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Database: UniProt
Entry: G3V1Q4_HUMAN
LinkDB: G3V1Q4_HUMAN
Original site: G3V1Q4_HUMAN 
ID   G3V1Q4_HUMAN            Unreviewed;       401 AA.
AC   G3V1Q4;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 2.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=Septin {ECO:0000256|PIRNR:PIRNR006698};
GN   Name=SEPTIN7 {ECO:0000313|Ensembl:ENSP00000413507.2};
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 {ECO:0000313|Ensembl:ENSP00000413507.2, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000413507.2, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [2] {ECO:0007829|PubMed:15592455}
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   [3] {ECO:0007829|PubMed:17081983}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [4] {ECO:0007829|PubMed:18669648}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [5] {ECO:0007829|PubMed:19413330}
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   [6] {ECO:0007829|PubMed:20068231}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [7] {ECO:0007829|PubMed:21269460}
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., Burckstummer 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   [8] {ECO:0007829|PubMed:23186163}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=23186163;
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   [9] {ECO:0007829|PubMed:24275569}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [10] {ECO:0007829|PubMed:25944712}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712;
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   [11] {ECO:0000313|Ensembl:ENSP00000413507.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Filament-forming cytoskeletal GTPase.
CC       {ECO:0000256|PIRNR:PIRNR006698}.
CC   -!- SUBUNIT: Septins polymerize into heterooligomeric protein complexes
CC       that form filaments. {ECO:0000256|PIRNR:PIRNR006698}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum
CC       {ECO:0000256|ARBA:ARBA00004230}. Chromosome, centromere, kinetochore
CC       {ECO:0000256|ARBA:ARBA00004629}. Cytoplasm, cytoskeleton, cilium
CC       axoneme {ECO:0000256|ARBA:ARBA00004430}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC       GTPase superfamily. Septin GTPase family.
CC       {ECO:0000256|PIRNR:PIRNR006698, ECO:0000256|RuleBase:RU004560}.
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DR   EMBL; AC007551; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC087072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001229885.1; NM_001242956.1.
DR   AlphaFoldDB; G3V1Q4; -.
DR   SMR; G3V1Q4; -.
DR   EPD; G3V1Q4; -.
DR   MassIVE; G3V1Q4; -.
DR   PeptideAtlas; G3V1Q4; -.
DR   ProteomicsDB; 32405; -.
DR   Antibodypedia; 26511; 326 antibodies from 37 providers.
DR   DNASU; 989; -.
DR   Ensembl; ENST00000435235.6; ENSP00000413507.2; ENSG00000122545.22.
DR   GeneID; 989; -.
DR   UCSC; uc064ctx.1; human.
DR   CTD; 989; -.
DR   HGNC; HGNC:1717; SEPTIN7.
DR   VEuPathDB; HostDB:ENSG00000122545; -.
DR   GeneTree; ENSGT00940000154222; -.
DR   OrthoDB; 5396944at2759; -.
DR   BioGRID-ORCS; 989; 38 hits in 273 CRISPR screens.
DR   GenomeRNAi; 989; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   Bgee; ENSG00000122545; Expressed in corpus callosum and 209 other cell types or tissues.
DR   ExpressionAtlas; G3V1Q4; baseline and differential.
DR   GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR   GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR   GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0031105; C:septin complex; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
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:SF129; SEPTIN-7; 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   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell projection {ECO:0000256|ARBA:ARBA00023069};
KW   Centromere {ECO:0000256|ARBA:ARBA00023328};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Cilium {ECO:0000256|ARBA:ARBA00023069};
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR006698};
KW   Cytoskeleton {ECO:0000256|PIRNR:PIRNR006698};
KW   Differentiation {ECO:0000256|ARBA:ARBA00022871};
KW   Flagellum {ECO:0000256|ARBA:ARBA00022846};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|RuleBase:RU004560};
KW   Kinetochore {ECO:0000256|ARBA:ARBA00022838};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004560};
KW   Proteomics identification {ECO:0007829|EPD:G3V1Q4,
KW   ECO:0007829|MaxQB:G3V1Q4};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Spermatogenesis {ECO:0000256|ARBA:ARBA00022871}.
FT   DOMAIN          11..280
FT                   /note="Septin-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51719"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          342..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..377
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   401 AA;  46566 MW;  3B79676A684FE210 CRC64;
     MSVSARSAAA EERSVNSSTM GESGLGKSTL INSLFLTDLY SPEYPGPSHR IKKTVQVEQS
     KVLIKEGGVQ LLLTIVDTPG FGDAVDNSNC WQPVIDYIDS KFEDYLNAES RVNRRQMPDN
     RVQCCLYFIA PSGHGLKPLD IEFMKRLHEK VNIIPLIAKA DTLTPEECQQ FKKQIMKEIQ
     EHKIKIYEFP ETDDEEENKL VKKIKDRLPL AVVGSNTIIE VNGKRVRGRQ YPWGVAEVEN
     GEHCDFTILR NMLIRTHMQD LKDVTNNVHY ENYRSRKLAA VTYNGVDNNK NKGQLTKSPL
     AQMEEERREH VAKMKKMEME MEQVFEMKVK EKVQKLKDSE AELQRRHEQM KKNLEAQHKE
     LEEKRRQFED EKANWEAQQR ILEQQNSSRT LEKNKKKGKI F
//
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