SEPT4_HUMAN
ID SEPT4_HUMAN Reviewed; 478 AA.
AC O43236; A0A5F9ZHH3; B2RD42; B3KSX9; B4DXC6; B4DXV5; Q6IAP3; Q8N821; Q8NEP4;
AC Q9H315; Q9UM58;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Septin-4 {ECO:0000312|HGNC:HGNC:9165};
DE AltName: Full=Bradeion beta {ECO:0000303|PubMed:11511094};
DE AltName: Full=Brain protein H5 {ECO:0000250|UniProtKB:P28661};
DE AltName: Full=CE5B3 beta {ECO:0000312|HGNC:HGNC:9165};
DE AltName: Full=Cell division control-related protein 2 {ECO:0000312|HGNC:HGNC:9165};
DE Short=hCDCREL-2 {ECO:0000312|HGNC:HGNC:9165};
DE AltName: Full=Peanut-like protein 2 {ECO:0000303|PubMed:9889007};
GN Name=SEPTIN4 {ECO:0000312|HGNC:HGNC:9165};
GN Synonyms=C17orf47 {ECO:0000312|HGNC:HGNC:9165},
GN PNUTL2 {ECO:0000303|PubMed:9889007}, SEP4 {ECO:0000312|HGNC:HGNC:9165},
GN SEPT4 {ECO:0000312|HGNC:HGNC:9165}; ORFNames=hucep-7;
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), AND TISSUE SPECIFICITY.
RX PubMed=9889007; DOI=10.1006/geno.1998.5612;
RA Paavola P., Horelli-Kuitunen N., Palotie A., Peltonen L.;
RT "Characterization of a novel gene, PNUTL2, on human chromosome 17q22-q23
RT and its exclusion as the Meckel syndrome gene.";
RL Genomics 55:122-125(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC TISSUE=Brain, and Fetal brain;
RX PubMed=11167005; DOI=10.1016/s0378-1119(00)00527-8;
RA Zieger B., Tran H., Hainmann I., Wunderle D., Zgaga-Griesz A., Blaeser S.,
RA Ware J.;
RT "Characterization and expression analysis of two human septin genes, PNUTL1
RT and PNUTL2.";
RL Gene 261:197-203(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ARTS), FUNCTION (ISOFORM ARTS), TISSUE
RP SPECIFICITY (ISOFORM ARTS), SUBCELLULAR LOCATION (ISOFORM ARTS), AND
RP MUTAGENESIS OF 156-GLY--SER-158 (ISOFORM ARTS).
RC TISSUE=Fetal brain;
RX PubMed=11146656; DOI=10.1038/35046566;
RA Larisch S., Yi Y., Lotan R., Kerner H., Eimerl S., Parks W.T., Yossi G.,
RA Reffey S.B., de Caestecker M.P., Danielpour D., Book-Melamed N.,
RA Timberg R., Duckett C., Lechleider R.J., Steller H., Orly J., Kim S.-J.,
RA Roberts A.B.;
RT "A novel mitochondrial septin-like protein, ARTS, mediates apoptosis
RT dependent on its P-loop motif.";
RL Nat. Cell Biol. 2:915-921(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11511094; DOI=10.1006/bbrc.2001.5413;
RA Tanaka M., Tanaka T., Kijima H., Itoh J., Matsuda T., Hori S., Yamamoto M.;
RT "Characterization of tissue- and cell-type-specific expression of a novel
RT human septin family gene, Bradeion.";
RL Biochem. Biophys. Res. Commun. 286:547-553(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Yoshimoto M., Yazaki M., Matsumoto K., Takayama K.;
RT "Molecular cloning of a new GTP binding protein from human brain.";
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Zha D., Hu G.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4; 5 AND 8).
RC TISSUE=Amygdala, Brain cortex, Subthalamic nucleus, and Testis;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [10]
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 [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 8).
RC TISSUE=Hippocampus, and Testis;
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 [12]
RP INTERACTION WITH SEPTIN8, SUBCELLULAR LOCATION, AND TISSUE 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 [13]
RP PROTEIN SEQUENCE OF 141-157 AND 282-290, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Fetal brain;
RA Lubec G., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [14]
RP FUNCTION (ISOFORM ARTS).
RX PubMed=15837787; DOI=10.1074/jbc.m501955200;
RA Lotan R., Rotem A., Gonen H., Finberg J.P.M., Kemeny S., Steller H.,
RA Ciechanover A., Larisch S.;
RT "Regulation of the proapoptotic ARTS protein by ubiquitin-mediated
RT degradation.";
RL J. Biol. Chem. 280:25802-25810(2005).
RN [15]
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 [16]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17296554; DOI=10.1016/j.neuron.2007.01.019;
RA Ihara M., Yamasaki N., Hagiwara A., Tanigaki A., Kitano A., Hikawa R.,
RA Tomimoto H., Noda M., Takanashi M., Mori H., Hattori N., Miyakawa T.,
RA Kinoshita M.;
RT "Sept4, a component of presynaptic scaffold and Lewy bodies, is required
RT for the suppression of alpha-synuclein neurotoxicity.";
RL Neuron 53:519-533(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [18]
RP INTERACTION WITH XIAP, AND SUBCELLULAR LOCATION.
RX PubMed=21695558; DOI=10.1007/s10495-011-0622-0;
RA Bornstein B., Gottfried Y., Edison N., Shekhtman A., Lev T., Glaser F.,
RA Larisch S.;
RT "ARTS binds to a distinct domain in XIAP-BIR3 and promotes apoptosis by a
RT mechanism that is different from other IAP-antagonists.";
RL Apoptosis 16:869-881(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117; SER-118 AND SER-325, AND
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 [20]
RP INTERACTION WITH SEPTIN9 HNA VARIANTS.
RX PubMed=17546647; DOI=10.1002/humu.20554;
RA Sudo K., Ito H., Iwamoto I., Morishita R., Asano T., Nagata K.;
RT "SEPT9 sequence alternations causing hereditary neuralgic amyotrophy are
RT associated with altered interactions with SEPT4/SEPT11 and resistance to
RT Rho/Rhotekin-signaling.";
RL Hum. Mutat. 28:1005-1013(2007).
RN [21]
RP FUNCTION (ISOFORM ARTS), SUBCELLULAR LOCATION (ISOFORM ARTS), INTERACTION
RP WITH XIAP (ISOFORM ARTS), AND MUTAGENESIS OF 156-GLY--SER-158 (ISOFORM
RP ARTS).
RX PubMed=15029247; DOI=10.1038/sj.emboj.7600155;
RA Gottfried Y., Rotem A., Lotan R., Steller H., Larisch S.;
RT "The mitochondrial ARTS protein promotes apoptosis through targeting
RT XIAP.";
RL EMBO J. 23:1627-1635(2004).
RN [22]
RP INTERACTION WITH AREL1, AND UBIQUITINATION.
RX PubMed=23479728; DOI=10.1074/jbc.m112.436113;
RA Kim J.B., Kim S.Y., Kim B.M., Lee H., Kim I., Yun J., Jo Y., Oh T., Jo Y.,
RA Chae H.D., Shin D.Y.;
RT "Identification of a novel anti-apoptotic E3 ubiquitin ligase that
RT ubiquitinates antagonists of inhibitor of apoptosis proteins SMAC, HtrA2,
RT and ARTS.";
RL J. Biol. Chem. 288:12014-12021(2013).
RN [23]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=25588830; DOI=10.1242/jcs.158998;
RA Kuo Y.C., Shen Y.R., Chen H.I., Lin Y.H., Wang Y.Y., Chen Y.R., Wang C.Y.,
RA Kuo P.L.;
RT "SEPT12 orchestrates the formation of mammalian sperm annulus by organizing
RT core octomeric complexes with other SEPT proteins.";
RL J. Cell Sci. 128:923-934(2015).
RN [24]
RP FUNCTION, IDENTIFICATION IN A COMPLEX WITH BCL2 AND XIAP, AND INTERACTION
RP WITH BCL2 AND XIAP.
RX PubMed=29020630; DOI=10.1016/j.celrep.2017.09.052;
RA Edison N., Curtz Y., Paland N., Mamriev D., Chorubczyk N.,
RA Haviv-Reingewertz T., Kfir N., Morgenstern D., Kupervaser M., Kagan J.,
RA Kim H.T., Larisch S.;
RT "Degradation of Bcl-2 by XIAP and ARTS Promotes Apoptosis.";
RL Cell Rep. 21:442-454(2017).
RN [25]
RP TISSUE SPECIFICITY.
RX PubMed=30389919; DOI=10.1038/s41467-018-06941-4;
RA Koren E., Yosefzon Y., Ankawa R., Soteriou D., Jacob A., Nevelsky A.,
RA Ben-Yosef R., Bar-Sela G., Fuchs Y.;
RT "ARTS mediates apoptosis and regeneration of the intestinal stem cell
RT niche.";
RL Nat. Commun. 9:4582-4582(2018).
CC -!- FUNCTION: Filament-forming cytoskeletal GTPase (Probable). Pro-
CC apoptotic protein involved in LGR5-positive intestinal stem cell and
CC Paneth cell expansion in the intestines, via its interaction with XIAP
CC (By similarity). May also play a role in the regulation of cell fate in
CC the intestine (By similarity). Positive regulator of apoptosis involved
CC in hematopoietic stem cell homeostasis; via its interaction with XIAP
CC (By similarity). Negative regulator of repair and hair follicle
CC regeneration in response to injury, due to inhibition of hair follicle
CC stem cell proliferation, potentially via its interaction with XIAP (By
CC similarity). Plays an important role in male fertility and sperm
CC motility (By similarity). During spermiogenesis, essential for the
CC establishment of the annulus (a fibrous ring structure connecting the
CC midpiece and the principal piece of the sperm flagellum) which is a
CC requisite for the structural and mechanical integrity of the sperm (By
CC similarity). Involved in the migration of cortical neurons and the
CC formation of neuron leading processes during embryonic development (By
CC similarity). Required for dopaminergic metabolism in presynaptic
CC autoreceptors; potentially via activity as a presynaptic scaffold
CC protein (By similarity). {ECO:0000250|UniProtKB:P28661, ECO:0000305}.
CC -!- FUNCTION: [Isoform ARTS]: Required for the induction of cell death
CC mediated by TGF-beta and possibly by other apoptotic stimuli
CC (PubMed:11146656, PubMed:15837787). Induces apoptosis through binding
CC and inhibition of XIAP resulting in significant reduction in XIAP
CC levels, leading to caspase activation and cell death (PubMed:15029247).
CC Mediates the interaction between BCL2 and XIAP, thereby positively
CC regulating the ubiquitination and degradation of BCL2 and promoting
CC apoptosis (PubMed:29020630). {ECO:0000269|PubMed:11146656,
CC ECO:0000269|PubMed:15029247, ECO:0000269|PubMed:15837787,
CC ECO:0000269|PubMed:29020630}.
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. Interacts with SEPTIN8 (PubMed:15116257). In a mesenchymal
CC cell line, interacts with SEPTIN9 isoform 2 variants HNA Trp-106 and
CC Phe-111, but not the wild type SEPTIN9 (PubMed:17546647). Component of
CC a septin core octomeric complex consisting of SEPTIN12, SEPTIN7,
CC SEPTIN6 and SEPTIN2 or SEPTIN4 in the order 12-7-6-2-2-6-7-12 or 12-7-
CC 6-4-4-6-7-12 (PubMed:25588830). Interacts with SEPTIN14 (via C-
CC terminus) (By similarity). Interacts with DYRK1A (By similarity).
CC Interacts with SLC6A3/DAT and SNCA/alpha-synuclein (By similarity).
CC Interacts with STX1A; in the striatum (By similarity). Interacts with
CC XIAP (via BIR3 domain) following the induction of apoptosis (By
CC similarity). Interacts with AREL1 (via HECT domain); in the cytoplasm
CC following induction of apoptosis (PubMed:23479728).
CC {ECO:0000250|UniProtKB:P28661, ECO:0000269|PubMed:15116257,
CC ECO:0000269|PubMed:17546647, ECO:0000269|PubMed:23479728,
CC ECO:0000269|PubMed:25588830}.
CC -!- SUBUNIT: [Isoform ARTS]: Part of a complex composed of SEPTIN4 isoform
CC ARTS, XIAP and BCL2, within the complex interacts with both BCL2 (via
CC BH3 domain) and XIAP, ARTS acts as a scaffold protein and stabilizes
CC the complex (PubMed:29020630). Interacts with XIAP (via BIR3 domain)
CC following the induction of apoptosis (PubMed:15029247,
CC PubMed:21695558). {ECO:0000269|PubMed:15029247,
CC ECO:0000269|PubMed:21695558, ECO:0000269|PubMed:29020630}.
CC -!- INTERACTION:
CC O43236; P05067: APP; NbExp=3; IntAct=EBI-1047513, EBI-77613;
CC O43236; P63167: DYNLL1; NbExp=5; IntAct=EBI-1047513, EBI-349105;
CC O43236; Q96FJ2: DYNLL2; NbExp=3; IntAct=EBI-1047513, EBI-742371;
CC O43236; P42858: HTT; NbExp=3; IntAct=EBI-1047513, EBI-466029;
CC O43236; Q8IYM1: SEPTIN12; NbExp=5; IntAct=EBI-1047513, EBI-2585067;
CC O43236; P37840: SNCA; NbExp=3; IntAct=EBI-1047513, EBI-985879;
CC O43236-6; Q8IUQ4: SIAH1; NbExp=2; IntAct=EBI-4372019, EBI-747107;
CC O43236-6; P98170: XIAP; NbExp=4; IntAct=EBI-4372019, EBI-517127;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P28661}. Cell
CC projection, cilium, flagellum {ECO:0000269|PubMed:25588830}.
CC Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:15116257}.
CC Cell projection, axon {ECO:0000250|UniProtKB:P28661}. Cell projection,
CC dendrite {ECO:0000250|UniProtKB:P28661}. Perikaryon
CC {ECO:0000250|UniProtKB:P28661}. Synapse {ECO:0000269|PubMed:17296554}.
CC Note=In platelets, found in areas surrounding alpha-granules
CC (PubMed:15116257). Found in the sperm annulus, a fibrous ring structure
CC connecting the midpiece and the principal piece of the sperm flagellum
CC (PubMed:25588830). Expressed and colocalized with SLC6A3 and SNCA in
CC axon terminals, especially at the varicosities (By similarity).
CC {ECO:0000250|UniProtKB:P28661, ECO:0000269|PubMed:15116257,
CC ECO:0000269|PubMed:25588830}.
CC -!- SUBCELLULAR LOCATION: [Isoform ARTS]: Mitochondrion
CC {ECO:0000269|PubMed:11146656, ECO:0000269|PubMed:15029247,
CC ECO:0000269|PubMed:21695558}. Nucleus {ECO:0000269|PubMed:11146656,
CC ECO:0000269|PubMed:15029247}. Note=While predominantly localized in the
CC mitochondria under resting conditions, translocates into the nucleus
CC after TGF-beta treatment and apoptosis induction.
CC {ECO:0000269|PubMed:11146656}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1; Synonyms=PNUTL2, PNUTL2a, H5/CDCrel-2
CC {ECO:0000303|PubMed:11167005}, SEPT4_i1;
CC IsoId=O43236-1; Sequence=Displayed;
CC Name=2; Synonyms=PNUTL2b, CDCrel-1 {ECO:0000303|PubMed:11167005};
CC IsoId=O43236-2; Sequence=VSP_006050;
CC Name=3;
CC IsoId=O43236-3; Sequence=VSP_038303;
CC Name=4;
CC IsoId=O43236-4; Sequence=VSP_038304;
CC Name=5;
CC IsoId=O43236-5; Sequence=VSP_038302;
CC Name=ARTS {ECO:0000303|PubMed:11146656}; Synonyms=SEPT4_i2;
CC IsoId=O43236-6; Sequence=VSP_006050, VSP_038305, VSP_038306;
CC Name=7;
CC IsoId=O43236-7; Sequence=VSP_060789;
CC Name=8;
CC IsoId=O43236-8; Sequence=VSP_060788;
CC -!- TISSUE SPECIFICITY: Widely expressed in adult and fetal tissues with
CC highest expression in adult brain (at protein level), heart, liver and
CC adrenal gland and fetal heart, kidney, liver and lung. Expressed in
CC presynaptic terminals of dopaminergic neurons projecting from the
CC substantia nigra pars compacta to the striatum (at protein level)
CC (PubMed:17296554). Expressed in axonal varicosities in dopaminergic
CC nerve terminals (at protein level) (PubMed:17296554). Expressed in the
CC putamen and in the adjacent cerebral cortex (at protein level)
CC (PubMed:17296554). Expressed in colonic crypts (at protein level)
CC (PubMed:30389919). Also expressed in colorectal cancers and malignant
CC melanomas. Expressed in platelets. {ECO:0000269|PubMed:11146656,
CC ECO:0000269|PubMed:11167005, ECO:0000269|PubMed:11511094,
CC ECO:0000269|PubMed:15116257, ECO:0000269|PubMed:15915442,
CC ECO:0000269|PubMed:17296554, ECO:0000269|PubMed:30389919,
CC ECO:0000269|PubMed:9889007}.
CC -!- TISSUE SPECIFICITY: [Isoform ARTS]: Highly expressed in the brain and
CC heart. {ECO:0000269|PubMed:11146656}.
CC -!- PTM: Phosphorylated by DYRK1A. {ECO:0000250|UniProtKB:P28661}.
CC -!- PTM: Ubiquitinated by AREL1. {ECO:0000269|PubMed:23479728}.
CC -!- MISCELLANEOUS: Colocalizes with alpha-synuclein in Lewy bodies in the
CC substantia nigra pars compacta of Parkinson disease patients
CC (PubMed:17296554). Shows reduced expression in dopaminergic nerve
CC terminals of the striatum in sporadic Parkinson disease
CC (PubMed:17296554). {ECO:0000269|PubMed:17296554}.
CC -!- MISCELLANEOUS: [Isoform ARTS]: May be defective in GTP-binding.
CC {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}.
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DR EMBL; AF073312; AAC25673.1; -; mRNA.
DR EMBL; U88829; AAD00653.1; -; mRNA.
DR EMBL; U88870; AAD00657.1; -; mRNA.
DR EMBL; AF176379; AAG45673.1; -; mRNA.
DR EMBL; AB008753; BAB70695.1; -; mRNA.
DR EMBL; D89278; BAB46922.1; -; mRNA.
DR EMBL; AF035811; AAB88512.1; -; mRNA.
DR EMBL; CR457111; CAG33392.1; -; mRNA.
DR EMBL; AK315396; BAG37789.1; -; mRNA.
DR EMBL; AK094579; BAG52891.1; -; mRNA.
DR EMBL; AK294094; BAG57432.1; -; mRNA.
DR EMBL; AK301914; BAG63338.1; -; mRNA.
DR EMBL; AK302146; BAG63517.1; -; mRNA.
DR EMBL; AK097440; BAC05054.1; -; mRNA.
DR EMBL; AC005666; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94440.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94442.1; -; Genomic_DNA.
DR EMBL; BC018056; AAH18056.3; -; mRNA.
DR EMBL; BC022189; AAH22189.2; -; mRNA.
DR CCDS; CCDS11609.1; -. [O43236-2]
DR CCDS; CCDS11610.1; -. [O43236-1]
DR CCDS; CCDS32691.1; -. [O43236-8]
DR CCDS; CCDS45743.1; -. [O43236-6]
DR CCDS; CCDS56041.1; -. [O43236-3]
DR CCDS; CCDS58581.1; -. [O43236-5]
DR CCDS; CCDS58582.1; -. [O43236-4]
DR RefSeq; NP_001033793.2; NM_001038704.2. [O43236-8]
DR RefSeq; NP_001185642.1; NM_001198713.1. [O43236-3]
DR RefSeq; NP_001243711.1; NM_001256782.1. [O43236-4]
DR RefSeq; NP_001243751.1; NM_001256822.1. [O43236-5]
DR RefSeq; NP_004565.1; NM_004574.4. [O43236-1]
DR RefSeq; NP_536340.1; NM_080415.3. [O43236-6]
DR RefSeq; NP_536341.1; NM_080416.3. [O43236-2]
DR RefSeq; XP_006722017.1; XM_006721954.2. [O43236-5]
DR RefSeq; XP_006722018.1; XM_006721955.2. [O43236-5]
DR RefSeq; XP_011523213.1; XM_011524911.1. [O43236-5]
DR RefSeq; XP_011523214.1; XM_011524912.1. [O43236-5]
DR PDB; 6WB3; X-ray; 1.35 A; A/B=448-477.
DR PDBsum; 6WB3; -.
DR AlphaFoldDB; O43236; -.
DR SMR; O43236; -.
DR BioGRID; 111415; 26.
DR BioGRID; 129753; 3.
DR IntAct; O43236; 23.
DR MINT; O43236; -.
DR STRING; 9606.ENSP00000354874; -.
DR iPTMnet; O43236; -.
DR PhosphoSitePlus; O43236; -.
DR BioMuta; C17orf47; -.
DR BioMuta; SEPT4; -.
DR DMDM; 300669697; -.
DR EPD; O43236; -.
DR jPOST; O43236; -.
DR MassIVE; O43236; -.
DR MaxQB; O43236; -.
DR PaxDb; O43236; -.
DR PeptideAtlas; O43236; -.
DR PRIDE; O43236; -.
DR ProteomicsDB; 48814; -. [O43236-1]
DR ProteomicsDB; 48815; -. [O43236-2]
DR ProteomicsDB; 48816; -. [O43236-3]
DR ProteomicsDB; 48817; -. [O43236-4]
DR ProteomicsDB; 48818; -. [O43236-5]
DR ProteomicsDB; 48819; -. [O43236-6]
DR ProteomicsDB; 73193; -.
DR Antibodypedia; 3484; 277 antibodies from 37 providers.
DR DNASU; 284083; -.
DR DNASU; 5414; -.
DR Ensembl; ENST00000317256.10; ENSP00000321071.6; ENSG00000108387.16. [O43236-2]
DR Ensembl; ENST00000317268.7; ENSP00000321674.3; ENSG00000108387.16. [O43236-1]
DR Ensembl; ENST00000321691.3; ENSP00000354874.2; ENSG00000108387.16. [O43236-8]
DR Ensembl; ENST00000393086.5; ENSP00000376801.1; ENSG00000108387.16. [O43236-2]
DR Ensembl; ENST00000412945.7; ENSP00000414779.3; ENSG00000108387.16. [O43236-3]
DR Ensembl; ENST00000426861.5; ENSP00000402348.1; ENSG00000108387.16. [O43236-6]
DR Ensembl; ENST00000457347.6; ENSP00000402000.2; ENSG00000108387.16. [O43236-4]
DR Ensembl; ENST00000583114.5; ENSP00000463768.1; ENSG00000108387.16. [O43236-5]
DR Ensembl; ENST00000672673.2; ENSP00000500383.1; ENSG00000108387.16. [O43236-7]
DR Ensembl; ENST00000672699.1; ENSP00000500355.1; ENSG00000108387.16. [O43236-4]
DR GeneID; 5414; -.
DR KEGG; hsa:5414; -.
DR MANE-Select; ENST00000672673.2; ENSP00000500383.1; NM_001368771.2; NP_001355700.1. [O43236-7]
DR UCSC; uc002iwm.4; human. [O43236-1]
DR CTD; 5414; -.
DR DisGeNET; 5414; -.
DR GeneCards; SEPTIN4; -.
DR HGNC; HGNC:9165; SEPTIN4.
DR HPA; ENSG00000108387; Group enriched (brain, choroid plexus, retina).
DR MIM; 603696; gene.
DR neXtProt; NX_O43236; -.
DR OpenTargets; ENSG00000108387; -.
DR PharmGKB; PA33487; -.
DR VEuPathDB; HostDB:ENSG00000108387; -.
DR eggNOG; ENOG502SETZ; Eukaryota.
DR eggNOG; KOG2655; Eukaryota.
DR GeneTree; ENSGT00390000018146; -.
DR HOGENOM; CLU_575631_0_0_1; -.
DR InParanoid; O43236; -.
DR OMA; SSICTEP; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; O43236; -.
DR TreeFam; TF101079; -.
DR TreeFam; TF338016; -.
DR PathwayCommons; O43236; -.
DR Reactome; R-HSA-111457; Release of apoptotic factors from the mitochondria. [O43236-6]
DR Reactome; R-HSA-111469; SMAC, XIAP-regulated apoptotic response. [O43236-6]
DR SignaLink; O43236; -.
DR SIGNOR; O43236; -.
DR BioGRID-ORCS; 284083; 6 hits in 1033 CRISPR screens.
DR BioGRID-ORCS; 5414; 8 hits in 1021 CRISPR screens.
DR ChiTaRS; SEPT4; human.
DR GeneWiki; SEPT4; -.
DR GenomeRNAi; 5414; -.
DR Pharos; O43236; Tbio.
DR PRO; PR:Q8NEP4; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O43236; protein.
DR Bgee; ENSG00000108387; Expressed in C1 segment of cervical spinal cord and 147 other tissues.
DR ExpressionAtlas; O43236; baseline and differential.
DR Genevisible; O43236; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
DR GO; GO:0031105; C:septin complex; IDA:UniProtKB.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0097227; C:sperm annulus; IDA:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IMP:CAFA.
DR GO; GO:0003924; F:GTPase activity; IMP:CAFA.
DR GO; GO:0042802; F:identical protein binding; IPI:CAFA.
DR GO; GO:0000287; F:magnesium ion binding; IMP:CAFA.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0005198; F:structural molecule activity; TAS:ProtInc.
DR GO; GO:0006915; P:apoptotic process; NAS:UniProtKB.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0030317; P:flagellated sperm motility; ISS:UniProtKB.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; ISS:UniProtKB.
DR GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0042981; P:regulation of apoptotic process; NAS:UniProtKB.
DR GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
DR GO; GO:0048515; P:spermatid differentiation; ISS:UniProtKB.
DR CDD; cd01850; CDC_Septin; 1.
DR DisProt; DP00537; -.
DR DisProt; DP01325; -. [O43236-6]
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 SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division;
KW Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Differentiation; Direct protein sequencing; Flagellum; GTP-binding;
KW Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Spermatogenesis; Synapse; Ubl conjugation.
FT CHAIN 1..478
FT /note="Septin-4"
FT /id="PRO_0000173519"
FT DOMAIN 141..414
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..158
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 208..211
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 289..292
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 428..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 447..478
FT /evidence="ECO:0000255"
FT COMPBIAS 16..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 151..158
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UH03"
FT BINDING 185
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UH03"
FT BINDING 290..298
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UH03"
FT BINDING 348
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UH03"
FT BINDING 363
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UH03"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28661"
FT MOD_RES 434
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P28661"
FT VAR_SEQ 1..478
FT /note="MDRSLGWQGNSVPEDRTEAGIKRFLEDTTDDGELSKFVKDFSGNASCHPPEA
FT KTWASRPQVPEPRPQAPDLYDDDLEFRPPSRPQSSDNQQYFCAPAPLSPSARPRSPWGK
FT LDPYDSSEDDKEYVGFATLPNQVHRKSVKKGFDFTLMVAGESGLGKSTLVNSLFLTDLY
FT RDRKLLGAEERIMQTVEITKHAVDIEEKGVRLRLTIVDTPGFGDAVNNTECWKPVAEYI
FT DQQFEQYFRDESGLNRKNIQDNRVHCCLYFISPFGHGLRPLDVEFMKALHQRVNIVPIL
FT AKADTLTPPEVDHKKRKIREEIEHFGIKIYQFPDCDSDEDEDFKLQDQALKESIPFAVI
FT GSNTVVEARGRRVRGRLYPWGIVEVENPGHCDFVKLRTMLVRTHMQDLKDVTRETHYEN
FT YRAQCIQSMTRLVVKERNRNKLTRESGTDFPIPAVPPGTDPETEKLIREKDEELRRMQE
FT MLHKIQKQMKENY -> MVKTNKPGAKVAVSAQRGSEVTTNTSPQQGHGYVLASSHRSA
FT AVSLNPSHRRSEAAHPTTPHSASDYPRSVSLQSGPGHYAVPTPRGPETGPRTESSRHSS
FT PHLKSQKTQTLASHASSRQWKVSPPREEAARRGSESKSGREVGHHASSIPDAKSTHQLS
FT FQDQKNNLQSQILEDDPPSKVQNPQGVRVPRRILSYPKDEAVQTEPIQRITTTSEIRSP
FT RSPSLLEHGSSCVSADYQTAQRRVPVEESETGPYGPIPSKPKALYRNMNLDSLLKLSVL
FT KDSDGVHRVSARVDPESLHKYSAYPETKPSAKVLVSSQVESNVRTPIRGNSEVGRRVTI
FT SPGVQSVEPTHHVTVPSVSEGSHKSSMFVTPEPIYKQQTQKPPEITYMSQGPTPRYPEL
FT SQKPSIHAELELTPRPLPPRSLPRYGPDSSWWPLLNPEVETPQSQLTTPDFEPKCSPSL
FT DLLLSGFKIDSSPFCEDLKFQREKASLSPPSPPKEFPSWAPLSEVPQTPKHTCKQPIQR
FT FTAFFLDVSEEMYNRVIWWLKGLCFSLLWAHCGSLGDGRTGEEWHLCIYRAGSFRR
FT (in isoform 8)"
FT /id="VSP_060788"
FT VAR_SEQ 1..147
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038302"
FT VAR_SEQ 1..20
FT /note="MDRSLGWQGNSVPEDRTEAG -> M (in isoform 2 and isoform
FT ARTS)"
FT /evidence="ECO:0000303|PubMed:11146656,
FT ECO:0000303|PubMed:11167005, ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_006050"
FT VAR_SEQ 1..20
FT /note="MDRSLGWQGNSVPEDRTEAG -> MPGFYSVMTDEE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038303"
FT VAR_SEQ 1..20
FT /note="MDRSLGWQGNSVPEDRTEAG -> MRSSPALFSSRAAPQKPRKEGSQAAGLL
FT VFSDSLE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038304"
FT VAR_SEQ 1..20
FT /note="MDRSLGWQGNSVPEDRTEAG -> MVKTNKPGAKVAVSAQRGSEVTTNTSPQ
FT QGHGYVLASSHRSAAVSLNPSHRRSEAAHPTTPHSASDYPRSVSLQSGPGHYAVPTPRG
FT PETGPRTESSRHSSPHLKSQKTQTLASHASSRQWKVSPPREEAARRGSESKSGREVGHH
FT ASSIPDAKSTHQLSFQDQKNNLQSQILEDDPPSKVQNPQGVRVPRRILSYPKDEAVQTE
FT PIQRITTTSEIRSPRSPSLLEHGSSCVSADYQTAQRRVPVEESETGPYGPIPSKPKALY
FT RNMNLDSLLKLSVLKDSDGVHRVSARVDPESLHKYSAYPETKPSAKVLVSSQVESNVRT
FT PIRGNSEVGRRVTISPGVQSVEPTHHVTVPSVSEGSHKSSMFVTPEPIYKQQTQKPPEI
FT TYMSQGPTPRYPELSQKPSIHAELELTPRPLPPRSLPRYGPDSSWWPLLNPEVETPQSQ
FT LTTPDFEPKCSPSLDLLLSGFKIDSSPFCEDLKFQREKASLSPPSPPKEFPSWAPLSEV
FT PQTPKHTCKQPIQRFTAFFLDVSEEMYNRVIWWLKDEE (in isoform 7)"
FT /id="VSP_060789"
FT VAR_SEQ 267..293
FT /note="LRPLDVEFMKALHQRVNIVPILAKADT -> YGPSLRLLAPPGAVKGTGQEH
FT QGQGCH (in isoform ARTS)"
FT /evidence="ECO:0000303|PubMed:11146656"
FT /id="VSP_038305"
FT VAR_SEQ 294..478
FT /note="Missing (in isoform ARTS)"
FT /evidence="ECO:0000303|PubMed:11146656"
FT /id="VSP_038306"
FT VARIANT 311
FT /note="E -> V (in dbSNP:rs17741424)"
FT /id="VAR_051935"
FT CONFLICT 156
FT /note="G -> D (in Ref. 7; BAG37789)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="K -> E (in Ref. 7; BAG63517)"
FT /evidence="ECO:0000305"
FT HELIX 449..476
FT /evidence="ECO:0007829|PDB:6WB3"
FT MUTAGEN O43236-6:156..158
FT /note="LLG->ENP: Loss of TGF-beta-induced apoptosis. No
FT translocation to the nucleus following TGF-beta treatment.
FT Loss of XIAP-binding."
FT /evidence="ECO:0000269|PubMed:11146656,
FT ECO:0000269|PubMed:15029247"
FT VARIANT O43236-8:88
FT /note="P -> T (in dbSNP:rs8071623)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_083877"
FT CONFLICT O43236-8:187
FT /note="V -> A (in Ref. 8)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 478 AA; 55098 MW; 2F08D3611EF6523D CRC64;
MDRSLGWQGN SVPEDRTEAG IKRFLEDTTD DGELSKFVKD FSGNASCHPP EAKTWASRPQ
VPEPRPQAPD LYDDDLEFRP PSRPQSSDNQ QYFCAPAPLS PSARPRSPWG KLDPYDSSED
DKEYVGFATL PNQVHRKSVK KGFDFTLMVA GESGLGKSTL VNSLFLTDLY RDRKLLGAEE
RIMQTVEITK HAVDIEEKGV RLRLTIVDTP GFGDAVNNTE CWKPVAEYID QQFEQYFRDE
SGLNRKNIQD NRVHCCLYFI SPFGHGLRPL DVEFMKALHQ RVNIVPILAK ADTLTPPEVD
HKKRKIREEI EHFGIKIYQF PDCDSDEDED FKLQDQALKE SIPFAVIGSN TVVEARGRRV
RGRLYPWGIV EVENPGHCDF VKLRTMLVRT HMQDLKDVTR ETHYENYRAQ CIQSMTRLVV
KERNRNKLTR ESGTDFPIPA VPPGTDPETE KLIREKDEEL RRMQEMLHKI QKQMKENY
