGNC:7323; SEPTIN9.
DR HPA; ENSG00000184640; Low tissue specificity.
DR MalaCards; SEPTIN9; -.
DR MIM; 162100; phenotype.
DR MIM; 604061; gene.
DR neXtProt; NX_Q9UHD8; -.
DR OpenTargets; ENSG00000184640; -.
DR Orphanet; 2901; Neuralgic amyotrophy.
DR PharmGKB; PA31132; -.
DR VEuPathDB; HostDB:ENSG00000184640; -.
DR eggNOG; KOG1547; Eukaryota.
DR GeneTree; ENSGT00940000157195; -.
DR HOGENOM; CLU_017718_5_0_1; -.
DR InParanoid; Q9UHD8; -.
DR OMA; HLVAHEM; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; Q9UHD8; -.
DR TreeFam; TF101078; -.
DR PathwayCommons; Q9UHD8; -.
DR SignaLink; Q9UHD8; -.
DR SIGNOR; Q9UHD8; -.
DR BioGRID-ORCS; 10801; 14 hits in 1018 CRISPR screens.
DR ChiTaRS; SEPT9; human.
DR GeneWiki; SEPT9; -.
DR GenomeRNAi; 10801; -.
DR Pharos; Q9UHD8; Tchem.
DR PRO; PR:Q9UHD8; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9UHD8; protein.
DR Bgee; ENSG00000184640; Expressed in ileal mucosa and 202 other tissues.
DR ExpressionAtlas; Q9UHD8; baseline and differential.
DR Genevisible; Q9UHD8; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005930; C:axoneme; IDA:GO_Central.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0097730; C:non-motile cilium; IDA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0031105; C:septin complex; IDA:UniProtKB.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:1902857; P:positive regulation of non-motile cilium assembly; IMP:GO_Central.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR CDD; cd01850; CDC_Septin; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR030645; SEPT9.
DR InterPro; IPR016491; Septin.
DR PANTHER; PTHR18884:SF47; PTHR18884:SF47; 1.
DR Pfam; PF00735; Septin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Chromosomal rearrangement; Cytoplasm; Cytoskeleton; Disease variant;
KW GTP-binding; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..586
FT /note="Septin-9"
FT /id="PRO_0000173535"
FT DOMAIN 295..567
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..312
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 362..365
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 444..447
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 305..312
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 339
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 365
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 445..453
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 501
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 516
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 38
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 42
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 49
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 62
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q80UG5"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 142
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 278
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..251
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10987277,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_012335"
FT VAR_SEQ 1..224
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038315"
FT VAR_SEQ 1..164
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10673329,
FT ECO:0000303|PubMed:10987277, ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_012336"
FT VAR_SEQ 1..112
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038316"
FT VAR_SEQ 1..25
FT /note="MKKSYSGGTRTSSGRLRRLGDSSGP -> MERDRIS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10339604,
FT ECO:0000303|PubMed:10987277, ECO:0000303|PubMed:15489334,
FT ECO:0000303|Ref.4, ECO:0000303|Ref.6"
FT /id="VSP_012337"
FT VAR_SEQ 1..25
FT /note="MKKSYSGGTRTSSGRLRRLGDSSGP -> MSDPAVNAQLDGIISDFE (in
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:10987277,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_012338"
FT VAR_SEQ 7..25
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038317"
FT VAR_SEQ 113..240
FT /note="DISSKQVENAGAIGPSRFGLKRAEVLGHKTPEPAPRRTEITIVKPQESAHRR
FT MEPPASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPAQTLENSEPAPVSQLQSRL
FT EPKPQPPVAEATPRSQE -> MGSSFWEGLQVAVGLPQGCWPQGLDSGEPAEGGQLEAA
FT PVCIVTRQSKETAGPTLGRGGWRQGSLRRGKGTSCRCRQLSPGHGPGRLTGCGECHRLP
FT CRGLVSGFTGLRGQEEDDLAFCLATIGSDRQ (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038318"
FT VAR_SEQ 225..240
FT /note="PKPQPPVAEATPRSQE -> MAGAGCTGTWSWLWGT (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038319"
FT VARIANT 76
FT /note="R -> C (in dbSNP:rs202079794)"
FT /evidence="ECO:0000269|PubMed:10987277"
FT /id="VAR_020667"
FT VARIANT 106
FT /note="R -> W (in HNA; dbSNP:rs80338761)"
FT /evidence="ECO:0000269|PubMed:16186812,
FT ECO:0000269|PubMed:17546647, ECO:0000269|PubMed:18492087,
FT ECO:0000269|PubMed:19451530"
FT /id="VAR_033101"
FT VARIANT 111
FT /note="S -> F (in HNA; dbSNP:rs80338762)"
FT /evidence="ECO:0000269|PubMed:16186812,
FT ECO:0000269|PubMed:17546647, ECO:0000269|PubMed:19451530"
FT /id="VAR_033102"
FT VARIANT 145
FT /note="P -> L (in dbSNP:rs34587622)"
FT /evidence="ECO:0000269|PubMed:10987277,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:19451530"
FT /id="VAR_020668"
FT VARIANT 576
FT /note="M -> V (in dbSNP:rs2627223)"
FT /evidence="ECO:0000269|PubMed:10231032,
FT ECO:0000269|PubMed:10339604, ECO:0000269|PubMed:10673329,
FT ECO:0000269|PubMed:10987277, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
FT ECO:0000269|Ref.4, ECO:0000269|Ref.6, ECO:0000269|Ref.7"
FT /id="VAR_020669"
FT CONFLICT 251
FT /note="D -> G (in Ref. 5; BAG64494)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="V -> E (in Ref. 5; BAB14057)"
FT /evidence="ECO:0000305"
FT STRAND 297..305
FT /evidence="ECO:0007829|PDB:5CYO"
FT HELIX 311..322
FT /evidence="ECO:0007829|PDB:5CYO"
FT STRAND 343..351
FT /evidence="ECO:0007829|PDB:5CYO"
FT STRAND 354..362
FT /evidence="ECO:0007829|PDB:5CYO"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:5CYO"
FT TURN 373..376
FT /evidence="ECO:0007829|PDB:5CYO"
FT HELIX 377..395
FT /evidence="ECO:0007829|PDB:5CYO"
FT STRAND 410..415
FT /evidence="ECO:0007829|PDB:5CYO"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:5CYP"
FT HELIX 424..434
FT /evidence="ECO:0007829|PDB:5CYO"
FT STRAND 437..443
FT /evidence="ECO:0007829|PDB:5CYO"
FT HELIX 446..448
FT /evidence="ECO:0007829|PDB:5CYO"
FT HELIX 451..467
FT /evidence="ECO:0007829|PDB:5CYO"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:4YQF"
FT HELIX 476..478
FT /evidence="ECO:0007829|PDB:5CYO"
FT HELIX 482..494
FT /evidence="ECO:0007829|PDB:5CYO"
FT STRAND 496..498
FT /evidence="ECO:0007829|PDB:5CYO"
FT STRAND 503..508
FT /evidence="ECO:0007829|PDB:5CYO"
FT STRAND 511..517
FT /evidence="ECO:0007829|PDB:5CYO"
FT STRAND 522..524
FT /evidence="ECO:0007829|PDB:5CYO"
FT TURN 528..530
FT /evidence="ECO:0007829|PDB:5CYO"
FT HELIX 533..539
FT /evidence="ECO:0007829|PDB:5CYO"
FT HELIX 542..554
FT /evidence="ECO:0007829|PDB:5CYO"
FT HELIX 556..567
FT /evidence="ECO:0007829|PDB:5CYO"
FT MOD_RES Q9UHD8-3:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 586 AA; 65401 MW; D4404578328CFCFE CRC64;
MKKSYSGGTR TSSGRLRRLG DSSGPALKRS FEVEEVETPN STPPRRVQTP LLRATVASST
QKFQDLGVKN SEPSARHVDS LSQRSPKASL RRVELSGPKA AEPVSRRTEL SIDISSKQVE
NAGAIGPSRF GLKRAEVLGH KTPEPAPRRT EITIVKPQES AHRRMEPPAS KVPEVPTAPA
TDAAPKRVEI QMPKPAEAPT APSPAQTLEN SEPAPVSQLQ SRLEPKPQPP VAEATPRSQE
ATEAAPSCVG DMADTPRDAG LKQAPASRNE KAPVDFGYVG IDSILEQMRR KAMKQGFEFN
IMVVGQSGLG KSTLINTLFK SKISRKSVQP TSEERIPKTI EIKSITHDIE EKGVRMKLTV
IDTPGFGDHI NNENCWQPIM KFINDQYEKY LQEEVNINRK KRIPDTRVHC CLYFIPATGH
SLRPLDIEFM KRLSKVVNIV PVIAKADTLT LEERVHFKQR ITADLLSNGI DVYPQKEFDE
DSEDRLVNEK FREMIPFAVV GSDHEYQVNG KRILGRKTKW GTIEVENTTH CEFAYLRDLL
IRTHMQNIKD ITSSIHFEAY RVKRLNEGSS AMANGMEEKE PEAPEM
