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Septin-2 (Neural precursor cell expressed developmentally down-regulated protein 5) (NEDD-5)

 SEPT2_MOUSE             Reviewed;         361 AA.
P42208; B2RRZ2; Q3U9Y5;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
23-MAY-2018, entry version 173.
RecName: Full=Septin-2;
AltName: Full=Neural precursor cell expressed developmentally down-regulated protein 5;
Short=NEDD-5;
Name=Sept2; Synonyms=Nedd-5, Nedd5;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF GLY-47;
SER-51 AND GLN-125.
TISSUE=Neural tube;
PubMed=9203580; DOI=10.1101/gad.11.12.1535;
Kinoshita M., Kumar S., Noda M.;
"Nedd5, a mammalian septin, is a novel cytoskeletal component
interacting with actin-based structures.";
Genes Dev. 11:1535-1547(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Bone marrow, and Placenta;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
[5]
PROTEIN SEQUENCE OF 51-66; 97-112 AND 117-128, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Brain, and Hippocampus;
Lubec G., Klug S., Yang J.W., Zigmond M.;
Submitted (JUL-2007) to UniProtKB.
[6]
INTERACTION WITH SEPT5 AND SEPT7, LACK OF INTERACTION WITH SEPT4, AND
DEVELOPMENTAL STAGE.
PubMed=11739749; DOI=10.1128/MCB.22.1.378-387.2002;
Peng X.-R., Jia Z., Zhang Y., Ware J., Trimble W.S.;
"The septin CDCrel-1 is dispensable for normal development and
neurotransmitter release.";
Mol. Cell. Biol. 22:378-387(2002).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-17, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18630941; DOI=10.1021/pr800223m;
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
"Specific phosphopeptide enrichment with immobilized titanium ion
affinity chromatography adsorbent for phosphoproteome analysis.";
J. Proteome Res. 7:3957-3967(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20558667; DOI=10.1126/science.1191054;
Hu Q., Milenkovic L., Jin H., Scott M.P., Nachury M.V.,
Spiliotis E.T., Nelson W.J.;
"A septin diffusion barrier at the base of the primary cilium
maintains ciliary membrane protein distribution.";
Science 329:436-439(2010).
[15]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=22179047; DOI=10.1038/ncb2410;
Chih B., Liu P., Chinn Y., Chalouni C., Komuves L.G., Hass P.E.,
Sandoval W., Peterson A.S.;
"A ciliopathy complex at the transition zone protects the cilia as a
privileged membrane domain.";
Nat. Cell Biol. 14:61-72(2012).
[16]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 33-306 IN COMPLEX WITH
GPPNHP, AND MUTAGENESIS OF SER-46 AND THR-78.
PubMed=19805342; DOI=10.1073/pnas.0902858106;
Sirajuddin M., Farkasovsky M., Zent E., Wittinghofer A.;
"GTP-induced conformational changes in septins and implications for
function.";
Proc. Natl. Acad. Sci. U.S.A. 106:16592-16597(2009).
-!- FUNCTION: Filament-forming cytoskeletal GTPase. Forms a
filamentous structure with SEPT12, SEPT6, SEPT2 and probably SEPT4
at the sperm annulus which is required for the structural
integrity and motility of the sperm tail during postmeiotic
differentiation (By similarity). Required for normal organization
of the actin cytoskeleton. Plays a role in the biogenesis of
polarized columnar-shaped epithelium by maintaining
polyglutamylated microtubules, thus facilitating efficient vesicle
transport, and by impeding MAP4 binding to tubulin. Required for
the progression through mitosis. Forms a scaffold at the midplane
of the mitotic splindle required to maintain CENPE localization at
kinetochores and consequently chromosome congression. During
anaphase, may be required for chromosome segregation and spindle
elongation. Plays a role in ciliogenesis and collective cell
movements (By similarity). In cilia, required for the integrity of
the diffusion barrier at the base of the primary cilium that
prevents diffusion of transmembrane proteins between the cilia and
plasma membranes: probably acts by regulating the assembly of the
tectonic-like complex (also named B9 complex) by localizing
TMEM231 protein. {ECO:0000250, ECO:0000250|UniProtKB:Q15019,
ECO:0000269|PubMed:20558667, ECO:0000269|PubMed:22179047,
ECO:0000269|PubMed:9203580}.
-!- SUBUNIT: Septins polymerize into heterooligomeric protein
complexes that form filaments, and associate with cellular
membranes, actin filaments and microtubules (By similarity).
GTPase activity is required for filament formation (By
similarity). Septin filaments are assembled from asymmetrical
heterotrimers, composed of SEPT2, SEPT6 and SEPT7 that associate
head-to-head to form a hexameric unit (By similarity). Interaction
between SEPT2 and SEPT7 seems indirect (By similarity). Interacts
also with SEPT9 and SEPT5 (PubMed:11739749). Interaction with
SEPT4 not detected (PubMed:11739749). Component of a septin core
octomeric complex consisting of SEPT12, SEPT7, SEPT6 and SEPT2 or
SEPT4 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 (By similarity). Interacts with MAP4
(By similarity). Interacts with DZIP1L (By similarity).
{ECO:0000250|UniProtKB:Q15019, ECO:0000269|PubMed:11739749}.
-!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton.
Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Chromosome,
centromere, kinetochore {ECO:0000250}. Cleavage furrow
{ECO:0000250}. Midbody {ECO:0000250}. Cytoplasm, cell cortex
{ECO:0000250}. Cell projection, cilium membrane. Cell projection,
cilium, flagellum {ECO:0000250|UniProtKB:Q15019}. Note=In
metaphase cells, localized within the microtubule spindle. At the
metaphase plate, in close apposition to the kinetochores of the
congressed chromosomes. In cells undergoing cytokinesis, localized
to the midbody, the ingressing cleavage furrow, and the central
spindle (By similarity). In interphase and postmitotic cells,
localised to fibrous or granular structures, depending on the
growth state of the cell. Localizes at the base of the cilia near
the morphological distinction between the cilia and plasma
membranes. Found in the sperm annulus. {ECO:0000250,
ECO:0000250|UniProtKB:Q15019}.
-!- TISSUE SPECIFICITY: Widely expressed.
-!- DEVELOPMENTAL STAGE: Expressed at 17 dpc in the brain with levels
remaining relatively stable up to adulthood (at protein level).
{ECO:0000269|PubMed:11739749}.
-!- MISCELLANEOUS: Coordinated expression with SEPT6 and SEPT7.
{ECO:0000250}.
-!- 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; D49382; BAA08380.1; -; mRNA.
EMBL; AK028072; BAC25737.1; -; mRNA.
EMBL; AK146616; BAE27305.1; -; mRNA.
EMBL; AK151591; BAE30531.1; -; mRNA.
EMBL; AK171331; BAE42396.1; -; mRNA.
EMBL; CH466520; EDL39946.1; -; Genomic_DNA.
EMBL; CH466520; EDL39948.1; -; Genomic_DNA.
EMBL; BC138636; AAI38637.1; -; mRNA.
EMBL; BC138637; AAI38638.1; -; mRNA.
CCDS; CCDS15190.1; -.
RefSeq; NP_001153189.1; NM_001159717.1.
RefSeq; NP_001153190.1; NM_001159718.1.
RefSeq; NP_001153191.1; NM_001159719.1.
RefSeq; NP_035021.1; NM_010891.2.
RefSeq; XP_006529304.1; XM_006529241.2.
RefSeq; XP_006529305.1; XM_006529242.1.
UniGene; Mm.428652; -.
PDB; 3FTQ; X-ray; 2.90 A; A/B/C/D=33-306.
PDBsum; 3FTQ; -.
ProteinModelPortal; P42208; -.
SMR; P42208; -.
BioGrid; 201724; 19.
DIP; DIP-32438N; -.
IntAct; P42208; 21.
MINT; P42208; -.
STRING; 10090.ENSMUSP00000027495; -.
iPTMnet; P42208; -.
PhosphoSitePlus; P42208; -.
SwissPalm; P42208; -.
REPRODUCTION-2DPAGE; IPI00114945; -.
REPRODUCTION-2DPAGE; P42208; -.
EPD; P42208; -.
MaxQB; P42208; -.
PaxDb; P42208; -.
PeptideAtlas; P42208; -.
PRIDE; P42208; -.
Ensembl; ENSMUST00000027495; ENSMUSP00000027495; ENSMUSG00000026276.
Ensembl; ENSMUST00000168776; ENSMUSP00000132850; ENSMUSG00000026276.
Ensembl; ENSMUST00000179353; ENSMUSP00000136366; ENSMUSG00000026276.
GeneID; 18000; -.
KEGG; mmu:18000; -.
UCSC; uc007cea.2; mouse.
CTD; 4735; -.
MGI; MGI:97298; Sept2.
eggNOG; KOG2655; Eukaryota.
eggNOG; COG5019; LUCA.
GeneTree; ENSGT00910000144020; -.
HOGENOM; HOG000233586; -.
HOVERGEN; HBG065093; -.
InParanoid; P42208; -.
KO; K16942; -.
OMA; QWEQHLI; -.
OrthoDB; EOG091G07TS; -.
PhylomeDB; P42208; -.
TreeFam; TF101079; -.
Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
ChiTaRS; Sept2; mouse.
EvolutionaryTrace; P42208; -.
PRO; PR:P42208; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000026276; -.
CleanEx; MM_SEPT2; -.
ExpressionAtlas; P42208; baseline and differential.
Genevisible; P42208; MM.
GO; GO:0015629; C:actin cytoskeleton; TAS:MGI.
GO; GO:0005826; C:actomyosin contractile ring; NAS:UniProtKB.
GO; GO:0005930; C:axoneme; ISO:MGI.
GO; GO:0005938; C:cell cortex; TAS:MGI.
GO; GO:0042995; C:cell projection; IDA:MGI.
GO; GO:0009986; C:cell surface; IDA:MGI.
GO; GO:0060170; C:ciliary membrane; IDA:UniProtKB.
GO; GO:0035869; C:ciliary transition zone; IDA:MGI.
GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0015630; C:microtubule cytoskeleton; TAS:MGI.
GO; GO:0030496; C:midbody; TAS:MGI.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0097730; C:non-motile cilium; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0032391; C:photoreceptor connecting cilium; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0031105; C:septin complex; ISO:MGI.
GO; GO:0097227; C:sperm annulus; ISO:MGI.
GO; GO:0005876; C:spindle microtubule; TAS:MGI.
GO; GO:0045202; C:synapse; IDA:MGI.
GO; GO:0045296; F:cadherin binding; ISO:MGI.
GO; GO:0030234; F:enzyme regulator activity; IDA:MGI.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; NAS:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0032947; F:protein-containing complex scaffold activity; IDA:MGI.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; NAS:UniProtKB.
GO; GO:0051258; P:protein polymerization; TAS:MGI.
GO; GO:0002036; P:regulation of L-glutamate import across plasma membrane; IDA:MGI.
GO; GO:0032880; P:regulation of protein localization; IDA:MGI.
GO; GO:0007224; P:smoothened signaling pathway; IMP:UniProtKB.
GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
CDD; cd01850; CDC_Septin; 1.
InterPro; IPR030379; G_SEPTIN_dom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR016491; Septin.
InterPro; IPR008113; Septin2.
Pfam; PF00735; Septin; 1.
PIRSF; PIRSF006698; Septin; 1.
PRINTS; PR01740; SEPTIN2.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS51719; G_SEPTIN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Cell cycle; Cell division; Cell membrane;
Cell projection; Centromere; Chromosome; Cilium; Complete proteome;
Cytoplasm; Cytoskeleton; Differentiation; Direct protein sequencing;
Flagellum; GTP-binding; Kinetochore; Membrane; Mitosis;
Nucleotide-binding; Phosphoprotein; Reference proteome;
Spermatogenesis.
CHAIN 1 361 Septin-2.
/FTId=PRO_0000173516.
DOMAIN 34 306 Septin-type G. {ECO:0000255|PROSITE-
ProRule:PRU01056}.
NP_BIND 44 52 GTP.
NP_BIND 183 186 GTP.
REGION 44 51 G1 motif. {ECO:0000255|PROSITE-
ProRule:PRU01056}.
REGION 101 104 G3 motif. {ECO:0000255|PROSITE-
ProRule:PRU01056}.
REGION 182 185 G4 motif. {ECO:0000255|PROSITE-
ProRule:PRU01056}.
REGION 260 270 Important for dimerization.
{ECO:0000250}.
BINDING 78 78 GTP.
BINDING 104 104 GTP; via amide nitrogen.
BINDING 241 241 GTP; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 256 256 GTP.
BINDING 258 258 GTP. {ECO:0000250}.
SITE 156 156 Important for dimerization.
{ECO:0000250}.
MOD_RES 17 17 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 190 190 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q15019}.
MOD_RES 211 211 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q15019}.
MOD_RES 218 218 Phosphoserine.
{ECO:0000244|PubMed:16452087,
ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:18630941,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MUTAGEN 46 46 S->D: Loss of GTP-binding.
{ECO:0000269|PubMed:19805342}.
MUTAGEN 47 47 G->V: Loss of GTP-binding activity.
{ECO:0000269|PubMed:9203580}.
MUTAGEN 51 51 S->N: Loss of GTP-binding activity.
{ECO:0000269|PubMed:9203580}.
MUTAGEN 78 78 T->G: Reduces affinity for GTP 20-fold.
{ECO:0000269|PubMed:19805342}.
MUTAGEN 125 125 Q->L: Loss of GTP-binding activity.
{ECO:0000269|PubMed:9203580}.
STRAND 35 45 {ECO:0000244|PDB:3FTQ}.
HELIX 50 55 {ECO:0000244|PDB:3FTQ}.
STRAND 59 61 {ECO:0000244|PDB:3FTQ}.
STRAND 82 90 {ECO:0000244|PDB:3FTQ}.
STRAND 93 101 {ECO:0000244|PDB:3FTQ}.
STRAND 105 109 {ECO:0000244|PDB:3FTQ}.
HELIX 111 133 {ECO:0000244|PDB:3FTQ}.
STRAND 148 153 {ECO:0000244|PDB:3FTQ}.
STRAND 157 160 {ECO:0000244|PDB:3FTQ}.
HELIX 162 171 {ECO:0000244|PDB:3FTQ}.
TURN 172 174 {ECO:0000244|PDB:3FTQ}.
STRAND 177 182 {ECO:0000244|PDB:3FTQ}.
HELIX 184 186 {ECO:0000244|PDB:3FTQ}.
HELIX 189 205 {ECO:0000244|PDB:3FTQ}.
HELIX 222 233 {ECO:0000244|PDB:3FTQ}.
STRAND 236 238 {ECO:0000244|PDB:3FTQ}.
STRAND 245 247 {ECO:0000244|PDB:3FTQ}.
STRAND 249 258 {ECO:0000244|PDB:3FTQ}.
STRAND 261 264 {ECO:0000244|PDB:3FTQ}.
TURN 268 270 {ECO:0000244|PDB:3FTQ}.
HELIX 273 293 {ECO:0000244|PDB:3FTQ}.
HELIX 295 303 {ECO:0000244|PDB:3FTQ}.
SEQUENCE 361 AA; 41526 MW; C4BFFB3F1815E081 CRC64;
MSKQQPTQFI NPETPGYVGF ANLPNQVHRK SVKKGFEFTL MVVGESGLGK STLINSLFLT
DLYPERIIPG AAEKIERTVQ IEASTVEIEE RGVKLRLTVV DTPGYGDAIN CRDCFKTIIS
YIDEQFERYL HDESGLNRRH IIDNRVHCCF YFISPFGHGL KPLDVAFMKA IHNKVNIVPV
IAKADTLTLK ERERLKKRIL DEIEEHSIKI YHLPDAESDE DEDFKEQTRL LKASIPFSVV
GSNQLIEAKG KKVRGRLYPW GVVEVENPEH NDFLKLRTML ITHMQDLQEV TQDLHYENFR
SERLKRGGRK VENEDMNKDQ ILLEKEAELR RMQEMIARMQ AQMQMQMQGG DSDSGALGQH
V


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EIAAB11922 Developmentally-regulated GTP-binding protein 1,Drg,Drg1,DRG-1,Mouse,Mus musculus,Nedd3,NEDD-3,Nedd-3,Neural precursor cell expressed developmentally down-regulated protein 3
EIAAB11921 Developmentally-regulated GTP-binding protein 1,DRG1,DRG-1,Homo sapiens,Human,NEDD3,NEDD-3,Neural precursor cell expressed developmentally down-regulated protein 3
EIAAB05382 Casp2,CASP-2,Caspase-2,Ich1,Mouse,Mus musculus,Nedd2,NEDD-2,Nedd-2,Neural precursor cell expressed developmentally down-regulated protein 2,Protease ICH-1
EIAAB34914 60S ribosomal protein L10a,CSA-19,Mouse,Mus musculus,Nedd6,NEDD-6,Nedd-6,Neural precursor cell expressed developmentally down-regulated protein 6,Rpl10a
EIAAB26860 Mouse,Mus musculus,Nedd1,NEDD-1,Nedd-1,Neural precursor cell expressed developmentally down-regulated protein 1,Protein NEDD1
EIAAB26870 Mouse,Mus musculus,NEDD8,Nedd8,NEDD-8,Nedd-8,Neddylin,Neural precursor cell expressed developmentally down-regulated protein 8,Ubiquitin-like protein Nedd8
EIAAB26864 E3 ubiquitin-protein ligase NEDD4,Kiaa0093,Mouse,Mus musculus,Nedd4,NEDD-4,Nedd-4,Nedd4-1,Nedd4a,Neural precursor cell expressed developmentally down-regulated protein 4
EIAAB34913 60S ribosomal protein L10a,CSA-19,Homo sapiens,Human,NEDD6,NEDD-6,Neural precursor cell expressed developmentally down-regulated protein 6,RPL10A
EIAAB05383 CASP2,CASP-2,Caspase-2,Homo sapiens,Human,ICH1,NEDD2,NEDD-2,Neural precursor cell expressed developmentally down-regulated protein 2,Protease ICH-1
EIAAB05377 Casl,CAS-L,CRK-associated substrate-related protein,Enhancer of filamentation 1,mEF1,Mouse,Mus musculus,Nedd9,NEDD-9,Neural precursor cell expressed developmentally down-regulated protein 9,p105
EIAAB26861 Bos taurus,Bovine,NEDD1,NEDD-1,Neural precursor cell expressed developmentally down-regulated protein 1,Protein NEDD1
EIAAB26862 Homo sapiens,Human,NEDD1,NEDD-1,Neural precursor cell expressed developmentally down-regulated protein 1,Protein NEDD1
EIAAB26868 Homo sapiens,Human,NEDD8,NEDD8,NEDD-8,Neddylin,Neural precursor cell expressed developmentally down-regulated protein 8,Ubiquitin-like protein Nedd8
EIAAB26863 Cell proliferation-inducing gene 53 protein,E3 ubiquitin-protein ligase NEDD4,Homo sapiens,Human,KIAA0093,NEDD4,NEDD-4,NEDD4-1,Neural precursor cell expressed developmentally down-regulated protein 4,
20-272-191628 Caspase 2 - Mouse monoclonal [3G63] to Caspase 2; EC 3.4.22.55; CASP-2; ICH-1 protease; NEDD2 protein; Neural precursor cell expressed developmentally down-regulated protein 2; NEDD-2 Monoclonal 0.1 mg
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CG48 Recombinant Human Neural precursor cell expressed developmentally down-regulated protein 8_NEDD8 500 ug
CG48 Recombinant Human Neural precursor cell expressed developmentally down-regulated protein 8_NEDD8 50 ug
CG48 Recombinant Human Neural precursor cell expressed developmentally down-regulated protein 8_NEDD8 10 ug
CG48 Recombinant Human Neural precursor cell expressed developmentally down-regulated protein 8_NEDD8 1 mg
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