SEPT6_HUMAN
ID SEPT6_HUMAN Reviewed; 434 AA.
AC Q14141; Q5JTK0; Q969W5; Q96A13; Q96GR1; Q96P86; Q96P87;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Septin-6;
GN Name=SEPTIN6 {ECO:0000312|HGNC:HGNC:15848}; Synonyms=KIAA0128, SEP2, SEPT6;
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] (ISOFORMS I; II; IV AND V).
RX PubMed=11809673;
RA Ono R., Taki T., Taketani T., Kawaguchi H., Taniwaki M., Okamura T.,
RA Kawa K., Hanada R., Kobayashi M., Hayashi Y.;
RT "SEPTIN6, a human homologue to mouse Septin6, is fused to MLL in infant
RT acute myeloid leukemia with complex chromosomal abnormalities involving
RT 11q23 and Xq24.";
RL Cancer Res. 62:333-337(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS II AND V).
RC TISSUE=Muscle, Placenta, and Testis;
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 [4]
RP PROTEIN SEQUENCE OF 2-8, AND ACETYLATION AT ALA-2.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-427 (ISOFORM I).
RC TISSUE=Bone marrow;
RX PubMed=8590280; DOI=10.1093/dnares/2.4.167;
RA Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. IV. The
RT coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:167-174(1995).
RN [6]
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 [7]
RP COORDINATED EXPRESSION WITH SEPTIN2 AND SEPTIN7.
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 [8]
RP SUBCELLULAR LOCATION.
RX PubMed=15774761; DOI=10.1126/science.1106823;
RA Spiliotis E.T., Kinoshita M., Nelson W.J.;
RT "A mitotic septin scaffold required for mammalian chromosome congression
RT and segregation.";
RL Science 307:1781-1785(2005).
RN [9]
RP INTERACTION WITH SEPTIN2 AND SEPTIN7.
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 [10]
RP FUNCTION, AND INTERACTION WITH SOCS7.
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 [11]
RP INTERACTION WITH SEPTIN12.
RX PubMed=18047794; DOI=10.5483/bmbrep.2007.40.6.973;
RA Ding X., Yu W., Liu M., Shen S., Chen F., Wan B., Yu L.;
RT "SEPT12 interacts with SEPT6 and this interaction alters the filament
RT structure of SEPT6 in Hela cells.";
RL J. Biochem. Mol. Biol. 40:973-978(2007).
RN [12]
RP INTERACTION WITH HNRNPA1 AND HCV NS5B (MICROBIAL INFECTION), AND FUNCTION.
RX PubMed=17229681; DOI=10.1128/jvi.01311-06;
RA Kim C.S., Seol S.K., Song O.-K., Park J.H., Jang S.K.;
RT "An RNA-binding protein, hnRNP A1, and a scaffold protein, septin 6,
RT facilitate hepatitis C virus replication.";
RL J. Virol. 81:3852-3865(2007).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 [15]
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 [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-367, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-416 AND THR-418, 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 [19]
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 [20]
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 [21]
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 [22]
RP X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 1-427 IN COMPLEX WITH GTP,
RP ELECTRON MICROSCOPY OF SEPTIN COMPLEX, AND 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. Involved in cytokinesis. May
CC play a role in HCV RNA replication. 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:17229681, ECO:0000269|PubMed:17803907,
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 SEPTIN2 and SEPTIN7. Also interacts with SEPTIN9 and SEPTIN12.
CC Interaction with SEPTIN12 alters filament structure. Component of a
CC septin core octomeric complex consisting of SEPTIN12, SEPTIN7, SEPTIN6
CC and SEPTIN2 or SEPTIN4 in the order 12-7-6-2-2-6-7-12 or 12-7-6-4-4-6-
CC 7-12 and located in the sperm annulus. Interacts with SOCS7. Interacts
CC with HNRNPA1. {ECO:0000269|PubMed:16914550,
CC ECO:0000269|PubMed:17229681, ECO:0000269|PubMed:17637674,
CC ECO:0000269|PubMed:17803907, ECO:0000269|PubMed:18047794,
CC ECO:0000269|PubMed:19145258, ECO:0000269|PubMed:25588830}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HCV NS5B.
CC {ECO:0000269|PubMed:17229681}.
CC -!- INTERACTION:
CC Q14141; O00213-2: APBB1; NbExp=3; IntAct=EBI-745901, EBI-13307975;
CC Q14141; P21964-2: COMT; NbExp=3; IntAct=EBI-745901, EBI-10200977;
CC Q14141; P28799: GRN; NbExp=3; IntAct=EBI-745901, EBI-747754;
CC Q14141; P09651: HNRNPA1; NbExp=3; IntAct=EBI-745901, EBI-352662;
CC Q14141; P42858: HTT; NbExp=18; IntAct=EBI-745901, EBI-466029;
CC Q14141; Q92993: KAT5; NbExp=3; IntAct=EBI-745901, EBI-399080;
CC Q14141; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-745901, EBI-11742507;
CC Q14141; Q8NDC4: MORN4; NbExp=6; IntAct=EBI-745901, EBI-10269566;
CC Q14141; P04150: NR3C1; NbExp=3; IntAct=EBI-745901, EBI-493507;
CC Q14141; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-745901, EBI-742388;
CC Q14141; P17252: PRKCA; NbExp=3; IntAct=EBI-745901, EBI-1383528;
CC Q14141; A0A0S2Z5W9: SEPT9; NbExp=3; IntAct=EBI-745901, EBI-16437910;
CC Q14141; Q8WYJ6: SEPTIN1; NbExp=9; IntAct=EBI-745901, EBI-693002;
CC Q14141; Q8IYM1: SEPTIN12; NbExp=14; IntAct=EBI-745901, EBI-2585067;
CC Q14141; Q15019: SEPTIN2; NbExp=11; IntAct=EBI-745901, EBI-741220;
CC Q14141; Q9UH03: SEPTIN3; NbExp=3; IntAct=EBI-745901, EBI-727037;
CC Q14141; Q99719: SEPTIN5; NbExp=9; IntAct=EBI-745901, EBI-373345;
CC Q14141; Q16181: SEPTIN7; NbExp=3; IntAct=EBI-745901, EBI-2009373;
CC Q14141; Q9UHD8: SEPTIN9; NbExp=4; IntAct=EBI-745901, EBI-851542;
CC Q14141; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-745901, EBI-9090795;
CC Q14141; O14512-1: SOCS7; NbExp=2; IntAct=EBI-745901, EBI-1539617;
CC Q14141; P21980-2: TGM2; NbExp=3; IntAct=EBI-745901, EBI-25842075;
CC Q14141; O76024: WFS1; NbExp=3; IntAct=EBI-745901, EBI-720609;
CC Q14141; P61981: YWHAG; NbExp=3; IntAct=EBI-745901, EBI-359832;
CC Q14141; PRO_0000037577 [P27958]; Xeno; NbExp=4; IntAct=EBI-745901, EBI-6904388;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15774761}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15774761}.
CC Chromosome, centromere, kinetochore {ECO:0000269|PubMed:15774761}.
CC Cleavage furrow {ECO:0000269|PubMed:15774761}. Midbody
CC {ECO:0000269|PubMed:15774761}. Cell projection, cilium, flagellum
CC {ECO:0000269|PubMed:25588830}. Note=In metaphase cells, localized
CC within the microtubule spindle. At the metaphase plate, in close
CC apposition to the kinetochores of the congressed chromosomes. In cells
CC undergoing cytokinesis, localized to the midbody, the ingressing
CC cleavage furrow, and the central spindle. Found in the sperm annulus
CC (PubMed:25588830). {ECO:0000269|PubMed:25588830}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=II;
CC IsoId=Q14141-1; Sequence=Displayed;
CC Name=I; Synonyms=III;
CC IsoId=Q14141-2; Sequence=VSP_006053;
CC Name=IV;
CC IsoId=Q14141-3; Sequence=VSP_006051, VSP_006052;
CC Name=V;
CC IsoId=Q14141-4; Sequence=VSP_006054;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15915442}.
CC -!- MISCELLANEOUS: Coordinated expression with SEPTIN2 and SEPTIN7.
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 -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SEPTIN6ID376.html";
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DR EMBL; AF403058; AAK98547.1; -; mRNA.
DR EMBL; AF403059; AAK98548.1; -; mRNA.
DR EMBL; AF403060; AAK98549.1; -; mRNA.
DR EMBL; AF403061; AAK98550.1; -; mRNA.
DR EMBL; AF403062; AAK98551.1; -; mRNA.
DR EMBL; AC004913; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005052; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355348; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009291; AAH09291.1; -; mRNA.
DR EMBL; BC011922; AAH11922.3; -; mRNA.
DR EMBL; BC036240; AAH36240.1; -; mRNA.
DR EMBL; D50918; BAA09477.1; -; mRNA.
DR CCDS; CCDS14583.1; -. [Q14141-4]
DR CCDS; CCDS14584.1; -. [Q14141-1]
DR CCDS; CCDS14585.1; -. [Q14141-2]
DR RefSeq; NP_055944.2; NM_015129.5. [Q14141-1]
DR RefSeq; NP_665798.1; NM_145799.3. [Q14141-2]
DR RefSeq; NP_665799.1; NM_145800.3. [Q14141-2]
DR RefSeq; NP_665801.1; NM_145802.3. [Q14141-4]
DR RefSeq; XP_006724813.1; XM_006724750.2. [Q14141-2]
DR PDB; 2QAG; X-ray; 4.00 A; B=1-427.
DR PDB; 6UPA; X-ray; 2.51 A; B=40-305.
DR PDB; 6WBP; X-ray; 1.80 A; A/B=347-399.
DR PDB; 7M6J; EM; 3.60 A; B/E=1-427.
DR PDBsum; 2QAG; -.
DR PDBsum; 6UPA; -.
DR PDBsum; 6WBP; -.
DR PDBsum; 7M6J; -.
DR AlphaFoldDB; Q14141; -.
DR SMR; Q14141; -.
DR BioGRID; 116770; 63.
DR DIP; DIP-38218N; -.
DR IntAct; Q14141; 50.
DR MINT; Q14141; -.
DR STRING; 9606.ENSP00000341524; -.
DR iPTMnet; Q14141; -.
DR MetOSite; Q14141; -.
DR PhosphoSitePlus; Q14141; -.
DR SwissPalm; Q14141; -.
DR BioMuta; SEPT6; -.
DR DMDM; 20178343; -.
DR OGP; Q14141; -.
DR EPD; Q14141; -.
DR jPOST; Q14141; -.
DR MassIVE; Q14141; -.
DR MaxQB; Q14141; -.
DR PaxDb; Q14141; -.
DR PeptideAtlas; Q14141; -.
DR PRIDE; Q14141; -.
DR ProteomicsDB; 59843; -. [Q14141-1]
DR ProteomicsDB; 59844; -. [Q14141-2]
DR ProteomicsDB; 59845; -. [Q14141-3]
DR ProteomicsDB; 59846; -. [Q14141-4]
DR Antibodypedia; 465; 289 antibodies from 35 providers.
DR DNASU; 23157; -.
DR Ensembl; ENST00000343984.5; ENSP00000341524.5; ENSG00000125354.24. [Q14141-1]
DR Ensembl; ENST00000354228.8; ENSP00000346169.4; ENSG00000125354.24. [Q14141-4]
DR Ensembl; ENST00000360156.11; ENSP00000353278.7; ENSG00000125354.24. [Q14141-2]
DR Ensembl; ENST00000394610.7; ENSP00000378108.1; ENSG00000125354.24. [Q14141-2]
DR Ensembl; ENST00000460411.5; ENSP00000435818.1; ENSG00000125354.24. [Q14141-3]
DR Ensembl; ENST00000489216.5; ENSP00000418715.1; ENSG00000125354.24. [Q14141-2]
DR GeneID; 23157; -.
DR KEGG; hsa:23157; -.
DR MANE-Select; ENST00000394610.7; ENSP00000378108.1; NM_145799.4; NP_665798.1. [Q14141-2]
DR UCSC; uc004erv.4; human. [Q14141-1]
DR CTD; 23157; -.
DR DisGeNET; 23157; -.
DR GeneCards; SEPTIN6; -.
DR HGNC; HGNC:15848; SEPTIN6.
DR HPA; ENSG00000125354; Tissue enhanced (lymphoid).
DR MIM; 300683; gene.
DR neXtProt; NX_Q14141; -.
DR OpenTargets; ENSG00000125354; -.
DR PharmGKB; PA134941944; -.
DR VEuPathDB; HostDB:ENSG00000125354; -.
DR eggNOG; KOG3859; Eukaryota.
DR GeneTree; ENSGT00940000158026; -.
DR HOGENOM; CLU_017718_8_1_1; -.
DR InParanoid; Q14141; -.
DR OMA; TSEGWAI; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; Q14141; -.
DR TreeFam; TF101080; -.
DR PathwayCommons; Q14141; -.
DR SignaLink; Q14141; -.
DR SIGNOR; Q14141; -.
DR BioGRID-ORCS; 23157; 10 hits in 644 CRISPR screens.
DR ChiTaRS; SEPT6; human.
DR EvolutionaryTrace; Q14141; -.
DR GeneWiki; SEPT6; -.
DR GenomeRNAi; 23157; -.
DR Pharos; Q14141; Tbio.
DR PRO; PR:Q14141; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q14141; protein.
DR Bgee; ENSG00000125354; Expressed in thymus and 198 other tissues.
DR ExpressionAtlas; Q14141; baseline and differential.
DR Genevisible; Q14141; HS.
DR GO; GO:0043679; C:axon terminus; IEA:Ensembl.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
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:0032173; C:septin collar; IEA:Ensembl.
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:0008021; C:synaptic vesicle; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; TAS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0000281; P:mitotic cytokinesis; TAS:UniProtKB.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
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; IPR030644; SEPT6.
DR InterPro; IPR016491; Septin.
DR PANTHER; PTHR18884:SF55; PTHR18884:SF55; 1.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; 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 Cell projection; Centromere; Chromosome; Cilium; Coiled coil; Cytoplasm;
KW Cytoskeleton; Differentiation; Direct protein sequencing; Flagellum;
KW GTP-binding; Host-virus interaction; Kinetochore; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Spermatogenesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0007744|PubMed:19413330"
FT CHAIN 2..434
FT /note="Septin-6"
FT /id="PRO_0000173525"
FT DOMAIN 39..305
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 49..56
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 101..104
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 184..187
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 405..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 321..409
FT /evidence="ECO:0000255"
FT COMPBIAS 418..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 49..56
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:17637674"
FT BINDING 104
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 185..193
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:17637674"
FT BINDING 239
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 254
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0007744|PubMed:19413330"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 367
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 418
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 263..267
FT /note="VENEA -> AAREV (in isoform IV)"
FT /evidence="ECO:0000303|PubMed:11809673"
FT /id="VSP_006051"
FT VAR_SEQ 268..434
FT /note="Missing (in isoform IV)"
FT /evidence="ECO:0000303|PubMed:11809673"
FT /id="VSP_006052"
FT VAR_SEQ 428..434
FT /note="Missing (in isoform I)"
FT /evidence="ECO:0000303|PubMed:11809673,
FT ECO:0000303|PubMed:8590280"
FT /id="VSP_006053"
FT VAR_SEQ 428..434
FT /note="NPWLCTE -> FF (in isoform V)"
FT /evidence="ECO:0000303|PubMed:11809673,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_006054"
FT CONFLICT 406
FT /note="L -> P (in Ref. 3; AAH09291)"
FT /evidence="ECO:0000305"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:6UPA"
FT HELIX 55..63
FT /evidence="ECO:0007829|PDB:6UPA"
FT STRAND 80..87
FT /evidence="ECO:0007829|PDB:6UPA"
FT STRAND 96..104
FT /evidence="ECO:0007829|PDB:6UPA"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:6UPA"
FT HELIX 115..133
FT /evidence="ECO:0007829|PDB:6UPA"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:6UPA"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:6UPA"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:6UPA"
FT HELIX 164..172
FT /evidence="ECO:0007829|PDB:6UPA"
FT TURN 173..176
FT /evidence="ECO:0007829|PDB:6UPA"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:6UPA"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:6UPA"
FT HELIX 191..207
FT /evidence="ECO:0007829|PDB:6UPA"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:6UPA"
FT HELIX 223..231
FT /evidence="ECO:0007829|PDB:6UPA"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:6UPA"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:6UPA"
FT STRAND 249..256
FT /evidence="ECO:0007829|PDB:6UPA"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:6UPA"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:6UPA"
FT HELIX 271..275
FT /evidence="ECO:0007829|PDB:6UPA"
FT HELIX 280..292
FT /evidence="ECO:0007829|PDB:6UPA"
FT HELIX 294..304
FT /evidence="ECO:0007829|PDB:6UPA"
FT HELIX 347..396
FT /evidence="ECO:0007829|PDB:6WBP"
SQ SEQUENCE 434 AA; 49717 MW; E684AE6A93B32362 CRC64;
MAATDIARQV GEGCRTVPLA GHVGFDSLPD QLVNKSVSQG FCFNILCVGE TGLGKSTLMD
TLFNTKFEGE PATHTQPGVQ LQSNTYDLQE SNVRLKLTIV STVGFGDQIN KEDSYKPIVE
FIDAQFEAYL QEELKIRRVL HTYHDSRIHV CLYFIAPTGH SLKSLDLVTM KKLDSKVNII
PIIAKADAIS KSELTKFKIK ITSELVSNGV QIYQFPTDDE SVAEINGTMN AHLPFAVIGS
TEELKIGNKM MRARQYPWGT VQVENEAHCD FVKLREMLIR VNMEDLREQT HTRHYELYRR
CKLEEMGFKD TDPDSKPFSL QETYEAKRNE FLGELQKKEE EMRQMFVQRV KEKEAELKEA
EKELHEKFDR LKKLHQDEKK KLEDKKKSLD DEVNAFKQRK TAAELLQSQG SQAGGSQTLK
RDKEKKNNPW LCTE
