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P42208 · SEPT2_MOUSE

  • Protein
    Septin-2
  • Gene
    Septin2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Filament-forming cytoskeletal GTPase. Forms a filamentous structure with SEPTIN12, SEPTIN6, SEPTIN2 and probably SEPTIN4 at the sperm annulus which is required for the structural integrity and motility of the sperm tail during postmeiotic differentiation (By similarity).
Required for normal organization of the actin cytoskeleton. Plays a role in the biogenesis of polarized columnar-shaped epithelium by maintaining polyglutamylated microtubules, thus facilitating efficient vesicle transport, and by impeding MAP4 binding to tubulin. Required for the progression through mitosis. Forms a scaffold at the midplane of the mitotic splindle required to maintain CENPE localization at kinetochores and consequently chromosome congression. During anaphase, may be required for chromosome segregation and spindle elongation. Plays a role in ciliogenesis and collective cell movements (By similarity).
In cilia, required for the integrity of the diffusion barrier at the base of the primary cilium that prevents diffusion of transmembrane proteins between the cilia and plasma membranes: probably acts by regulating the assembly of the tectonic-like complex (also named B9 complex) by localizing TMEM231 protein

Miscellaneous

Coordinated expression with SEPTIN6 and SEPTIN7.

Features

Showing features for binding site, site.

136150100150200250300350
Type
IDPosition(s)Description
Binding site44-52GTP (UniProtKB | ChEBI)
Binding site78GTP (UniProtKB | ChEBI)
Binding site104GTP (UniProtKB | ChEBI)
Site156Important for dimerization
Binding site183-186GTP (UniProtKB | ChEBI)
Binding site241GTP (UniProtKB | ChEBI)
Binding site256GTP (UniProtKB | ChEBI)
Binding site258GTP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentactin cytoskeleton
Cellular Componentactomyosin contractile ring
Cellular Componentcell cortex
Cellular Componentcell projection
Cellular Componentcell surface
Cellular Componentciliary membrane
Cellular Componentciliary transition zone
Cellular Componentcleavage furrow
Cellular Componentcytoplasm
Cellular Componentkinetochore
Cellular Componentmicrotubule cytoskeleton
Cellular Componentmidbody
Cellular Componentmotile cilium
Cellular Componentmyelin sheath
Cellular Componentplasma membrane
Cellular Componentseptin complex
Cellular Componentspindle microtubule
Cellular Componentsynapse
Molecular Functionenzyme regulator activity
Molecular FunctionGTP binding
Molecular FunctionGTPase activity
Molecular Functionidentical protein binding
Molecular Functionmolecular adaptor activity
Biological Processcell differentiation
Biological Processcilium assembly
Biological Processcytoskeleton-dependent cytokinesis
Biological Processprotein polymerization
Biological Processregulation of L-glutamate import across plasma membrane
Biological Processregulation of protein localization
Biological Processsmoothened signaling pathway
Biological Processspermatogenesis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Septin-2
  • Alternative names
    • Neural precursor cell expressed developmentally down-regulated protein 5 (NEDD-5)

Gene names

    • Name
      Septin2
    • Synonyms
      Nedd5
      , Sept2

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P42208
  • Secondary accessions
    • B2RRZ2
    • Q3U9Y5

Proteomes

Organism-specific databases

Subcellular Location

Cleavage furrow
Midbody
Note: In metaphase cells, localized within the microtubule spindle. At the metaphase plate, in close apposition to the kinetochores of the congressed chromosomes. In cells undergoing cytokinesis, localized to the midbody, the ingressing cleavage furrow, and the central spindle (By similarity).
In interphase and postmitotic cells, localized to fibrous or granular structures, depending on the growth state of the cell. Localizes at the base of the cilia near the morphological distinction between the cilia and plasma membranes. Found in the sperm annulus

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis46Loss of GTP-binding.
Mutagenesis47Loss of GTP-binding activity.
Mutagenesis51Loss of GTP-binding activity.
Mutagenesis78Reduces affinity for GTP 20-fold.
Mutagenesis125Loss of GTP-binding activity.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 11 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

Type
IDPosition(s)Description
ChainPRO_00001735161-361Septin-2
Modified residue17Phosphotyrosine
Modified residue190N6-acetyllysine
Modified residue211Phosphotyrosine
Modified residue218Phosphoserine

Keywords

Proteomic databases

2D gel databases

PTM databases

Expression

Tissue specificity

Widely expressed.

Developmental stage

Expressed at 17 dpc in the brain with levels remaining relatively stable up to adulthood (at protein level).

Gene expression databases

Interaction

Subunit

Septins polymerize into heterooligomeric protein complexes that form filaments, and associate with cellular membranes, actin filaments and microtubules (By similarity).
GTPase activity is required for filament formation (By similarity).
Septin filaments are assembled from asymmetrical heterotrimers, composed of SEPTIN2, SEPTIN6 and SEPTIN7 that associate head-to-head to form a hexameric unit (By similarity).
Interaction between SEPTIN2 and SEPTIN7 seems indirect (By similarity).
Interacts also with SEPTIN9 and SEPTIN5 (PubMed:11739749).
Interaction with SEPTIN4 not detected (PubMed:11739749).
Component of a septin core octameric complex consisting of SEPTIN12, SEPTIN7, SEPTIN6 and SEPTIN2 or SEPTIN4 in the order 12-7-6-2-2-6-7-12 or 12-7-6-4-4-6-7-12 and located in the sperm annulus (By similarity).
Interacts with MAP4 (By similarity).
Interacts with DZIP1L (By similarity).

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain, region.

Type
IDPosition(s)Description
Domain34-306Septin-type G
Region44-51G1 motif
Region101-104G3 motif
Region182-185G4 motif
Region260-270Important for dimerization

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    361
  • Mass (Da)
    41,526
  • Last updated
    1996-02-01 v2
  • MD5 Checksum
    FADC449AA9E21C3EED0AD8B486F7298F
MSKQQPTQFINPETPGYVGFANLPNQVHRKSVKKGFEFTLMVVGESGLGKSTLINSLFLTDLYPERIIPGAAEKIERTVQIEASTVEIEERGVKLRLTVVDTPGYGDAINCRDCFKTIISYIDEQFERYLHDESGLNRRHIIDNRVHCCFYFISPFGHGLKPLDVAFMKAIHNKVNIVPVIAKADTLTLKERERLKKRILDEIEEHSIKIYHLPDAESDEDEDFKEQTRLLKASIPFSVVGSNQLIEAKGKKVRGRLYPWGVVEVENPEHNDFLKLRTMLITHMQDLQEVTQDLHYENFRSERLKRGGRKVENEDMNKDQILLEKEAELRRMQEMIARMQAQMQMQMQGGDSDSGALGQHV

Computationally mapped potential isoform sequences

There are 9 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
E9Q3V6E9Q3V6_MOUSESeptin2321
F6WYM0F6WYM0_MOUSESeptin2212
D3YYB1D3YYB1_MOUSESeptin2213
D3YZU7D3YZU7_MOUSESeptin2120
D3YV76D3YV76_MOUSESeptin277
F6UKN5F6UKN5_MOUSESeptin2107
D3Z1S1D3Z1S1_MOUSESeptin2177
D3Z3C0D3Z3C0_MOUSESeptin2221
G3UYQ0G3UYQ0_MOUSESeptin245

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
D49382
EMBL· GenBank· DDBJ
BAA08380.1
EMBL· GenBank· DDBJ
mRNA
AK028072
EMBL· GenBank· DDBJ
BAC25737.1
EMBL· GenBank· DDBJ
mRNA
AK146616
EMBL· GenBank· DDBJ
BAE27305.1
EMBL· GenBank· DDBJ
mRNA
AK151591
EMBL· GenBank· DDBJ
BAE30531.1
EMBL· GenBank· DDBJ
mRNA
AK171331
EMBL· GenBank· DDBJ
BAE42396.1
EMBL· GenBank· DDBJ
mRNA
CH466520
EMBL· GenBank· DDBJ
EDL39946.1
EMBL· GenBank· DDBJ
Genomic DNA
CH466520
EMBL· GenBank· DDBJ
EDL39948.1
EMBL· GenBank· DDBJ
Genomic DNA
BC138636
EMBL· GenBank· DDBJ
AAI38637.1
EMBL· GenBank· DDBJ
mRNA
BC138637
EMBL· GenBank· DDBJ
AAI38638.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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