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Protein

Septin-2

Gene

Sept2

Organism
Mus musculus (Mouse)
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. 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.By similarity3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei78GTP1
Binding sitei104GTP; via amide nitrogen1
Sitei156Important for dimerizationBy similarity1
Binding sitei241GTP; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei256GTP1
Binding sitei258GTPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi44 – 52GTP9
Nucleotide bindingi183 – 186GTP4

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: MGI
  • enzyme regulator activity Source: MGI
  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB-KW
  • identical protein binding Source: MGI
  • protein complex scaffold Source: MGI

GO - Biological processi

  • cilium assembly Source: UniProtKB
  • cytokinesis Source: UniProtKB
  • mitotic nuclear division Source: UniProtKB-KW
  • neuron projection development Source: Ensembl
  • protein polymerization Source: MGI
  • regulation of L-glutamate transport Source: MGI
  • regulation of protein localization Source: MGI
  • smoothened signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-5620912. Anchoring of the basal body to the plasma membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Septin-2
Alternative name(s):
Neural precursor cell expressed developmentally down-regulated protein 5
Short name:
NEDD-5
Gene namesi
Name:Sept2
Synonyms:Nedd-5, Nedd5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:97298. Sept2.

Subcellular locationi

  • Cytoplasm
  • Cytoplasmcytoskeleton
  • Cytoplasmcytoskeletonspindle By similarity
  • Chromosomecentromerekinetochore By similarity
  • Cleavage furrow By similarity
  • Midbody By similarity
  • Cytoplasmcell cortex By similarity
  • Cell projectioncilium membrane

  • 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, localised 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.By similarity

GO - Cellular componenti

  • actin cytoskeleton Source: MGI
  • actomyosin contractile ring Source: UniProtKB
  • axoneme Source: MGI
  • cell-cell adherens junction Source: MGI
  • cell cortex Source: MGI
  • cell projection Source: MGI
  • cell surface Source: MGI
  • ciliary membrane Source: UniProtKB
  • ciliary transition zone Source: MGI
  • cleavage furrow Source: UniProtKB-SubCell
  • condensed chromosome kinetochore Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB
  • exocyst Source: Ensembl
  • extracellular exosome Source: MGI
  • microtubule cytoskeleton Source: MGI
  • midbody Source: MGI
  • myelin sheath Source: UniProtKB
  • nucleolus Source: MGI
  • nucleus Source: MGI
  • perinuclear region of cytoplasm Source: Ensembl
  • photoreceptor connecting cilium Source: MGI
  • plasma membrane Source: MGI
  • septin complex Source: MGI
  • spindle microtubule Source: MGI
  • synapse Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi46S → D: Loss of GTP-binding. 1 Publication1
Mutagenesisi47G → V: Loss of GTP-binding activity. 1 Publication1
Mutagenesisi51S → N: Loss of GTP-binding activity. 1 Publication1
Mutagenesisi78T → G: Reduces affinity for GTP 20-fold. 1 Publication1
Mutagenesisi125Q → L: Loss of GTP-binding activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001735161 – 361Septin-2Add BLAST361

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei17PhosphotyrosineCombined sources1
Modified residuei190N6-acetyllysineBy similarity1
Modified residuei211PhosphotyrosineBy similarity1
Modified residuei218PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP42208.
MaxQBiP42208.
PaxDbiP42208.
PeptideAtlasiP42208.
PRIDEiP42208.

2D gel databases

REPRODUCTION-2DPAGEIPI00114945.
P42208.

PTM databases

iPTMnetiP42208.
PhosphoSitePlusiP42208.
SwissPalmiP42208.

Expressioni

Tissue specificityi

Widely expressed.

Developmental stagei

Expressed at 17 dpc in the brain with levels remaining relatively stable up to adulthood (at protein level).1 Publication

Gene expression databases

BgeeiENSMUSG00000026276.
CleanExiMM_SEPT2.
ExpressionAtlasiP42208. baseline and differential.
GenevisibleiP42208. MM.

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. Septin filaments are assembled from asymmetrical heterotrimers, composed of SEPT2, SEPT6 and SEPT7 that associate head-to-head to form a hexameric unit. Interaction between SEPT2 and SEPT7 seems indirect. Interacts also with SEPT9 and SEPT5. Interaction with SEPT4 not detected. Interacts with MAP4 (By similarity).By similarity

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: MGI
  • identical protein binding Source: MGI
  • protein complex scaffold Source: MGI

Protein-protein interaction databases

BioGridi201724. 18 interactors.
DIPiDIP-32438N.
IntActiP42208. 17 interactors.
MINTiMINT-3378243.
STRINGi10090.ENSMUSP00000027495.

Structurei

Secondary structure

1361
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi35 – 45Combined sources11
Helixi50 – 55Combined sources6
Beta strandi59 – 61Combined sources3
Beta strandi82 – 90Combined sources9
Beta strandi93 – 101Combined sources9
Beta strandi105 – 109Combined sources5
Helixi111 – 133Combined sources23
Beta strandi148 – 153Combined sources6
Beta strandi157 – 160Combined sources4
Helixi162 – 171Combined sources10
Turni172 – 174Combined sources3
Beta strandi177 – 182Combined sources6
Helixi184 – 186Combined sources3
Helixi189 – 205Combined sources17
Helixi222 – 233Combined sources12
Beta strandi236 – 238Combined sources3
Beta strandi245 – 247Combined sources3
Beta strandi249 – 258Combined sources10
Beta strandi261 – 264Combined sources4
Turni268 – 270Combined sources3
Helixi273 – 293Combined sources21
Helixi295 – 303Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FTQX-ray2.90A/B/C/D33-306[»]
ProteinModelPortaliP42208.
SMRiP42208.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42208.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini34 – 306Septin-type GAdd BLAST273

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni260 – 270Important for dimerizationBy similarityAdd BLAST11

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2655. Eukaryota.
COG5019. LUCA.
GeneTreeiENSGT00860000133688.
HOGENOMiHOG000233586.
HOVERGENiHBG065093.
InParanoidiP42208.
KOiK16942.
OMAiQFMKAIH.
OrthoDBiEOG091G07TS.
PhylomeDBiP42208.
TreeFamiTF101079.

Family and domain databases

CDDicd01850. CDC_Septin. 1 hit.
Gene3Di3.40.50.300. 1 hit.
InterProiIPR030379. G_SEPTIN_dom.
IPR027417. P-loop_NTPase.
IPR016491. Septin.
IPR008113. Septin2.
[Graphical view]
PANTHERiPTHR18884. PTHR18884. 1 hit.
PfamiPF00735. Septin. 1 hit.
[Graphical view]
PIRSFiPIRSF006698. Septin. 1 hit.
PRINTSiPR01740. SEPTIN2.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51719. G_SEPTIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P42208-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKQQPTQFI NPETPGYVGF ANLPNQVHRK SVKKGFEFTL MVVGESGLGK
60 70 80 90 100
STLINSLFLT DLYPERIIPG AAEKIERTVQ IEASTVEIEE RGVKLRLTVV
110 120 130 140 150
DTPGYGDAIN CRDCFKTIIS YIDEQFERYL HDESGLNRRH IIDNRVHCCF
160 170 180 190 200
YFISPFGHGL KPLDVAFMKA IHNKVNIVPV IAKADTLTLK ERERLKKRIL
210 220 230 240 250
DEIEEHSIKI YHLPDAESDE DEDFKEQTRL LKASIPFSVV GSNQLIEAKG
260 270 280 290 300
KKVRGRLYPW GVVEVENPEH NDFLKLRTML ITHMQDLQEV TQDLHYENFR
310 320 330 340 350
SERLKRGGRK VENEDMNKDQ ILLEKEAELR RMQEMIARMQ AQMQMQMQGG
360
DSDSGALGQH V
Length:361
Mass (Da):41,526
Last modified:February 1, 1996 - v2
Checksum:iC4BFFB3F1815E081
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D49382 mRNA. Translation: BAA08380.1.
AK028072 mRNA. Translation: BAC25737.1.
AK146616 mRNA. Translation: BAE27305.1.
AK151591 mRNA. Translation: BAE30531.1.
AK171331 mRNA. Translation: BAE42396.1.
CH466520 Genomic DNA. Translation: EDL39946.1.
CH466520 Genomic DNA. Translation: EDL39948.1.
BC138636 mRNA. Translation: AAI38637.1.
BC138637 mRNA. Translation: AAI38638.1.
CCDSiCCDS15190.1.
RefSeqiNP_001153189.1. NM_001159717.1.
NP_001153190.1. NM_001159718.1.
NP_001153191.1. NM_001159719.1.
NP_035021.1. NM_010891.2.
XP_006529304.1. XM_006529241.2.
XP_006529305.1. XM_006529242.1.
UniGeneiMm.428652.

Genome annotation databases

EnsembliENSMUST00000027495; ENSMUSP00000027495; ENSMUSG00000026276.
ENSMUST00000168776; ENSMUSP00000132850; ENSMUSG00000026276.
ENSMUST00000179353; ENSMUSP00000136366; ENSMUSG00000026276.
GeneIDi18000.
KEGGimmu:18000.
UCSCiuc007cea.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D49382 mRNA. Translation: BAA08380.1.
AK028072 mRNA. Translation: BAC25737.1.
AK146616 mRNA. Translation: BAE27305.1.
AK151591 mRNA. Translation: BAE30531.1.
AK171331 mRNA. Translation: BAE42396.1.
CH466520 Genomic DNA. Translation: EDL39946.1.
CH466520 Genomic DNA. Translation: EDL39948.1.
BC138636 mRNA. Translation: AAI38637.1.
BC138637 mRNA. Translation: AAI38638.1.
CCDSiCCDS15190.1.
RefSeqiNP_001153189.1. NM_001159717.1.
NP_001153190.1. NM_001159718.1.
NP_001153191.1. NM_001159719.1.
NP_035021.1. NM_010891.2.
XP_006529304.1. XM_006529241.2.
XP_006529305.1. XM_006529242.1.
UniGeneiMm.428652.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FTQX-ray2.90A/B/C/D33-306[»]
ProteinModelPortaliP42208.
SMRiP42208.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201724. 18 interactors.
DIPiDIP-32438N.
IntActiP42208. 17 interactors.
MINTiMINT-3378243.
STRINGi10090.ENSMUSP00000027495.

PTM databases

iPTMnetiP42208.
PhosphoSitePlusiP42208.
SwissPalmiP42208.

2D gel databases

REPRODUCTION-2DPAGEIPI00114945.
P42208.

Proteomic databases

EPDiP42208.
MaxQBiP42208.
PaxDbiP42208.
PeptideAtlasiP42208.
PRIDEiP42208.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027495; ENSMUSP00000027495; ENSMUSG00000026276.
ENSMUST00000168776; ENSMUSP00000132850; ENSMUSG00000026276.
ENSMUST00000179353; ENSMUSP00000136366; ENSMUSG00000026276.
GeneIDi18000.
KEGGimmu:18000.
UCSCiuc007cea.2. mouse.

Organism-specific databases

CTDi4735.
MGIiMGI:97298. Sept2.

Phylogenomic databases

eggNOGiKOG2655. Eukaryota.
COG5019. LUCA.
GeneTreeiENSGT00860000133688.
HOGENOMiHOG000233586.
HOVERGENiHBG065093.
InParanoidiP42208.
KOiK16942.
OMAiQFMKAIH.
OrthoDBiEOG091G07TS.
PhylomeDBiP42208.
TreeFamiTF101079.

Enzyme and pathway databases

ReactomeiR-MMU-5620912. Anchoring of the basal body to the plasma membrane.

Miscellaneous databases

ChiTaRSiSept2. mouse.
EvolutionaryTraceiP42208.
PROiP42208.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026276.
CleanExiMM_SEPT2.
ExpressionAtlasiP42208. baseline and differential.
GenevisibleiP42208. MM.

Family and domain databases

CDDicd01850. CDC_Septin. 1 hit.
Gene3Di3.40.50.300. 1 hit.
InterProiIPR030379. G_SEPTIN_dom.
IPR027417. P-loop_NTPase.
IPR016491. Septin.
IPR008113. Septin2.
[Graphical view]
PANTHERiPTHR18884. PTHR18884. 1 hit.
PfamiPF00735. Septin. 1 hit.
[Graphical view]
PIRSFiPIRSF006698. Septin. 1 hit.
PRINTSiPR01740. SEPTIN2.
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51719. G_SEPTIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSEPT2_MOUSE
AccessioniPrimary (citable) accession number: P42208
Secondary accession number(s): B2RRZ2, Q3U9Y5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: February 1, 1996
Last modified: November 30, 2016
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Coordinated expression with SEPT6 and SEPT7.By similarity

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.