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Q16181

- SEPT7_HUMAN

UniProt

Q16181 - SEPT7_HUMAN

Protein

Septin-7

Gene

SEPT7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (10 May 2005)
      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.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei90 – 901GTPBy similarity
    Binding sitei116 – 1161GTP; via amide nitrogenBy similarity
    Binding sitei250 – 2501GTP; via amide nitrogen and carbonyl oxygenBy similarity
    Binding sitei265 – 2651GTPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi57 – 648GTP
    Nucleotide bindingi195 – 2039GTPBy similarity

    GO - Molecular functioni

    1. GTP binding Source: ProtInc
    2. identical protein binding Source: IntAct
    3. protein binding Source: UniProtKB
    4. structural molecule activity Source: ProtInc

    GO - Biological processi

    1. cilium morphogenesis Source: UniProtKB
    2. cytokinesis Source: ProtInc
    3. mitotic nuclear division Source: UniProtKB-KW
    4. protein heterooligomerization Source: UniProtKB
    5. 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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:1717. SEPT7.

    Subcellular locationi

    Cytoplasm 1 Publication. Chromosomecentromerekinetochore 1 Publication. Cytoplasmcytoskeletonspindle 1 Publication. Cleavage furrow 1 Publication. Midbody 1 Publication. 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. Associated with actin stress fibers By similarity.By similarity

    GO - Cellular componenti

    1. actin cytoskeleton Source: HPA
    2. axoneme Source: UniProtKB
    3. axon terminus Source: Ensembl
    4. cleavage furrow Source: UniProtKB-SubCell
    5. condensed chromosome kinetochore Source: UniProtKB-SubCell
    6. cytoplasm Source: HPA
    7. extracellular vesicular exosome Source: UniProt
    8. microtubule cytoskeleton Source: HPA
    9. midbody Source: UniProtKB-SubCell
    10. nucleolus Source: HPA
    11. nucleus Source: UniProtKB
    12. plasma membrane Source: HPA
    13. septin complex Source: InterPro
    14. spindle Source: UniProtKB-SubCell
    15. stress fiber Source: UniProtKB
    16. synapse Source: Ensembl

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26253.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 437436Septin-7PRO_0000173528Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei30 – 301PhosphotyrosineBy similarity
    Modified residuei334 – 3341Phosphoserine2 Publications
    Modified residuei373 – 3731N6-acetyllysineBy similarity
    Modified residuei424 – 4241Phosphoserine1 Publication
    Modified residuei426 – 4261Phosphothreonine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ16181.
    PaxDbiQ16181.
    PRIDEiQ16181.

    2D gel databases

    OGPiQ16181.
    UCD-2DPAGEQ16181.

    PTM databases

    PhosphoSiteiQ16181.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ16181.
    BgeeiQ16181.
    CleanExiHS_SEPT7.
    GenevestigatoriQ16181.

    Organism-specific databases

    HPAiHPA023309.
    HPA029524.

    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 and SEPT8 By similarity. Interacts with SEPT9 and SEPT11.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-2009373,EBI-2009373

    Protein-protein interaction databases

    BioGridi107425. 53 interactions.
    DIPiDIP-47093N.
    IntActiQ16181. 11 interactions.
    MINTiMINT-5006116.
    STRINGi9606.ENSP00000381992.

    Structurei

    Secondary structure

    1
    437
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi50 – 578
    Helixi63 – 708
    Beta strandi71 – 733
    Beta strandi94 – 1007
    Beta strandi107 – 1137
    Turni124 – 1274
    Helixi128 – 14619
    Beta strandi147 – 1493
    Beta strandi160 – 1656
    Helixi174 – 18310
    Turni184 – 1863
    Beta strandi189 – 1957
    Helixi196 – 1983
    Helixi201 – 21717
    Helixi238 – 2425
    Beta strandi245 – 2473
    Beta strandi264 – 2663
    Beta strandi271 – 2755
    Turni277 – 2793
    Helixi282 – 2909
    Turni291 – 2933
    Helixi294 – 30310
    Helixi305 – 31511

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2QAGX-ray4.00C20-437[»]
    3T5DX-ray3.30A/C48-316[»]
    3TW4X-ray3.35A/B48-317[»]
    ProteinModelPortaliQ16181.
    SMRiQ16181. Positions 49-316.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16181.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini47 – 316270Septin-type GAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili332 – 437106Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG5019.
    HOGENOMiHOG000233586.
    HOVERGENiHBG065093.
    InParanoidiQ16181.
    KOiK16944.
    OrthoDBiEOG79KPF0.
    PhylomeDBiQ16181.
    TreeFamiTF101079.

    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]

    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: Q16181-1) [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

    MSVSARSAAA EERSVNSSTM VAQQKNLEGY VGFANLPNQV YRKSVKRGFE    50
    FTLMVVGESG LGKSTLINSL FLTDLYSPEY PGPSHRIKKT VQVEQSKVLI 100
    KEGGVQLLLT IVDTPGFGDA VDNSNCWQPV IDYIDSKFED YLNAESRVNR 150
    RQMPDNRVQC CLYFIAPSGH GLKPLDIEFM KRLHEKVNII PLIAKADTLT 200
    PEECQQFKKQ IMKEIQEHKI KIYEFPETDD EEENKLVKKI KDRLPLAVVG 250
    SNTIIEVNGK RVRGRQYPWG VAEVENGEHC DFTILRNMLI RTHMQDLKDV 300
    TNNVHYENYR SRKLAAVTYN GVDNNKNKGQ LTKSPLAQME EERREHVAKM 350
    KKMEMEMEQV FEMKVKEKVQ KLKDSEAELQ RRHEQMKKNL EAQHKELEEK 400
    RRQFEDEKAN WEAQQRILEQ QNSSRTLEKN KKKGKIF 437
    Length:437
    Mass (Da):50,680
    Last modified:May 10, 2005 - v2
    Checksum:i946A08C54B7124FF
    GO
    Isoform 2 (identifier: Q16181-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         21-21: Missing.

    Show »
    Length:436
    Mass (Da):50,581
    Checksum:i803345D98374253B
    GO

    Sequence cautioni

    The sequence AAB31337.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAH67264.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAH93640.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAH93642.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti271 – 2711V → I in AAB31337. (PubMed:8037772)Curated
    Sequence conflicti289 – 2891L → K in AAB31337. (PubMed:8037772)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei21 – 211Missing in isoform 2. 1 PublicationVSP_022202

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S72008 mRNA. Translation: AAB31337.1. Different initiation.
    BC067264 mRNA. Translation: AAH67264.2. Different initiation.
    BC093640 mRNA. Translation: AAH93640.2. Different initiation.
    BC093642 mRNA. Translation: AAH93642.2. Different initiation.
    PIRiJC2352.
    RefSeqiNP_001779.3. NM_001788.5. [Q16181-1]
    UniGeneiHs.191346.

    Genome annotation databases

    EnsembliENST00000399034; ENSP00000381992; ENSG00000122545.
    GeneIDi989.
    KEGGihsa:989.
    UCSCiuc010kxc.3. human. [Q16181-1]
    uc011kat.2. human. [Q16181-2]

    Polymorphism databases

    DMDMi67472677.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S72008 mRNA. Translation: AAB31337.1 . Different initiation.
    BC067264 mRNA. Translation: AAH67264.2 . Different initiation.
    BC093640 mRNA. Translation: AAH93640.2 . Different initiation.
    BC093642 mRNA. Translation: AAH93642.2 . Different initiation.
    PIRi JC2352.
    RefSeqi NP_001779.3. NM_001788.5. [Q16181-1 ]
    UniGenei Hs.191346.

    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 C 20-437 [» ]
    3T5D X-ray 3.30 A/C 48-316 [» ]
    3TW4 X-ray 3.35 A/B 48-317 [» ]
    ProteinModelPortali Q16181.
    SMRi Q16181. Positions 49-316.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107425. 53 interactions.
    DIPi DIP-47093N.
    IntActi Q16181. 11 interactions.
    MINTi MINT-5006116.
    STRINGi 9606.ENSP00000381992.

    PTM databases

    PhosphoSitei Q16181.

    Polymorphism databases

    DMDMi 67472677.

    2D gel databases

    OGPi Q16181.
    UCD-2DPAGE Q16181.

    Proteomic databases

    MaxQBi Q16181.
    PaxDbi Q16181.
    PRIDEi Q16181.

    Protocols and materials databases

    DNASUi 989.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000399034 ; ENSP00000381992 ; ENSG00000122545 .
    GeneIDi 989.
    KEGGi hsa:989.
    UCSCi uc010kxc.3. human. [Q16181-1 ]
    uc011kat.2. human. [Q16181-2 ]

    Organism-specific databases

    CTDi 989.
    GeneCardsi GC07P035807.
    H-InvDB HIX0006599.
    HIX0032379.
    HGNCi HGNC:1717. SEPT7.
    HPAi HPA023309.
    HPA029524.
    MIMi 603151. gene.
    neXtProti NX_Q16181.
    PharmGKBi PA26253.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5019.
    HOGENOMi HOG000233586.
    HOVERGENi HBG065093.
    InParanoidi Q16181.
    KOi K16944.
    OrthoDBi EOG79KPF0.
    PhylomeDBi Q16181.
    TreeFami TF101079.

    Miscellaneous databases

    ChiTaRSi SEPT7. human.
    EvolutionaryTracei Q16181.
    GeneWikii SEPT7.
    GenomeRNAii 989.
    NextBioi 4150.
    PROi Q16181.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16181.
    Bgeei Q16181.
    CleanExi HS_SEPT7.
    Genevestigatori Q16181.

    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. "Molecular cloning of a novel human cDNA homologous to CDC10 in Saccharomyces cerevisiae."
      Nakatsuru S., Sudo K., Nakamura Y.
      Biochem. Biophys. Res. Commun. 202:82-87(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-437 (ISOFORM 1).
      Tissue: Fetal lung.
    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] OF 5-437 (ISOFORMS 1 AND 2).
      Tissue: Brain and Uterus.
    3. "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 SEPT9 AND SEPT11.
    4. "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.
    5. "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 SEPT6.
    6. "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].
    7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "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 SEPT6, HOMODIMERIZATION.
    9. "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.
    10. "Septin 7 interacts with centromere-associated protein E and is required for its kinetochore localization."
      Zhu M., Wang F., Yan F., Yao P.Y., Du J., Gao X., Wang X., Wu Q., Ward T., Li J., Kioko S., Hu R., Xie W., Ding X., Yao X.
      J. Biol. Chem. 283:18916-18925(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CENPE, SUBCELLULAR LOCATION, FUNCTION.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424 AND THR-426, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    13. Cited for: INTERACTION WITH SEPT9.
    14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334 AND THR-426, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 20-437 IN COMPLEX WITH GDP, SUBUNIT.

    Entry informationi

    Entry nameiSEPT7_HUMAN
    AccessioniPrimary (citable) accession number: Q16181
    Secondary accession number(s): Q52M76, Q6NX50
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: May 10, 2005
    Last modified: October 1, 2014
    This is version 136 of the entry and version 2 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 SEPT6.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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