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Reviewed, UniProtKB/Swiss-Prot Q16181 (SEPT7_HUMAN)

Last modified June 16, 2009. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Septin-7
Alternative name(s):
    CDC10 protein homolog
Gene names
Name: SEPT7
Synonyms: CDC10
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length437 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Required for normal progress through mitosis. Involved in cytokinesis. Required for normal association of CENPE with the kinetochore. Ref.7

Subunit structure

Heterohexamer composed of two heterotrimers containing one copy each of SEPT2, SEPT6 and SEPT7. The asymmetrical heterotrimers associate head-to-head to form a hexameric unit that assembles into filaments. Interacts directly with CENPE and links CENPE to septin filaments composed of SEPT2, SEPT6 and SEPT7. Ref.7 Ref.10

Subcellular location

Cytoplasm. Kinetochore. Spindle. 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. Ref.7

Sequence similarities

Belongs to the septin family.

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Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCytoplasm
Kinetochore
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   LigandGTP-binding
Nucleotide-binding
   PTMPhosphoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processcytokinesis Ref.1

Traceable author statement. Source: ProtInc

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

protein heterooligomerization

Inferred from direct assay. Source: UniProtKB

   Cellular componentcondensed chromosome kinetochore

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay. Source: UniProtKB

septin complex

Inferred from electronic annotation. Source: InterPro

spindle

Inferred from electronic annotation. Source: UniProtKB-SubCell

stress fiber

Inferred from direct assay. Source: UniProtKB

   Molecular functionGTP binding Ref.1

Traceable author statement. Source: ProtInc

protein binding

Inferred from physical interaction. Source: UniProtKB

structural molecule activity Ref.1

Traceable author statement. Source: ProtInc

Complete GO annotation...

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Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q16181-1)

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.
Isoform 2 (identifier: Q16181-2)

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

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 437437Septin-7
PRO_0000173528

Regions

Nucleotide binding57 – 648GTP
Nucleotide binding197 – 2037GTP By similarity
Coiled coil332 – 437106 Potential

Sites

Binding site2501GTP; via amide nitrogen and carbonyl oxygen
Binding site2671GTP

Amino acid modifications

Modified residue301Phosphotyrosine Ref.5
Modified residue2281Phosphothreonine By similarity
Modified residue3191Phosphotyrosine Ref.3
Modified residue3341Phosphoserine Ref.4 Ref.8
Modified residue4231Phosphoserine Ref.6
Modified residue4241Phosphoserine Ref.8
Modified residue4261Phosphothreonine Ref.8 Ref.6

Natural variations

Alternative sequence211Missing in isoform 2.
VSP_022202

Experimental info

Sequence conflict2711V → I in AAB31337. Ref.1
Sequence conflict2891L → K in AAB31337. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 10, 2005. Version 2.
Checksum: 946A08C54B7124FF

FASTA43750,680
        10         20         30         40         50         60 
MSVSARSAAA EERSVNSSTM VAQQKNLEGY VGFANLPNQV YRKSVKRGFE FTLMVVGESG 

        70         80         90        100        110        120 
LGKSTLINSL FLTDLYSPEY PGPSHRIKKT VQVEQSKVLI KEGGVQLLLT IVDTPGFGDA 

       130        140        150        160        170        180 
VDNSNCWQPV IDYIDSKFED YLNAESRVNR RQMPDNRVQC CLYFIAPSGH GLKPLDIEFM 

       190        200        210        220        230        240 
KRLHEKVNII PLIAKADTLT PEECQQFKKQ IMKEIQEHKI KIYEFPETDD EEENKLVKKI 

       250        260        270        280        290        300 
KDRLPLAVVG SNTIIEVNGK RVRGRQYPWG VAEVENGEHC DFTILRNMLI RTHMQDLKDV 

       310        320        330        340        350        360 
TNNVHYENYR SRKLAAVTYN GVDNNKNKGQ LTKSPLAQME EERREHVAKM KKMEMEMEQV 

       370        380        390        400        410        420 
FEMKVKEKVQ KLKDSEAELQ RRHEQMKKNL EAQHKELEEK RRQFEDEKAN WEAQQRILEQ 

       430 
QNSSRTLEKN KKKGKIF

« Hide

Isoform 2.

Checksum: 803345D98374253B
Show »

FASTA43650,581

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References

« Hide 'large scale' references
[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: 8037772] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-437 (ISOFORMS 1 AND 2).
Tissue: Brain and Uterus.
[3]"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: 15592455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-319, MASS SPECTROMETRY.
[4]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, MASS SPECTROMETRY.
Tissue: Epithelium.
[5]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-30, MASS SPECTROMETRY.
[6]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423 AND THR-426, MASS SPECTROMETRY.
[7]"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: 18460473] [Abstract]
Cited for: INTERACTION WITH CENPE, SUBCELLULAR LOCATION, FUNCTION.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334; SER-424 AND THR-426, MASS SPECTROMETRY.
[9]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[10]"Structural insight into filament formation by mammalian septins."
Sirajuddin M., Farkasovsky M., Hauer F., Kuehlmann D., Macara I.G., Weyand M., Stark H., Wittinghofer A.
Nature 449:311-315(2007) [PubMed: 17637674] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 20-437 IN COMPLEX WITH GDP, SUBUNIT.
+Additional computationally mapped references.

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Cross-references

Sequence databases

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.
IPIIPI00033025.
IPI00816201.
PIRJC2352.
RefSeqNP_001779.3.
UniGeneHs.191346

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2QAGX-ray4.00C20-437[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ16181. 1 interaction.

PTM databases

PhosphoSiteQ16181.

2-D gel databases

OGPQ16181.

Proteomic databases

PRIDEQ16181.

Genome annotation databases

EnsemblENSG00000122545. Homo sapiens. [Contig view]
GeneID989.

Organism-specific databases

GeneCardsGC07P035807.
HGNCHGNC:1717. SEPT7.
MIM603151. gene.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ16181.
HOVERGENQ16181.

Gene expression databases

ArrayExpressQ16181.
BgeeQ16181.
CleanExHS_SEPT7.
GermOnlineENSG00000122545. Homo sapiens.

Family and domain databases

InterProIPR000038. Cell_Div_GTP_bd.
IPR016491. Septin.
IPR008115. Septin7.
[Graphical view]
PANTHERPTHR18884. Cell_Div_GTP_bd. 1 hit.
PfamPF00735. Septin. 1 hit.
[Graphical view]
PIRSFPIRSF006698. Septin. 1 hit.
PRINTSPR01742. SEPTIN7.
ProDomPD002565. GTP_Cell_Div. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Other Resources

NextBio4150.
SOURCESearch...

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Entry information

Entry nameSEPT7_HUMAN
AccessionPrimary (citable) accession number: Q16181
Secondary accession number(s): Q52M76, Q6NX50
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 10, 2005
Last modified: June 16, 2009
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents