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O55131

- SEPT7_MOUSE

UniProt

O55131 - SEPT7_MOUSE

Protein

Septin-7

Gene

Sept7

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
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    Functioni

    Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Required for normal progress through mitosis. Involved in cytokinesis. Required for normal association of CENPE with the kinetochore. Plays a role in ciliogenesis and collective cell movements By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei89 – 891GTPBy similarity
    Binding sitei115 – 1151GTP; via amide nitrogenBy similarity
    Binding sitei249 – 2491GTP; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei264 – 2641GTPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi56 – 638GTPBy similarity
    Nucleotide bindingi194 – 2029GTPBy similarity

    GO - Molecular functioni

    1. GTP binding Source: UniProtKB-KW
    2. protein binding Source: MGI

    GO - Biological processi

    1. cilium morphogenesis Source: UniProtKB
    2. mitotic nuclear division Source: UniProtKB-KW
    3. protein heterooligomerization Source: Ensembl
    4. regulation of embryonic cell shape Source: UniProtKB

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Septin-7
    Alternative name(s):
    CDC10 protein homolog
    Gene namesi
    Name:Sept7
    Synonyms:Cdc10
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:1335094. Sept7.

    Subcellular locationi

    Cytoplasm 1 Publication. Chromosomecentromerekinetochore By similarity. Cytoplasmcytoskeletonspindle By similarity. Cleavage furrow By similarity. Midbody By similarity. Cytoplasmcytoskeletoncilium axoneme By similarity
    Note: Distributed throughout the cytoplasm in prometaphase cells. Associated with the spindle during metaphase. Associated with the central spindle and at the cleavage furrow in anaphase cells. Detected at the midbody in telophase By similarity. Associated with actin stress fibers By similarity.By similarity

    GO - Cellular componenti

    1. axoneme Source: UniProtKB
    2. axon terminus Source: MGI
    3. cell cortex Source: MGI
    4. cleavage furrow Source: UniProtKB-SubCell
    5. condensed chromosome kinetochore Source: UniProtKB-SubCell
    6. midbody Source: UniProtKB-SubCell
    7. nucleolus Source: Ensembl
    8. plasma membrane Source: Ensembl
    9. septin complex Source: InterPro
    10. spindle Source: UniProtKB-SubCell
    11. stress fiber Source: Ensembl
    12. synapse Source: MGI

    Keywords - Cellular componenti

    Cell projection, Centromere, Chromosome, Cilium, Cytoplasm, Cytoskeleton, Kinetochore

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 436435Septin-7PRO_0000173529Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei29 – 291Phosphotyrosine1 Publication
    Modified residuei333 – 3331PhosphoserineBy similarity
    Modified residuei372 – 3721N6-acetyllysine1 Publication
    Modified residuei423 – 4231PhosphoserineBy similarity
    Modified residuei425 – 4251PhosphothreonineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO55131.
    PaxDbiO55131.
    PRIDEiO55131.

    PTM databases

    PhosphoSiteiO55131.

    Expressioni

    Gene expression databases

    ArrayExpressiO55131.
    BgeeiO55131.
    CleanExiMM_SEPT7.
    GenevestigatoriO55131.

    Interactioni

    Subunit structurei

    Septins polymerize into heterooligomeric protein complexes that form filaments, and associate with cellular membranes, actin filaments and microtubules. GTPase activity is required for filament formation. Filaments are assembled from asymmetrical heterotrimers, composed of SEPT2, SEPT6 and SEPT7 that associate head-to-head to form a hexameric unit. Within the trimer, directly interacts with SEPT6, while interaction with SEPT2 seems indirect. In the absence of SEPT6, forms homodimers. Interacts directly with CENPE and links CENPE to septin filaments composed of SEPT2, SEPT6 and SEPT7. Interacts with SEPT5, SEPT8, SEPT9 and SEPT11 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi231619. 4 interactions.
    IntActiO55131. 5 interactions.
    MINTiMINT-1865824.

    Structurei

    3D structure databases

    ProteinModelPortaliO55131.
    SMRiO55131. Positions 48-315.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini46 – 315270Septin-type GAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili331 – 436106Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG5019.
    HOGENOMiHOG000233586.
    HOVERGENiHBG065093.
    KOiK16944.
    PhylomeDBiO55131.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR000038. Cell_div_GTP-bd.
    IPR027417. P-loop_NTPase.
    IPR016491. Septin.
    IPR008115. Septin7.
    [Graphical view]
    PANTHERiPTHR18884. PTHR18884. 1 hit.
    PfamiPF00735. Septin. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006698. Septin. 1 hit.
    PRINTSiPR01742. SEPTIN7.
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS51719. G_SEPTIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O55131-1 [UniParc]FASTAAdd to Basket

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    MSVSARSAAA EERSVNCGTM AQPKNLEGYV GFANLPNQVY RKSVKRGFEF    50
    TLMVVGESGL GKSTLINSLF LTDLYSPEYP GPSHRIKKTV QVEQSKVLIK 100
    EGGVQLLLTI VDTPGFGDAV DNSNCWQPVI DYIDSKFEDY LNAESRVNRR 150
    QMPDNRVQCC LYFIAPSGHG LKPLDIEFMK RLHEKVNIIP LIAKADTLTP 200
    EECQQFKKQI MKEIQEHKIK IYEFPETDDE EENKLVKKIK DRLPLAVVGS 250
    NTIIEVNGKR VRGRQYPWGV AEVENGEHCD FTILRNMLIR THMQDLKDVT 300
    NNVHYENYRS RKLAAVTYNG VDNNKNKGQL TKSPLAQMEE ERREHVAKMK 350
    KMEMEMEQVF EMKVKEKVQK LKDSEAELQR RHEQMKKNLE AQHKELEEKR 400
    RQFEEEKANW EAQQRILEQQ NSSRTLEKNK KKGKIF 436
    Length:436
    Mass (Da):50,550
    Last modified:June 1, 1998 - v1
    Checksum:i1028CCF14023059C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ223782
    , AJ223783, AJ223784, AJ223785, AJ223786, AJ223787, AJ223788, AJ223789, AJ223790, AJ223791, AJ223792, AJ223793, AJ223794 Genomic DNA. Translation: CAA11547.1.
    BC058587 mRNA. Translation: AAH58587.1.
    RefSeqiNP_001192296.1. NM_001205367.1.
    UniGeneiMm.270259.

    Genome annotation databases

    GeneIDi235072.
    KEGGimmu:235072.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ223782
    , AJ223783 , AJ223784 , AJ223785 , AJ223786 , AJ223787 , AJ223788 , AJ223789 , AJ223790 , AJ223791 , AJ223792 , AJ223793 , AJ223794 Genomic DNA. Translation: CAA11547.1 .
    BC058587 mRNA. Translation: AAH58587.1 .
    RefSeqi NP_001192296.1. NM_001205367.1.
    UniGenei Mm.270259.

    3D structure databases

    ProteinModelPortali O55131.
    SMRi O55131. Positions 48-315.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 231619. 4 interactions.
    IntActi O55131. 5 interactions.
    MINTi MINT-1865824.

    PTM databases

    PhosphoSitei O55131.

    Proteomic databases

    MaxQBi O55131.
    PaxDbi O55131.
    PRIDEi O55131.

    Protocols and materials databases

    DNASUi 235072.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 235072.
    KEGGi mmu:235072.

    Organism-specific databases

    CTDi 989.
    MGIi MGI:1335094. Sept7.

    Phylogenomic databases

    eggNOGi COG5019.
    HOGENOMi HOG000233586.
    HOVERGENi HBG065093.
    KOi K16944.
    PhylomeDBi O55131.

    Miscellaneous databases

    ChiTaRSi SEPT7. mouse.
    NextBioi 382505.
    PROi O55131.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O55131.
    Bgeei O55131.
    CleanExi MM_SEPT7.
    Genevestigatori O55131.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR000038. Cell_div_GTP-bd.
    IPR027417. P-loop_NTPase.
    IPR016491. Septin.
    IPR008115. Septin7.
    [Graphical view ]
    PANTHERi PTHR18884. PTHR18884. 1 hit.
    Pfami PF00735. Septin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF006698. Septin. 1 hit.
    PRINTSi PR01742. SEPTIN7.
    SUPFAMi SSF52540. SSF52540. 1 hit.
    PROSITEi PS51719. G_SEPTIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of murine CDC10 cDNA, gene organization and expression analysis."
      Soulier S., Vilotte J.-L.
      Biochim. Biophys. Acta 1442:339-346(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Strain: BALB/c.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Colon.
    3. Lubec G., Kang S.U., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 25-41; 63-95; 137-146; 186-207; 221-234; 298-309; 333-342 AND 416-424, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6 and OF1.
      Tissue: Brain and Hippocampus.
    4. "The septin CDCrel-1 is dispensable for normal development and neurotransmitter release."
      Peng X.-R., Jia Z., Zhang Y., Ware J., Trimble W.S.
      Mol. Cell. Biol. 22:378-387(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SEPT2 AND SEPT5.
    5. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. "SEPT9 sequence alternations causing hereditary neuralgic amyotrophy are associated with altered interactions with SEPT4/SEPT11 and resistance to Rho/Rhotekin-signaling."
      Sudo K., Ito H., Iwamoto I., Morishita R., Asano T., Nagata K.
      Hum. Mutat. 28:1005-1013(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
      Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
      Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain cortex.
    8. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
      Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
      J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    9. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-372, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiSEPT7_MOUSE
    AccessioniPrimary (citable) accession number: O55131
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 125 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Coordinated expression with SEPT2 and SEPT6.By similarity

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3