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Septin-4 (Apoptosis-related protein in the TGF-beta signaling pathway) (ARTS) (Bradeion beta) (Brain protein H5) (CE5B3 beta) (Cell division control-related protein 2) (hCDCREL-2) (Cerebral protein 7) (Peanut-like protein 2)

 SEPT4_HUMAN             Reviewed;         478 AA.
O43236; B2RD42; B3KSX9; B4DXC6; B4DXV5; Q6IAP3; Q9H315; Q9UM58;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
13-NOV-2019, entry version 178.
RecName: Full=Septin-4;
AltName: Full=Apoptosis-related protein in the TGF-beta signaling pathway;
Short=ARTS;
AltName: Full=Bradeion beta;
AltName: Full=Brain protein H5;
AltName: Full=CE5B3 beta;
AltName: Full=Cell division control-related protein 2;
Short=hCDCREL-2;
AltName: Full=Cerebral protein 7;
AltName: Full=Peanut-like protein 2;
Name=SEPTIN4 {ECO:0000312|HGNC:HGNC:9165};
Synonyms=ARTS, PNUTL2, SEP4, SEPT4; ORFNames=hucep-7;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
SPECIFICITY.
PubMed=9889007; DOI=10.1006/geno.1998.5612;
Paavola P., Horelli-Kuitunen N., Palotie A., Peltonen L.;
"Characterization of a novel gene, PNUTL2, on human chromosome 17q22-
q23 and its exclusion as the Meckel syndrome gene.";
Genomics 55:122-125(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
TISSUE=Brain, and Fetal brain;
PubMed=11167005; DOI=10.1016/s0378-1119(00)00527-8;
Zieger B., Tran H., Hainmann I., Wunderle D., Zgaga-Griesz A.,
Blaeser S., Ware J.;
"Characterization and expression analysis of two human septin genes,
PNUTL1 and PNUTL2.";
Gene 261:197-203(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ARTS), FUNCTION, TISSUE
SPECIFICITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
156-GLY--SER-158.
TISSUE=Fetal brain;
PubMed=11146656; DOI=10.1038/35046566;
Larisch S., Yi Y., Lotan R., Kerner H., Eimerl S., Parks W.T.,
Yossi G., Reffey S.B., de Caestecker M.P., Danielpour D.,
Book-Melamed N., Timberg R., Duckett C., Lechleider R.J., Steller H.,
Orly J., Kim S.-J., Roberts A.B.;
"A novel mitochondrial septin-like protein, ARTS, mediates apoptosis
dependent on its P-loop motif.";
Nat. Cell Biol. 2:915-921(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=11511094; DOI=10.1006/bbrc.2001.5413;
Tanaka M., Tanaka T., Kijima H., Itoh J., Matsuda T., Hori S.,
Yamamoto M.;
"Characterization of tissue- and cell-type-specific expression of a
novel human septin family gene, Bradeion.";
Biochem. Biophys. Res. Commun. 286:547-553(2001).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
Yoshimoto M., Yazaki M., Matsumoto K., Takayama K.;
"Molecular cloning of a new GTP binding protein from human brain.";
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Zha D., Hu G.;
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 5).
TISSUE=Amygdala, Brain cortex, Subthalamic nucleus, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Hippocampus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
FUNCTION, INTERACTION WITH SEPTIN8, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=15116257; DOI=10.1267/THRO04050959;
Blaeser S., Horn J., Wuermell P., Bauer H., Struempell S., Nurden P.,
Pagenstecher A., Busse A., Wunderle D., Hainmann I., Zieger B.;
"The novel human platelet septin SEPT8 is an interaction partner of
SEPT4.";
Thromb. Haemost. 91:959-966(2004).
[12]
PROTEIN SEQUENCE OF 141-157 AND 282-290, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Fetal brain;
Lubec G., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[13]
FUNCTION.
PubMed=15837787; DOI=10.1074/jbc.m501955200;
Lotan R., Rotem A., Gonen H., Finberg J.P.M., Kemeny S., Steller H.,
Ciechanover A., Larisch S.;
"Regulation of the proapoptotic ARTS protein by ubiquitin-mediated
degradation.";
J. Biol. Chem. 280:25802-25810(2005).
[14]
TISSUE SPECIFICITY.
PubMed=15915442; DOI=10.1002/path.1789;
Hall P.A., Jung K., Hillan K.J., Russell S.E.H.;
"Expression profiling the human septin gene family.";
J. Pathol. 206:269-278(2005).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117; SER-118 AND
SER-325, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
INTERACTION WITH SEPTIN9 HNA VARIANTS.
PubMed=17546647; DOI=10.1002/humu.20554;
Sudo K., Ito H., Iwamoto I., Morishita R., Asano T., Nagata K.;
"SEPT9 sequence alternations causing hereditary neuralgic amyotrophy
are associated with altered interactions with SEPT4/SEPT11 and
resistance to Rho/Rhotekin-signaling.";
Hum. Mutat. 28:1005-1013(2007).
[18]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH XIAP.
PubMed=15029247; DOI=10.1038/sj.emboj.7600155;
Gottfried Y., Rotem A., Lotan R., Steller H., Larisch S.;
"The mitochondrial ARTS protein promotes apoptosis through targeting
XIAP.";
EMBO J. 23:1627-1635(2004).
[19]
FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=25588830; DOI=10.1242/jcs.158998;
Kuo Y.C., Shen Y.R., Chen H.I., Lin Y.H., Wang Y.Y., Chen Y.R.,
Wang C.Y., Kuo P.L.;
"SEPT12 orchestrates the formation of mammalian sperm annulus by
organizing core octomeric complexes with other SEPT proteins.";
J. Cell Sci. 128:923-934(2015).
-!- FUNCTION: Filament-forming cytoskeletal GTPase (By similarity).
May play a role in cytokinesis (Potential). Forms a filamentous
structure with SEPTIN12, SEPTIN6, SEPTIN2 and probably SEPTIN4 at
the sperm annulus which is required for the structural integrity
and motility of the sperm tail during postmeiotic differentiation
(PubMed:25588830). May play a role in platelet secretion. Isoform
ARTS, but not the other isoforms, is required for the induction of
cell death mediated by TGF-beta and by other apoptotic stimuli.
{ECO:0000250, ECO:0000269|PubMed:11146656,
ECO:0000269|PubMed:15029247, ECO:0000269|PubMed:15116257,
ECO:0000269|PubMed:15837787, ECO:0000269|PubMed:9889007,
ECO:0000305, ECO:0000305|PubMed:25588830}.
-!- SUBUNIT: Septins polymerize into heterooligomeric protein
complexes that form filaments, and can associate with cellular
membranes, actin filaments and microtubules. GTPase activity is
required for filament formation (By similarity). Interacts with
SEPTIN8. In a mesenchymal cell line, interacts with SEPTIN9
isoform 2 variants HNA Trp-106 and Phe-111, but not the wild type
SEPTIN9. Component of a septin core octomeric complex consisting
of SEPTIN12, SEPTIN7, SEPTIN6 and SEPTIN2 or SEPTIN4 in the order
12-7-6-2-2-6-7-12 or 12-7-6-4-4-6-7-12 and located in the sperm
annulus. Isoform ARTS, but no other isoforms, interacts with XIAP
after the induction of apoptosis. {ECO:0000250,
ECO:0000269|PubMed:15029247, ECO:0000269|PubMed:15116257,
ECO:0000269|PubMed:17546647, ECO:0000269|PubMed:25588830}.
-!- INTERACTION:
Q8IYM1:SEPTIN12; NbExp=5; IntAct=EBI-1047513, EBI-2585067;
Q8IUQ4:SIAH1; NbExp=2; IntAct=EBI-4372019, EBI-747107;
P98170:XIAP; NbExp=4; IntAct=EBI-4372019, EBI-517127;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm,
cytoskeleton {ECO:0000250}. Cell projection, cilium, flagellum
{ECO:0000269|PubMed:25588830}. Note=In platelets, found in areas
surrounding alpha-granules. Found in the sperm annulus
(PubMed:25588830). {ECO:0000269|PubMed:11146656,
ECO:0000269|PubMed:15029247, ECO:0000269|PubMed:15116257,
ECO:0000269|PubMed:25588830}.
-!- SUBCELLULAR LOCATION: Isoform ARTS: Mitochondrion. Nucleus.
Note=While predominantly localized in the mitochondria under
resting conditions, isoform ARTS translocates into the nucleus
after TGF-beta treatment and apoptosis induction.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1; Synonyms=PNUTL2, PNUTL2a, H5/CDCrel2, SEPT4_i1;
IsoId=O43236-1; Sequence=Displayed;
Name=2; Synonyms=PNUTL2b;
IsoId=O43236-2; Sequence=VSP_006050;
Name=3;
IsoId=O43236-3; Sequence=VSP_038303;
Note=No experimental confirmation available.;
Name=4;
IsoId=O43236-4; Sequence=VSP_038304;
Note=No experimental confirmation available.;
Name=5;
IsoId=O43236-5; Sequence=VSP_038302;
Note=No experimental confirmation available.;
Name=ARTS; Synonyms=SEPT4_i2;
IsoId=O43236-6; Sequence=VSP_006050, VSP_038305, VSP_038306;
Note=May be defective in GTP-binding.;
-!- TISSUE SPECIFICITY: Widely expressed in adult and fetal tissues
with highest expression in adult brain (at protein level), heart,
liver and adrenal gland and fetal heart, kidney, liver and lung.
Also expressed in colorectal cancers and malignant melanomas.
Expressed in platelets. {ECO:0000269|PubMed:11146656,
ECO:0000269|PubMed:11167005, ECO:0000269|PubMed:11511094,
ECO:0000269|PubMed:15116257, ECO:0000269|PubMed:15915442,
ECO:0000269|PubMed:9889007}.
-!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-
like GTPase superfamily. Septin GTPase family.
{ECO:0000255|PROSITE-ProRule:PRU01056}.
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EMBL; AF073312; AAC25673.1; -; mRNA.
EMBL; U88829; AAD00653.1; -; mRNA.
EMBL; U88870; AAD00657.1; -; mRNA.
EMBL; AF176379; AAG45673.1; -; mRNA.
EMBL; AB008753; BAB70695.1; -; mRNA.
EMBL; D89278; BAB46922.1; -; mRNA.
EMBL; AF035811; AAB88512.1; -; mRNA.
EMBL; CR457111; CAG33392.1; -; mRNA.
EMBL; AK315396; BAG37789.1; -; mRNA.
EMBL; AK094579; BAG52891.1; -; mRNA.
EMBL; AK294094; BAG57432.1; -; mRNA.
EMBL; AK301914; BAG63338.1; -; mRNA.
EMBL; AK302146; BAG63517.1; -; mRNA.
EMBL; CH471109; EAW94440.1; -; Genomic_DNA.
EMBL; CH471109; EAW94442.1; -; Genomic_DNA.
EMBL; BC018056; AAH18056.3; -; mRNA.
CCDS; CCDS11609.1; -. [O43236-2]
CCDS; CCDS11610.1; -. [O43236-1]
CCDS; CCDS45743.1; -. [O43236-6]
CCDS; CCDS56041.1; -. [O43236-3]
CCDS; CCDS58581.1; -. [O43236-5]
CCDS; CCDS58582.1; -. [O43236-4]
RefSeq; NP_001185642.1; NM_001198713.1. [O43236-3]
RefSeq; NP_001243711.1; NM_001256782.1. [O43236-4]
RefSeq; NP_001243751.1; NM_001256822.1. [O43236-5]
RefSeq; NP_004565.1; NM_004574.4. [O43236-1]
RefSeq; NP_536340.1; NM_080415.3. [O43236-6]
RefSeq; NP_536341.1; NM_080416.3. [O43236-2]
RefSeq; XP_006722017.1; XM_006721954.2. [O43236-5]
RefSeq; XP_006722018.1; XM_006721955.2. [O43236-5]
RefSeq; XP_011523213.1; XM_011524911.1. [O43236-5]
RefSeq; XP_011523214.1; XM_011524912.1. [O43236-5]
SMR; O43236; -.
BioGrid; 111415; 20.
IntAct; O43236; 17.
MINT; O43236; -.
STRING; 9606.ENSP00000402000; -.
iPTMnet; O43236; -.
PhosphoSitePlus; O43236; -.
BioMuta; SEPT4; -.
jPOST; O43236; -.
MassIVE; O43236; -.
MaxQB; O43236; -.
PaxDb; O43236; -.
PeptideAtlas; O43236; -.
PRIDE; O43236; -.
ProteomicsDB; 48814; -. [O43236-1]
ProteomicsDB; 48815; -. [O43236-2]
ProteomicsDB; 48816; -. [O43236-3]
ProteomicsDB; 48817; -. [O43236-4]
ProteomicsDB; 48818; -. [O43236-5]
ProteomicsDB; 48819; -. [O43236-6]
DNASU; 5414; -.
Ensembl; ENST00000317256; ENSP00000321071; ENSG00000108387. [O43236-2]
Ensembl; ENST00000317268; ENSP00000321674; ENSG00000108387. [O43236-1]
Ensembl; ENST00000393086; ENSP00000376801; ENSG00000108387. [O43236-2]
Ensembl; ENST00000412945; ENSP00000414779; ENSG00000108387. [O43236-3]
Ensembl; ENST00000426861; ENSP00000402348; ENSG00000108387. [O43236-6]
Ensembl; ENST00000457347; ENSP00000402000; ENSG00000108387. [O43236-4]
Ensembl; ENST00000583114; ENSP00000463768; ENSG00000108387. [O43236-5]
GeneID; 5414; -.
UCSC; uc002iwm.4; human. [O43236-1]
CTD; 5414; -.
DisGeNET; 5414; -.
HGNC; HGNC:9165; SEPTIN4.
HPA; CAB006855; -.
HPA; HPA021587; -.
HPA; HPA022905; -.
MIM; 603696; gene.
neXtProt; NX_O43236; -.
OpenTargets; ENSG00000108387; -.
PharmGKB; PA33487; -.
eggNOG; KOG2655; Eukaryota.
eggNOG; COG5019; LUCA.
GeneTree; ENSGT00940000157152; -.
InParanoid; O43236; -.
OMA; HYENYRT; -.
OrthoDB; 845354at2759; -.
PhylomeDB; O43236; -.
TreeFam; TF101079; -.
Reactome; R-HSA-111457; Release of apoptotic factors from the mitochondria. [O43236-6]
Reactome; R-HSA-111469; SMAC, XIAP-regulated apoptotic response. [O43236-6]
ChiTaRS; SEPT4; human.
GeneWiki; SEPT4; -.
GenomeRNAi; 5414; -.
Pharos; O43236; -.
PRO; PR:O43236; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000108387; Expressed in 180 organ(s), highest expression level in corpus callosum.
ExpressionAtlas; O43236; baseline and differential.
Genevisible; O43236; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; NAS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; NAS:UniProtKB.
GO; GO:0031105; C:septin complex; IDA:UniProtKB.
GO; GO:0005940; C:septin ring; IBA:GO_Central.
GO; GO:0097227; C:sperm annulus; IDA:UniProtKB.
GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
GO; GO:0005525; F:GTP binding; IMP:CAFA.
GO; GO:0003924; F:GTPase activity; IMP:CAFA.
GO; GO:0000287; F:magnesium ion binding; IMP:CAFA.
GO; GO:0042803; F:protein homodimerization activity; IMP:CAFA.
GO; GO:0005198; F:structural molecule activity; TAS:ProtInc.
GO; GO:0006915; P:apoptotic process; NAS:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IMP:CAFA.
GO; GO:0042981; P:regulation of apoptotic process; NAS:UniProtKB.
GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
CDD; cd01850; CDC_Septin; 1.
DisProt; DP00537; -.
DisProt; DP01325; -. [O43236-6]
InterPro; IPR030379; G_SEPTIN_dom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR016491; Septin.
InterPro; IPR030643; Septin4.
PANTHER; PTHR18884:SF71; PTHR18884:SF71; 1.
Pfam; PF00735; Septin; 1.
PIRSF; PIRSF006698; Septin; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS51719; G_SEPTIN; 1.
1: Evidence at protein level;
Alternative splicing; Cell cycle; Cell division; Cell projection;
Cilium; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
Differentiation; Direct protein sequencing; Flagellum; GTP-binding;
Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Spermatogenesis.
CHAIN 1 478 Septin-4.
/FTId=PRO_0000173519.
DOMAIN 141 414 Septin-type G. {ECO:0000255|PROSITE-
ProRule:PRU01056}.
NP_BIND 151 158 GTP. {ECO:0000250}.
NP_BIND 290 298 GTP. {ECO:0000250}.
REGION 151 158 G1 motif. {ECO:0000255|PROSITE-
ProRule:PRU01056}.
REGION 208 211 G3 motif. {ECO:0000255|PROSITE-
ProRule:PRU01056}.
REGION 289 292 G4 motif. {ECO:0000255|PROSITE-
ProRule:PRU01056}.
COILED 447 478 {ECO:0000255}.
BINDING 185 185 GTP. {ECO:0000250}.
BINDING 211 211 GTP; via amide nitrogen. {ECO:0000250}.
BINDING 348 348 GTP; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 363 363 GTP. {ECO:0000250}.
MOD_RES 117 117 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 118 118 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 325 325 Phosphoserine.
{ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:24275569}.
MOD_RES 432 432 Phosphoserine.
{ECO:0000250|UniProtKB:P28661}.
MOD_RES 434 434 Phosphothreonine.
{ECO:0000250|UniProtKB:P28661}.
VAR_SEQ 1 147 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038302.
VAR_SEQ 1 20 MDRSLGWQGNSVPEDRTEAG -> M (in isoform 2
and isoform ARTS).
{ECO:0000303|PubMed:11146656,
ECO:0000303|PubMed:11167005,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_006050.
VAR_SEQ 1 20 MDRSLGWQGNSVPEDRTEAG -> MPGFYSVMTDEE (in
isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038303.
VAR_SEQ 1 20 MDRSLGWQGNSVPEDRTEAG -> MRSSPALFSSRAAPQKP
RKEGSQAAGLLVFSDSLE (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038304.
VAR_SEQ 267 293 LRPLDVEFMKALHQRVNIVPILAKADT -> YGPSLRLLAP
PGAVKGTGQEHQGQGCH (in isoform ARTS).
{ECO:0000303|PubMed:11146656}.
/FTId=VSP_038305.
VAR_SEQ 294 478 Missing (in isoform ARTS).
{ECO:0000303|PubMed:11146656}.
/FTId=VSP_038306.
VARIANT 311 311 E -> V (in dbSNP:rs17741424).
/FTId=VAR_051935.
MUTAGEN 156 158 GKS->ENP: Loss of TGF-beta-induced
apoptosis. No translocation to the
nucleus following TGF-beta treatment.
Loss of XIAP-binding.
{ECO:0000269|PubMed:11146656}.
CONFLICT 156 156 G -> D (in Ref. 7; BAG37789).
{ECO:0000305}.
CONFLICT 382 382 K -> E (in Ref. 7; BAG63517).
{ECO:0000305}.
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


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