ID SEP10_HUMAN Reviewed; 454 AA. AC Q9P0V9; B3KRQ9; Q86VP5; Q9HAH6; DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 2. DT 24-JAN-2024, entry version 166. DE RecName: Full=Septin-10; GN Name=SEPTIN10 {ECO:0000312|HGNC:HGNC:14349}; Synonyms=SEPT10; 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] (ISOFOSRM 1), GTPASE ACTIVITY, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RC TISSUE=Dendritic cell; RX PubMed=12711328; DOI=10.1016/s0006-291x(03)00601-6; RA Sui L., Zhang W., Liu Q., Chen T., Li N., Wan T., Yu M., Cao X.; RT "Cloning and functional characterization of human septin 10, a novel member RT of septin family cloned from dendritic cells."; RL Biochem. Biophys. Res. Commun. 304:393-398(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [4] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Testis, and Uterus; 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 [6] 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 [7] 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). CC -!- FUNCTION: Filament-forming cytoskeletal GTPase. May play a role in CC cytokinesis (Potential). {ECO:0000305}. 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 ADGB (By similarity). CC {ECO:0000250|UniProtKB:Q8C650}. CC -!- INTERACTION: CC Q9P0V9; Q99719: SEPTIN5; NbExp=6; IntAct=EBI-3943788, EBI-373345; CC Q9P0V9; Q16181-2: SEPTIN7; NbExp=6; IntAct=EBI-3943788, EBI-10176094; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12711328}. CC Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, cilium, CC flagellum {ECO:0000250|UniProtKB:Q8C650}. Note=Detected in the annulus CC of the sperm flagellum and in the neck region in spermatids and mature CC sperm (By similarity). Using a GFP-fusion protein, detected in the CC nucleus. {ECO:0000250|UniProtKB:Q8C650, ECO:0000269|PubMed:12711328}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9P0V9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9P0V9-2; Sequence=VSP_014091; CC Name=3; CC IsoId=Q9P0V9-3; Sequence=VSP_041479; CC -!- TISSUE SPECIFICITY: Widely expressed. Abundantly expressed in heart and CC kidney, placenta, skeletal muscles, liver and lung, as well as various CC tumor cell lines. {ECO:0000269|PubMed:12711328, CC ECO:0000269|PubMed:15915442}. CC -!- PTM: Proteolytically cleaved in vitro in a calmodulin-dependent manner. CC {ECO:0000250|UniProtKB:Q8C650}. 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=AAF67469.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAH50345.2; Type=Frameshift; 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; AF146760; AAF67469.1; ALT_FRAME; mRNA. DR EMBL; AK092033; BAG52471.1; -; mRNA. DR EMBL; AK021681; BAB13873.1; -; mRNA. DR EMBL; AC140485; AAY24142.1; -; Genomic_DNA. DR EMBL; CH471182; EAW53864.1; -; Genomic_DNA. DR EMBL; BC020502; AAH20502.1; -; mRNA. DR EMBL; BC050345; AAH50345.2; ALT_FRAME; mRNA. DR CCDS; CCDS42726.1; -. [Q9P0V9-3] DR CCDS; CCDS46383.1; -. [Q9P0V9-1] DR RefSeq; NP_001308425.1; NM_001321496.1. DR RefSeq; NP_001308427.1; NM_001321498.1. DR RefSeq; NP_001308428.1; NM_001321499.1. DR RefSeq; NP_001308429.1; NM_001321500.1. DR RefSeq; NP_001308430.1; NM_001321501.1. DR RefSeq; NP_001308431.1; NM_001321502.1. DR RefSeq; NP_001308432.1; NM_001321503.1. DR RefSeq; NP_001308433.1; NM_001321504.1. DR RefSeq; NP_001308434.1; NM_001321505.1. DR RefSeq; NP_001308435.1; NM_001321506.1. DR RefSeq; NP_001308436.1; NM_001321507.1. DR RefSeq; NP_001308437.1; NM_001321508.1. DR RefSeq; NP_001308438.1; NM_001321509.1. DR RefSeq; NP_001308439.1; NM_001321510.1. DR RefSeq; NP_001308440.1; NM_001321511.1. DR RefSeq; NP_001308441.1; NM_001321512.1. DR RefSeq; NP_653311.1; NM_144710.4. [Q9P0V9-1] DR RefSeq; NP_848699.1; NM_178584.3. [Q9P0V9-3] DR AlphaFoldDB; Q9P0V9; -. DR SASBDB; Q9P0V9; -. DR SMR; Q9P0V9; -. DR BioGRID; 127339; 147. DR IntAct; Q9P0V9; 28. DR STRING; 9606.ENSP00000349116; -. DR GlyGen; Q9P0V9; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9P0V9; -. DR PhosphoSitePlus; Q9P0V9; -. DR BioMuta; SEPT10; -. DR DMDM; 160400057; -. DR EPD; Q9P0V9; -. DR jPOST; Q9P0V9; -. DR MassIVE; Q9P0V9; -. DR MaxQB; Q9P0V9; -. DR PaxDb; 9606-ENSP00000380824; -. DR PeptideAtlas; Q9P0V9; -. DR ProteomicsDB; 83606; -. [Q9P0V9-1] DR ProteomicsDB; 83607; -. [Q9P0V9-2] DR ProteomicsDB; 83608; -. [Q9P0V9-3] DR Pumba; Q9P0V9; -. DR Antibodypedia; 33157; 232 antibodies from 29 providers. DR DNASU; 151011; -. DR Ensembl; ENST00000397712.7; ENSP00000380824.2; ENSG00000186522.15. [Q9P0V9-1] DR Ensembl; ENST00000397714.6; ENSP00000380826.2; ENSG00000186522.15. [Q9P0V9-3] DR GeneID; 151011; -. DR KEGG; hsa:151011; -. DR MANE-Select; ENST00000397712.7; ENSP00000380824.2; NM_144710.5; NP_653311.1. DR UCSC; uc002tew.5; human. [Q9P0V9-1] DR AGR; HGNC:14349; -. DR CTD; 151011; -. DR DisGeNET; 151011; -. DR GeneCards; SEPTIN10; -. DR HGNC; HGNC:14349; SEPTIN10. DR HPA; ENSG00000186522; Low tissue specificity. DR MIM; 611737; gene. DR neXtProt; NX_Q9P0V9; -. DR OpenTargets; ENSG00000186522; -. DR PharmGKB; PA134918683; -. DR VEuPathDB; HostDB:ENSG00000186522; -. DR eggNOG; KOG3859; Eukaryota. DR GeneTree; ENSGT00940000155238; -. DR HOGENOM; CLU_017718_8_1_1; -. DR InParanoid; Q9P0V9; -. DR OMA; XLQAKFE; -. DR OrthoDB; 5396944at2759; -. DR PhylomeDB; Q9P0V9; -. DR TreeFam; TF101080; -. DR PathwayCommons; Q9P0V9; -. DR SignaLink; Q9P0V9; -. DR BioGRID-ORCS; 151011; 10 hits in 1085 CRISPR screens. DR ChiTaRS; SEPT10; human. DR GenomeRNAi; 151011; -. DR Pharos; Q9P0V9; Tbio. DR PRO; PR:Q9P0V9; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q9P0V9; Protein. DR Bgee; ENSG00000186522; Expressed in skin of hip and 210 other cell types or tissues. DR ExpressionAtlas; Q9P0V9; baseline and differential. DR GO; GO:0032153; C:cell division site; IBA:GO_Central. DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell. DR GO; GO:0031105; C:septin complex; IBA:GO_Central. DR GO; GO:0005940; C:septin ring; IBA:GO_Central. 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 CDD; cd01850; CDC_Septin; 1. DR CDD; cd22249; UDM1_RNF168_RNF169-like; 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:SF50; SEPTIN-10; 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; Q9P0V9; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cell cycle; Cell division; Cell projection; Cilium; KW Cytoplasm; Cytoskeleton; Flagellum; GTP-binding; Nucleotide-binding; KW Reference proteome. FT CHAIN 1..454 FT /note="Septin-10" FT /id="PRO_0000173538" FT DOMAIN 63..329 FT /note="Septin-type G" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056" FT REGION 73..80 FT /note="G1 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056" FT REGION 125..128 FT /note="G3 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056" FT REGION 208..211 FT /note="G4 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056" FT BINDING 73..80 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 128 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 209..217 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 263 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 278 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT VAR_SEQ 11..33 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_041479" FT VAR_SEQ 450..454 FT /note="NSNFL -> KEPGCRFELLCIDVRACETNGGRKDAEKAPIFCKTEVPEHRRS FT SSQANFIKKKN (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_014091" FT VARIANT 189 FT /note="L -> P (in dbSNP:rs3829701)" FT /id="VAR_051936" SQ SEQUENCE 454 AA; 52593 MW; 95C8F7FAA266BC10 CRC64; MASSEVARHL LFQSHMATKT TCMSSQGSDD EQIKRENIRS LTMSGHVGFE SLPDQLVNRS IQQGFCFNIL CVGETGIGKS TLIDTLFNTN FEDYESSHFC PNVKLKAQTY ELQESNVQLK LTIVNTVGFG DQINKEESYQ PIVDYIDAQF EAYLQEELKI KRSLFTYHDS RIHVCLYFIS PTGHSLKTLD LLTMKNLDSK VNIIPVIAKA DTVSKTELQK FKIKLMSELV SNGVQIYQFP TDDDTIAKVN AAMNGQLPFA VVGSMDEVKV GNKMVKARQY PWGVVQVENE NHCDFVKLRE MLICTNMEDL REQTHTRHYE LYRRCKLEEM GFTDVGPENK PVSVQETYEA KRHEFHGERQ RKEEEMKQMF VQRVKEKEAI LKEAERELQA KFEHLKRLHQ EERMKLEEKR RLLEEEIIAF SKKKATSEIF HSQSFLATGS NLRKDKDRKN SNFL //