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Q9R1T4

- SEPT6_MOUSE

UniProt

Q9R1T4 - SEPT6_MOUSE

Protein

Septin-6

Gene

Sept6

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Involved in cytokinesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei104 – 1041GTP; via amide nitrogenBy similarity
    Binding sitei239 – 2391GTP; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei254 – 2541GTPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi49 – 568GTPBy similarity
    Nucleotide bindingi185 – 1939GTPBy 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-6
    Gene namesi
    Name:Sept6
    Synonyms:Kiaa0128
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:1888939. Sept6.

    Subcellular locationi

    Cytoplasm. Cytoplasmcytoskeletonspindle. Chromosomecentromerekinetochore By similarity. Cleavage furrow By similarity. Midbody By similarity
    Note: In metaphase cells, localized within the microtubule spindle. At the metaphase plate, in close apposition to the kinetochores of the congressed chromosomes. In cells undergoing cytokinesis, localized to the midbody, the ingressing cleavage furrow, and the central spindle By similarity.By similarity

    GO - Cellular componenti

    1. axon terminus Source: MGI
    2. cleavage furrow Source: UniProtKB-SubCell
    3. condensed chromosome kinetochore Source: UniProtKB-SubCell
    4. midbody Source: UniProtKB-SubCell
    5. septin complex Source: InterPro
    6. spindle Source: UniProtKB-SubCell
    7. synaptic vesicle Source: MGI

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 434433Septin-6PRO_0000173526Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei367 – 3671N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9R1T4.
    PaxDbiQ9R1T4.
    PRIDEiQ9R1T4.

    PTM databases

    PhosphoSiteiQ9R1T4.

    Expressioni

    Tissue specificityi

    Associated with synaptic vesicles in various brain regions, including glomeruli of the olfactory bulb.1 Publication

    Gene expression databases

    ArrayExpressiQ9R1T4.
    BgeeiQ9R1T4.
    CleanExiMM_SEPT6.
    GenevestigatoriQ9R1T4.

    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 SEPT2 and SEPT7. Also interacts with SEPT9 and SEPT12. Interaction with SEPT12 alters filament structure. Interacts with SOCS7. Interacts with HNRNPA1 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi208037. 4 interactions.
    IntActiQ9R1T4. 3 interactions.
    MINTiMINT-4134187.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9R1T4.
    SMRiQ9R1T4. Positions 41-307.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini39 – 305267Septin-type GAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili321 – 40787Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG5019.
    GeneTreeiENSGT00640000091237.
    HOVERGENiHBG065093.
    InParanoidiQ9R1T4.
    KOiK16939.
    OMAiNHGFCFN.
    OrthoDBiEOG7J9VQK.
    PhylomeDBiQ9R1T4.
    TreeFamiTF101080.

    Family and domain databases

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

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform II (identifier: Q9R1T4-1) [UniParc]FASTAAdd to Basket

    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

    MAAADIARQV GEDCRTVPLA GHVGFDSLPD QLVNKSVSQG FCFNILCVGE    50
    TGLGKSTLMD TLFNTKFEGE PATHTQPGVQ LQSNTYDLQE SNVGLKLTIV 100
    STVGFGDQIN KEDSYKPIVE FIDAQFEAYL QEELKIRRVL HSYHDSRIHV 150
    CLYFIAPTGH SLKSLDLVTM KKLDSKVNII PVIAKSDAIS KSELAKFKIK 200
    ITSELVSNGV QIYQFPTDDE SVSEINGTMN AHLPFAVVGS TEEVKIGNKM 250
    MRARQYPWGT VQVENEAHCD FVKLREMLIR VNMEDLREQT HARHYELYRR 300
    CKLEEMGFKD TDPDSKPFSL QETYEAKRNE FLGELQKKEE EMRQMFVQRV 350
    KEKEAELKEA EKELHEKFDR LKKLHQEEKK KLEDKKKCLD EEMNAFKQRK 400
    AAAELLQSQG SQAGGSQTLK RDKEKKNNPW LCIE 434
    Length:434
    Mass (Da):49,620
    Last modified:January 23, 2007 - v4
    Checksum:i33DCD4F44607168A
    GO
    Isoform I (identifier: Q9R1T4-2) [UniParc]FASTAAdd to Basket

    Also known as: III

    The sequence of this isoform differs from the canonical sequence as follows:
         428-434: Missing.

    Show »
    Length:427
    Mass (Da):48,764
    Checksum:i6A6315BB1E6B24C4
    GO
    Isoform V (identifier: Q9R1T4-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         428-434: NPWLCIE → FF

    Show »
    Length:429
    Mass (Da):49,058
    Checksum:i59BB0A6315BB1E6B
    GO

    Sequence cautioni

    The sequence BAD32172.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAM19782.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti10 – 101V → L in BAB28516. (PubMed:16141072)Curated
    Sequence conflicti10 – 101Missing in BAC33342. (PubMed:16141072)Curated
    Sequence conflicti62 – 621L → P in BAC40335. (PubMed:16141072)Curated
    Sequence conflicti141 – 1411H → Y in BAA82838. 1 PublicationCurated
    Sequence conflicti170 – 1701M → I in BAE36069. (PubMed:16141072)Curated
    Sequence conflicti238 – 2392VG → C in BAB28516. (PubMed:16141072)Curated
    Sequence conflicti350 – 3501V → A in BAC40335. (PubMed:16141072)Curated
    Sequence conflicti403 – 4031A → R in BAA82838. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei428 – 4347Missing in isoform I. 1 PublicationVSP_006055
    Alternative sequencei428 – 4347NPWLCIE → FF in isoform V. 2 PublicationsVSP_006056

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB023622 mRNA. Translation: BAA82838.1.
    AK012858 mRNA. Translation: BAB28516.1.
    AK048455 mRNA. Translation: BAC33342.1.
    AK088406 mRNA. Translation: BAC40335.1.
    AK088614 mRNA. Translation: BAC40453.1.
    AK160884 mRNA. Translation: BAE36069.1.
    AK162755 mRNA. Translation: BAE37050.1.
    AL450399 Genomic DNA. Translation: CAM19780.1.
    AL450399 Genomic DNA. Translation: CAM19781.1.
    AL450399 Genomic DNA. Translation: CAM19782.1. Sequence problems.
    BC010489 mRNA. Translation: AAH10489.1.
    AK172894 mRNA. Translation: BAD32172.1. Different initiation.
    CCDSiCCDS30066.1. [Q9R1T4-3]
    CCDS53051.1. [Q9R1T4-1]
    CCDS57749.1. [Q9R1T4-2]
    RefSeqiNP_001170794.1. NM_001177323.2.
    NP_001170795.1. NM_001177324.1. [Q9R1T4-1]
    NP_001240635.1. NM_001253706.1. [Q9R1T4-2]
    NP_064326.2. NM_019942.5. [Q9R1T4-3]
    XP_006541452.1. XM_006541389.1. [Q9R1T4-2]
    XP_006541453.1. XM_006541390.1. [Q9R1T4-2]
    UniGeneiMm.260036.
    Mm.470184.

    Genome annotation databases

    EnsembliENSMUST00000053456; ENSMUSP00000054034; ENSMUSG00000050379. [Q9R1T4-2]
    ENSMUST00000060474; ENSMUSP00000062014; ENSMUSG00000050379. [Q9R1T4-3]
    ENSMUST00000115239; ENSMUSP00000110894; ENSMUSG00000050379. [Q9R1T4-1]
    GeneIDi56526.
    KEGGimmu:56526.
    UCSCiuc009sxx.2. mouse. [Q9R1T4-3]
    uc009sxz.2. mouse. [Q9R1T4-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB023622 mRNA. Translation: BAA82838.1 .
    AK012858 mRNA. Translation: BAB28516.1 .
    AK048455 mRNA. Translation: BAC33342.1 .
    AK088406 mRNA. Translation: BAC40335.1 .
    AK088614 mRNA. Translation: BAC40453.1 .
    AK160884 mRNA. Translation: BAE36069.1 .
    AK162755 mRNA. Translation: BAE37050.1 .
    AL450399 Genomic DNA. Translation: CAM19780.1 .
    AL450399 Genomic DNA. Translation: CAM19781.1 .
    AL450399 Genomic DNA. Translation: CAM19782.1 . Sequence problems.
    BC010489 mRNA. Translation: AAH10489.1 .
    AK172894 mRNA. Translation: BAD32172.1 . Different initiation.
    CCDSi CCDS30066.1. [Q9R1T4-3 ]
    CCDS53051.1. [Q9R1T4-1 ]
    CCDS57749.1. [Q9R1T4-2 ]
    RefSeqi NP_001170794.1. NM_001177323.2.
    NP_001170795.1. NM_001177324.1. [Q9R1T4-1 ]
    NP_001240635.1. NM_001253706.1. [Q9R1T4-2 ]
    NP_064326.2. NM_019942.5. [Q9R1T4-3 ]
    XP_006541452.1. XM_006541389.1. [Q9R1T4-2 ]
    XP_006541453.1. XM_006541390.1. [Q9R1T4-2 ]
    UniGenei Mm.260036.
    Mm.470184.

    3D structure databases

    ProteinModelPortali Q9R1T4.
    SMRi Q9R1T4. Positions 41-307.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 208037. 4 interactions.
    IntActi Q9R1T4. 3 interactions.
    MINTi MINT-4134187.

    PTM databases

    PhosphoSitei Q9R1T4.

    Proteomic databases

    MaxQBi Q9R1T4.
    PaxDbi Q9R1T4.
    PRIDEi Q9R1T4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000053456 ; ENSMUSP00000054034 ; ENSMUSG00000050379 . [Q9R1T4-2 ]
    ENSMUST00000060474 ; ENSMUSP00000062014 ; ENSMUSG00000050379 . [Q9R1T4-3 ]
    ENSMUST00000115239 ; ENSMUSP00000110894 ; ENSMUSG00000050379 . [Q9R1T4-1 ]
    GeneIDi 56526.
    KEGGi mmu:56526.
    UCSCi uc009sxx.2. mouse. [Q9R1T4-3 ]
    uc009sxz.2. mouse. [Q9R1T4-1 ]

    Organism-specific databases

    CTDi 23157.
    MGIi MGI:1888939. Sept6.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG5019.
    GeneTreei ENSGT00640000091237.
    HOVERGENi HBG065093.
    InParanoidi Q9R1T4.
    KOi K16939.
    OMAi NHGFCFN.
    OrthoDBi EOG7J9VQK.
    PhylomeDBi Q9R1T4.
    TreeFami TF101080.

    Miscellaneous databases

    ChiTaRSi SEPT6. mouse.
    NextBioi 312866.
    PROi Q9R1T4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9R1T4.
    Bgeei Q9R1T4.
    CleanExi MM_SEPT6.
    Genevestigatori Q9R1T4.

    Family and domain databases

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

    Publicationsi

    1. "Identification of mouse Septin6 gene and its product."
      Kinoshita M.
      Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM V).
      Strain: NIH Swiss.
      Tissue: Heart.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS II AND V).
      Strain: C57BL/6J and NOD.
      Tissue: Embryo, Head and Thymus.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "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] (ISOFORM I).
      Tissue: Salivary gland.
    5. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
      DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-427.
      Tissue: Fetal brain.
    6. Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 16-111; 164-171; 177-185; 255-273; 281-287; 294-299; 310-337; 388-397 AND 400-420, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6 and OF1.
      Tissue: Brain and Hippocampus.
    7. "Differential localization of septins in the mouse brain."
      Kinoshita A., Noda M., Kinoshita M.
      J. Comp. Neurol. 428:223-239(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiSEPT6_MOUSE
    AccessioniPrimary (citable) accession number: Q9R1T4
    Secondary accession number(s): A2A3V9
    , A2A3W0, Q3TRH9, Q3TUA2, Q542H3, Q6A0C4, Q8C2L2, Q8C848, Q91XH2, Q9CZ94
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 128 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Coordinated expression with SEPT2 and SEPT7.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