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Q99719 (SEPT5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·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
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

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

General annotation (Comments)

Function

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

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. In platelets, associated with a complex containing STX4. Interacts with PARK2. This interaction leads to SEPT5 ubiquitination and degradation By similarity. Ref.7

Subcellular location

Cytoplasm By similarity. Cytoplasmcytoskeleton By similarity. Note: In platelets, found in areas surrounding alpha-granules.

Tissue specificity

Expressed at high levels in the CNS, as well as in heart and platelets (at protein level). Ref.7 Ref.10

Post-translational modification

In platelets, phosphorylated in response to thrombin, phorbol-12-myristate-13-acetate and collagen. Ref.8 Ref.11 Ref.12

Miscellaneous

In a heterologous system, SEPT5 overexpression has been shown to exert dopamine-dependent neurotoxicity. As wild-type PARK2, but not familial-linked PARK2 mutants, ubiquinates mouse SEPT5 and promotes its degradation, it has been sugested that a deficiency in SEPT5 degradation may contribute to the development of early onset Parkinson disease 2 (PARK2).

Sequence similarities

Belongs to the septin family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SEPT11Q9NVA26EBI-373345,EBI-957999

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 369369Septin-5
PRO_0000173521

Regions

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.11 Ref.12
Modified residue3271Phosphoserine Ref.12
Modified residue3361Phosphothreonine By similarity

Experimental info

Sequence conflict2241D → N in CAA72332. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q99719 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 47054765DEA10D33

FASTA36942,777
        10         20         30         40         50         60 
MSTGLRYKSK LATPEDKQDI DKQYVGFATL PNQVHRKSVK KGFDFTLMVA GESGLGKSTL 

        70         80         90        100        110        120 
VHSLFLTDLY KDRKLLSAEE RISQTVEILK HTVDIEEKGV KLKLTIVDTP GFGDAVNNTE 

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

       190        200        210        220        230        240 
KVNIVPLIAK ADCLVPSEIR KLKERIREEI 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 


RMKQQMQDQ 

« Hide

References

« Hide 'large scale' references
[1]"Alternative expression of platelet glycoprotein Ib(beta) mRNA from an adjacent 5' gene with an imperfect polyadenylation signal sequence."
Zieger B., Hashimoto Y., Ware J.
J. Clin. Invest. 99:520-525(1997) [PubMed: 9022087] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"A human gene similar to Drosophila melanogaster peanut maps to the DiGeorge syndrome region of 22q11."
McKie J., Sutherland H., Harvey E., Kim U.J., Scambler P.J.
Hum. Genet. 101:6-12(1997) [PubMed: 9385360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart.
[3]"Structure and expression of the human septin gene HCDCREL-1."
Yagi M., Zieger B., Roth G.J., Ware J.
Gene 212:229-236(1998) [PubMed: 9611266] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Brain.
[4]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed: 15461802] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[6]Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 23-36; 42-71; 82-90; 182-190; 297-308 AND 325-343, MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[7]"Human septin-septin interaction: CDCrel-1 partners with KIAA0202."
Blaeser S., Jersch K., Hainmann I., Wunderle D., Zgaga-Griesz A., Busse A., Zieger B.
FEBS Lett. 519:169-172(2002) [PubMed: 12023038] [Abstract]
Cited for: INTERACTION WITH SEPT8, TISSUE SPECIFICITY.
[8]"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: 11880646] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH STX4, PHOSPHORYLATION.
[9]"Dopamine-dependent neurodegeneration in rats induced by viral vector-mediated overexpression of the parkin target protein, CDCrel-1."
Dong Z., Ferger B., Paterna J.-C., Vogel D., Furler S., Osinde M., Feldon J., Bueeler H.
Proc. Natl. Acad. Sci. U.S.A. 100:12438-12443(2003) [PubMed: 14530399] [Abstract]
Cited for: POSSIBLE INVOLVEMENT IN PARK2.
[10]"Expression profiling the human septin gene family."
Hall P.A., Jung K., Hillan K.J., Russell S.E.H.
J. Pathol. 206:269-278(2005) [PubMed: 15915442] [Abstract]
Cited for: TISSUE SPECIFICITY.
[11]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, MASS SPECTROMETRY.
Tissue: Platelet.
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225 AND SER-327, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U74628 mRNA. Translation: AAB93438.1.
Y11593 mRNA. Translation: CAA72332.1.
AF006988 Genomic DNA. Translation: AAC39779.1.
CR456545 mRNA. Translation: CAG30431.1.
BC025261 mRNA. Translation: AAH25261.1.
IPIIPI00017731.
RefSeqNP_002679.2. NM_002688.5.
UniGeneHs.728762.

3D structure databases

ProteinModelPortalQ99719.
SMRQ99719. Positions 41-309.
ModBaseSearch...

Protein-protein interaction databases

IntActQ99719. 6 interactions.
STRINGQ99719.

PTM databases

PhosphoSiteQ99719.

Polymorphism databases

DMDM6685760.

2D gel databases

UCD-2DPAGEQ99719.

Proteomic databases

PRIDEQ99719.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000455784; ENSP00000391311; ENSG00000184702.
GeneID5413.
KEGGhsa:5413.
UCSCuc002zpv.1. human.

Organism-specific databases

CTD5413.
GeneCardsGC22P019701.
H-InvDBHIX0016241.
HGNCHGNC:9164. SEPT5.
HPACAB016120.
MIM602724. gene.
neXtProtNX_Q99719.
PharmGKBPA33486.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG13188.
GeneTreeENSGT00590000082878.
HOVERGENHBG065093.
OrthoDBEOG447FTF.
PhylomeDBQ99719.

Gene expression databases

ArrayExpressQ99719.
BgeeQ99719.
CleanExHS_SEPT5.
GenevestigatorQ99719.
GermOnlineENSG00000184702. Homo sapiens.

Family and domain databases

InterProIPR000038. Cell_div_GTP-bd.
IPR016491. Septin.
[Graphical view]
KOK04557.
PANTHERPTHR18884. Cell_Div_GTP_bd. 1 hit.
PfamPF00735. Septin. 1 hit.
[Graphical view]
PIRSFPIRSF006698. Septin. 1 hit.
ProtoNetSearch...

Other

NextBio20957.
SOURCESearch...

Entry information

Entry nameSEPT5_HUMAN
AccessionPrimary (citable) accession number: Q99719
Secondary accession number(s): O15251
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1997
Last modified: January 25, 2012
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families