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Protein

Septin-2

Gene

Sept2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Filament-forming cytoskeletal GTPase. Forms a filamentous structure with SEPT12, SEPT6, SEPT2 and probably SEPT4 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.By similarity3 Publications

Miscellaneous

Coordinated expression with SEPT6 and SEPT7.By similarity

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

  • enzyme regulator activity Source: MGI
  • GTPase activity Source: GO_Central
  • GTP binding Source: UniProtKB-KW
  • identical protein binding Source: MGI
  • protein-containing complex scaffold activity Source: MGI

GO - Biological processi

  • cilium assembly Source: UniProtKB
  • cytoskeleton-dependent cytokinesis Source: UniProtKB
  • mitotic cytokinesis Source: GO_Central
  • neuron projection development Source: MGI
  • protein polymerization Source: MGI
  • regulation of L-glutamate import across plasma membrane Source: MGI
  • regulation of protein localization Source: MGI
  • septin ring assembly Source: GO_Central
  • smoothened signaling pathway Source: UniProtKB
  • spermatogenesis Source: UniProtKB-KW

Keywordsi

Biological processCell cycle, Cell division, Differentiation, Mitosis, Spermatogenesis
LigandGTP-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:97298 Sept2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cell projection, Centromere, Chromosome, Cilium, Cytoplasm, Cytoskeleton, Flagellum, 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-2DPAGEiIPI00114945
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 Expressed in 301 organ(s), highest expression level in fibroblast
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 (By similarity). GTPase activity is required for filament formation (By similarity). Septin filaments are assembled from asymmetrical heterotrimers, composed of SEPT2, SEPT6 and SEPT7 that associate head-to-head to form a hexameric unit (By similarity). Interaction between SEPT2 and SEPT7 seems indirect (By similarity). Interacts also with SEPT9 and SEPT5 (PubMed:11739749). Interaction with SEPT4 not detected (PubMed:11739749). Component of a septin core octomeric complex consisting of SEPT12, SEPT7, SEPT6 and SEPT2 or SEPT4 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).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi201724, 19 interactors
DIPiDIP-32438N
IntActiP42208, 21 interactors
MINTiP42208
STRINGi10090.ENSMUSP00000027495

Structurei

Secondary structure

1361
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP42208
SMRiP42208
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42208

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini34 – 306Septin-type GPROSITE-ProRule annotationAdd BLAST273

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni44 – 51G1 motifPROSITE-ProRule annotation8
Regioni101 – 104G3 motifPROSITE-ProRule annotation4
Regioni182 – 185G4 motifPROSITE-ProRule annotation4
Regioni260 – 270Important for dimerizationBy similarityAdd BLAST11

Sequence similaritiesi

Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Septin GTPase family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2655 Eukaryota
COG5019 LUCA
GeneTreeiENSGT00910000144020
HOGENOMiHOG000233586
HOVERGENiHBG065093
InParanoidiP42208
KOiK16942
OMAiQWEQHLI
OrthoDBiEOG091G07TS
PhylomeDBiP42208
TreeFamiTF101079

Family and domain databases

CDDicd01850 CDC_Septin, 1 hit
InterProiView protein in InterPro
IPR030379 G_SEPTIN_dom
IPR027417 P-loop_NTPase
IPR016491 Septin
IPR008113 Septin2
PfamiView protein in Pfam
PF00735 Septin, 1 hit
PIRSFiPIRSF006698 Septin, 1 hit
PRINTSiPR01740 SEPTIN2
SUPFAMiSSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS51719 G_SEPTIN, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

This entry has 1 described isoform and 9 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 9 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9Q3V6E9Q3V6_MOUSE
Septin-2
Sept2
321Annotation score:
D3YYB1D3YYB1_MOUSE
Septin-2
Sept2
213Annotation score:
F6WYM0F6WYM0_MOUSE
Septin-2
Sept2
212Annotation score:
D3Z3C0D3Z3C0_MOUSE
Septin-2
Sept2
221Annotation score:
D3YZU7D3YZU7_MOUSE
Septin-2
Sept2
120Annotation score:
D3YV76D3YV76_MOUSE
Septin-2
Sept2
77Annotation score:
D3Z1S1D3Z1S1_MOUSE
Septin-2
Sept2
177Annotation score:
F6UKN5F6UKN5_MOUSE
Septin-2
Sept2
107Annotation score:
G3UYQ0G3UYQ0_MOUSE
Septin-2
Sept2
45Annotation score:

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; ENSMUSG00000116048
ENSMUST00000179353; ENSMUSP00000136366; ENSMUSG00000116048
GeneIDi18000
KEGGimmu:18000
UCSCiuc007cea.2 mouse

Similar proteinsi

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, 19 interactors
DIPiDIP-32438N
IntActiP42208, 21 interactors
MINTiP42208
STRINGi10090.ENSMUSP00000027495

PTM databases

iPTMnetiP42208
PhosphoSitePlusiP42208
SwissPalmiP42208

2D gel databases

REPRODUCTION-2DPAGEiIPI00114945
P42208

Proteomic databases

EPDiP42208
MaxQBiP42208
PaxDbiP42208
PeptideAtlasiP42208
PRIDEiP42208

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027495; ENSMUSP00000027495; ENSMUSG00000026276
ENSMUST00000168776; ENSMUSP00000132850; ENSMUSG00000116048
ENSMUST00000179353; ENSMUSP00000136366; ENSMUSG00000116048
GeneIDi18000
KEGGimmu:18000
UCSCiuc007cea.2 mouse

Organism-specific databases

CTDi4735
MGIiMGI:97298 Sept2

Phylogenomic databases

eggNOGiKOG2655 Eukaryota
COG5019 LUCA
GeneTreeiENSGT00910000144020
HOGENOMiHOG000233586
HOVERGENiHBG065093
InParanoidiP42208
KOiK16942
OMAiQWEQHLI
OrthoDBiEOG091G07TS
PhylomeDBiP42208
TreeFamiTF101079

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiSept2 mouse
EvolutionaryTraceiP42208
PROiPR:P42208
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026276 Expressed in 301 organ(s), highest expression level in fibroblast
CleanExiMM_SEPT2
ExpressionAtlasiP42208 baseline and differential
GenevisibleiP42208 MM

Family and domain databases

CDDicd01850 CDC_Septin, 1 hit
InterProiView protein in InterPro
IPR030379 G_SEPTIN_dom
IPR027417 P-loop_NTPase
IPR016491 Septin
IPR008113 Septin2
PfamiView protein in Pfam
PF00735 Septin, 1 hit
PIRSFiPIRSF006698 Septin, 1 hit
PRINTSiPR01740 SEPTIN2
SUPFAMiSSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS51719 G_SEPTIN, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiSEPT2_MOUSE
AccessioniPrimary (citable) accession number: P42208
Secondary accession number(s): B2RRZ2, Q3U9Y5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: February 1, 1996
Last modified: November 7, 2018
This is version 177 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

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