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Nuclear distribution protein nudE-like 1 (Protein mNudE-like) (Protein Nudel) (mNudE-L)

 NDEL1_MOUSE             Reviewed;         345 AA.
Q9ERR1; Q9D0Q4; Q9EPT6;
13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
13-JUN-2006, sequence version 2.
07-NOV-2018, entry version 138.
RecName: Full=Nuclear distribution protein nudE-like 1;
AltName: Full=Protein mNudE-like;
Short=Protein Nudel;
Short=mNudE-L;
Name=Ndel1; Synonyms=Nudel;
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] (ISOFORM 1), SELF-ASSOCIATION, INTERACTION
WITH PAFAH1B1 AND DYNEIN, TISSUE SPECIFICITY, AND PHOSPHORYLATION BY
CDK5.
PubMed=11163259; DOI=10.1016/S0896-6273(00)00146-X;
Sasaki S., Shionoya A., Ishida M., Gambello M.J., Yingling J.,
Wynshaw-Boris A., Hirotsune S.;
"A LIS1/NUDEL/cytoplasmic dynein heavy chain complex in the developing
and adult nervous system.";
Neuron 28:681-696(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH PAFAH1B1,
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=Swiss Webster / NIH;
PubMed=11231056; DOI=10.1016/S0925-4773(00)00543-8;
Sweeney K.J., Prokscha A., Eichele G.;
"NudE-L, a novel Lis1-interacting protein, belongs to a family of
vertebrate coiled-coil proteins.";
Mech. Dev. 101:21-33(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; 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).
[6]
INTERACTION WITH PAFAH1B1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
AND DEVELOPMENTAL STAGE.
PubMed=11163260; DOI=10.1016/S0896-6273(00)00147-1;
Niethammer M., Smith D.S., Ayala R., Peng J., Ko J., Lee M.-S.,
Morabito M., Tsai L.-H.;
"NUDEL is a novel cdk5 substrate that associates with LIS1 and
cytoplasmic dynein.";
Neuron 28:697-711(2000).
[7]
FUNCTION, INTERACTION WITH PAFAH1B1 AND YWHAE, SUBCELLULAR LOCATION,
PHOSPHORYLATION BY CDK5, AND MUTAGENESIS OF SER-198; THR-219 AND
SER-231.
PubMed=12796778; DOI=10.1038/ng1169;
Toyo-oka K., Shionoya A., Gambello M.J., Cardoso C., Leventer R.,
Ward H.L., Ayala R., Tsai L.-H., Dobyns W., Ledbetter D.,
Hirotsune S., Wynshaw-Boris A.;
"14-3-3epsilon is important for neuronal migration by binding to
NUDEL: a molecular explanation for Miller-Dieker syndrome.";
Nat. Genet. 34:274-285(2003).
[8]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=15147871; DOI=10.1016/j.febslet.2004.04.009;
Yamaguchi N., Takanezawa Y., Koizumi H., Umezu-Goto M., Aoki J.,
Arai H.;
"Expression of NUDEL in manchette and its implication in
spermatogenesis.";
FEBS Lett. 566:71-76(2004).
[9]
INTERACTION WITH DISC1; DYNEIN; TUBULIN GAMMA AND MICROTUBULES,
SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-266 AND GLU-267.
PubMed=14962739; DOI=10.1016/j.mcn.2003.09.009;
Brandon N.J., Handford E.J., Schurov I., Rain J.-C., Pelling M.,
Duran-Jimeniz B., Camargo L.M., Oliver K.R., Beher D., Shearman M.S.,
Whiting P.J.;
"Disrupted in Schizophrenia 1 and Nudel form a neurodevelopmentally
regulated protein complex: implications for schizophrenia and other
major neurological disorders.";
Mol. Cell. Neurosci. 25:42-55(2004).
[10]
FUNCTION, INTERACTION WITH NEFH; NEFL AND PAFAH1B1, AND SUBCELLULAR
LOCATION.
PubMed=15208636; DOI=10.1038/ncb1139;
Nguyen M.-D., Shu T., Sanada K., Lariviere R.C., Tseng H.-C.,
Park S.K., Julien J.-P., Tsai L.-H.;
"A NUDEL-dependent mechanism of neurofilament assembly regulates the
integrity of CNS neurons.";
Nat. Cell Biol. 6:595-608(2004).
[11]
FUNCTION, INTERACTION WITH DYNEIN, SUBCELLULAR LOCATION, AND
DEVELOPMENTAL STAGE.
PubMed=15473966; DOI=10.1016/j.neuron.2004.09.030;
Shu T., Ayala R., Nguyen M.-D., Xie Z., Gleeson J.G., Tsai L.-H.;
"Ndel1 operates in a common pathway with LIS1 and cytoplasmic dynein
to regulate cortical neuronal positioning.";
Neuron 44:263-277(2004).
[12]
DEVELOPMENTAL STAGE.
PubMed=15473967; DOI=10.1016/j.neuron.2004.09.023;
Feng Y., Walsh C.A.;
"Mitotic spindle regulation by Nde1 controls cerebral cortical size.";
Neuron 44:279-293(2004).
[13]
FUNCTION, INTERACTION WITH KATNA1 AND KATNB1, SUBCELLULAR LOCATION,
PHOSPHORYLATION BY CDK5, AND MUTAGENESIS OF SER-198; THR-219 AND
SER-231.
PubMed=16203747; DOI=10.1093/hmg/ddi339;
Toyo-Oka K., Sasaki S., Yano Y., Mori D., Kobayashi T.,
Toyoshima Y.Y., Tokuoka S.M., Ishii S., Shimizu T., Muramatsu M.,
Hiraiwa N., Yoshiki A., Wynshaw-Boris A., Hirotsune S.;
"Recruitment of katanin p60 by phosphorylated NDEL1, an LIS1
interacting protein, is essential for mitotic cell division and
neuronal migration.";
Hum. Mol. Genet. 14:3113-3128(2005).
[14]
FUNCTION.
PubMed=16107726; DOI=10.1128/MCB.25.17.7812-7827.2005;
Sasaki S., Mori D., Toyo-oka K., Chen A., Garrett-Beal L.,
Muramatsu M., Miyagawa S., Hiraiwa N., Yoshiki A., Wynshaw-Boris A.,
Hirotsune S.;
"Complete loss of Ndel1 results in neuronal migration defects and
early embryonic lethality.";
Mol. Cell. Biol. 25:7812-7827(2005).
[15]
SUBCELLULAR LOCATION.
PubMed=15797709; DOI=10.1016/j.mcn.2004.11.003;
Brandon N.J., Schurov I., Camargo L.M., Handford E.J.,
Duran-Jimeniz B., Hunt P., Millar J.K., Porteous D.J., Shearman M.S.,
Whiting P.J.;
"Subcellular targeting of DISC1 is dependent on a domain independent
from the Nudel binding site.";
Mol. Cell. Neurosci. 28:613-624(2005).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215 AND THR-219, 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).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215 AND THR-219, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, and Spleen;
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).
[18]
FUNCTION, AND INTERACTION WITH PLEKHM1.
PubMed=27777970; DOI=10.1172/jci.insight.86330;
Fujiwara T., Ye S., Castro-Gomes T., Winchell C.G., Andrews N.W.,
Voth D.E., Varughese K.I., Mackintosh S.G., Feng Y., Pavlos N.,
Nakamura T., Manolagas S.C., Zhao H.;
"PLEKHM1/DEF8/RAB7 complex regulates lysosome positioning and bone
homeostasis.";
JCI Insight 1:E86330-E86330(2016).
-!- FUNCTION: Required for organization of the cellular microtubule
array and microtubule anchoring at the centrosome. May regulate
microtubule organization at least in part by targeting the
microtubule severing protein KATNA1 to the centrosome. Also
positively regulates the activity of the minus-end directed
microtubule motor protein dynein. May enhance dynein-mediated
microtubule sliding by targeting dynein to the microtubule plus
ends. Required for several dynein- and microtubule-dependent
processes such as the maintenance of Golgi integrity, the
centripetal motion of secretory vesicles and the coupling of the
nucleus and centrosome. Also required during brain development for
the migration of newly formed neurons from the
ventricular/subventricular zone toward the cortical plate. Plays a
role, together with DISC1, in the regulation of neurite outgrowth.
Required for mitosis in some cell types but appears to be
dispensible for mitosis in cortical neuronal progenitors, which
instead requires NDE1. Facilitates the polymerization of
neurofilaments from the individual subunits NEFH and NEFL.
Positively regulates lysosome peripheral distribution and ruffled
border formation in osteoclasts (PubMed:27777970).
{ECO:0000269|PubMed:12796778, ECO:0000269|PubMed:15208636,
ECO:0000269|PubMed:15473966, ECO:0000269|PubMed:16107726,
ECO:0000269|PubMed:16203747, ECO:0000269|PubMed:27777970}.
-!- SUBUNIT: Interacts with PLEKHM1 (via N- and C-terminus)
(PubMed:27777970). Interacts with dynactin, PCM1 and PCNT.
Interacts (via C-terminus) with CENPF (By similarity). Self-
associates. Interacts with DISC1, dynein, tubulin gamma, KATNA1,
KATNB1, microtubules, PAFAHB1 and YWHAE. Interacts directly with
NEFL and indirectly with NEFH. Interacts with ZNF365 (By
similarity). {ECO:0000250, ECO:0000269|PubMed:27777970}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-646668, EBI-646668;
P63005:Pafah1b1; NbExp=9; IntAct=EBI-646668, EBI-917499;
P62259:Ywhae; NbExp=7; IntAct=EBI-646668, EBI-356480;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm,
cytoskeleton, microtubule organizing center, centrosome.
Chromosome, centromere, kinetochore {ECO:0000250}. Cytoplasm,
cytoskeleton, spindle. Note=Localizes to the kinetochore in a
CENPF-dependent manner. Colocalizes with DISC1 in the perinuclear
region, including the centrosome (By similarity). Localizes to the
interphase centrosome and the mitotic spindle. Localizes to the
cell body of the motor neurons and colocalizes with assembled
neurofilaments within axonal processes. Localizes to the
microtubules of the manchette in elongated spermatids. Localizes
to the interphase centrosome and the mitotic spindle.
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9ERR1-1; Sequence=Displayed;
Name=2;
IsoId=Q9ERR1-2; Sequence=VSP_019311;
-!- TISSUE SPECIFICITY: Expressed in brain, liver, lung and testis (at
protein level). Expressed in brain, epididymis, eye, heart,
kidney, large intestine, liver, ovary, pancreas, prostate,
skeletal muscle, smooth muscle, spleen, submaxillary gland,
testis, thymus and thyroid. Within the brain expression is
pronounced in the cortex, hippocampus, olfactory bulb, striatum,
thalamic and hypothalamic structures and in the molecular layer of
the cerebellum. Largely excluded from cortical progenitor cells
which express NDE1. {ECO:0000269|PubMed:11163259,
ECO:0000269|PubMed:11163260, ECO:0000269|PubMed:11231056,
ECO:0000269|PubMed:15147871}.
-!- DEVELOPMENTAL STAGE: Expression in the brain is detectable from
E7, rises at E15 and E17 and peaks at P5. Enriched in the
developing cortex, particularly in neuroblasts of the ventricular
zone and postmitotic migrating cortical plate neurons. Interaction
with DISC1 in the brain is developmentally regulated, peaking at
E17 and decreasing at P16 so as to be undetectable in the adult
brain. Expressed in the testis from P12, when zygotene
spermatocytes first appear, and expression subsequently rises at
P27. {ECO:0000269|PubMed:11163260, ECO:0000269|PubMed:11231056,
ECO:0000269|PubMed:15147871, ECO:0000269|PubMed:15473966,
ECO:0000269|PubMed:15473967}.
-!- PTM: Phosphorylated by CDK1 and MAPK1 (By similarity).
Phosphorylated in mitosis. Phosphorylated by CDK5. Phosphorylation
by CDK5 promotes interaction with KATNA1 and YWHAE. {ECO:0000250,
ECO:0000269|PubMed:11163259, ECO:0000269|PubMed:12796778,
ECO:0000269|PubMed:16203747}.
-!- PTM: Palmitoylation at Cys-273 reduces affinity for dynein.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the nudE family. {ECO:0000305}.
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EMBL; AF290472; AAG10061.1; -; mRNA.
EMBL; AF323918; AAG42496.1; -; mRNA.
EMBL; AK011168; BAB27443.1; -; mRNA.
EMBL; AL603662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC021434; AAH21434.1; -; mRNA.
EMBL; BC046796; AAH46796.1; -; mRNA.
CCDS; CCDS24870.1; -. [Q9ERR1-1]
RefSeq; NP_076157.2; NM_023668.2. [Q9ERR1-1]
UniGene; Mm.31979; -.
PDB; 5YI4; NMR; -; A=238-284.
PDBsum; 5YI4; -.
ProteinModelPortal; Q9ERR1; -.
SMR; Q9ERR1; -.
BioGrid; 219922; 29.
DIP; DIP-29553N; -.
IntAct; Q9ERR1; 23.
MINT; Q9ERR1; -.
STRING; 10090.ENSMUSP00000018880; -.
iPTMnet; Q9ERR1; -.
PhosphoSitePlus; Q9ERR1; -.
SwissPalm; Q9ERR1; -.
PaxDb; Q9ERR1; -.
PeptideAtlas; Q9ERR1; -.
PRIDE; Q9ERR1; -.
Ensembl; ENSMUST00000018880; ENSMUSP00000018880; ENSMUSG00000018736. [Q9ERR1-1]
Ensembl; ENSMUST00000101017; ENSMUSP00000098579; ENSMUSG00000018736. [Q9ERR1-2]
Ensembl; ENSMUST00000108672; ENSMUSP00000104312; ENSMUSG00000018736. [Q9ERR1-2]
GeneID; 83431; -.
KEGG; mmu:83431; -.
UCSC; uc007joc.3; mouse. [Q9ERR1-1]
CTD; 81565; -.
MGI; MGI:1932915; Ndel1.
eggNOG; KOG1853; Eukaryota.
eggNOG; ENOG410XPMP; LUCA.
GeneTree; ENSGT00390000000111; -.
HOGENOM; HOG000280681; -.
HOVERGEN; HBG082010; -.
InParanoid; Q9ERR1; -.
KO; K16739; -.
OMA; APPMFNS; -.
OrthoDB; EOG091G0GBV; -.
PhylomeDB; Q9ERR1; -.
TreeFam; TF325693; -.
Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-MMU-2467813; Separation of Sister Chromatids.
Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
Reactome; R-MMU-68877; Mitotic Prometaphase.
ChiTaRS; Ndel1; mouse.
PRO; PR:Q9ERR1; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000018736; Expressed in 332 organ(s), highest expression level in secondary oocyte.
Genevisible; Q9ERR1; MM.
GO; GO:0030424; C:axon; IDA:MGI.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0043203; C:axon hillock; IDA:MGI.
GO; GO:0044297; C:cell body; ISO:MGI.
GO; GO:0031252; C:cell leading edge; IDA:MGI.
GO; GO:0090724; C:central region of growth cone; ISO:MGI.
GO; GO:0005813; C:centrosome; IDA:CAFA.
GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005871; C:kinesin complex; ISO:MGI.
GO; GO:0000776; C:kinetochore; ISO:MGI.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0005875; C:microtubule associated complex; IDA:MGI.
GO; GO:0005815; C:microtubule organizing center; IGI:MGI.
GO; GO:0060053; C:neurofilament cytoskeleton; IDA:MGI.
GO; GO:0005635; C:nuclear envelope; ISS:MGI.
GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
GO; GO:0043014; F:alpha-tubulin binding; IDA:MGI.
GO; GO:0048487; F:beta-tubulin binding; IDA:MGI.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008017; F:microtubule binding; IDA:MGI.
GO; GO:0070012; F:oligopeptidase activity; ISO:MGI.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0090630; P:activation of GTPase activity; IDA:MGI.
GO; GO:0016477; P:cell migration; IMP:MGI.
GO; GO:0021955; P:central nervous system neuron axonogenesis; IMP:MGI.
GO; GO:0051642; P:centrosome localization; IMP:MGI.
GO; GO:0021799; P:cerebral cortex radially oriented cell migration; IMP:DFLAT.
GO; GO:0007059; P:chromosome segregation; ISO:MGI.
GO; GO:0051303; P:establishment of chromosome localization; IBA:GO_Central.
GO; GO:0000132; P:establishment of mitotic spindle orientation; IBA:GO_Central.
GO; GO:0001833; P:inner cell mass cell proliferation; IMP:MGI.
GO; GO:0008286; P:insulin receptor signaling pathway; IDA:CAFA.
GO; GO:0032418; P:lysosome localization; IMP:UniProtKB.
GO; GO:0000226; P:microtubule cytoskeleton organization; IGI:MGI.
GO; GO:0007020; P:microtubule nucleation; IBA:GO_Central.
GO; GO:0007100; P:mitotic centrosome separation; IMP:MGI.
GO; GO:0060052; P:neurofilament cytoskeleton organization; IMP:MGI.
GO; GO:0001764; P:neuron migration; IGI:MGI.
GO; GO:0031175; P:neuron projection development; ISO:MGI.
GO; GO:1990138; P:neuron projection extension; IGI:MGI.
GO; GO:0051081; P:nuclear envelope disassembly; ISS:MGI.
GO; GO:0045773; P:positive regulation of axon extension; ISO:MGI.
GO; GO:0048680; P:positive regulation of axon regeneration; ISO:MGI.
GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
GO; GO:1900029; P:positive regulation of ruffle assembly; IMP:UniProtKB.
GO; GO:0033157; P:regulation of intracellular protein transport; ISO:MGI.
GO; GO:2000574; P:regulation of microtubule motor activity; IEA:InterPro.
GO; GO:0010975; P:regulation of neuron projection development; IMP:UniProtKB.
GO; GO:0008090; P:retrograde axonal transport; IDA:MGI.
GO; GO:0047496; P:vesicle transport along microtubule; IGI:MGI.
InterPro; IPR033493; NDEL1.
InterPro; IPR033494; NUDE.
InterPro; IPR006964; NUDE_dom.
PANTHER; PTHR10921; PTHR10921; 1.
PANTHER; PTHR10921:SF0; PTHR10921:SF0; 1.
Pfam; PF04880; NUDE_C; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Centromere; Chromosome;
Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton;
Developmental protein; Differentiation; Kinetochore; Lipoprotein;
Microtubule; Neurogenesis; Palmitate; Phosphoprotein;
Reference proteome; Transport.
CHAIN 1 345 Nuclear distribution protein nudE-like 1.
/FTId=PRO_0000240212.
REGION 56 166 Self-association.
REGION 64 189 Interaction with KATNB1.
{ECO:0000269|PubMed:16203747}.
REGION 114 133 Required for interaction with PAFAH1B1.
{ECO:0000250}.
REGION 175 345 Interaction with CENPF. {ECO:0000250}.
REGION 189 256 Interaction with YWHAE.
{ECO:0000269|PubMed:12796778}.
REGION 191 345 Interaction with NEFL.
{ECO:0000269|PubMed:15208636}.
REGION 195 256 Interaction with KATNA1.
{ECO:0000269|PubMed:16203747}.
REGION 241 280 Interaction with DISC1. {ECO:0000250}.
REGION 256 291 Required for localization to the
centrosome and interaction with dynein,
dynactin, tubulin gamma, PCM1 and PCNT.
{ECO:0000250}.
COILED 28 190 {ECO:0000255}.
MOD_RES 215 215 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 219 219 Phosphothreonine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 231 231 Phosphoserine.
{ECO:0000250|UniProtKB:Q9GZM8}.
MOD_RES 242 242 Phosphoserine; by CDK1.
{ECO:0000250|UniProtKB:Q9GZM8}.
MOD_RES 245 245 Phosphothreonine; by CDK1 and MAPK1.
{ECO:0000250|UniProtKB:Q9GZM8}.
MOD_RES 344 344 Phosphoserine.
{ECO:0000250|UniProtKB:Q78PB6}.
LIPID 273 273 S-palmitoyl cysteine; by ZDHHC2, ZDHHC3
and ZDHHC7. {ECO:0000250}.
VAR_SEQ 316 345 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_019311.
MUTAGEN 198 198 S->A: Reduces phosphorylation by CDK5 and
impairs interaction with YWHAE. Impairs
interaction with KATNA1; when associated
with A-219 and A-231.
{ECO:0000269|PubMed:12796778,
ECO:0000269|PubMed:16203747}.
MUTAGEN 219 219 T->A: Reduces phosphorylation by CDK5 and
impairs interaction with YWHAE. Impairs
interaction with KATNA1; when associated
with A-198 and A-231.
{ECO:0000269|PubMed:12796778,
ECO:0000269|PubMed:16203747}.
MUTAGEN 231 231 S->A: Reduces phosphorylation by CDK5 and
impairs interaction with YWHAE. Impairs
interaction with KATNA1; when associated
with A-198 and A-219.
{ECO:0000269|PubMed:12796778,
ECO:0000269|PubMed:16203747}.
MUTAGEN 266 266 L->A: Impairs interaction with DISC1.
{ECO:0000269|PubMed:14962739}.
MUTAGEN 267 267 E->A: Impairs interaction with DISC1.
{ECO:0000269|PubMed:14962739}.
CONFLICT 302 302 E -> K (in Ref. 1; AAG10061).
{ECO:0000305}.
HELIX 248 281 {ECO:0000244|PDB:5YI4}.
SEQUENCE 345 AA; 38366 MW; CB3059DFD998E9EC CRC64;
MDGEDIPDFS SLKEETAYWK ELSLKYKQSF QEARDELVEF QEGSRELEAE LEAQLVQAEQ
RNRDLQADNQ RLKYEVEALK EKLEHQYAQS YKQVSVLEDD LSQTRAIKEQ LHKYVRELEQ
ANDDLERAKR ATIVSLEDFE QRLNQAIERN AFLESELDEK ESLLVSVQRL KDEARDLRQE
LAVRERQQEV TRKSAPSSPT LDCEKMDSAV QASLSLPATP VGKGTENSFP SPKAIPNGFG
TSPLTPSARI SALNIVGDLL RKVGALESKL AACRNFAKDQ ASRKSYVPGS VNCGVMNSNG
PECPRSGRAT FFHKGAVNGF DPAPPPPGLG SSRPSSAPGM LPLSV


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