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Protein

Septin-2

Gene

SEPT2

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. 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. May play a role in the internalization of 2 intracellular microbial pathogens, Listeria monocytogenes and Shigella flexneri.4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei78GTPBy similarity1
Binding sitei104GTP; via amide nitrogenBy similarity1
Sitei156Important for dimerization1
Binding sitei241GTP; via amide nitrogen and carbonyl oxygen1
Binding sitei256GTP1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi44 – 51GTP8
Nucleotide bindingi183 – 191GTP9

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000168385-MONOMER.
ReactomeiR-HSA-5620912. Anchoring of the basal body to the plasma membrane.
SIGNORiQ15019.

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:DIFF6, KIAA0158, NEDD5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:7729. SEPT2.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Cytoplasmcytoskeleton 1 Publication
  • Cytoplasmcytoskeletonspindle 1 Publication
  • Chromosomecentromerekinetochore 1 Publication
  • Cleavage furrow 1 Publication
  • Midbody 1 Publication
  • Cytoplasmcell cortex 1 Publication
  • 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. During bacterial infection, displays a collar shape structure next to actin at the pole of invading bacteria. In epithelial cells, colocalizes with polyglutamylated tubulin around the trans-Golgi network, as well as juxatnuclear and proximal Golgi apparatus. Localizes at the base of the cilia near the morphological distinction between the cilia and plasma membranes.

GO - Cellular componenti

  • actin cytoskeleton Source: HPA
  • axoneme Source: GO_Central
  • cell-cell adherens junction Source: BHF-UCL
  • ciliary membrane Source: UniProtKB
  • cleavage furrow Source: UniProtKB-SubCell
  • condensed chromosome kinetochore Source: UniProtKB-SubCell
  • cytoplasm Source: UniProtKB
  • exocyst Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • midbody Source: UniProtKB-SubCell
  • myelin sheath Source: Ensembl
  • non-motile cilium Source: GO_Central
  • nucleolus Source: HPA
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: Ensembl
  • photoreceptor connecting cilium Source: GO_Central
  • septin complex Source: GO_Central
  • spindle Source: UniProtKB-SubCell
  • synapse Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi156F → D: Loss of dimerization. 1 Publication1
Mutagenesisi218S → A: Loss of phosphorylation. 1 Publication1
Mutagenesisi260W → A: Loss of dimerization. 1 Publication1
Mutagenesisi270H → D: Loss of dimerization. 1 Publication1

Organism-specific databases

DisGeNETi4735.
OpenTargetsiENSG00000168385.
PharmGKBiPA31535.

Polymorphism and mutation databases

DMDMi2500769.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001735151 – 361Septin-2Add BLAST361

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei17PhosphotyrosineBy similarity1
Modified residuei190N6-acetyllysineCombined sources1
Modified residuei211PhosphotyrosineCombined sources1
Modified residuei218PhosphoserineCombined sources2 Publications1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ15019.
MaxQBiQ15019.
PaxDbiQ15019.
PeptideAtlasiQ15019.
PRIDEiQ15019.
TopDownProteomicsiQ15019-1. [Q15019-1]

2D gel databases

OGPiQ15019.

PTM databases

iPTMnetiQ15019.
PhosphoSitePlusiQ15019.
SwissPalmiQ15019.

Expressioni

Tissue specificityi

Widely expressed. Up-regulated in liver cancer.2 Publications

Gene expression databases

BgeeiENSG00000168385.
CleanExiHS_SEPT2.
ExpressionAtlasiQ15019. baseline and differential.
GenevisibleiQ15019. HS.

Organism-specific databases

HPAiCAB017190.
HPA018481.

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. Interaction between SEPT2 and SEPT7 seems indirect. Interacts with SEPT5 (By similarity). Interaction with SEPT4 not detected (By similarity). Interacts with SEPT9. Interacts with MAP4.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PLEKHF2Q9H8W43EBI-741220,EBI-742388
SEPT5Q997193EBI-741220,EBI-373345
SEPT6Q141419EBI-741220,EBI-745901

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL

Protein-protein interaction databases

BioGridi110812. 86 interactors.
DIPiDIP-38220N.
IntActiQ15019. 25 interactors.
MINTiMINT-1433588.
STRINGi9606.ENSP00000353157.

Structurei

Secondary structure

1361
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi23 – 34Combined sources12
Beta strandi38 – 45Combined sources8
Helixi50 – 58Combined sources9
Helixi78 – 83Combined sources6
Beta strandi85 – 88Combined sources4
Beta strandi95 – 102Combined sources8
Helixi118 – 133Combined sources16
Beta strandi148 – 153Combined sources6
Beta strandi155 – 159Combined sources5
Helixi162 – 171Combined sources10
Turni172 – 174Combined sources3
Beta strandi177 – 181Combined sources5
Helixi184 – 186Combined sources3
Helixi189 – 205Combined sources17
Helixi225 – 232Combined sources8
Beta strandi236 – 238Combined sources3
Beta strandi243 – 245Combined sources3
Beta strandi254 – 258Combined sources5
Beta strandi261 – 264Combined sources4
Turni268 – 270Combined sources3
Helixi273 – 282Combined sources10
Helixi284 – 293Combined sources10
Helixi295 – 305Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QA5X-ray3.40A/B1-315[»]
2QAGX-ray4.00A1-361[»]
2QNRX-ray2.60A/B22-320[»]
ProteinModelPortaliQ15019.
SMRiQ15019.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15019.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2655. Eukaryota.
COG5019. LUCA.
GeneTreeiENSGT00860000133688.
HOGENOMiHOG000233586.
HOVERGENiHBG065093.
InParanoidiQ15019.
KOiK16942.
OMAiQFMKAIH.
OrthoDBiEOG091G07TS.
PhylomeDBiQ15019.
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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15019-1) [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
MSKQQPTQFI NPETPGYVGF ANLPNQVHRK SVKKGFEFTL MVVGESGLGK
60 70 80 90 100
STLINSLFLT DLYPERVIPG 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
DEIEEHNIKI 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
DGDGGALGHH V
Length:361
Mass (Da):41,487
Last modified:November 1, 1997 - v1
Checksum:i12CCBBE30806F92F
GO
Isoform 2 (identifier: Q15019-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MPWISEGRATRPCLRVPSARRGDEGLHQRDEASQKM

Note: No experimental confirmation available.
Show »
Length:396
Mass (Da):45,461
Checksum:i4BD59305219D99B5
GO
Isoform 3 (identifier: Q15019-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     72-72: A → AALNTRKTLLW

Note: No experimental confirmation available.
Show »
Length:371
Mass (Da):42,685
Checksum:i0ED0C05E2DA308B4
GO

Sequence cautioni

The sequence AAY14718 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence BAA09928 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti69P → S in AAH14455 (PubMed:15489334).Curated1
Sequence conflicti360 – 361HV → TCKVMCTYKKSEKTLSWIKK KTFQMHDPAVCFQSLGGCHP HFNSTCA in BAA05893 (PubMed:8697812).Curated2

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0382711M → MPWISEGRATRPCLRVPSAR RGDEGLHQRDEASQKM in isoform 2. 1 Publication1
Alternative sequenceiVSP_05517672A → AALNTRKTLLW in isoform 3. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D63878 mRNA. Translation: BAA09928.2. Different initiation.
D28540 mRNA. Translation: BAA05893.1.
AF038404 mRNA. Translation: AAB92377.1.
AK294563 mRNA. Translation: BAG57759.1.
AC005104 Genomic DNA. No translation available.
AC104841 Genomic DNA. Translation: AAY14718.1. Sequence problems.
BC014455 mRNA. Translation: AAH14455.1.
BC033559 mRNA. Translation: AAH33559.1.
CCDSiCCDS2548.1. [Q15019-1]
CCDS63195.1. [Q15019-3]
CCDS74682.1. [Q15019-2]
RefSeqiNP_001008491.1. NM_001008491.2. [Q15019-1]
NP_001008492.1. NM_001008492.2. [Q15019-1]
NP_001269901.1. NM_001282972.1. [Q15019-2]
NP_001269902.1. NM_001282973.1. [Q15019-3]
NP_001307958.1. NM_001321029.1.
NP_001307959.1. NM_001321030.1. [Q15019-1]
NP_001307960.1. NM_001321031.1. [Q15019-1]
NP_001307961.1. NM_001321032.1. [Q15019-1]
NP_001307962.1. NM_001321033.1. [Q15019-1]
NP_001307963.1. NM_001321034.1. [Q15019-1]
NP_001307964.1. NM_001321035.1. [Q15019-1]
NP_004395.1. NM_004404.4. [Q15019-1]
NP_006146.1. NM_006155.2. [Q15019-1]
XP_016859694.1. XM_017004205.1. [Q15019-1]
XP_016859695.1. XM_017004206.1. [Q15019-1]
UniGeneiHs.721234.

Genome annotation databases

EnsembliENST00000360051; ENSP00000353157; ENSG00000168385. [Q15019-1]
ENST00000391971; ENSP00000375832; ENSG00000168385. [Q15019-1]
ENST00000391973; ENSP00000375834; ENSG00000168385. [Q15019-1]
ENST00000401990; ENSP00000385109; ENSG00000168385. [Q15019-3]
ENST00000402092; ENSP00000385172; ENSG00000168385. [Q15019-1]
ENST00000616972; ENSP00000479861; ENSG00000168385. [Q15019-2]
GeneIDi4735.
KEGGihsa:4735.
UCSCiuc002wbc.5. human. [Q15019-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D63878 mRNA. Translation: BAA09928.2. Different initiation.
D28540 mRNA. Translation: BAA05893.1.
AF038404 mRNA. Translation: AAB92377.1.
AK294563 mRNA. Translation: BAG57759.1.
AC005104 Genomic DNA. No translation available.
AC104841 Genomic DNA. Translation: AAY14718.1. Sequence problems.
BC014455 mRNA. Translation: AAH14455.1.
BC033559 mRNA. Translation: AAH33559.1.
CCDSiCCDS2548.1. [Q15019-1]
CCDS63195.1. [Q15019-3]
CCDS74682.1. [Q15019-2]
RefSeqiNP_001008491.1. NM_001008491.2. [Q15019-1]
NP_001008492.1. NM_001008492.2. [Q15019-1]
NP_001269901.1. NM_001282972.1. [Q15019-2]
NP_001269902.1. NM_001282973.1. [Q15019-3]
NP_001307958.1. NM_001321029.1.
NP_001307959.1. NM_001321030.1. [Q15019-1]
NP_001307960.1. NM_001321031.1. [Q15019-1]
NP_001307961.1. NM_001321032.1. [Q15019-1]
NP_001307962.1. NM_001321033.1. [Q15019-1]
NP_001307963.1. NM_001321034.1. [Q15019-1]
NP_001307964.1. NM_001321035.1. [Q15019-1]
NP_004395.1. NM_004404.4. [Q15019-1]
NP_006146.1. NM_006155.2. [Q15019-1]
XP_016859694.1. XM_017004205.1. [Q15019-1]
XP_016859695.1. XM_017004206.1. [Q15019-1]
UniGeneiHs.721234.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2QA5X-ray3.40A/B1-315[»]
2QAGX-ray4.00A1-361[»]
2QNRX-ray2.60A/B22-320[»]
ProteinModelPortaliQ15019.
SMRiQ15019.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110812. 86 interactors.
DIPiDIP-38220N.
IntActiQ15019. 25 interactors.
MINTiMINT-1433588.
STRINGi9606.ENSP00000353157.

PTM databases

iPTMnetiQ15019.
PhosphoSitePlusiQ15019.
SwissPalmiQ15019.

Polymorphism and mutation databases

DMDMi2500769.

2D gel databases

OGPiQ15019.

Proteomic databases

EPDiQ15019.
MaxQBiQ15019.
PaxDbiQ15019.
PeptideAtlasiQ15019.
PRIDEiQ15019.
TopDownProteomicsiQ15019-1. [Q15019-1]

Protocols and materials databases

DNASUi4735.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000360051; ENSP00000353157; ENSG00000168385. [Q15019-1]
ENST00000391971; ENSP00000375832; ENSG00000168385. [Q15019-1]
ENST00000391973; ENSP00000375834; ENSG00000168385. [Q15019-1]
ENST00000401990; ENSP00000385109; ENSG00000168385. [Q15019-3]
ENST00000402092; ENSP00000385172; ENSG00000168385. [Q15019-1]
ENST00000616972; ENSP00000479861; ENSG00000168385. [Q15019-2]
GeneIDi4735.
KEGGihsa:4735.
UCSCiuc002wbc.5. human. [Q15019-1]

Organism-specific databases

CTDi4735.
DisGeNETi4735.
GeneCardsiSEPT2.
HGNCiHGNC:7729. SEPT2.
HPAiCAB017190.
HPA018481.
MIMi601506. gene.
neXtProtiNX_Q15019.
OpenTargetsiENSG00000168385.
PharmGKBiPA31535.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2655. Eukaryota.
COG5019. LUCA.
GeneTreeiENSGT00860000133688.
HOGENOMiHOG000233586.
HOVERGENiHBG065093.
InParanoidiQ15019.
KOiK16942.
OMAiQFMKAIH.
OrthoDBiEOG091G07TS.
PhylomeDBiQ15019.
TreeFamiTF101079.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000168385-MONOMER.
ReactomeiR-HSA-5620912. Anchoring of the basal body to the plasma membrane.
SIGNORiQ15019.

Miscellaneous databases

ChiTaRSiSEPT2. human.
EvolutionaryTraceiQ15019.
GeneWikiiSEPT2.
GenomeRNAii4735.
PROiQ15019.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000168385.
CleanExiHS_SEPT2.
ExpressionAtlasiQ15019. baseline and differential.
GenevisibleiQ15019. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: Q15019
Secondary accession number(s): B4DGE8
, Q14132, Q53QU3, Q8IUK9, Q96CB0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: November 30, 2016
This is version 183 of the entry and version 1 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 SEPT6 and SEPT7.

Keywords - Technical termi

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

Documents

  1. Human chromosome 2
    Human chromosome 2: 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

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.