SEP10_HUMAN
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 03-AUG-2022, entry version 158.
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] (ISOFORM 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). {ECO:0000250}.
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}. Note=Using a GFP-fusion protein,
CC detected in the nucleus. {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 -!- 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 CAUTION: [Isoform 2]:
CC Sequence=AAH50345.2; Type=Frameshift; Evidence={ECO:0000305};
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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 SMR; Q9P0V9; -.
DR BioGRID; 127339; 130.
DR IntAct; Q9P0V9; 21.
DR STRING; 9606.ENSP00000380824; -.
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; Q9P0V9; -.
DR PeptideAtlas; Q9P0V9; -.
DR PRIDE; Q9P0V9; -.
DR ProteomicsDB; 83606; -. [Q9P0V9-1]
DR ProteomicsDB; 83607; -. [Q9P0V9-2]
DR ProteomicsDB; 83608; -. [Q9P0V9-3]
DR Antibodypedia; 33157; 207 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 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; NKSIYQG; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; Q9P0V9; -.
DR TreeFam; TF101080; -.
DR PathwayCommons; Q9P0V9; -.
DR SignaLink; Q9P0V9; -.
DR BioGRID-ORCS; 151011; 9 hits in 1021 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 208 other tissues.
DR ExpressionAtlas; Q9P0V9; baseline and differential.
DR Genevisible; Q9P0V9; HS.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
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 GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR CDD; cd01850; CDC_Septin; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016491; Septin.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW GTP-binding; Nucleotide-binding; 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
