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Protein

Septin-1

Gene

Sep1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in cytokinesis.Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei76 – 761GTPBy similarity
Binding sitei102 – 1021GTP; via amide nitrogenBy similarity
Binding sitei239 – 2391GTP; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei254 – 2541GTPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi42 – 498GTPBy similarity
Nucleotide bindingi181 – 1899GTPBy similarity

GO - Molecular functioni

  • GTPase activity Source: FlyBase
  • GTP binding Source: FlyBase
  • protein homodimerization activity Source: FlyBase
  • ubiquitin protein ligase binding Source: FlyBase

GO - Biological processi

  • cellularization Source: FlyBase
  • mitotic cytokinesis Source: FlyBase
  • positive regulation of apoptotic process Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Septin-1
Alternative name(s):
DIFF6 protein homolog
Protein innocent bystander
Gene namesi
Name:Sep1
Synonyms:Diff6, iby
ORF Names:CG1403
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0011710. Sep1.

Subcellular locationi

GO - Cellular componenti

  • germline ring canal Source: FlyBase
  • microtubule associated complex Source: FlyBase
  • septin complex Source: FlyBase
  • septin ring Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 361361Septin-1PRO_0000173511Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei319 – 3191Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP42207.
PRIDEiP42207.

PTM databases

iPTMnetiP42207.

Expressioni

Gene expression databases

ExpressionAtlasiP42207. differential.
GenevisibleiP42207. DM.

Interactioni

Subunit structurei

May assemble into a multicomponent structure.

GO - Molecular functioni

  • protein homodimerization activity Source: FlyBase
  • ubiquitin protein ligase binding Source: FlyBase

Protein-protein interaction databases

BioGridi59391. 9 interactions.
DIPiDIP-18454N.
MINTiMINT-305134.
STRINGi7227.FBpp0076897.

Structurei

3D structure databases

ProteinModelPortaliP42207.
SMRiP42207. Positions 32-302.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 304273Septin-type GAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2655. Eukaryota.
COG5019. LUCA.
InParanoidiP42207.
KOiK16942.
OMAiQDCFSTI.
OrthoDBiEOG79KPF0.
PhylomeDBiP42207.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

P42207-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADTKGFSSI ETPGYVGFAN LPNQVHRKSV KKGFEFTLMV VGESGLGKST
60 70 80 90 100
LVNSLFLTDL YPERIIPDAI EKQKQTVKLE ASTVEIEERG VKLRLTVVDT
110 120 130 140 150
PGFGDAIDNS NSFGAILEYI DEQYERFLRD ESGLNRRNIV DNRIHCCFYF
160 170 180 190 200
ISPFGHGLKP LDVEFMKKLH SKVNIVPVIA KADCLTKKEI LRLKCRIMQE
210 220 230 240 250
IESHGIKIYP LPDCDSDEDE DYKEQVKQLK EAVPFAVCGA NTLLEVKGKK
260 270 280 290 300
VRGRLYPWGV VEVENPDHCD FIKLRTMLIT HMQDLQEVTQ EVHYENYRSD
310 320 330 340 350
RLAKGIKGKE NGVKAERDSS SQVVSNSVLG EKDRILQEKE AELRRMQEML
360
AQMQARMQAQ Q
Length:361
Mass (Da):41,131
Last modified:November 1, 1995 - v1
Checksum:iAE7D4860B625AB00
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L33246 Genomic DNA. Translation: AAC34305.1.
X67202 mRNA. Translation: CAA47638.1.
AF017777 Genomic DNA. Translation: AAC28401.1.
AE014298 Genomic DNA. Translation: AAF50825.1.
PIRiS25063.
RefSeqiNP_523430.1. NM_078706.4.
UniGeneiDm.2682.

Genome annotation databases

EnsemblMetazoaiFBtr0077198; FBpp0076897; FBgn0011710.
GeneIDi33114.
KEGGidme:Dmel_CG1403.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L33246 Genomic DNA. Translation: AAC34305.1.
X67202 mRNA. Translation: CAA47638.1.
AF017777 Genomic DNA. Translation: AAC28401.1.
AE014298 Genomic DNA. Translation: AAF50825.1.
PIRiS25063.
RefSeqiNP_523430.1. NM_078706.4.
UniGeneiDm.2682.

3D structure databases

ProteinModelPortaliP42207.
SMRiP42207. Positions 32-302.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi59391. 9 interactions.
DIPiDIP-18454N.
MINTiMINT-305134.
STRINGi7227.FBpp0076897.

PTM databases

iPTMnetiP42207.

Proteomic databases

PaxDbiP42207.
PRIDEiP42207.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0077198; FBpp0076897; FBgn0011710.
GeneIDi33114.
KEGGidme:Dmel_CG1403.

Organism-specific databases

CTDi33114.
FlyBaseiFBgn0011710. Sep1.

Phylogenomic databases

eggNOGiKOG2655. Eukaryota.
COG5019. LUCA.
InParanoidiP42207.
KOiK16942.
OMAiQDCFSTI.
OrthoDBiEOG79KPF0.
PhylomeDBiP42207.

Miscellaneous databases

GenomeRNAii33114.
NextBioi781972.
PROiP42207.

Gene expression databases

ExpressionAtlasiP42207. differential.
GenevisibleiP42207. DM.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Localization and possible functions of Drosophila septins."
    Fares H., Peifer M., Pringle J.R.
    Mol. Biol. Cell 6:1843-1859(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Embryo.
  2. Hayward D.C., Delaney S.J., Miklos G.L.G.
    Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Embryo.
  3. "Data transferability from model organisms to human beings: insights from the functional genomics of the flightless region of Drosophila."
    Maleszka R., de Couet H.G., Miklos G.L.G.
    Proc. Natl. Acad. Sci. U.S.A. 95:3731-3736(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Canton-S.
  4. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  5. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  6. "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
    Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
    Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiSEPT1_DROME
AccessioniPrimary (citable) accession number: P42207
Secondary accession number(s): Q8IQ47, Q9VRH5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 11, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. 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.