SEPT5

From Wikipedia, the free encyclopedia

Septin 5

Identifiers

SEPT5; CDCREL; CDCREL-1; CDCREL1; H5; PNUTL1

External IDs

OMIM: 602724 MGI: 1195461 HomoloGene: 74446

Gene ontology
Molecular Function:	• nucleotide binding • GTPase activity • structural molecule activity • protein binding • GTP binding
Cellular Component:	• plasma membrane • synaptic vesicle
Biological Process:	• cytokinesis • cell cycle • synaptic vesicle targeting • regulation of exocytosis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_002688 (mRNA)
NP_002679 (protein)

NM_213614 (mRNA)
NP_998779 (protein)

Location

Chr 22: 18.08 - 18.09 Mb

Chr 16: 18.54 - 18.54 Mb

Pubmed search

[1]

[2]

Septin 5, also known as SEPT5, is a human gene.^[1]

This gene is a member of the septin gene family of nucleotide binding proteins, originally described in yeast as cell division cycle regulatory proteins. Septins are highly conserved in yeast, Drosophila, and mouse and appear to regulate cytoskeletal organization. Disruption of septin function disturbs cytokinesis and results in large multinucleate or polyploid cells. This gene is mapped to 22q11, the region frequently deleted in DiGeorge and velocardiofacial syndromes. A translocation involving the MLL gene and this gene has also been reported in patients with acute myeloid leukemia. Two transcripts of this gene, a major one of 2.2 kb and a minor one of 3.5 kb, have been observed. The 2.2 kb form results from the utilization of a non-consensus polyA signal (AACAAT). In the absence of polyadenylation from this imperfect site, the consensus polyA signal of the downstream neighboring gene (GP1BB; platelet glycoprotein Ib) is used, resulting in the 3.5 kb transcript. An alternatively spliced transcript variant with a different 5' end has also been identified, but its full-length nature has not been completely determined.^[1]

[edit] References

^ ^a ^b Entrez Gene: SEPT5 septin 5.

[edit] Further reading

Yagi M, Edelhoff S, Disteche CM, Roth GJ (1994). "Structural characterization and chromosomal location of the gene encoding human platelet glycoprotein Ib beta.". J. Biol. Chem. 269 (26): 17424–7. PMID 8021244.
Zieger B, Hashimoto Y, Ware J (1997). "Alternative expression of platelet glycoprotein Ib(beta) mRNA from an adjacent 5' gene with an imperfect polyadenylation signal sequence.". J. Clin. Invest. 99 (3): 520–5. PMID 9022087.
McKie JM, Sutherland HF, Harvey E, et al. (1997). "A human gene similar to Drosophila melanogaster peanut maps to the DiGeorge syndrome region of 22q11.". Hum. Genet. 101 (1): 6–12. PMID 9385360.
Megonigal MD, Rappaport EF, Jones DH, et al. (1998). "t(11;22)(q23;q11.2) In acute myeloid leukemia of infant twins fuses MLL with hCDCrel, a cell division cycle gene in the genomic region of deletion in DiGeorge and velocardiofacial syndromes.". Proc. Natl. Acad. Sci. U.S.A. 95 (11): 6413–8. PMID 9600980.
Yagi M, Zieger B, Roth GJ, Ware J (1998). "Structure and expression of the human septin gene HCDCREL-1.". Gene 212 (2): 229–36. PMID 9611266.
Hsu SC, Hazuka CD, Roth R, et al. (1998). "Subunit composition, protein interactions, and structures of the mammalian brain sec6/8 complex and septin filaments.". Neuron 20 (6): 1111–22. PMID 9655500.
Caltagarone J, Rhodes J, Honer WG, Bowser R (1998). "Localization of a novel septin protein, hCDCrel-1, in neurons of human brain.". Neuroreport 9 (12): 2907–12. PMID 9760144.
Beites CL, Xie H, Bowser R, Trimble WS (1999). "The septin CDCrel-1 binds syntaxin and inhibits exocytosis.". Nat. Neurosci. 2 (5): 434–9. doi:10.1038/8100. PMID 10321247.
Zhang Y, Gao J, Chung KK, et al. (2001). "Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1.". Proc. Natl. Acad. Sci. U.S.A. 97 (24): 13354–9. doi:10.1073/pnas.240347797. PMID 11078524.
Larisch S, Yi Y, Lotan R, et al. (2001). "A novel mitochondrial septin-like protein, ARTS, mediates apoptosis dependent on its P-loop motif.". Nat. Cell Biol. 2 (12): 915–21. doi:10.1038/35046566. PMID 11146656.
Dent J, Kato K, Peng XR, et al. (2002). "A prototypic platelet septin and its participation in secretion.". Proc. Natl. Acad. Sci. U.S.A. 99 (5): 3064–9. doi:10.1073/pnas.052715199. PMID 11880646.
Bläser S, Jersch K, Hainmann I, et al. (2002). "Human septin-septin interaction: CDCrel-1 partners with KIAA0202.". FEBS Lett. 519 (1-3): 169–72. PMID 12023038.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Bläser S, Jersch K, Hainmann I, et al. (2003). "Isolation of new splice isoforms, characterization and expression analysis of the human septin SEPT8 (KIAA0202).". Gene 312: 313–20. PMID 12909369.
Dong Z, Ferger B, Paterna JC, et al. (2003). "Dopamine-dependent neurodegeneration in rats induced by viral vector-mediated overexpression of the parkin target protein, CDCrel-1.". Proc. Natl. Acad. Sci. U.S.A. 100 (21): 12438–43. doi:10.1073/pnas.2132992100. PMID 14530399.
Choi P, Snyder H, Petrucelli L, et al. (2004). "SEPT5_v2 is a parkin-binding protein.". Brain Res. Mol. Brain Res. 117 (2): 179–89. PMID 14559152.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Bläser S, Horn J, Würmell P, et al. (2004). "The novel human platelet septin SEPT8 is an interaction partner of SEPT4.". Thromb. Haemost. 91 (5): 959–66. doi:10.1267/THRO04050959. PMID 15116257.
Martínez C, Sanjuan MA, Dent JA, et al. (2005). "Human septin-septin interactions as a prerequisite for targeting septin complexes in the cytosol.". Biochem. J. 382 (Pt 3): 783–91. doi:10.1042/BJ20040372. PMID 15214843.
Lehner B, Sanderson CM (2004). "A protein interaction framework for human mRNA degradation.". Genome Res. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMID 15231747.