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Protein

Septin homolog spn1

Gene

spn1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a role in the cell cycle. Involved in a late stage of septum formation leading to the separation of the daughter cells.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei139 – 1391GTPBy similarity
Binding sitei165 – 1651GTP; via amide nitrogenBy similarity
Binding sitei317 – 3171GTPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi102 – 1098GTPBy similarity
Nucleotide bindingi244 – 2529GTPBy similarity

GO - Molecular functioni

GO - Biological processi

  • cellular protein localization Source: PomBase
  • mitotic cytokinesis Source: PomBase
  • mitotic nuclear division Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Septin homolog spn1
Gene namesi
Name:spn1
ORF Names:SPAC4F10.11
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC4F10.11.
PomBaseiSPAC4F10.11. spn1.

Subcellular locationi

  • Cytoplasmcell cortex 1 Publication

  • Note: Localizes to the medial ring at the cell cortex of dividing cells.

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • nucleus Source: PomBase
  • septin complex Source: PomBase
  • septin ring Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 469469Septin homolog spn1PRO_0000173503Add
BLAST

Proteomic databases

MaxQBiO36023.
PRIDEiO36023.

Interactioni

Subunit structurei

Component of the septin complex composed of two copies of each spn1, spn2, spn3 and spn4.1 Publication

Protein-protein interaction databases

BioGridi279934. 69 interactions.
MINTiMINT-4672971.

Structurei

3D structure databases

ProteinModelPortaliO36023.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini92 – 367276Septin-type GAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili383 – 46987Sequence analysisAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

HOGENOMiHOG000233586.
InParanoidiO36023.
KOiK16944.
OMAiTEKLKRM.
OrthoDBiEOG76HQBH.
PhylomeDBiO36023.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR030379. G_SEPTIN_dom.
IPR027417. P-loop_NTPase.
IPR016491. Septin.
IPR025662. Sigma_54_int_dom_ATP-bd_1.
[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.

O36023-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASMVLADGM PTVKDDSTRS RGSDVDSFTS TDNVTQINVE AAISENKNEE
60 70 80 90 100
KPIQDNSEQE FNPHVSIIQR QLNGYVGFAS LPNQWHRRCV RQGFNFNVLV
110 120 130 140 150
LGESGSGKST LVNTLLNRDV YPPTQKSLTG DFGVNPEPTV MINSSAVEIV
160 170 180 190 200
ENGISLQLNV IDTPGFGDFI DNTDCWQPVL TDIEGRYDQY LELEKHNPRS
210 220 230 240 250
TIQDPRVHAC IFFIQPTGHA ISAMELRVML ALHEKVNIIP IIAKADTLTD
260 270 280 290 300
DELNFTKEMI LRDIQYHNIR IFFPPTYETD DPESVAENAD IMSRIPFAII
310 320 330 340 350
ASNTFVVNNE GKRVRGRRYP WGVVEVDNEE HSDFPKLREM LIRTHLEELK
360 370 380 390 400
EQTNKLYEAY RTERLLSSGI SQDHSVFREV NPSAKLEEER ALHEEKLMKM
410 420 430 440 450
EAEMKTIFSQ KVQEKEDRLK QSENELRTRH REMKAALEKQ KADLIDHKNR
460
LMQAKAAAEN EKSKRKFFK
Length:469
Mass (Da):53,738
Last modified:June 1, 2000 - v2
Checksum:i3CCC9AD0052897A4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31742 Genomic DNA. Translation: AAB53692.2.
CU329670 Genomic DNA. Translation: CAB11714.2.
PIRiT38815.
T52562.
RefSeqiNP_594754.1. NM_001020181.2.

Genome annotation databases

EnsemblFungiiSPAC4F10.11.1; SPAC4F10.11.1:pep; SPAC4F10.11.
GeneIDi2543516.
KEGGispo:SPAC4F10.11.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U31742 Genomic DNA. Translation: AAB53692.2.
CU329670 Genomic DNA. Translation: CAB11714.2.
PIRiT38815.
T52562.
RefSeqiNP_594754.1. NM_001020181.2.

3D structure databases

ProteinModelPortaliO36023.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279934. 69 interactions.
MINTiMINT-4672971.

Proteomic databases

MaxQBiO36023.
PRIDEiO36023.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC4F10.11.1; SPAC4F10.11.1:pep; SPAC4F10.11.
GeneIDi2543516.
KEGGispo:SPAC4F10.11.

Organism-specific databases

EuPathDBiFungiDB:SPAC4F10.11.
PomBaseiSPAC4F10.11. spn1.

Phylogenomic databases

HOGENOMiHOG000233586.
InParanoidiO36023.
KOiK16944.
OMAiTEKLKRM.
OrthoDBiEOG76HQBH.
PhylomeDBiO36023.

Miscellaneous databases

PROiO36023.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR030379. G_SEPTIN_dom.
IPR027417. P-loop_NTPase.
IPR016491. Septin.
IPR025662. Sigma_54_int_dom_ATP-bd_1.
[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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Al-Awar O.S.
    Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  4. "Requirements of fission yeast septins for complex formation, localization, and function."
    An H., Morrell J.L., Jennings J.L., Link A.J., Gould K.L.
    Mol. Biol. Cell 15:5551-5564(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE SEPTIN COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiSPN1_SCHPO
AccessioniPrimary (citable) accession number: O36023
Secondary accession number(s): Q09126
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: June 1, 2000
Last modified: June 8, 2016
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  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.