ID SEPT7_HUMAN Reviewed; 437 AA.
AC Q16181; Q52M76; Q6NX50;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 27-MAR-2024, entry version 210.
DE RecName: Full=Septin-7;
DE AltName: Full=CDC10 protein homolog;
GN Name=SEPTIN7 {ECO:0000312|HGNC:HGNC:1717}; Synonyms=CDC10, SEPT7;
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] OF 4-437 (ISOFORM 1).
RC TISSUE=Fetal lung;
RX PubMed=8037772; DOI=10.1006/bbrc.1994.1896;
RA Nakatsuru S., Sudo K., Nakamura Y.;
RT "Molecular cloning of a novel human cDNA homologous to CDC10 in
RT Saccharomyces cerevisiae.";
RL Biochem. Biophys. Res. Commun. 202:82-87(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-437 (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Uterus;
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 [3]
RP INTERACTION WITH SEPTIN9 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 [4]
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 [5]
RP COORDINATED EXPRESSION WITH SEPTIN2 AND SEPTIN6.
RX PubMed=16093351; DOI=10.1091/mbc.e05-03-0267;
RA Kremer B.E., Haystead T., Macara I.G.;
RT "Mammalian septins regulate microtubule stability through interaction with
RT the microtubule-binding protein MAP4.";
RL Mol. Biol. Cell 16:4648-4659(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, 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 [8]
RP INTERACTION WITH SEPTIN2 AND SEPTIN6, AND HOMODIMERIZATION.
RX PubMed=16914550; DOI=10.1074/jbc.m605179200;
RA Low C., Macara I.G.;
RT "Structural analysis of septin 2, 6, and 7 complexes.";
RL J. Biol. Chem. 281:30697-30706(2006).
RN [9]
RP FUNCTION.
RX PubMed=17803907; DOI=10.1016/j.cell.2007.06.053;
RA Kremer B.E., Adang L.A., Macara I.G.;
RT "Septins regulate actin organization and cell-cycle arrest through nuclear
RT accumulation of NCK mediated by SOCS7.";
RL Cell 130:837-850(2007).
RN [10]
RP INTERACTION WITH CENPE, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=18460473; DOI=10.1074/jbc.m710591200;
RA Zhu M., Wang F., Yan F., Yao P.Y., Du J., Gao X., Wang X., Wu Q., Ward T.,
RA Li J., Kioko S., Hu R., Xie W., Ding X., Yao X.;
RT "Septin 7 interacts with centromere-associated protein E and is required
RT for its kinetochore localization.";
RL J. Biol. Chem. 283:18916-18925(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424 AND THR-426, 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 [12]
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=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 INTERACTION WITH SEPTIN9.
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334 AND THR-426, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-228; SER-334 AND THR-426, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
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 [18]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=25588830; DOI=10.1242/jcs.158998;
RA Kuo Y.C., Shen Y.R., Chen H.I., Lin Y.H., Wang Y.Y., Chen Y.R., Wang C.Y.,
RA Kuo P.L.;
RT "SEPT12 orchestrates the formation of mammalian sperm annulus by organizing
RT core octomeric complexes with other SEPT proteins.";
RL J. Cell Sci. 128:923-934(2015).
RN [19]
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 [20]
RP X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 20-437 IN COMPLEX WITH GDP, AND
RP SUBUNIT.
RX PubMed=17637674; DOI=10.1038/nature06052;
RA Sirajuddin M., Farkasovsky M., Hauer F., Kuehlmann D., Macara I.G.,
RA Weyand M., Stark H., Wittinghofer A.;
RT "Structural insight into filament formation by mammalian septins.";
RL Nature 449:311-315(2007).
CC -!- FUNCTION: Filament-forming cytoskeletal GTPase. Required for normal
CC organization of the actin cytoskeleton. Required for normal progress
CC through mitosis. Involved in cytokinesis. Required for normal
CC association of CENPE with the kinetochore. Plays a role in ciliogenesis
CC and collective cell movements. Forms a filamentous structure with
CC SEPTIN12, SEPTIN6, SEPTIN2 and probably SEPTIN4 at the sperm annulus
CC which is required for the structural integrity and motility of the
CC sperm tail during postmeiotic differentiation (PubMed:25588830).
CC {ECO:0000269|PubMed:17803907, ECO:0000269|PubMed:18460473,
CC ECO:0000305|PubMed:25588830}.
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. Filaments are assembled from asymmetrical heterotrimers,
CC composed of SEPTIN2, SEPTIN6 and SEPTIN7 that associate head-to-head to
CC form a hexameric unit. Within the trimer, directly interacts with
CC SEPTIN6, while interaction with SEPTIN2 seems indirect. In the absence
CC of SEPTIN6, forms homodimers. Interacts directly with CENPE and links
CC CENPE to septin filaments composed of SEPTIN2, SEPTIN6 and SEPTIN7.
CC Interacts with SEPTIN5 and SEPTIN8 (By similarity). Interacts with
CC SEPTIN9 and SEPTIN11. Component of a septin core octameric complex
CC consisting of SEPTIN12, SEPTIN7, SEPTIN6 and SEPTIN2 or SEPTIN4 in the
CC order 12-7-6-2-2-6-7-12 or 12-7-6-4-4-6-7-12 and located in the sperm
CC annulus; the SEPTIN12:SEPTIN7 association is mediated by the respective
CC GTP-binding domains (PubMed:25588830). {ECO:0000250,
CC ECO:0000269|PubMed:15485874, ECO:0000269|PubMed:16914550,
CC ECO:0000269|PubMed:17637674, ECO:0000269|PubMed:18460473,
CC ECO:0000269|PubMed:19145258, ECO:0000269|PubMed:25588830}.
CC -!- INTERACTION:
CC Q16181; Q8IYM1: SEPTIN12; NbExp=17; IntAct=EBI-2009373, EBI-2585067;
CC Q16181; Q14141: SEPTIN6; NbExp=3; IntAct=EBI-2009373, EBI-745901;
CC Q16181; Q16181: SEPTIN7; NbExp=2; IntAct=EBI-2009373, EBI-2009373;
CC Q16181-2; P42858: HTT; NbExp=9; IntAct=EBI-10176094, EBI-466029;
CC Q16181-2; Q04864: REL; NbExp=3; IntAct=EBI-10176094, EBI-307352;
CC Q16181-2; Q9P0V9: SEPTIN10; NbExp=6; IntAct=EBI-10176094, EBI-3943788;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18460473}.
CC Chromosome, centromere, kinetochore {ECO:0000269|PubMed:18460473}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18460473}.
CC Cleavage furrow {ECO:0000269|PubMed:18460473}. Midbody
CC {ECO:0000269|PubMed:18460473}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250}. Cell projection, cilium, flagellum
CC {ECO:0000269|PubMed:25588830}. Note=Distributed throughout the
CC cytoplasm in prometaphase cells. Associated with the spindle during
CC metaphase. Associated with the central spindle and at the cleavage
CC furrow in anaphase cells. Detected at the midbody in telophase.
CC Associated with actin stress fibers (By similarity). Found in the sperm
CC annulus (PubMed:25588830). {ECO:0000250, ECO:0000269|PubMed:25588830}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q16181-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16181-2; Sequence=VSP_022202;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15915442}.
CC -!- MISCELLANEOUS: Coordinated expression with SEPTIN2 and SEPTIN6.
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=AAB31337.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH67264.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH93640.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH93642.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; S72008; AAB31337.1; ALT_INIT; mRNA.
DR EMBL; BC067264; AAH67264.2; ALT_INIT; mRNA.
DR EMBL; BC093640; AAH93640.2; ALT_INIT; mRNA.
DR EMBL; BC093642; AAH93642.2; ALT_INIT; mRNA.
DR CCDS; CCDS94085.1; -. [Q16181-1]
DR CCDS; CCDS94086.1; -. [Q16181-2]
DR PIR; JC2352; JC2352.
DR RefSeq; NP_001779.3; NM_001788.5. [Q16181-1]
DR PDB; 2QAG; X-ray; 4.00 A; C=20-437.
DR PDB; 3T5D; X-ray; 3.30 A; A/C=48-316.
DR PDB; 3TW4; X-ray; 3.35 A; A/B=48-317.
DR PDB; 6N0B; X-ray; 1.74 A; A/B/C/D=48-318.
DR PDB; 6N12; X-ray; 2.23 A; A/B=48-318.
DR PDB; 6UQQ; X-ray; 2.75 A; A/B=48-318.
DR PDB; 7M6J; EM; 3.60 A; C/D=20-437.
DR PDBsum; 2QAG; -.
DR PDBsum; 3T5D; -.
DR PDBsum; 3TW4; -.
DR PDBsum; 6N0B; -.
DR PDBsum; 6N12; -.
DR PDBsum; 6UQQ; -.
DR PDBsum; 7M6J; -.
DR AlphaFoldDB; Q16181; -.
DR EMDB; EMD-23698; -.
DR SASBDB; Q16181; -.
DR SMR; Q16181; -.
DR BioGRID; 107425; 203.
DR CORUM; Q16181; -.
DR DIP; DIP-47093N; -.
DR IntAct; Q16181; 56.
DR MINT; Q16181; -.
DR STRING; 9606.ENSP00000413507; -.
DR GlyCosmos; Q16181; 1 site, 1 glycan.
DR GlyGen; Q16181; 6 sites, 1 O-linked glycan (6 sites).
DR iPTMnet; Q16181; -.
DR MetOSite; Q16181; -.
DR PhosphoSitePlus; Q16181; -.
DR SwissPalm; Q16181; -.
DR BioMuta; SEPT7; -.
DR DMDM; 67472677; -.
DR OGP; Q16181; -.
DR UCD-2DPAGE; Q16181; -.
DR EPD; Q16181; -.
DR jPOST; Q16181; -.
DR MassIVE; Q16181; -.
DR MaxQB; Q16181; -.
DR PaxDb; 9606-ENSP00000381992; -.
DR PeptideAtlas; Q16181; -.
DR ProteomicsDB; 60834; -. [Q16181-1]
DR ProteomicsDB; 60835; -. [Q16181-2]
DR Pumba; Q16181; -.
DR Antibodypedia; 26511; 326 antibodies from 37 providers.
DR DNASU; 989; -.
DR Ensembl; ENST00000350320.11; ENSP00000344868.8; ENSG00000122545.22. [Q16181-1]
DR Ensembl; ENST00000705486.1; ENSP00000516132.1; ENSG00000122545.22. [Q16181-2]
DR GeneID; 989; -.
DR KEGG; hsa:989; -.
DR MANE-Select; ENST00000350320.11; ENSP00000344868.8; NM_001788.6; NP_001779.3.
DR UCSC; uc011kau.2; human. [Q16181-1]
DR AGR; HGNC:1717; -.
DR CTD; 989; -.
DR DisGeNET; 989; -.
DR GeneCards; SEPTIN7; -.
DR HGNC; HGNC:1717; SEPTIN7.
DR HPA; ENSG00000122545; Low tissue specificity.
DR MIM; 603151; gene.
DR neXtProt; NX_Q16181; -.
DR OpenTargets; ENSG00000122545; -.
DR PharmGKB; PA26253; -.
DR VEuPathDB; HostDB:ENSG00000122545; -.
DR eggNOG; KOG2655; Eukaryota.
DR GeneTree; ENSGT00940000154222; -.
DR InParanoid; Q16181; -.
DR OrthoDB; 5396944at2759; -.
DR PhylomeDB; Q16181; -.
DR TreeFam; TF101079; -.
DR PathwayCommons; Q16181; -.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR SignaLink; Q16181; -.
DR SIGNOR; Q16181; -.
DR BioGRID-ORCS; 989; 38 hits in 273 CRISPR screens.
DR ChiTaRS; SEPT7; human.
DR EvolutionaryTrace; Q16181; -.
DR GeneWiki; SEPT7; -.
DR GenomeRNAi; 989; -.
DR Pharos; Q16181; Tbio.
DR PRO; PR:Q16181; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q16181; Protein.
DR Bgee; ENSG00000122545; Expressed in corpus callosum and 209 other cell types or tissues.
DR ExpressionAtlas; Q16181; baseline and differential.
DR Genevisible; Q16181; HS.
DR GO; GO:0005930; C:axoneme; IDA:GO_Central.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0097730; C:non-motile cilium; IDA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031105; C:septin complex; IDA:UniProtKB.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0097227; C:sperm annulus; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
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; TAS:ProtInc.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; TAS:ProtInc.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
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:0016476; P:regulation of embryonic cell shape; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR CDD; cd01850; CDC_Septin; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016491; Septin.
DR InterPro; IPR008115; Septin7.
DR PANTHER; PTHR18884; SEPTIN; 1.
DR PANTHER; PTHR18884:SF126; SEPTIN; 1.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR PRINTS; PR01742; SEPTIN7.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Cell projection; Centromere; Chromosome; Cilium; Coiled coil; Cytoplasm;
KW Cytoskeleton; Differentiation; Flagellum; GTP-binding; Kinetochore;
KW Mitosis; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Spermatogenesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..437
FT /note="Septin-7"
FT /id="PRO_0000173528"
FT DOMAIN 47..316
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 47..317
FT /note="Interaction with SEPTIN12"
FT /evidence="ECO:0000269|PubMed:25588830"
FT REGION 57..64
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 113..116
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 194..197
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 378..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 332..437
FT /evidence="ECO:0000255"
FT COMPBIAS 378..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 57..64
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 90
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 195..203
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 265
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 30
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O55131"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O55131"
FT MOD_RES 228
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 373
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O55131"
FT MOD_RES 424
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 426
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 21
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022202"
FT CONFLICT 271
FT /note="V -> I (in Ref. 1; AAB31337)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="L -> K (in Ref. 1; AAB31337)"
FT /evidence="ECO:0000305"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:6N0B"
FT HELIX 63..70
FT /evidence="ECO:0007829|PDB:6N0B"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:3T5D"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:6UQQ"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:6N0B"
FT STRAND 94..102
FT /evidence="ECO:0007829|PDB:6N0B"
FT STRAND 105..113
FT /evidence="ECO:0007829|PDB:6N0B"
FT TURN 115..118
FT /evidence="ECO:0007829|PDB:6N0B"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:6N12"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:6N0B"
FT HELIX 128..146
FT /evidence="ECO:0007829|PDB:6N0B"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:3TW4"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:6N0B"
FT HELIX 174..183
FT /evidence="ECO:0007829|PDB:6N0B"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:6N0B"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:6N0B"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:6N0B"
FT HELIX 201..217
FT /evidence="ECO:0007829|PDB:6N0B"
FT HELIX 240..243
FT /evidence="ECO:0007829|PDB:6N0B"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:6N0B"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:6N0B"
FT STRAND 260..267
FT /evidence="ECO:0007829|PDB:6N0B"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:6N0B"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:6N0B"
FT HELIX 282..290
FT /evidence="ECO:0007829|PDB:6N0B"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:6N12"
FT HELIX 294..303
FT /evidence="ECO:0007829|PDB:6N0B"
FT HELIX 305..315
FT /evidence="ECO:0007829|PDB:6N0B"
SQ SEQUENCE 437 AA; 50680 MW; 946A08C54B7124FF CRC64;
MSVSARSAAA EERSVNSSTM VAQQKNLEGY VGFANLPNQV YRKSVKRGFE FTLMVVGESG
LGKSTLINSL FLTDLYSPEY PGPSHRIKKT VQVEQSKVLI KEGGVQLLLT IVDTPGFGDA
VDNSNCWQPV IDYIDSKFED YLNAESRVNR RQMPDNRVQC CLYFIAPSGH GLKPLDIEFM
KRLHEKVNII PLIAKADTLT PEECQQFKKQ IMKEIQEHKI KIYEFPETDD EEENKLVKKI
KDRLPLAVVG SNTIIEVNGK RVRGRQYPWG VAEVENGEHC DFTILRNMLI RTHMQDLKDV
TNNVHYENYR SRKLAAVTYN GVDNNKNKGQ LTKSPLAQME EERREHVAKM KKMEMEMEQV
FEMKVKEKVQ KLKDSEAELQ RRHEQMKKNL EAQHKELEEK RRQFEDEKAN WEAQQRILEQ
QNSSRTLEKN KKKGKIF
//
