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Q9NVA2

- SEP11_HUMAN

UniProt

Q9NVA2 - SEP11_HUMAN

Protein

Septin-11

Gene

SEPT11

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Filament-forming cytoskeletal GTPase. May play a role in cytokinesis Potential. May play a role in the cytoarchitecture of neurons, including dendritic arborization and dendritic spines, and in GABAergic synaptic connectivity By similarity. During Listeria monocytogenes infection, not required for the bacterial entry process, but restricts its efficacy.By similarity2 PublicationsCurated

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei103 – 1031GTP; via amide nitrogenBy similarity
    Binding sitei238 – 2381GTP; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei253 – 2531GTPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi48 – 558GTPBy similarity
    Nucleotide bindingi184 – 1929GTPBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cell division Source: UniProtKB-KW
    3. protein heterooligomerization Source: UniProtKB

    Keywords - Biological processi

    Cell cycle, Cell division

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Septin-11
    Gene namesi
    Name:SEPT11
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:25589. SEPT11.

    Subcellular locationi

    Cytoplasmcytoskeleton. Cell junctionsynapse. Cell projectiondendritic spine. Cell projectionaxon By similarity
    Note: Partly colocalizes with stress fibers and microtubules. During bacterial infection, displays a collar shape structure next to actin at the pole of invading bacteria.

    GO - Cellular componenti

    1. axon Source: UniProtKB-SubCell
    2. cell junction Source: UniProtKB-KW
    3. dendritic spine Source: UniProtKB-SubCell
    4. extracellular vesicular exosome Source: UniProt
    5. septin complex Source: InterPro
    6. stress fiber Source: UniProtKB
    7. synapse Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell projection, Cytoplasm, Cytoskeleton, Synapse

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving SEPT11 may be a cause of chronic neutrophilic leukemia. Translocation t(4;11)(q21;q23) with KMT2A/MLL1.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi48 – 481G → A: High reduction in GTPase activity. No effect on GTP-binding. Loss of filament formation. 1 Publication

    Organism-specific databases

    PharmGKBiPA128394688.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 429428Septin-11PRO_0000173542Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9NVA2.
    PaxDbiQ9NVA2.
    PeptideAtlasiQ9NVA2.
    PRIDEiQ9NVA2.

    2D gel databases

    OGPiQ9NVA2.
    UCD-2DPAGEQ9NVA2.

    PTM databases

    PhosphoSiteiQ9NVA2.

    Expressioni

    Tissue specificityi

    Widely expressed, except in leukocytes.2 Publications

    Gene expression databases

    ArrayExpressiQ9NVA2.
    BgeeiQ9NVA2.
    CleanExiHS_SEPT11.
    GenevestigatoriQ9NVA2.

    Organism-specific databases

    HPAiHPA003459.
    HPA005665.

    Interactioni

    Subunit structurei

    Septins polymerize into heterooligomeric protein complexes that form filaments, and can associate with cellular membranes, actin filaments and microtubules. GTPase activity is required for filament formation. Interacts with SEPT7, SEPT9 and SEPT12. Forms homooligomers.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SEPT5Q997196EBI-957999,EBI-373345

    Protein-protein interaction databases

    BioGridi120870. 32 interactions.
    IntActiQ9NVA2. 2 interactions.
    MINTiMINT-3074824.
    STRINGi9606.ENSP00000264893.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NVA2.
    SMRiQ9NVA2. Positions 18-306.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini38 – 304267Septin-type GAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili320 – 41596Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG5019.
    HOGENOMiHOG000233586.
    HOVERGENiHBG065093.
    InParanoidiQ9NVA2.
    KOiK16939.
    OMAiEVSNFQK.
    OrthoDBiEOG7J9VQK.
    PhylomeDBiQ9NVA2.
    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 (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NVA2-1) [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

    MAVAVGRPSN EELRNLSLSG HVGFDSLPDQ LVNKSTSQGF CFNILCVGET    50
    GIGKSTLMDT LFNTKFESDP ATHNEPGVRL KARSYELQES NVRLKLTIVD 100
    TVGFGDQINK DDSYKPIVEY IDAQFEAYLQ EELKIKRSLF NYHDTRIHAC 150
    LYFIAPTGHS LKSLDLVTMK KLDSKVNIIP IIAKADTIAK NELHKFKSKI 200
    MSELVSNGVQ IYQFPTDEET VAEINATMSV HLPFAVVGST EEVKIGNKMA 250
    KARQYPWGVV QVENENHCDF VKLREMLIRV NMEDLREQTH TRHYELYRRC 300
    KLEEMGFKDT DPDSKPFSLQ ETYEAKRNEF LGELQKKEEE MRQMFVMRVK 350
    EKEAELKEAE KELHEKFDLL KRTHQEEKKK VEDKKKELEE EVNNFQKKKA 400
    AAQLLQSQAQ QSGAQQTKKD KDKKNASFT 429
    Length:429
    Mass (Da):49,398
    Last modified:January 23, 2007 - v3
    Checksum:iD467F1F315FFD028
    GO
    Isoform 2 (identifier: Q9NVA2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-9: MAVAVGRPS → MEERKPAHVLRSFKYAAFM

    Note: No experimental confirmation available.

    Show »
    Length:439
    Mass (Da):50,823
    Checksum:iC8E82F016C56A392
    GO

    Sequence cautioni

    The sequence CAB53741.2 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence BAB55250.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti142 – 1421Y → H in CAB53741. (PubMed:15489334)Curated
    Sequence conflicti298 – 2981R → H in CAB53741. (PubMed:15489334)Curated
    Sequence conflicti321 – 3211E → G in CAB53741. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 99MAVAVGRPS → MEERKPAHVLRSFKYAAFM in isoform 2. 1 PublicationVSP_038320

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    GU727629 mRNA. Translation: ADU87631.1.
    AK001711 mRNA. Translation: BAA91853.1.
    AK027633 mRNA. Translation: BAB55250.1. Different initiation.
    AK302700 mRNA. Translation: BAH13782.1.
    AC104687 Genomic DNA. Translation: AAY40922.1.
    AC111196 Genomic DNA. No translation available.
    CH471057 Genomic DNA. Translation: EAX05805.1.
    BC008083 mRNA. Translation: AAH08083.3.
    BC063615 mRNA. Translation: AAH63615.1.
    AL110300 mRNA. Translation: CAB53741.2. Sequence problems.
    CCDSiCCDS34018.1. [Q9NVA2-1]
    RefSeqiNP_060713.1. NM_018243.2. [Q9NVA2-1]
    XP_005263177.1. XM_005263120.1. [Q9NVA2-2]
    UniGeneiHs.128199.

    Genome annotation databases

    EnsembliENST00000264893; ENSP00000264893; ENSG00000138758. [Q9NVA2-1]
    ENST00000510515; ENSP00000422896; ENSG00000138758. [Q9NVA2-2]
    GeneIDi55752.
    KEGGihsa:55752.
    UCSCiuc003hkj.3. human. [Q9NVA2-1]
    uc010ijh.1. human. [Q9NVA2-2]

    Polymorphism databases

    DMDMi50401687.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    GU727629 mRNA. Translation: ADU87631.1 .
    AK001711 mRNA. Translation: BAA91853.1 .
    AK027633 mRNA. Translation: BAB55250.1 . Different initiation.
    AK302700 mRNA. Translation: BAH13782.1 .
    AC104687 Genomic DNA. Translation: AAY40922.1 .
    AC111196 Genomic DNA. No translation available.
    CH471057 Genomic DNA. Translation: EAX05805.1 .
    BC008083 mRNA. Translation: AAH08083.3 .
    BC063615 mRNA. Translation: AAH63615.1 .
    AL110300 mRNA. Translation: CAB53741.2 . Sequence problems.
    CCDSi CCDS34018.1. [Q9NVA2-1 ]
    RefSeqi NP_060713.1. NM_018243.2. [Q9NVA2-1 ]
    XP_005263177.1. XM_005263120.1. [Q9NVA2-2 ]
    UniGenei Hs.128199.

    3D structure databases

    ProteinModelPortali Q9NVA2.
    SMRi Q9NVA2. Positions 18-306.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120870. 32 interactions.
    IntActi Q9NVA2. 2 interactions.
    MINTi MINT-3074824.
    STRINGi 9606.ENSP00000264893.

    PTM databases

    PhosphoSitei Q9NVA2.

    Polymorphism databases

    DMDMi 50401687.

    2D gel databases

    OGPi Q9NVA2.
    UCD-2DPAGE Q9NVA2.

    Proteomic databases

    MaxQBi Q9NVA2.
    PaxDbi Q9NVA2.
    PeptideAtlasi Q9NVA2.
    PRIDEi Q9NVA2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264893 ; ENSP00000264893 ; ENSG00000138758 . [Q9NVA2-1 ]
    ENST00000510515 ; ENSP00000422896 ; ENSG00000138758 . [Q9NVA2-2 ]
    GeneIDi 55752.
    KEGGi hsa:55752.
    UCSCi uc003hkj.3. human. [Q9NVA2-1 ]
    uc010ijh.1. human. [Q9NVA2-2 ]

    Organism-specific databases

    CTDi 55752.
    GeneCardsi GC04P077870.
    HGNCi HGNC:25589. SEPT11.
    HPAi HPA003459.
    HPA005665.
    MIMi 612887. gene.
    neXtProti NX_Q9NVA2.
    PharmGKBi PA128394688.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5019.
    HOGENOMi HOG000233586.
    HOVERGENi HBG065093.
    InParanoidi Q9NVA2.
    KOi K16939.
    OMAi EVSNFQK.
    OrthoDBi EOG7J9VQK.
    PhylomeDBi Q9NVA2.
    TreeFami TF101080.

    Miscellaneous databases

    ChiTaRSi SEPT11. human.
    GeneWikii SEPT11.
    GenomeRNAii 55752.
    NextBioi 60745.
    PROi Q9NVA2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NVA2.
    Bgeei Q9NVA2.
    CleanExi HS_SEPT11.
    Genevestigatori Q9NVA2.

    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. "Systematic mapping and functional analysis of a family of human epididymal secretory sperm-located proteins."
      Li J., Liu F., Wang H., Liu X., Liu J., Li N., Wan F., Wang W., Zhang C., Jin S., Liu J., Zhu P., Liu Y.
      Mol. Cell. Proteomics 9:2517-2528(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Epididymis.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Teratocarcinoma and Testis.
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 1).
      Tissue: Colon and Skin.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-337.
      Tissue: Fetal kidney.
    7. "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 2-14 (ISOFORM 1), ACETYLATION AT ALA-2.
      Tissue: Platelet.
    8. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 15-34; 55-79; 84-93; 96-110; 176-184; 309-336; 387-397 AND 400-418, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    9. "Biochemical and cell biological characterization of a mammalian septin, Sept11."
      Hanai N., Nagata K., Kawajiri A., Shiromizu T., Saitoh N., Hasegawa Y., Murakami S., Inagaki M.
      FEBS Lett. 568:83-88(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF GLY-48, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    10. "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: INTERACTION WITH SEPT7 AND SEPT9.
    11. "FLJ10849, a septin family gene, fuses MLL in a novel leukemia cell line CNLBC1 derived from chronic neutrophilic leukemia in transformation with t(4;11)(q21;q23)."
      Kojima K., Sakai I., Hasegawa A., Niiya H., Azuma T., Matsuo Y., Fujii N., Tanimoto M., Fujita S.
      Leukemia 18:998-1005(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH KMT2A/MLL1.
    12. "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.
    13. "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.
    14. "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.
    15. Cited for: ROLE IN BACTERIAL INFECTION.
    16. Cited for: INTERACTION WITH SEPT9, SUBCELLULAR LOCATION.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSEP11_HUMAN
    AccessioniPrimary (citable) accession number: Q9NVA2
    Secondary accession number(s): B7Z7Z6
    , E9KL32, Q4W5G1, Q7L4N1, Q96SP1, Q9UFY9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 117 of the entry and version 3 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

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3