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SEPT7_HUMAN
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   03-AUG-2022, entry version 201.
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 octomeric 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   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   SMR; Q16181; -.
DR   BioGRID; 107425; 166.
DR   CORUM; Q16181; -.
DR   DIP; DIP-47093N; -.
DR   IntAct; Q16181; 52.
DR   MINT; Q16181; -.
DR   STRING; 9606.ENSP00000381992; -.
DR   GlyGen; Q16181; 1 site, 1 O-linked glycan (1 site).
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; Q16181; -.
DR   PeptideAtlas; Q16181; -.
DR   PRIDE; Q16181; -.
DR   ProteomicsDB; 60834; -. [Q16181-1]
DR   ProteomicsDB; 60835; -. [Q16181-2]
DR   Antibodypedia; 26511; 297 antibodies from 37 providers.
DR   DNASU; 989; -.
DR   Ensembl; ENST00000350320.11; ENSP00000344868.8; ENSG00000122545.21. [Q16181-1]
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   CTD; 989; -.
DR   DisGeNET; 989; -.
DR   GeneCards; SEPTIN7; -.
DR   HGNC; HGNC:1717; SEPTIN7.
DR   HPA; ENSG00000122545; Tissue enhanced (brain).
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; 845354at2759; -.
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; 32 hits in 213 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 207 other 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:0008104; P:protein localization; IBA: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; -; 1.
DR   InterPro; IPR030379; G_SEPTIN_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR016491; Septin.
DR   InterPro; IPR008115; Septin7.
DR   Pfam; PF00735; Septin; 1.
DR   PIRSF; PIRSF006698; Septin; 1.
DR   PRINTS; PR01742; SEPTIN7.
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; 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
 
 
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