ID SEPT8_HUMAN Reviewed; 483 AA. AC Q92599; A6NC65; A6NKP6; F6W7K9; Q8IX36; Q8IX37; Q9BVB3; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 27-MAR-2024, entry version 195. DE RecName: Full=Septin-8 {ECO:0000305}; GN Name=SEPTIN8 {ECO:0000312|HGNC:HGNC:16511}; GN Synonyms=KIAA0202 {ECO:0000303|PubMed:12023038}, SEPT8; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH SEPTIN5, AND RP TISSUE SPECIFICITY. RX PubMed=12023038; DOI=10.1016/s0014-5793(02)02749-7; RA Blaeser S., Jersch K., Hainmann I., Wunderle D., Zgaga-Griesz A., Busse A., RA Zieger B.; RT "Human septin-septin interaction: CDCrel-1 partners with KIAA0202."; RL FEBS Lett. 519:169-172(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), ALTERNATIVE SPLICING, RP INTERACTION WITH SEPTIN5, AND TISSUE SPECIFICITY. RX PubMed=12909369; DOI=10.1016/s0378-1119(03)00635-8; RA Blaeser S., Jersch K., Hainmann I., Zieger W., Wunderle D., Busse A., RA Zieger B.; RT "Isolation of new splice isoforms, characterization and expression analysis RT of the human septin SEPT8 (KIAA0202)."; RL Gene 312:313-320(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Bone marrow; RX PubMed=9039502; DOI=10.1093/dnares/3.5.321; RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., RA Tanaka A., Kotani H., Miyajima N., Nomura N.; RT "Prediction of the coding sequences of unidentified human genes. VI. The RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of RT cDNA clones from cell line KG-1 and brain."; RL DNA Res. 3:321-329(1996). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=10704283; DOI=10.1006/geno.1999.6100; RA Wenderfer S.E., Slack J.P., McCluskey T.S., Monaco J.J.; RT "Identification of 40 genes on a 1-Mb contig around the IL-4 cytokine RT family gene cluster on mouse chromosome 11."; RL Genomics 63:354-373(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 122-483 (ISOFORMS 2/3). RC TISSUE=Cervix; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP IDENTIFICATION OF INITIATOR METHIONINE. RX PubMed=12475938; DOI=10.1091/mbc.e02-07-0438; RA Macara I.G., Baldarelli R., Field C.M., Glotzer M., Hayashi Y., Hsu S.-C., RA Kennedy M.B., Kinoshita M., Longtine M., Low C., Maltais L.J., McKenzie L., RA Mitchison T.J., Nishikawa T., Noda M., Petty E.M., Peifer M., Pringle J.R., RA Robinson P.J., Roth D., Russell S.E.H., Stuhlmann H., Tanaka M., Tanaka T., RA Trimble W.S., Ware J., Zeleznik-Le N.J., Zieger B.; RT "Mammalian septins nomenclature."; RL Mol. Biol. Cell 13:4111-4113(2002). RN [10] RP INTERACTION WITH CDK14. RX PubMed=12098780; RA Yang T., Gao Y.K., Chen J.Y.; RT "KIAA0202, a human septin family member, interacting with hPFTAIRE1."; RL Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao 34:520-525(2002). RN [11] RP FUNCTION, INTERACTION WITH SEPTIN4, SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RX PubMed=15116257; DOI=10.1160/th03-09-0578; RA Blaeser S., Horn J., Wuermell P., Bauer H., Struempell S., Nurden P., RA Pagenstecher A., Busse A., Wunderle D., Hainmann I., Zieger B.; RT "The novel human platelet septin SEPT8 is an interaction partner of RT SEPT4."; RL Thromb. Haemost. 91:959-966(2004). RN [12] RP TISSUE SPECIFICITY. RX PubMed=15915442; DOI=10.1002/path.1789; RA Hall P.A., Jung K., Hillan K.J., Russell S.E.H.; RT "Expression profiling the human septin gene family."; RL J. Pathol. 206:269-278(2005). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [17] RP FUNCTION (ISOFORM 4), ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY. RX PubMed=27084579; DOI=10.1242/jcs.185215; RA Kurkinen K.M., Marttinen M., Turner L., Natunen T., Maekinen P., RA Haapalinna F., Sarajaervi T., Gabbouj S., Kurki M., Paananen J., RA Koivisto A.M., Rauramaa T., Leinonen V., Tanila H., Soininen H., RA Lucas F.R., Haapasalo A., Hiltunen M.; RT "SEPT8 modulates beta-amyloidogenic processing of APP by affecting the RT sorting and accumulation of BACE1."; RL J. Cell Sci. 129:2224-2238(2016). CC -!- FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). May CC play a role in platelet secretion (PubMed:15116257). Seems to CC participate in the process of SNARE complex formation in synaptic CC vesicles (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:B0BNF1, CC ECO:0000269|PubMed:15116257}. CC -!- FUNCTION: [Isoform 4]: Stabilizes BACE1 protein levels and promotes the CC sorting and accumulation of BACE1 to the recycling or endosomal CC compartments, modulating the beta-amyloidogenic processing of APP. CC {ECO:0000269|PubMed:27084579}. CC -!- SUBUNIT: Septins polymerize into heterooligomeric protein complexes CC that form filaments, and can associate with cellular membranes, actin CC filaments and microtubules. GTPase activity is required for filament CC formation (By similarity). Interacts with CDK14 (PubMed:12098780). CC Interacts with SEPTIN5 (PubMed:12909369). Interacts with SEPTIN7 (By CC similarity). Interacts with SEPTIN4 (PubMed:15116257). Interacts with CC VAMP2; the interaction inhibits interaction of VAMP2 with SYP (By CC similarity). Interacts with STX1A (By similarity). CC {ECO:0000250|UniProtKB:B0BNF1, ECO:0000250|UniProtKB:Q8CHH9, CC ECO:0000269|PubMed:12098780, ECO:0000269|PubMed:12909369, CC ECO:0000269|PubMed:15116257}. CC -!- INTERACTION: CC Q92599; Q99719: SEPTIN5; NbExp=6; IntAct=EBI-958021, EBI-373345; CC Q92599-3; P05067: APP; NbExp=3; IntAct=EBI-25891137, EBI-77613; CC Q92599-3; P04271: S100B; NbExp=3; IntAct=EBI-25891137, EBI-458391; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B0BNF1}. CC Cytoplasm, cytoskeleton {ECO:0000250}. Synapse CC {ECO:0000250|UniProtKB:B0BNF1}. Cell projection, axon CC {ECO:0000250|UniProtKB:B0BNF1}. Cytoplasmic vesicle, secretory vesicle, CC synaptic vesicle membrane {ECO:0000250|UniProtKB:B0BNF1}. Presynapse CC {ECO:0000250|UniProtKB:B0BNF1}. Note=Expressed in axons of immature CC neurons, localizes to synapses in mature neurons (By similarity). In CC platelets, found in areas surrounding alpha-granules (PubMed:15116257). CC {ECO:0000250|UniProtKB:B0BNF1, ECO:0000269|PubMed:15116257}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=KIAA0202b {ECO:0000303|PubMed:12023038}, SEPT8_v2 CC {ECO:0000303|PubMed:12023038}, SEPT8 TV1 {ECO:0000303|PubMed:27084579}; CC IsoId=Q92599-1; Sequence=Displayed; CC Name=2; Synonyms=KIAA0202a {ECO:0000303|PubMed:12023038}, SEPT8_v1 CC {ECO:0000303|PubMed:12023038}, KIAA0202c {ECO:0000303|PubMed:12023038}, CC SEPT8_v1* {ECO:0000303|PubMed:12023038}, SEPT8 TV2 CC {ECO:0000303|PubMed:27084579}; CC IsoId=Q92599-2; Sequence=VSP_009644; CC Name=3; Synonyms=KIAA0202d {ECO:0000303|PubMed:12023038}, SEPT8_v3 CC {ECO:0000303|PubMed:12023038}, SEPT8 TV4 {ECO:0000303|PubMed:27084579}; CC IsoId=Q92599-3; Sequence=VSP_009643, VSP_009644; CC Name=4; Synonyms=SEPT8 TV3 {ECO:0000303|PubMed:27084579}; CC IsoId=Q92599-4; Sequence=VSP_054085, VSP_054086; CC -!- TISSUE SPECIFICITY: Widely expressed, including in brain, heart and CC platelets; most abundant in aorta. Isoform 2 is expressed at low levels CC in specific brain areas, such as occipital pole, frontal lobe, temporal CC lobe and putamen. Isoform 1 and 3 are highly expressed in specific CC brain areas, such as occipital pole, frontal lobe, temporal lobe and CC putamen. Isoform 2 is highly expressed in prostate, testis and ovary. CC Isoform 1 and isoform 3 are expressed at low levels in prostate, testis CC and ovary. {ECO:0000269|PubMed:12023038, ECO:0000269|PubMed:12909369, CC ECO:0000269|PubMed:15116257, ECO:0000269|PubMed:15915442, CC ECO:0000269|PubMed:27084579}. CC -!- MISCELLANEOUS: [Isoform 2]: KIAA0202a differs from KIAA0202c at the CC level of the 3'-UTR. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like CC GTPase superfamily. Septin GTPase family. {ECO:0000255|PROSITE- CC ProRule:PRU01056}. CC -!- SEQUENCE CAUTION: CC Sequence=AAG09407.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH01329.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAO13878.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAO13879.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAO13880.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAA13193.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D86957; BAA13193.1; ALT_INIT; mRNA. DR EMBL; AF179995; AAG09407.1; ALT_INIT; mRNA. DR EMBL; AF440761; AAO13878.1; ALT_INIT; mRNA. DR EMBL; AF440762; AAO13879.1; ALT_INIT; mRNA. DR EMBL; AF440763; AAO13880.1; ALT_INIT; mRNA. DR EMBL; AK057797; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AC004775; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471062; EAW62315.1; -; Genomic_DNA. DR EMBL; CH471062; EAW62317.1; -; Genomic_DNA. DR EMBL; BC001329; AAH01329.1; ALT_INIT; mRNA. DR CCDS; CCDS43358.1; -. [Q92599-1] DR CCDS; CCDS43359.1; -. [Q92599-4] DR CCDS; CCDS43360.1; -. [Q92599-2] DR CCDS; CCDS47262.1; -. [Q92599-3] DR RefSeq; NP_001092281.1; NM_001098811.1. [Q92599-1] DR RefSeq; NP_001092282.1; NM_001098812.1. [Q92599-4] DR RefSeq; NP_001092283.1; NM_001098813.1. [Q92599-3] DR RefSeq; NP_001287727.1; NM_001300798.1. DR RefSeq; NP_001287728.1; NM_001300799.1. DR RefSeq; NP_055961.1; NM_015146.1. [Q92599-2] DR PDB; 6UPR; X-ray; 2.30 A; B=36-311. DR PDB; 6WSM; X-ray; 2.45 A; A=309-429. DR PDBsum; 6UPR; -. DR PDBsum; 6WSM; -. DR AlphaFoldDB; Q92599; -. DR SASBDB; Q92599; -. DR SMR; Q92599; -. DR BioGRID; 116788; 92. DR CORUM; Q92599; -. DR IntAct; Q92599; 40. DR MINT; Q92599; -. DR STRING; 9606.ENSP00000367991; -. DR GlyGen; Q92599; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q92599; -. DR PhosphoSitePlus; Q92599; -. DR SwissPalm; Q92599; -. DR BioMuta; SEPT8; -. DR DMDM; 45645200; -. DR EPD; Q92599; -. DR jPOST; Q92599; -. DR MassIVE; Q92599; -. DR MaxQB; Q92599; -. DR PaxDb; 9606-ENSP00000367991; -. DR PeptideAtlas; Q92599; -. DR ProteomicsDB; 28101; -. DR ProteomicsDB; 75347; -. [Q92599-1] DR ProteomicsDB; 75348; -. [Q92599-2] DR ProteomicsDB; 75349; -. [Q92599-3] DR Pumba; Q92599; -. DR Antibodypedia; 26134; 272 antibodies from 30 providers. DR DNASU; 23176; -. DR Ensembl; ENST00000296873.11; ENSP00000296873.7; ENSG00000164402.14. [Q92599-2] DR Ensembl; ENST00000378699.6; ENSP00000367971.2; ENSG00000164402.14. [Q92599-3] DR Ensembl; ENST00000378719.7; ENSP00000367991.2; ENSG00000164402.14. [Q92599-1] DR Ensembl; ENST00000448933.5; ENSP00000399840.1; ENSG00000164402.14. [Q92599-3] DR Ensembl; ENST00000458488.2; ENSP00000394766.2; ENSG00000164402.14. [Q92599-4] DR GeneID; 23176; -. DR KEGG; hsa:23176; -. DR MANE-Select; ENST00000378719.7; ENSP00000367991.2; NM_001098811.2; NP_001092281.1. DR UCSC; uc003kxr.2; human. [Q92599-1] DR AGR; HGNC:16511; -. DR CTD; 23176; -. DR DisGeNET; 23176; -. DR GeneCards; SEPTIN8; -. DR HGNC; HGNC:16511; SEPTIN8. DR HPA; ENSG00000164402; Tissue enriched (brain). DR MIM; 608418; gene. DR neXtProt; NX_Q92599; -. DR OpenTargets; ENSG00000164402; -. DR PharmGKB; PA134879270; -. DR VEuPathDB; HostDB:ENSG00000164402; -. DR eggNOG; KOG3859; Eukaryota. DR GeneTree; ENSGT00940000156068; -. DR HOGENOM; CLU_017718_6_4_1; -. DR InParanoid; Q92599; -. DR OMA; CKNANEE; -. DR OrthoDB; 5396944at2759; -. DR PhylomeDB; Q92599; -. DR TreeFam; TF101080; -. DR PathwayCommons; Q92599; -. DR SignaLink; Q92599; -. DR BioGRID-ORCS; 23176; 10 hits in 1084 CRISPR screens. DR ChiTaRS; SEPT8; human. DR GeneWiki; SEPT8; -. DR GenomeRNAi; 23176; -. DR Pharos; Q92599; Tbio. DR PRO; PR:Q92599; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q92599; Protein. DR Bgee; ENSG00000164402; Expressed in middle temporal gyrus and 196 other cell types or tissues. DR ExpressionAtlas; Q92599; baseline and differential. DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell. DR GO; GO:0032153; C:cell division site; IBA:GO_Central. DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central. DR GO; GO:0098793; C:presynapse; ISS:UniProtKB. DR GO; GO:0031105; C:septin complex; IBA:GO_Central. DR GO; GO:0005940; C:septin ring; IBA:GO_Central. DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central. DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central. DR GO; GO:0033157; P:regulation of intracellular protein transport; IDA:UniProtKB. DR GO; GO:0031647; P:regulation of protein stability; IDA:UniProtKB. DR GO; GO:0035542; P:regulation of SNARE complex assembly; ISS:UniProtKB. DR CDD; cd01850; CDC_Septin; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR030379; G_SEPTIN_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR016491; Septin. DR PANTHER; PTHR18884; SEPTIN; 1. DR PANTHER; PTHR18884:SF54; SEPTIN-8; 1. DR Pfam; PF00735; Septin; 1. DR PIRSF; PIRSF006698; Septin; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51719; G_SEPTIN; 1. DR Genevisible; Q92599; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cell projection; KW Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; GTP-binding; KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Synapse. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..483 FT /note="Septin-8" FT /id="PRO_0000173533" FT DOMAIN 41..307 FT /note="Septin-type G" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056" FT REGION 1..22 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 51..58 FT /note="G1 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056" FT REGION 103..106 FT /note="G3 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056" FT REGION 186..189 FT /note="G4 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056" FT REGION 411..443 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 320..413 FT /evidence="ECO:0000255" FT COMPBIAS 419..433 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 51..58 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 106 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 187..195 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 241 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 256 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 10 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..60 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12909369" FT /id="VSP_009643" FT VAR_SEQ 429..442 FT /note="NRSDIGAHQPGMSL -> KASGWSSIYSVTIP (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054085" FT VAR_SEQ 430..483 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:10704283, FT ECO:0000303|PubMed:12909369, ECO:0000303|PubMed:9039502" FT /id="VSP_009644" FT VAR_SEQ 443..483 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054086" FT CONFLICT 116..117 FT /note="Missing (in Ref. 5; AK057797)" FT /evidence="ECO:0000305" FT CONFLICT 365 FT /note="E -> V (in Ref. 5; AK057797)" FT /evidence="ECO:0000305" FT STRAND 43..50 FT /evidence="ECO:0007829|PDB:6UPR" FT HELIX 57..64 FT /evidence="ECO:0007829|PDB:6UPR" FT STRAND 82..94 FT /evidence="ECO:0007829|PDB:6UPR" FT STRAND 96..105 FT /evidence="ECO:0007829|PDB:6UPR" FT TURN 106..108 FT /evidence="ECO:0007829|PDB:6UPR" FT HELIX 118..135 FT /evidence="ECO:0007829|PDB:6UPR" FT TURN 142..144 FT /evidence="ECO:0007829|PDB:6UPR" FT STRAND 152..157 FT /evidence="ECO:0007829|PDB:6UPR" FT STRAND 161..163 FT /evidence="ECO:0007829|PDB:6UPR" FT HELIX 166..175 FT /evidence="ECO:0007829|PDB:6UPR" FT TURN 176..178 FT /evidence="ECO:0007829|PDB:6UPR" FT STRAND 181..185 FT /evidence="ECO:0007829|PDB:6UPR" FT HELIX 188..190 FT /evidence="ECO:0007829|PDB:6UPR" FT HELIX 193..210 FT /evidence="ECO:0007829|PDB:6UPR" FT HELIX 222..224 FT /evidence="ECO:0007829|PDB:6UPR" FT HELIX 225..233 FT /evidence="ECO:0007829|PDB:6UPR" FT STRAND 236..238 FT /evidence="ECO:0007829|PDB:6UPR" FT STRAND 245..248 FT /evidence="ECO:0007829|PDB:6UPR" FT STRAND 251..258 FT /evidence="ECO:0007829|PDB:6UPR" FT STRAND 261..264 FT /evidence="ECO:0007829|PDB:6UPR" FT TURN 268..270 FT /evidence="ECO:0007829|PDB:6UPR" FT HELIX 273..277 FT /evidence="ECO:0007829|PDB:6UPR" FT HELIX 278..280 FT /evidence="ECO:0007829|PDB:6UPR" FT HELIX 282..294 FT /evidence="ECO:0007829|PDB:6UPR" FT HELIX 296..308 FT /evidence="ECO:0007829|PDB:6UPR" FT HELIX 336..406 FT /evidence="ECO:0007829|PDB:6WSM" SQ SEQUENCE 483 AA; 55756 MW; 35E1ACF95F5DBA6B CRC64; MAATDLERFS NAEPEPRSLS LGGHVGFDSL PDQLVSKSVT QGFSFNILCV GETGIGKSTL MNTLFNTTFE TEEASHHEAC VRLRPQTYDL QESNVQLKLT IVDAVGFGDQ INKDESYRPI VDYIDAQFEN YLQEELKIRR SLFDYHDTRI HVCLYFITPT GHSLKSLDLV TMKKLDSKVN IIPIIAKADT ISKSELHKFK IKIMGELVSN GVQIYQFPTD DEAVAEINAV MNAHLPFAVV GSTEEVKVGN KLVRARQYPW GVVQVENENH CDFVKLREML IRVNMEDLRE QTHSRHYELY RRCKLEEMGF QDSDGDSQPF SLQETYEAKR KEFLSELQRK EEEMRQMFVN KVKETELELK EKERELHEKF EHLKRVHQEE KRKVEEKRRE LEEETNAFNR RKAAVEALQS QALHATSQQP LRKDKDKKNR SDIGAHQPGM SLSSSKVMMT KASVEPLNCS SWWPAIQCCS CLVRDATWRE GFL //