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Protein

Septin-2

Gene

Sept2

Organism
Rattus norvegicus (Rat)
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. 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 similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei78 – 781GTPBy similarity
Binding sitei104 – 1041GTP; via amide nitrogenBy similarity
Sitei156 – 1561Important for dimerizationBy similarity
Binding sitei241 – 2411GTP; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei256 – 2561GTPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi44 – 518GTPBy similarity
Nucleotide bindingi183 – 1919GTPBy similarity

GO - Molecular functioni

  • enzyme regulator activity Source: Ensembl
  • GTPase activity Source: RGD
  • GTP binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Septin-2
Alternative name(s):
Vascular endothelial cell specific protein 11
Gene namesi
Name:Sept2
Synonyms:Vesp11
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 9

Organism-specific databases

RGDi620056. Sept2.

Subcellular locationi

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

  • 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. Localizes at the base of the cilia near the morphological distinction between the cilia and plasma membranes (By similarity).By similarity

GO - Cellular componenti

  • actin cytoskeleton Source: Ensembl
  • ciliary membrane Source: UniProtKB
  • ciliary transition zone Source: Ensembl
  • cleavage furrow Source: UniProtKB-SubCell
  • exocyst Source: RGD
  • extracellular exosome Source: Ensembl
  • midbody Source: UniProtKB-SubCell
  • myelin sheath Source: Ensembl
  • nucleolus Source: Ensembl
  • perinuclear region of cytoplasm Source: RGD
  • spindle Source: UniProtKB-SubCell
  • synapse Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 361361Septin-2PRO_0000270208Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171PhosphotyrosineBy similarity
Modified residuei190 – 1901N6-acetyllysineBy similarity
Modified residuei211 – 2111PhosphotyrosineBy similarity
Modified residuei218 – 2181PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ91Y81.
PRIDEiQ91Y81.

2D gel databases

World-2DPAGE0004:Q91Y81.

PTM databases

iPTMnetiQ91Y81.
PhosphoSiteiQ91Y81.

Expressioni

Gene expression databases

BgeeiENSRNOG00000017952.
GenevisibleiQ91Y81. RN.

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

Protein-protein interaction databases

BioGridi250737. 2 interactions.
IntActiQ91Y81. 3 interactions.
MINTiMINT-3381912.
STRINGi10116.ENSRNOP00000024261.

Structurei

3D structure databases

ProteinModelPortaliQ91Y81.
SMRiQ91Y81. Positions 36-306.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 306273Septin-type GAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni260 – 27011Important for dimerizationBy similarityAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2655. Eukaryota.
COG5019. LUCA.
GeneTreeiENSGT00760000118899.
HOGENOMiHOG000233586.
HOVERGENiHBG065093.
InParanoidiQ91Y81.
KOiK16942.
OMAiQFMKAIH.
OrthoDBiEOG091G07TS.
PhylomeDBiQ91Y81.
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.

Q91Y81-1 [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 SRDCFKTIIS 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
DTDSSTLGHH V
Length:361
Mass (Da):41,593
Last modified:December 1, 2001 - v1
Checksum:iC4B9335F18098641
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB027561 mRNA. Translation: BAB47151.1.
BC081745 mRNA. Translation: AAH81745.1.
RefSeqiNP_476489.1. NM_057148.2.
XP_006245574.1. XM_006245512.2.
XP_006245575.1. XM_006245513.2.
XP_006245576.1. XM_006245514.1.
UniGeneiRn.98570.

Genome annotation databases

EnsembliENSRNOT00000024261; ENSRNOP00000024261; ENSRNOG00000017952.
GeneIDi117515.
KEGGirno:117515.
UCSCiRGD:620056. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB027561 mRNA. Translation: BAB47151.1.
BC081745 mRNA. Translation: AAH81745.1.
RefSeqiNP_476489.1. NM_057148.2.
XP_006245574.1. XM_006245512.2.
XP_006245575.1. XM_006245513.2.
XP_006245576.1. XM_006245514.1.
UniGeneiRn.98570.

3D structure databases

ProteinModelPortaliQ91Y81.
SMRiQ91Y81. Positions 36-306.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250737. 2 interactions.
IntActiQ91Y81. 3 interactions.
MINTiMINT-3381912.
STRINGi10116.ENSRNOP00000024261.

PTM databases

iPTMnetiQ91Y81.
PhosphoSiteiQ91Y81.

2D gel databases

World-2DPAGE0004:Q91Y81.

Proteomic databases

PaxDbiQ91Y81.
PRIDEiQ91Y81.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000024261; ENSRNOP00000024261; ENSRNOG00000017952.
GeneIDi117515.
KEGGirno:117515.
UCSCiRGD:620056. rat.

Organism-specific databases

CTDi4735.
RGDi620056. Sept2.

Phylogenomic databases

eggNOGiKOG2655. Eukaryota.
COG5019. LUCA.
GeneTreeiENSGT00760000118899.
HOGENOMiHOG000233586.
HOVERGENiHBG065093.
InParanoidiQ91Y81.
KOiK16942.
OMAiQFMKAIH.
OrthoDBiEOG091G07TS.
PhylomeDBiQ91Y81.
TreeFamiTF101079.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ91Y81.

Gene expression databases

BgeeiENSRNOG00000017952.
GenevisibleiQ91Y81. RN.

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_RAT
AccessioniPrimary (citable) accession number: Q91Y81
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: December 1, 2001
Last modified: September 7, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Coordinated expression with SEPT2 and SEPT7.By similarity

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. 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.