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Q16181 (SEPT7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Septin-7
Alternative name(s):
CDC10 protein homolog
Gene names
Name:SEPT7
Synonyms:CDC10
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length437 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.10

Subunit structure

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. Ref.3 Ref.8 Ref.10 Ref.13 Ref.17

Subcellular location

Cytoplasm. Chromosomecentromerekinetochore. Cytoplasmcytoskeletonspindle. Cleavage furrow. Midbody. 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. Ref.10

Tissue specificity

Widely expressed. Ref.4

Miscellaneous

Coordinated expression with SEPT2 and SEPT6.

Sequence similarities

Belongs to the septin family.

Sequence caution

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.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
   Cellular componentCell projection
Centromere
Chromosome
Cilium
Cytoplasm
Cytoskeleton
Kinetochore
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   LigandGTP-binding
Nucleotide-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcilium morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

cytokinesis

Traceable author statement Ref.1. Source: ProtInc

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

protein heterooligomerization

Inferred from direct assay Ref.3. Source: UniProtKB

regulation of embryonic cell shape

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentactin cytoskeleton

Inferred from direct assay. Source: HPA

axon terminus

Inferred from electronic annotation. Source: Ensembl

axoneme

Inferred from sequence or structural similarity. Source: UniProtKB

cleavage furrow

Inferred from electronic annotation. Source: UniProtKB-SubCell

condensed chromosome kinetochore

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay. Source: HPA

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

microtubule cytoskeleton

Inferred from direct assay. Source: HPA

midbody

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay Ref.3. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: HPA

septin complex

Inferred from electronic annotation. Source: InterPro

spindle

Inferred from electronic annotation. Source: UniProtKB-SubCell

stress fiber

Inferred from direct assay Ref.3. Source: UniProtKB

synapse

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionGTP binding

Traceable author statement Ref.1. Source: ProtInc

identical protein binding

Inferred from physical interaction PubMed 22064074. Source: IntAct

structural molecule activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-2009373,EBI-2009373

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.12
Chain2 – 437436Septin-7
PRO_0000173528

Regions

Nucleotide binding57 – 648GTP
Nucleotide binding195 – 2039GTP By similarity
Coiled coil332 – 437106 Potential

Sites

Binding site901GTP By similarity
Binding site1161GTP; via amide nitrogen By similarity
Binding site2501GTP; via amide nitrogen and carbonyl oxygen By similarity
Binding site2651GTP By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.12
Modified residue301Phosphotyrosine By similarity
Modified residue3341Phosphoserine Ref.7 Ref.14
Modified residue3731N6-acetyllysine By similarity
Modified residue4241Phosphoserine Ref.11
Modified residue4261Phosphothreonine Ref.11 Ref.14

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

Secondary structure

........................................ 437
Helix Strand Turn

Details...

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 [UniParc].

Checksum: 803345D98374253B
Show »

FASTA43650,581

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] [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]"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] [Europe PMC] [Abstract]
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]"Septins regulate bacterial entry into host cells."
Mostowy S., Nam Tham T., Danckaert A., Guadagnini S., Boisson-Dupuis S., Pizarro-Cerda J., Cossart P.
PLoS ONE 4:E4196-E4196(2009) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 20-437 IN COMPLEX WITH GDP, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJC2352.
RefSeqNP_001779.3. NM_001788.5.
UniGeneHs.191346.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2QAGX-ray4.00C20-437[»]
3T5DX-ray3.30A/C48-316[»]
3TW4X-ray3.35A/B48-318[»]
ProteinModelPortalQ16181.
SMRQ16181. Positions 49-316.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107425. 53 interactions.
DIPDIP-47093N.
IntActQ16181. 11 interactions.
MINTMINT-5006116.
STRING9606.ENSP00000381992.

PTM databases

PhosphoSiteQ16181.

Polymorphism databases

DMDM67472677.

2D gel databases

OGPQ16181.
UCD-2DPAGEQ16181.

Proteomic databases

PaxDbQ16181.
PRIDEQ16181.

Protocols and materials databases

DNASU989.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000399034; ENSP00000381992; ENSG00000122545.
GeneID989.
KEGGhsa:989.
UCSCuc010kxc.3. human. [Q16181-1]
uc011kat.2. human. [Q16181-2]

Organism-specific databases

CTD989.
GeneCardsGC07P035807.
H-InvDBHIX0006599.
HIX0032379.
HGNCHGNC:1717. SEPT7.
HPAHPA023309.
HPA029524.
MIM603151. gene.
neXtProtNX_Q16181.
PharmGKBPA26253.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5019.
HOGENOMHOG000233586.
HOVERGENHBG065093.
InParanoidQ16181.
KOK16944.
OrthoDBEOG79KPF0.
PhylomeDBQ16181.
TreeFamTF101079.

Gene expression databases

ArrayExpressQ16181.
BgeeQ16181.
CleanExHS_SEPT7.
GenevestigatorQ16181.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR000038. Cell_div_GTP-bd.
IPR027417. P-loop_NTPase.
IPR016491. Septin.
IPR008115. Septin7.
[Graphical view]
PANTHERPTHR18884. PTHR18884. 1 hit.
PfamPF00735. Septin. 1 hit.
[Graphical view]
PIRSFPIRSF006698. Septin. 1 hit.
PRINTSPR01742. SEPTIN7.
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSEPT7. human.
EvolutionaryTraceQ16181.
GeneWikiSEPT7.
GenomeRNAi989.
NextBio4150.
PROQ16181.
SOURCESearch...

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: April 16, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 7

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