Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Septin-10

Gene

SEPT10

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential).By similarityCurated

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei128GTP; via amide nitrogenBy similarity1
Binding sitei263GTP; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei278GTPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi73 – 80GTPBy similarity8
Nucleotide bindingi209 – 217GTPBy similarity9

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processCell cycle, Cell division
LigandGTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Septin-10
Gene namesi
Name:SEPT10
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
Proteomesi
  • UP000001595 Componenti: Unplaced

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

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001735401 – 467Septin-10Add BLAST467

Proteomic databases

PRIDEiQ5REG8

Interactioni

Subunit structurei

Septins polymerize into heterooligomeric protein complexes that form filaments, and can associate with cellular membranes, actin filaments and microtubules. GTPase activity is required for filament formation (By similarity).By similarity

Protein-protein interaction databases

STRINGi9601.ENSPPYP00000013540

Structurei

3D structure databases

ProteinModelPortaliQ5REG8
SMRiQ5REG8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini63 – 329Septin-type GPROSITE-ProRule annotationAdd BLAST267

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni73 – 80G1 motifPROSITE-ProRule annotation8
Regioni125 – 128G3 motifPROSITE-ProRule annotation4
Regioni208 – 211G4 motifPROSITE-ProRule annotation4

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
HOVERGENiHBG065093
InParanoidiQ5REG8

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q5REG8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSEVARHL LFQSHMATKT TCMSSQGSDD EQRKRENIRS LTMSDHVGFE
60 70 80 90 100
SLPDQLVNRS IQQGFCFNIL CVGETGIGKS TLIDTLFNTN FEDYESSHFC
110 120 130 140 150
PNVKLKAQTY ELQESNVQLK LTIVNTVGFG DQINKEESYQ PIVDYIDAQF
160 170 180 190 200
EAYLQEELKI KRSLFTYHDS RIHVCLYFIS PTGHSLKTLD LLTMKNLDSK
210 220 230 240 250
VNIIPVIAKA DTVSKTELQK FKIKLMSELV SNGVQIYQFP TDDDTIAKVN
260 270 280 290 300
AAMNGQLPFA VVGSMDEVKV GNKMVKARQY PWGVVQVENE NHCDFVKLRE
310 320 330 340 350
VLICTNMEDL REQTHTRHYE LYRRCKLEEM GFTDVGPENK PVSLQETYEA
360 370 380 390 400
KRHEFHGERQ RKEEEMKQMF VQRVKEKEAI LKEAERELQA KFEHLKRLHQ
410 420 430 440 450
EERMKLEEKR KLLEEEIIAF SKKKATSEIF HSQSFLATGS NLRKQPQLLI
460
FMEKYFQVQG QYVSQSE
Length:467
Mass (Da):54,203
Last modified:December 21, 2004 - v1
Checksum:i5B70FC4F2F69CDEF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR857561 mRNA Translation: CAH89839.1
UniGeneiPab.1378

Similar proteinsi

Entry informationi

Entry nameiSEP10_PONAB
AccessioniPrimary (citable) accession number: Q5REG8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: December 21, 2004
Last modified: June 20, 2018
This is version 53 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health