ID SEPT1_HUMAN Reviewed; 367 AA. AC Q8WYJ6; B4DVE6; Q658T1; Q8NEZ1; Q96EL4; Q9H285; DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot. DT 16-APR-2002, sequence version 2. DT 11-NOV-2015, entry version 129. DE RecName: Full=Septin-1; DE AltName: Full=LARP; DE AltName: Full=Peanut-like protein 3; DE AltName: Full=Serologically defined breast cancer antigen NY-BR-24; GN Name=SEPT1; Synonyms=DIFF6, PNUTL3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Tu Q., Yu L., Bi A., Zhang H., Zhao Y., Zhao S.; RT "Isolation and characterization of a novel human gene, HSLARP."; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Peng J., Yu L.; RT "Molecular cloning and characterization of human septins which are RT expressed in liver."; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Spleen; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=B-cell; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 79-367. RC TISSUE=Stomach; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 93-367. RC TISSUE=Mammary gland; RX PubMed=12747765; RA Scanlan M.J., Gout I., Gordon C.M., Williamson B., Stockert E., RA Gure A.O., Jaeger D., Chen Y.-T., Mackay A., O'Hare M.J., Old L.J.; RT "Humoral immunity to human breast cancer: antigen definition and RT quantitative analysis of mRNA expression."; RL Cancer Immun. 1:4-4(2001). RN [7] RP SUBCELLULAR LOCATION, INTERACTION WITH AURKB, PHOSPHORYLATION AT RP SER-248; SER-307 AND SER-315, AND MUTAGENESIS OF SER-19; SER-206; RP SER-248; SER-307; SER-312 AND SER-315. RX PubMed=16179162; DOI=10.1016/j.bbrc.2005.06.212; RA Qi M., Yu W., Liu S., Jia H., Tang L., Shen M., Yan X., Saiyin H., RA Lang Q., Wan B., Zhao S., Yu L.; RT "Septin1, a new interaction partner for human serine/threonine kinase RT aurora-B."; RL Biochem. Biophys. Res. Commun. 336:994-1000(2005). RN [8] 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 [9] RP SUBCELLULAR LOCATION. RX PubMed=19799413; DOI=10.1021/pr900325f; RA Chen T.C., Lee S.A., Hong T.M., Shih J.Y., Lai J.M., Chiou H.Y., RA Yang S.C., Chan C.H., Kao C.Y., Yang P.C., Huang C.Y.; RT "From midbody protein-protein interaction network construction to RT novel regulators in cytokinesis."; RL J. Proteome Res. 8:4943-4953(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248 AND SER-315, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [11] 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., RA Buerckstuemmer T., 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, AND IDENTIFICATION RP 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Filament-forming cytoskeletal GTPase (By similarity). CC May play a role in cytokinesis (Potential). {ECO:0000250, CC ECO:0000305}. CC -!- SUBUNIT: Septins polymerize into heterooligomeric protein CC complexes that form filaments, and can associate with cellular CC membranes, actin filaments and microtubules. GTPase activity is CC required for filament formation (By similarity). Interacts with CC AURKB. {ECO:0000250, ECO:0000269|PubMed:16179162}. CC -!- INTERACTION: CC Q4VCS5-2:AMOT; NbExp=3; IntAct=EBI-693002, EBI-3891843; CC Q96GD4:AURKB; NbExp=6; IntAct=EBI-693002, EBI-624291; CC Q8IYM1:SEPT12; NbExp=3; IntAct=EBI-693002, EBI-2585067; CC Q99719:SEPT5; NbExp=5; IntAct=EBI-693002, EBI-373345; CC Q14141:SEPT6; NbExp=4; IntAct=EBI-693002, EBI-745901; CC Q8IYF3:TEX11; NbExp=3; IntAct=EBI-693002, EBI-742397; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, CC cytoskeleton {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule CC organizing center, centrosome. Midbody. Note=Remains at the CC centrosomes and the nearby microtubules throughout mitosis. CC Localizes to the midbody during cytokinesis. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8WYJ6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8WYJ6-2; Sequence=VSP_038269, VSP_038270; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Expressed at high levels in lymphoid and CC hematopoietic tissues. {ECO:0000269|PubMed:15915442}. CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin- CC like GTPase superfamily. Septin GTPase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 septin-type G (guanine nucleotide-binding) CC domain. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAK61491.1; Type=Erroneous initiation; 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; AF085235; AAL40393.1; -; mRNA. DR EMBL; AY034176; AAK61491.1; ALT_INIT; mRNA. DR EMBL; AK301045; BAG62658.1; -; mRNA. DR EMBL; BC012161; AAH12161.1; -; mRNA. DR EMBL; AL833004; CAH56484.1; -; mRNA. DR EMBL; AF308288; AAG48256.1; -; Genomic_DNA. DR RefSeq; NP_443070.5; NM_052838.4. DR UniGene; Hs.632176; -. DR ProteinModelPortal; Q8WYJ6; -. DR SMR; Q8WYJ6; 22-295. DR BioGrid; 108075; 22. DR IntAct; Q8WYJ6; 9. DR MINT; MINT-1435466; -. DR STRING; 9606.ENSP00000460441; -. DR PhosphoSite; Q8WYJ6; -. DR DMDM; 20178107; -. DR MaxQB; Q8WYJ6; -. DR PaxDb; Q8WYJ6; -. DR PRIDE; Q8WYJ6; -. DR DNASU; 1731; -. DR Ensembl; ENST00000571393; ENSP00000460441; ENSG00000180096. DR GeneID; 1731; -. DR KEGG; hsa:1731; -. DR CTD; 1731; -. DR GeneCards; SEPT1; -. DR HGNC; HGNC:2879; SEPT1. DR HPA; HPA041566; -. DR MIM; 612897; gene. DR neXtProt; NX_Q8WYJ6; -. DR PharmGKB; PA24354; -. DR eggNOG; KOG2655; Eukaryota. DR eggNOG; COG5019; LUCA. DR HOGENOM; HOG000233586; -. DR HOVERGEN; HBG065093; -. DR InParanoid; Q8WYJ6; -. DR KO; K13737; -. DR PhylomeDB; Q8WYJ6; -. DR TreeFam; TF101079; -. DR ChiTaRS; SEPT1; human. DR GeneWiki; SEPT1; -. DR GenomeRNAi; 1731; -. DR NextBio; 7009; -. DR PRO; PR:Q8WYJ6; -. DR Proteomes; UP000005640; Unplaced. DR Bgee; Q8WYJ6; -. DR CleanEx; HS_SEPT1; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell. DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR030379; G_SEPTIN_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR016491; Septin. DR PANTHER; PTHR18884; PTHR18884; 1. 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; Complete proteome; KW Cytoplasm; Cytoskeleton; GTP-binding; Nucleotide-binding; KW Phosphoprotein; Polymorphism; Reference proteome. FT CHAIN 1 367 Septin-1. FT /FTId=PRO_0000173513. FT DOMAIN 22 296 Septin-type G. FT NP_BIND 32 39 GTP. {ECO:0000250}. FT NP_BIND 171 179 GTP. {ECO:0000250}. FT BINDING 66 66 GTP. {ECO:0000250}. FT BINDING 92 92 GTP; via amide nitrogen. {ECO:0000250}. FT BINDING 229 229 GTP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000250}. FT BINDING 245 245 GTP. {ECO:0000250}. FT MOD_RES 206 206 Phosphoserine. FT {ECO:0000244|PubMed:24275569}. FT MOD_RES 248 248 Phosphoserine; by AURKB. FT {ECO:0000244|PubMed:19690332, FT ECO:0000269|PubMed:16179162}. FT MOD_RES 251 251 Phosphothreonine. FT {ECO:0000250|UniProtKB:P42209}. FT MOD_RES 307 307 Phosphoserine; by AURKB. FT {ECO:0000269|PubMed:16179162}. FT MOD_RES 315 315 Phosphoserine; by AURKB. FT {ECO:0000244|PubMed:19690332, FT ECO:0000269|PubMed:16179162}. FT VAR_SEQ 148 167 LRPLDVAFLRAVHEKVNIIP -> SGGGILGAGAFREGWGV FT SAP (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_038269. FT VAR_SEQ 168 367 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_038270. FT VARIANT 80 80 G -> V (in dbSNP:rs34518080). FT /FTId=VAR_051934. FT MUTAGEN 19 19 S->A: No effect on phosphorylation. FT {ECO:0000269|PubMed:16179162}. FT MUTAGEN 206 206 S->A: No effect on phosphorylation. FT {ECO:0000269|PubMed:16179162}. FT MUTAGEN 248 248 S->A: Great reduction in phosphorylation. FT {ECO:0000269|PubMed:16179162}. FT MUTAGEN 307 307 S->A: Great reduction in phosphorylation. FT {ECO:0000269|PubMed:16179162}. FT MUTAGEN 312 312 S->A: No effect on phosphorylation. FT {ECO:0000269|PubMed:16179162}. FT MUTAGEN 315 315 S->A: Great reduction in phosphorylation. FT {ECO:0000269|PubMed:16179162}. FT CONFLICT 60 60 S -> G (in Ref. 1; AAL40393). FT {ECO:0000305}. FT CONFLICT 148 150 LRP -> SR (in Ref. 1; AAL40393). FT {ECO:0000305}. FT CONFLICT 240 241 RP -> GL (in Ref. 1; AAL40393). FT {ECO:0000305}. FT CONFLICT 324 324 L -> P (in Ref. 1; AAL40393). FT {ECO:0000305}. SQ SEQUENCE 367 AA; 41971 MW; E9C6BEF373CB0FC4 CRC64; MDKEYVGFAA LPNQLHRKSV KKGFDFTLMV AGESGLGKST LINSLFLTNL YEDRQVPEAS ARLTQTLAIE RRGVEIEEGG VKVKLTLVDT PGFGDSVDCS DCWLPVVKFI EEQFEQYLRD ESGLNRKNIQ DSRVHCCLYF ISPFGRGLRP LDVAFLRAVH EKVNIIPVIG KADALMPQET QALKQKIRDQ LKEEEIHIYQ FPECDSDEDE DFKRQDAEMK ESIPFAVVGS CEVVRDGGNR PVRGRRYSWG TVEVENPHHC DFLNLRRMLV QTHLQDLKEV THDLLYEGYR ARCLQSLARP GARDRASRSK LSRQSATEIP LPMLPLADTE KLIREKDEEL RRMQEMLEKM QAQMQQSQAQ GEQSDAL //