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Q14141

- SEPT6_HUMAN

UniProt

Q14141 - SEPT6_HUMAN

Protein

Septin-6

Gene

SEPT6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 134 (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. May play a role in HCV RNA replication.2 Publications

    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 – 568GTP1 Publication
    Nucleotide bindingi185 – 1939GTP1 Publication

    GO - Molecular functioni

    1. GTP binding Source: UniProtKB
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. cytokinesis Source: UniProtKB
    2. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Cell cycle, Cell division, Host-virus interaction

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Septin-6
    Gene namesi
    Name:SEPT6
    Synonyms:KIAA0128, SEP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:15848. SEPT6.

    Subcellular locationi

    Cytoplasm 1 Publication. Cytoplasmcytoskeletonspindle 1 Publication. Chromosomecentromerekinetochore 1 Publication. Cleavage furrow 1 Publication. Midbody 1 Publication
    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.

    GO - Cellular componenti

    1. axon terminus Source: Ensembl
    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: Ensembl

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134941944.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 434433Septin-6PRO_0000173525Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei367 – 3671N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ14141.
    PaxDbiQ14141.
    PeptideAtlasiQ14141.
    PRIDEiQ14141.

    2D gel databases

    OGPiQ14141.

    PTM databases

    PhosphoSiteiQ14141.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ14141.
    BgeeiQ14141.
    CleanExiHS_SEPT6.
    GenevestigatoriQ14141.

    Organism-specific databases

    HPAiHPA005665.

    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 HCV NS5B and with HNRNPA1.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P279584EBI-745901,EBI-6904388From a different organism.
    HNRNPA1P096513EBI-745901,EBI-352662
    SEPT12Q8IYM13EBI-745901,EBI-2585067
    SEPT2Q150196EBI-745901,EBI-741220
    SOCS7O14512-12EBI-745901,EBI-1539617

    Protein-protein interaction databases

    BioGridi116770. 13 interactions.
    DIPiDIP-38218N.
    IntActiQ14141. 10 interactions.
    MINTiMINT-4532787.
    STRINGi9606.ENSP00000341524.

    Structurei

    Secondary structure

    1
    434
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi30 – 356
    Beta strandi42 – 487
    Helixi56 – 638
    Beta strandi80 – 8910
    Beta strandi94 – 10310
    Helixi111 – 1144
    Helixi116 – 13217
    Beta strandi150 – 1556
    Helixi164 – 1729
    Beta strandi177 – 1848
    Helixi186 – 1883
    Helixi191 – 20515
    Turni229 – 2313
    Helixi272 – 2809
    Helixi285 – 2939
    Helixi296 – 3038
    Turni304 – 3063

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2QAGX-ray4.00B1-427[»]
    ProteinModelPortaliQ14141.
    SMRiQ14141. Positions 41-307.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ14141.

    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 – 40989Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG5019.
    HOVERGENiHBG065093.
    KOiK16939.
    OrthoDBiEOG7J9VQK.
    PhylomeDBiQ14141.
    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 (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform II (identifier: Q14141-1) [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

    MAATDIARQV GEGCRTVPLA GHVGFDSLPD QLVNKSVSQG FCFNILCVGE    50
    TGLGKSTLMD TLFNTKFEGE PATHTQPGVQ LQSNTYDLQE SNVRLKLTIV 100
    STVGFGDQIN KEDSYKPIVE FIDAQFEAYL QEELKIRRVL HTYHDSRIHV 150
    CLYFIAPTGH SLKSLDLVTM KKLDSKVNII PIIAKADAIS KSELTKFKIK 200
    ITSELVSNGV QIYQFPTDDE SVAEINGTMN AHLPFAVIGS TEELKIGNKM 250
    MRARQYPWGT VQVENEAHCD FVKLREMLIR VNMEDLREQT HTRHYELYRR 300
    CKLEEMGFKD TDPDSKPFSL QETYEAKRNE FLGELQKKEE EMRQMFVQRV 350
    KEKEAELKEA EKELHEKFDR LKKLHQDEKK KLEDKKKSLD DEVNAFKQRK 400
    TAAELLQSQG SQAGGSQTLK RDKEKKNNPW LCTE 434
    Length:434
    Mass (Da):49,717
    Last modified:January 23, 2007 - v4
    Checksum:iE684AE6A93B32362
    GO
    Isoform I (identifier: Q14141-2) [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):48,873
    Checksum:i62EB88E308386ADE
    GO
    Isoform IV (identifier: Q14141-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         263-267: VENEA → AAREV
         268-434: Missing.

    Show »
    Length:267
    Mass (Da):29,584
    Checksum:i7DD6D37AE3844845
    GO
    Isoform V (identifier: Q14141-4) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:429
    Mass (Da):49,167
    Checksum:i3D8EE2EB88E30838
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti406 – 4061L → P in AAH09291. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei263 – 2675VENEA → AAREV in isoform IV. 1 PublicationVSP_006051
    Alternative sequencei268 – 434167Missing in isoform IV. 1 PublicationVSP_006052Add
    BLAST
    Alternative sequencei428 – 4347Missing in isoform I. 2 PublicationsVSP_006053
    Alternative sequencei428 – 4347NPWLCTE → FF in isoform V. 2 PublicationsVSP_006054

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF403058 mRNA. Translation: AAK98547.1.
    AF403059 mRNA. Translation: AAK98548.1.
    AF403060 mRNA. Translation: AAK98549.1.
    AF403061 mRNA. Translation: AAK98550.1.
    AF403062 mRNA. Translation: AAK98551.1.
    AL355348, AC004913, AC005052 Genomic DNA. Translation: CAI41426.1.
    BC009291 mRNA. Translation: AAH09291.1.
    BC011922 mRNA. Translation: AAH11922.3.
    BC036240 mRNA. Translation: AAH36240.1.
    D50918 mRNA. Translation: BAA09477.1.
    CCDSiCCDS14583.1. [Q14141-4]
    CCDS14584.1. [Q14141-1]
    CCDS14585.1. [Q14141-2]
    RefSeqiNP_055944.2. NM_015129.5. [Q14141-1]
    NP_665798.1. NM_145799.3. [Q14141-2]
    NP_665799.1. NM_145800.3. [Q14141-2]
    NP_665801.1. NM_145802.3. [Q14141-4]
    XP_006724812.1. XM_006724749.1. [Q14141-2]
    XP_006724813.1. XM_006724750.1. [Q14141-2]
    UniGeneiHs.496666.

    Genome annotation databases

    EnsembliENST00000343984; ENSP00000341524; ENSG00000125354. [Q14141-1]
    ENST00000354228; ENSP00000346169; ENSG00000125354. [Q14141-4]
    ENST00000360156; ENSP00000353278; ENSG00000125354. [Q14141-2]
    ENST00000394610; ENSP00000378108; ENSG00000125354. [Q14141-2]
    ENST00000460411; ENSP00000435818; ENSG00000125354. [Q14141-3]
    ENST00000489216; ENSP00000418715; ENSG00000125354. [Q14141-2]
    GeneIDi23157.
    KEGGihsa:23157.
    UCSCiuc004ers.3. human. [Q14141-1]

    Polymorphism databases

    DMDMi20178343.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF403058 mRNA. Translation: AAK98547.1 .
    AF403059 mRNA. Translation: AAK98548.1 .
    AF403060 mRNA. Translation: AAK98549.1 .
    AF403061 mRNA. Translation: AAK98550.1 .
    AF403062 mRNA. Translation: AAK98551.1 .
    AL355348 , AC004913 , AC005052 Genomic DNA. Translation: CAI41426.1 .
    BC009291 mRNA. Translation: AAH09291.1 .
    BC011922 mRNA. Translation: AAH11922.3 .
    BC036240 mRNA. Translation: AAH36240.1 .
    D50918 mRNA. Translation: BAA09477.1 .
    CCDSi CCDS14583.1. [Q14141-4 ]
    CCDS14584.1. [Q14141-1 ]
    CCDS14585.1. [Q14141-2 ]
    RefSeqi NP_055944.2. NM_015129.5. [Q14141-1 ]
    NP_665798.1. NM_145799.3. [Q14141-2 ]
    NP_665799.1. NM_145800.3. [Q14141-2 ]
    NP_665801.1. NM_145802.3. [Q14141-4 ]
    XP_006724812.1. XM_006724749.1. [Q14141-2 ]
    XP_006724813.1. XM_006724750.1. [Q14141-2 ]
    UniGenei Hs.496666.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2QAG X-ray 4.00 B 1-427 [» ]
    ProteinModelPortali Q14141.
    SMRi Q14141. Positions 41-307.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116770. 13 interactions.
    DIPi DIP-38218N.
    IntActi Q14141. 10 interactions.
    MINTi MINT-4532787.
    STRINGi 9606.ENSP00000341524.

    PTM databases

    PhosphoSitei Q14141.

    Polymorphism databases

    DMDMi 20178343.

    2D gel databases

    OGPi Q14141.

    Proteomic databases

    MaxQBi Q14141.
    PaxDbi Q14141.
    PeptideAtlasi Q14141.
    PRIDEi Q14141.

    Protocols and materials databases

    DNASUi 23157.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000343984 ; ENSP00000341524 ; ENSG00000125354 . [Q14141-1 ]
    ENST00000354228 ; ENSP00000346169 ; ENSG00000125354 . [Q14141-4 ]
    ENST00000360156 ; ENSP00000353278 ; ENSG00000125354 . [Q14141-2 ]
    ENST00000394610 ; ENSP00000378108 ; ENSG00000125354 . [Q14141-2 ]
    ENST00000460411 ; ENSP00000435818 ; ENSG00000125354 . [Q14141-3 ]
    ENST00000489216 ; ENSP00000418715 ; ENSG00000125354 . [Q14141-2 ]
    GeneIDi 23157.
    KEGGi hsa:23157.
    UCSCi uc004ers.3. human. [Q14141-1 ]

    Organism-specific databases

    CTDi 23157.
    GeneCardsi GC0XM118750.
    HGNCi HGNC:15848. SEPT6.
    HPAi HPA005665.
    MIMi 300683. gene.
    neXtProti NX_Q14141.
    PharmGKBi PA134941944.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5019.
    HOVERGENi HBG065093.
    KOi K16939.
    OrthoDBi EOG7J9VQK.
    PhylomeDBi Q14141.
    TreeFami TF101080.

    Miscellaneous databases

    ChiTaRSi SEPT6. human.
    EvolutionaryTracei Q14141.
    GeneWikii SEPT6.
    GenomeRNAii 23157.
    NextBioi 44499.
    PROi Q14141.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14141.
    Bgeei Q14141.
    CleanExi HS_SEPT6.
    Genevestigatori Q14141.

    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. "SEPTIN6, a human homologue to mouse Septin6, is fused to MLL in infant acute myeloid leukemia with complex chromosomal abnormalities involving 11q23 and Xq24."
      Ono R., Taki T., Taketani T., Kawaguchi H., Taniwaki M., Okamura T., Kawa K., Hanada R., Kobayashi M., Hayashi Y.
      Cancer Res. 62:333-337(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS I; II; IV AND V).
    2. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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] (ISOFORMS II AND V).
      Tissue: Muscle, Placenta and Testis.
    4. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-8, ACETYLATION AT ALA-2.
      Tissue: Platelet.
    5. "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1."
      Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.
      DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-427 (ISOFORM I).
      Tissue: Bone marrow.
    6. "Expression profiling the human septin gene family."
      Hall P.A., Jung K., Hillan K.J., Russell S.E.H.
      J. Pathol. 206:269-278(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    7. "Mammalian septins regulate microtubule stability through interaction with the microtubule-binding protein MAP4."
      Kremer B.E., Haystead T., Macara I.G.
      Mol. Biol. Cell 16:4648-4659(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: COORDINATED EXPRESSION WITH SEPT2 AND SEPT7.
    8. "A mitotic septin scaffold required for mammalian chromosome congression and segregation."
      Spiliotis E.T., Kinoshita M., Nelson W.J.
      Science 307:1781-1785(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. "Structural analysis of septin 2, 6, and 7 complexes."
      Low C., Macara I.G.
      J. Biol. Chem. 281:30697-30706(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SEPT2 AND SEPT7.
    10. "Septins regulate actin organization and cell-cycle arrest through nuclear accumulation of NCK mediated by SOCS7."
      Kremer B.E., Adang L.A., Macara I.G.
      Cell 130:837-850(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SOCS7.
    11. "SEPT12 interacts with SEPT6 and this interaction alters the filament structure of SEPT6 in Hela cells."
      Ding X., Yu W., Liu M., Shen S., Chen F., Wan B., Yu L.
      J. Biochem. Mol. Biol. 40:973-978(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SEPT12.
    12. "An RNA-binding protein, hnRNP A1, and a scaffold protein, septin 6, facilitate hepatitis C virus replication."
      Kim C.S., Seol S.K., Song O.-K., Park J.H., Jang S.K.
      J. Virol. 81:3852-3865(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HNRNPA1 AND HCV NS5B, FUNCTION.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    14. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: INTERACTION WITH SEPT9.
    16. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-367, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 1-427 IN COMPLEX WITH GTP, ELECTRON MICROSCOPY OF SEPTIN COMPLEX, SUBUNIT.

    Entry informationi

    Entry nameiSEPT6_HUMAN
    AccessioniPrimary (citable) accession number: Q14141
    Secondary accession number(s): Q5JTK0
    , Q969W5, Q96A13, Q96GR1, Q96P86, Q96P87
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 134 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Coordinated expression with SEPT2 and SEPT7.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3