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Q9QZR6

- SEPT9_RAT

UniProt

Q9QZR6 - SEPT9_RAT

Protein

Septin-9

Gene

Sept9

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Filament-forming cytoskeletal GTPase By similarity. May play a role in cytokinesis Potential.By similarityCurated

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei319 – 3191GTPBy similarity
    Binding sitei345 – 3451GTP; via amide nitrogenBy similarity
    Binding sitei480 – 4801GTP; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei495 – 4951GTPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi285 – 2928GTPBy similarity
    Nucleotide bindingi425 – 4339GTPBy similarity

    GO - Molecular functioni

    1. GTP binding Source: UniProtKB-KW

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cell division Source: UniProtKB-KW

    Keywords - Biological processi

    Cell cycle, Cell division

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Septin-9
    Alternative name(s):
    Eighth septin
    Eseptin
    Septin-like protein
    Short name:
    SLP
    Gene namesi
    Name:Sept9
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi708523. Sept9.

    Subcellular locationi

    Cytoplasmcytoskeleton 2 Publications
    Note: In embryonic fibroblasts, associated with actin stress fibers. No apparent co-distribution with microtubules, but some colocalization with vimentin filaments in the perinuclear region.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. cytoskeleton Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi288 – 2881G → V: Abolishes the GTP binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 564564Septin-9PRO_0000173537Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei12 – 121PhosphoserineBy similarity
    Modified residuei24 – 241PhosphothreonineBy similarity
    Modified residuei44 – 441N6-acetyllysineBy similarity
    Modified residuei64 – 641PhosphoserineBy similarity
    Modified residuei67 – 671Phosphoserine1 Publication
    Modified residuei125 – 1251PhosphothreonineBy similarity
    Modified residuei258 – 2581PhosphotyrosineBy similarity
    Modified residuei307 – 3071PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiQ9QZR6.
    PRIDEiQ9QZR6.

    PTM databases

    PhosphoSiteiQ9QZR6.

    Expressioni

    Tissue specificityi

    Expressed in the brain, mainly in the perikarya and processes of astrocytes in the cerebellum, dentate gyrus and corpus callosum (at protein level). In the sciatic nerve, highly expressed in Schwann cells (at protein level). Isoforms are differentially expressed in testes, kidney, liver, heart, spleen and brain. Undetectable in skeletal muscle.3 Publications

    Gene expression databases

    GenevestigatoriQ9QZR6.

    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. Interacts with SEPT2, SEPT6, SEPT7, SEPT11 and SEPT14. Interacts with RTKN and ARHGEF18 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi249831. 1 interaction.
    IntActiQ9QZR6. 4 interactions.
    MINTiMINT-4567142.
    STRINGi10116.ENSRNOP00000010365.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9QZR6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini275 – 546272Septin-type GAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG5019.
    HOGENOMiHOG000233586.
    HOVERGENiHBG098529.
    InParanoidiQ9QZR6.
    KOiK16938.
    PhylomeDBiQ9QZR6.

    Family and domain databases

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

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9QZR6-1) [UniParc]FASTAAdd to Basket

    Also known as: SLP-a

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MERDRITALK RSFEVEEIEP PNSTPPRRVQ TPLLRATVAS SSQKFQDLGV    50
    KNSEPAARLV DTLSQRSPKP SLRRVDLAGA KAPEPMSRRT ELSIDISSKQ 100
    VESTASTPGP SRFGLKRAEV LGHKTPEPVP RRTEITIVKP QESGLRRVET 150
    PASKAPEGSA MPVTDAAPKR VEIQVPKPAE APNCPLPPQT LENSEAPMSQ 200
    LQSRLEPRPP VTEVPYRNQE DSEVAPSCVV DMADNPRDAM LKQAPVSRNE 250
    KAPVDFGYVG IDSILEQMRR KAMKQGFEFN IMVVGQSGLG KSTLINTLFK 300
    SKISRKSVQP ISEERIPKTI EIKSITHDIE EKGVRMKLTV IDTPGFGDHI 350
    NNENCWQPIM KFINDQYEKY LQEEVNINRK KRIPDTRVHC CLYFIPATGH 400
    SLRPLDIEFM KRLSKVVNIV PVIAKADTLT LEERVYFKQR ITSDLLSNGI 450
    DVYPQKEFDE AEDRLVNEKF REMIPFAVVG SDHEYQVNGK RILGRKTKWG 500
    TIEVENTTHC EFAYLRDLLI RTHMQNIKDI TSNIHFEAYR VKRLNEGNSA 550
    MANGIEKEPE TQEM 564
    Length:564
    Mass (Da):63,792
    Last modified:May 1, 2000 - v1
    Checksum:iB45160157F986C0C
    GO
    Isoform 2 (identifier: Q9QZR6-2) [UniParc]FASTAAdd to Basket

    Also known as: SLP-b

    The sequence of this isoform differs from the canonical sequence as follows:
         1-85: Missing.

    Show »
    Length:479
    Mass (Da):54,389
    Checksum:i60936B32230625BD
    GO
    Isoform 3 (identifier: Q9QZR6-3) [UniParc]FASTAAdd to Basket

    Also known as: E-septin long form

    The sequence of this isoform differs from the canonical sequence as follows:
         1-160: Missing.

    Show »
    Length:404
    Mass (Da):46,282
    Checksum:i7C81BC3E3F45859F
    GO
    Isoform 4 (identifier: Q9QZR6-4) [UniParc]FASTAAdd to Basket

    Also known as: E-septin short form

    The sequence of this isoform differs from the canonical sequence as follows:
         1-231: Missing.

    Show »
    Length:333
    Mass (Da):38,524
    Checksum:i02941CFB5584A557
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti230 – 2301V → G in AAF01206. (PubMed:10371165)Curated
    Sequence conflicti460 – 4601E → ED in AAF01206. (PubMed:10371165)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 231231Missing in isoform 4. 1 PublicationVSP_012343Add
    BLAST
    Alternative sequencei1 – 160160Missing in isoform 3. 1 PublicationVSP_012344Add
    BLAST
    Alternative sequencei1 – 8585Missing in isoform 2. 1 PublicationVSP_012345Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF180525 mRNA. Translation: AAF01206.1.
    AF180526 mRNA. Translation: AAF01207.1.
    AF170253 mRNA. Translation: AAF03376.1.
    AF173899 mRNA. Translation: AAF03391.1.
    PIRiJC7365.
    RefSeqiNP_001106969.1. NM_001113497.1.
    NP_114025.2. NM_031837.2.
    NP_789826.2. NM_176856.2.
    UniGeneiRn.91127.

    Genome annotation databases

    GeneIDi83788.
    KEGGirno:83788.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF180525 mRNA. Translation: AAF01206.1 .
    AF180526 mRNA. Translation: AAF01207.1 .
    AF170253 mRNA. Translation: AAF03376.1 .
    AF173899 mRNA. Translation: AAF03391.1 .
    PIRi JC7365.
    RefSeqi NP_001106969.1. NM_001113497.1.
    NP_114025.2. NM_031837.2.
    NP_789826.2. NM_176856.2.
    UniGenei Rn.91127.

    3D structure databases

    ProteinModelPortali Q9QZR6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 249831. 1 interaction.
    IntActi Q9QZR6. 4 interactions.
    MINTi MINT-4567142.
    STRINGi 10116.ENSRNOP00000010365.

    Chemistry

    ChEMBLi CHEMBL2176803.

    PTM databases

    PhosphoSitei Q9QZR6.

    Proteomic databases

    PaxDbi Q9QZR6.
    PRIDEi Q9QZR6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 83788.
    KEGGi rno:83788.

    Organism-specific databases

    CTDi 10801.
    RGDi 708523. Sept9.

    Phylogenomic databases

    eggNOGi COG5019.
    HOGENOMi HOG000233586.
    HOVERGENi HBG098529.
    InParanoidi Q9QZR6.
    KOi K16938.
    PhylomeDBi Q9QZR6.

    Miscellaneous databases

    NextBioi 616359.

    Gene expression databases

    Genevestigatori Q9QZR6.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR000038. Cell_div_GTP-bd.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    PANTHERi PTHR18884. PTHR18884. 1 hit.
    Pfami PF00735. Septin. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    PROSITEi PS51719. G_SEPTIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a novel alternatively spliced septin."
      Fung E.T., Scheller R.H.
      FEBS Lett. 451:203-208(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), TISSUE SPECIFICITY, ALTERNATIVE SPLICING, MUTAGENESIS OF GLY-288.
      Tissue: Brain.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ALTERNATIVE SPLICING.
      Tissue: Mesangial cell.
    3. Lubec G., Kang S.U.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 292-300, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Brain.
    4. "Biochemical and cell biological analyses of a mammalian septin complex, Sept7/9b/11."
      Nagata K., Asano T., Nozawa Y., Inagaki M.
      J. Biol. Chem. 279:55895-55904(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SEPT7.
    5. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
      Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
      Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, 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: TISSUE SPECIFICITY.
    7. "Characterization of a SEPT9 interacting protein, SEPT14, a novel testis-specific septin."
      Peterson E.A., Kalikin L.M., Steels J.D., Estey M.P., Trimble W.S., Petty E.M.
      Mamm. Genome 18:796-807(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SEPT14.

    Entry informationi

    Entry nameiSEPT9_RAT
    AccessioniPrimary (citable) accession number: Q9QZR6
    Secondary accession number(s): Q9QZJ7, Q9QZJ8, Q9QZP9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 21, 2004
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 98 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3