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Protein

Septin-7

Gene

SEPT7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. 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
Complete GO annotation...

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 Componenti: 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. cell cortex Source: Ensembl
  5. cleavage furrow Source: UniProtKB-SubCell
  6. condensed chromosome kinetochore Source: UniProtKB-SubCell
  7. cytoplasm Source: HPA
  8. extracellular vesicular exosome Source: UniProtKB
  9. microtubule cytoskeleton Source: HPA
  10. midbody Source: UniProtKB-SubCell
  11. nucleolus Source: HPA
  12. nucleus Source: UniProtKB
  13. plasma membrane Source: HPA
  14. spindle Source: UniProtKB-SubCell
  15. stress fiber Source: UniProtKB
  16. synapse Source: Ensembl
Complete GO annotation...

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

BgeeiQ16181.
CleanExiHS_SEPT7.
ExpressionAtlasiQ16181. baseline and differential.
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. 62 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 – 578Combined sources
Helixi63 – 708Combined sources
Beta strandi71 – 733Combined sources
Beta strandi94 – 1007Combined sources
Beta strandi107 – 1137Combined sources
Turni124 – 1274Combined sources
Helixi128 – 14619Combined sources
Beta strandi147 – 1493Combined sources
Beta strandi160 – 1656Combined sources
Helixi174 – 18310Combined sources
Turni184 – 1863Combined sources
Beta strandi189 – 1957Combined sources
Helixi196 – 1983Combined sources
Helixi201 – 21717Combined sources
Helixi238 – 2425Combined sources
Beta strandi245 – 2473Combined sources
Beta strandi264 – 2663Combined sources
Beta strandi271 – 2755Combined sources
Turni277 – 2793Combined sources
Helixi282 – 2909Combined sources
Turni291 – 2933Combined sources
Helixi294 – 30310Combined sources
Helixi305 – 31511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InterProiIPR030379. G_SEPTIN_dom.
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. AlignAdd to basket

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

        10         20         30         40         50
MSVSARSAAA EERSVNSSTM VAQQKNLEGY VGFANLPNQV YRKSVKRGFE
60 70 80 90 100
FTLMVVGESG LGKSTLINSL FLTDLYSPEY PGPSHRIKKT VQVEQSKVLI
110 120 130 140 150
KEGGVQLLLT IVDTPGFGDA VDNSNCWQPV IDYIDSKFED YLNAESRVNR
160 170 180 190 200
RQMPDNRVQC CLYFIAPSGH GLKPLDIEFM KRLHEKVNII PLIAKADTLT
210 220 230 240 250
PEECQQFKKQ IMKEIQEHKI KIYEFPETDD EEENKLVKKI KDRLPLAVVG
260 270 280 290 300
SNTIIEVNGK RVRGRQYPWG VAEVENGEHC DFTILRNMLI RTHMQDLKDV
310 320 330 340 350
TNNVHYENYR SRKLAAVTYN GVDNNKNKGQ LTKSPLAQME EERREHVAKM
360 370 380 390 400
KKMEMEMEQV FEMKVKEKVQ KLKDSEAELQ RRHEQMKKNL EAQHKELEEK
410 420 430
RRQFEDEKAN WEAQQRILEQ QNSSRTLEKN KKKGKIF
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.Curated
The sequence AAH67264.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH93640.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAH93642.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi107425. 62 interactions.
DIPiDIP-47093N.
IntActiQ16181. 11 interactions.
MINTiMINT-5006116.
STRINGi9606.ENSP00000381992.

PTM databases

PhosphoSiteiQ16181.

Polymorphism databases

DMDMi67472677.

2D gel databases

OGPiQ16181.
UCD-2DPAGEQ16181.

Proteomic databases

MaxQBiQ16181.
PaxDbiQ16181.
PRIDEiQ16181.

Protocols and materials databases

DNASUi989.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi989.
GeneCardsiGC07P035807.
H-InvDBHIX0006599.
HIX0032379.
HGNCiHGNC:1717. SEPT7.
HPAiHPA023309.
HPA029524.
MIMi603151. gene.
neXtProtiNX_Q16181.
PharmGKBiPA26253.
GenAtlasiSearch...

Phylogenomic databases

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

Miscellaneous databases

ChiTaRSiSEPT7. human.
EvolutionaryTraceiQ16181.
GeneWikiiSEPT7.
GenomeRNAii989.
NextBioi4150.
PROiQ16181.
SOURCEiSearch...

Gene expression databases

BgeeiQ16181.
CleanExiHS_SEPT7.
ExpressionAtlasiQ16181. baseline and differential.
GenevestigatoriQ16181.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR030379. G_SEPTIN_dom.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1993) [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(2003) [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(2003) [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(2004) [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(2004) [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(2004) [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(2005) [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(2005) [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(2006) [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(2007) [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(2008) [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(2009) [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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  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: March 4, 2015
This is version 141 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.