SEPT5

Septin 5
Identifiers
Symbols	SEPT5 ; CDCREL; CDCREL-1; CDCREL1; H5; HCDCREL-1; PNUTL1
External IDs	OMIM: 602724 MGI: 1195461 HomoloGene: 74446 GeneCards: SEPT5 Gene
EC number	3.1.5.1
Gene ontology Molecular function • GTPase activity • structural molecule activity • protein binding • GTP binding Cellular component • cytoskeleton • plasma membrane • cell cortex • synaptic vesicle • terminal bouton Biological process • cytokinesis • synaptic vesicle targeting • regulation of exocytosis • regulation of synaptic vesicle exocytosis Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5413	18951
Ensembl	ENSG00000184702	ENSMUSG00000072214
UniProt	Q99719	Q9Z2Q6
RefSeq (mRNA)	NM_001009939	NM_213614
RefSeq (protein)	NP_001009939	NP_998779
Location (UCSC)	Chr 22: 19.71 – 19.72 Mb	Chr 16: 18.62 – 18.63 Mb
PubMed search

Septin-5 is a protein that in humans is encoded by the SEPT5 gene.^[1][2][3]

Function

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.^[3]

Interactions

SEPT5 has been shown to interact with:

• PARK2,^[4][5] and
• SEPT8^[6][7]

References

1. McKie JM, Sutherland HF, Harvey E, Kim UJ, Scambler PJ (Dec 1997). "A human gene similar to Drosophila melanogaster peanut maps to the DiGeorge syndrome region of 22q11". Hum Genet 101 (1): 6–12. doi:10.1007/s004390050576. PMID 9385360.
2. Yagi M, Zieger B, Roth GJ, Ware J (Jul 1998). "Structure and expression of the human septin gene HCDCREL-1". Gene 212 (2): 229–36. doi:10.1016/S0378-1119(98)00146-2. PMID 9611266.
3. "Entrez Gene: SEPT5 septin 5".
4. Choi P, Snyder H, Petrucelli L, Theisler C, Chong M, Zhang Y, Lim K, Chung KK, Kehoe K, D'Adamio L, Lee JM, Cochran E, Bowser R, Dawson TM, Wolozin B (Oct 2003). "SEPT5_v2 is a parkin-binding protein". Brain Res. Mol. Brain Res. 117 (2): 179–89. doi:10.1016/S0169-328X(03)00318-8. PMID 14559152.
5. Liu M, Aneja R, Sun X, Xie S, Wang H, Wu X, Dong JT, Li M, Joshi HC, Zhou J (Dec 2008). "Parkin regulates Eg5 expression by Hsp70 ubiquitination-dependent inactivation of c-Jun NH2-terminal kinase". J. Biol. Chem. 283 (51): 35783–8. doi:10.1074/jbc.M806860200. PMID 18845538.
6. Bläser S, Jersch K, Hainmann I, Zieger W, Wunderle D, Busse A, Zieger B (Jul 2003). "Isolation of new splice isoforms, characterization and expression analysis of the human septin SEPT8 (KIAA0202)". Gene 312: 313–20. doi:10.1016/S0378-1119(03)00635-8. PMID 12909369.
7. Bläser S, Jersch K, Hainmann I, Wunderle D, Zgaga-Griesz A, Busse A, Zieger B (May 2002). "Human septin-septin interaction: CDCrel-1 partners with KIAA0202". FEBS Lett. 519 (1-3): 169–72. doi:10.1016/S0014-5793(02)02749-7. PMID 12023038.

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. doi:10.1172/JCI119188. PMC 507827. PMID 9022087.
• Megonigal MD, Rappaport EF, Jones DH, Williams TM, Lovett BD, Kelly KM, Lerou PH, Moulton T, Budarf ML, Felix CA (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. doi:10.1073/pnas.95.11.6413. PMC 27754. PMID 9600980.
• Hsu SC, Hazuka CD, Roth R, Foletti DL, Heuser J, Scheller RH (1998). "Subunit composition, protein interactions, and structures of the mammalian brain sec6/8 complex and septin filaments". Neuron 20 (6): 1111–22. doi:10.1016/S0896-6273(00)80493-6. 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. doi:10.1097/00001756-199808240-00042. 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, Huang H, Dawson VL, Dawson TM (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. PMC 27228. PMID 11078524.
• Larisch S, Yi Y, Lotan R, Kerner H, Eimerl S, Tony Parks W, Gottfried Y, Birkey Reffey S, de Caestecker MP, Danielpour D, Book-Melamed N, Timberg R, Duckett CS, Lechleider RJ, Steller H, Orly J, Kim SJ, Roberts AB (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, Martinez C, Cattaneo M, Poujol C, Nurden P, Nurden A, Trimble WS, Ware J (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. PMC 122473. PMID 11880646.
• Bläser S, Jersch K, Hainmann I, Wunderle D, Zgaga-Griesz A, Busse A, Zieger B (2002). "Human septin-septin interaction: CDCrel-1 partners with KIAA0202". FEBS Lett. 519 (1–3): 169–72. doi:10.1016/S0014-5793(02)02749-7. PMID 12023038.
• Bläser S, Jersch K, Hainmann I, Zieger W, Wunderle D, Busse A, Zieger B (2003). "Isolation of new splice isoforms, characterization and expression analysis of the human septin SEPT8 (KIAA0202)". Gene 312: 313–20. doi:10.1016/S0378-1119(03)00635-8. PMID 12909369.
• Dong Z, Ferger B, Paterna JC, Vogel D, Furler S, Osinde M, Feldon J, Büeler H (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. PMC 218776. PMID 14530399.
• Choi P, Snyder H, Petrucelli L, Theisler C, Chong M, Zhang Y, Lim K, Chung KK, Kehoe K, D'Adamio L, Lee JM, Cochran E, Bowser R, Dawson TM, Wolozin B (2004). "SEPT5_v2 is a parkin-binding protein". Brain Res. Mol. Brain Res. 117 (2): 179–89. doi:10.1016/S0169-328X(03)00318-8. PMID 14559152.
• Bläser S, Horn J, Würmell P, Bauer H, Strümpell S, Nurden P, Pagenstecher A, Busse A, Wunderle D, Hainmann I, Zieger B (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, Karlsson L, Ware J (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. PMC 1133953. 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. PMC 442147. PMID 15231747.