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Q9Z2Q6 (SEPT5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Septin-5
Alternative name(s):
Cell division control-related protein 1
Short name=CDCrel-1
Peanut-like protein 1
Gene names
Name:Sept5
Synonyms:Pnutl1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length369 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Filament-forming cytoskeletal GTPase By similarity. Involved in cytokinesis Potential. May play a role in platelet secretion. Ref.7

Subunit structure

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. Interacts with SEPT2 and SEPT5. Interaction with SEPT4 not detected. In platelets, associated with a complex containing STX4 By similarity. Interacts with PARK2. This interaction leads to SEPT5 ubiquitination and degradation. Ref.5 Ref.6

Subcellular location

Cytoplasm By similarity. Cytoplasmcytoskeleton By similarity.

Developmental stage

Detected at 17 dpc in the brain. Expression increases during postnatal life and reaches a plateau at approximately P10 (at protein level). Ref.6

Disruption phenotype

Mice have a normal life-span and show no apparent abnormalities, including synaptic properties and hippocampal neuron growth. In platelets, hyperresponsive degranulation phenotype. Ref.6 Ref.7

Sequence similarities

Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Septin GTPase family.

Contains 1 septin-type G (guanine nucleotide-binding) domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PARK2O602602EBI-772125,EBI-716346From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 369369Septin-5
PRO_0000173523

Regions

Domain41 – 314274Septin-type G
Nucleotide binding51 – 588GTP By similarity
Nucleotide binding190 – 1989GTP By similarity
Coiled coil338 – 36932 Potential

Sites

Binding site851GTP By similarity
Binding site1111GTP; via amide nitrogen By similarity
Binding site2481GTP; via amide nitrogen and carbonyl oxygen By similarity
Binding site2631GTP By similarity

Amino acid modifications

Modified residue2251Phosphoserine Ref.10
Modified residue3271Phosphoserine Ref.8
Modified residue3361Phosphothreonine Ref.8

Sequences

Sequence LengthMass (Da)Tools
Q9Z2Q6 [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: D58468DBA9ADE626

FASTA36942,748
        10         20         30         40         50         60 
MSTGLRYKSK LATPEDKQDI DKQYVGFATL PNQVHRKSVK KGFDFTLMVA GESGLGKSTL 

        70         80         90        100        110        120 
VHSLFLTDLY KDRKLLSAEE RINQTVEILK HTVDIEEKGV KLKLTIVDTP GFGDAVNNSE 

       130        140        150        160        170        180 
CWKPITDYVD QQFEQYFRDE SGLNRKNIQD NRVHCCLYFI SPFGHGLRPV DVGFMKALHE 

       190        200        210        220        230        240 
KVNIVPLIAK ADCLVPSEIR KLKDRIREEI DKFGIHVYQF PECDSDEDED FKQQDRELKE 

       250        260        270        280        290        300 
SAPFAVIGSN TVVEAKGQRV RGRLYPWGIV EVENQAHCDF VKLRNMLIRT HMHDLKDVTC 

       310        320        330        340        350        360 
DVHYENYRAH CIQQMTSKLT QDSRMESPIP ILPLPTPDAE TEKLIRMKDE ELRRMQEMLQ 


KMKQQMQDQ 

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Medulla oblongata.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[3]"CDCREL-1, a septin deleted in DiGeorge Syndrome, is expressed in the developing brain and cartilage primordia in mouse embryogenesis."
Botta A., Lindsay E.A., Jurecic V., Zieger B., Ware J., Baldini A.
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 23-369.
Strain: C57BL/6.
Tissue: Brain, Cartilage and Skin.
[4]Lubec G., Klug S., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 23-36; 58-71; 82-90; 182-190; 240-256; 264-282 AND 297-308, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
[5]"Parkin functions as an E2-dependent ubiquitin-protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1."
Zhang Y., Gao J., Chung K.K.K., Huang H., Dawson V.L., Dawson T.M.
Proc. Natl. Acad. Sci. U.S.A. 97:13354-13359(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PARK2, UBIQUITIN-MEDIATED DEGRADATION.
[6]"The septin CDCrel-1 is dispensable for normal development and neurotransmitter release."
Peng X.-R., Jia Z., Zhang Y., Ware J., Trimble W.S.
Mol. Cell. Biol. 22:378-387(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SEPT2 AND SEPT7, LACK OF INTERACTION WITH SEPT4, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
[7]"A prototypic platelet septin and its participation in secretion."
Dent J., Kato K., Peng X.-R., Martinez C., Cattaneo M., Poujol C., Nurden P., Nurden A., Trimble W.S., Ware J.
Proc. Natl. Acad. Sci. U.S.A. 99:3064-3069(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[8]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327 AND THR-336, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic brain.
[9]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain cortex.
[10]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK134700 mRNA. Translation: BAE22248.1.
BC059848 mRNA. Translation: AAH59848.1.
BC141073 mRNA. Translation: AAI41074.1.
BC145331 mRNA. Translation: AAI45332.1.
AF033350 mRNA. Translation: AAC83974.1.
CCDSCCDS57021.1.
RefSeqNP_998779.2. NM_213614.2.
UniGeneMm.20365.

3D structure databases

ProteinModelPortalQ9Z2Q6.
SMRQ9Z2Q6. Positions 41-309.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202285. 4 interactions.
IntActQ9Z2Q6. 5 interactions.
MINTMINT-4134165.
STRING10090.ENSMUSP00000094750.

PTM databases

PhosphoSiteQ9Z2Q6.

Proteomic databases

MaxQBQ9Z2Q6.
PaxDbQ9Z2Q6.
PRIDEQ9Z2Q6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000096987; ENSMUSP00000094750; ENSMUSG00000072214.
GeneID18951.
KEGGmmu:18951.
UCSCuc007yoj.1. mouse.

Organism-specific databases

CTD5413.
MGIMGI:1195461. Sept5.

Phylogenomic databases

eggNOGCOG5019.
GeneTreeENSGT00620000087649.
HOVERGENHBG065093.
InParanoidB2RUC5.
KOK04557.
OMAAVNNSEC.
OrthoDBEOG79KPF0.
TreeFamTF101079.

Gene expression databases

BgeeQ9Z2Q6.
CleanExMM_SEPT5.
GenevestigatorQ9Z2Q6.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR000038. Cell_div_GTP-bd.
IPR027417. P-loop_NTPase.
IPR016491. Septin.
[Graphical view]
PANTHERPTHR18884. PTHR18884. 1 hit.
PfamPF00735. Septin. 1 hit.
[Graphical view]
PIRSFPIRSF006698. Septin. 1 hit.
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS51719. G_SEPTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio295300.
PROQ9Z2Q6.
SOURCESearch...

Entry information

Entry nameSEPT5_MOUSE
AccessionPrimary (citable) accession number: Q9Z2Q6
Secondary accession number(s): B2RUC5, Q3UYG4, Q6PB74
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: December 6, 2005
Last modified: July 9, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot