NDEL1_MOUSE
ID NDEL1_MOUSE Reviewed; 345 AA.
AC Q9ERR1; Q9D0Q4; Q9EPT6;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Nuclear distribution protein nudE-like 1;
DE AltName: Full=Protein mNudE-like;
DE Short=Protein Nudel;
DE Short=mNudE-L;
GN Name=Ndel1; Synonyms=Nudel;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SELF-ASSOCIATION, INTERACTION WITH
RP PAFAH1B1 AND DYNEIN, TISSUE SPECIFICITY, AND PHOSPHORYLATION BY CDK5.
RX PubMed=11163259; DOI=10.1016/s0896-6273(00)00146-x;
RA Sasaki S., Shionoya A., Ishida M., Gambello M.J., Yingling J.,
RA Wynshaw-Boris A., Hirotsune S.;
RT "A LIS1/NUDEL/cytoplasmic dynein heavy chain complex in the developing and
RT adult nervous system.";
RL Neuron 28:681-696(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH PAFAH1B1, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Swiss Webster / NIH;
RX PubMed=11231056; DOI=10.1016/s0925-4773(00)00543-8;
RA Sweeney K.J., Prokscha A., Eichele G.;
RT "NudE-L, a novel Lis1-interacting protein, belongs to a family of
RT vertebrate coiled-coil proteins.";
RL Mech. Dev. 101:21-33(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [6]
RP INTERACTION WITH PAFAH1B1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=11163260; DOI=10.1016/s0896-6273(00)00147-1;
RA Niethammer M., Smith D.S., Ayala R., Peng J., Ko J., Lee M.-S.,
RA Morabito M., Tsai L.-H.;
RT "NUDEL is a novel cdk5 substrate that associates with LIS1 and cytoplasmic
RT dynein.";
RL Neuron 28:697-711(2000).
RN [7]
RP FUNCTION, INTERACTION WITH PAFAH1B1 AND YWHAE, SUBCELLULAR LOCATION,
RP PHOSPHORYLATION BY CDK5, AND MUTAGENESIS OF SER-198; THR-219 AND SER-231.
RX PubMed=12796778; DOI=10.1038/ng1169;
RA Toyo-oka K., Shionoya A., Gambello M.J., Cardoso C., Leventer R.,
RA Ward H.L., Ayala R., Tsai L.-H., Dobyns W., Ledbetter D., Hirotsune S.,
RA Wynshaw-Boris A.;
RT "14-3-3epsilon is important for neuronal migration by binding to NUDEL: a
RT molecular explanation for Miller-Dieker syndrome.";
RL Nat. Genet. 34:274-285(2003).
RN [8]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15147871; DOI=10.1016/j.febslet.2004.04.009;
RA Yamaguchi N., Takanezawa Y., Koizumi H., Umezu-Goto M., Aoki J., Arai H.;
RT "Expression of NUDEL in manchette and its implication in spermatogenesis.";
RL FEBS Lett. 566:71-76(2004).
RN [9]
RP INTERACTION WITH DISC1; DYNEIN; TUBULIN GAMMA AND MICROTUBULES, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF LEU-266 AND GLU-267.
RX PubMed=14962739; DOI=10.1016/j.mcn.2003.09.009;
RA Brandon N.J., Handford E.J., Schurov I., Rain J.-C., Pelling M.,
RA Duran-Jimeniz B., Camargo L.M., Oliver K.R., Beher D., Shearman M.S.,
RA Whiting P.J.;
RT "Disrupted in Schizophrenia 1 and Nudel form a neurodevelopmentally
RT regulated protein complex: implications for schizophrenia and other major
RT neurological disorders.";
RL Mol. Cell. Neurosci. 25:42-55(2004).
RN [10]
RP FUNCTION, INTERACTION WITH NEFH; NEFL AND PAFAH1B1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15208636; DOI=10.1038/ncb1139;
RA Nguyen M.-D., Shu T., Sanada K., Lariviere R.C., Tseng H.-C., Park S.K.,
RA Julien J.-P., Tsai L.-H.;
RT "A NUDEL-dependent mechanism of neurofilament assembly regulates the
RT integrity of CNS neurons.";
RL Nat. Cell Biol. 6:595-608(2004).
RN [11]
RP FUNCTION, INTERACTION WITH DYNEIN, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=15473966; DOI=10.1016/j.neuron.2004.09.030;
RA Shu T., Ayala R., Nguyen M.-D., Xie Z., Gleeson J.G., Tsai L.-H.;
RT "Ndel1 operates in a common pathway with LIS1 and cytoplasmic dynein to
RT regulate cortical neuronal positioning.";
RL Neuron 44:263-277(2004).
RN [12]
RP DEVELOPMENTAL STAGE.
RX PubMed=15473967; DOI=10.1016/j.neuron.2004.09.023;
RA Feng Y., Walsh C.A.;
RT "Mitotic spindle regulation by Nde1 controls cerebral cortical size.";
RL Neuron 44:279-293(2004).
RN [13]
RP FUNCTION, INTERACTION WITH KATNA1 AND KATNB1, SUBCELLULAR LOCATION,
RP PHOSPHORYLATION BY CDK5, AND MUTAGENESIS OF SER-198; THR-219 AND SER-231.
RX PubMed=16203747; DOI=10.1093/hmg/ddi339;
RA Toyo-Oka K., Sasaki S., Yano Y., Mori D., Kobayashi T., Toyoshima Y.Y.,
RA Tokuoka S.M., Ishii S., Shimizu T., Muramatsu M., Hiraiwa N., Yoshiki A.,
RA Wynshaw-Boris A., Hirotsune S.;
RT "Recruitment of katanin p60 by phosphorylated NDEL1, an LIS1 interacting
RT protein, is essential for mitotic cell division and neuronal migration.";
RL Hum. Mol. Genet. 14:3113-3128(2005).
RN [14]
RP FUNCTION.
RX PubMed=16107726; DOI=10.1128/mcb.25.17.7812-7827.2005;
RA Sasaki S., Mori D., Toyo-oka K., Chen A., Garrett-Beal L., Muramatsu M.,
RA Miyagawa S., Hiraiwa N., Yoshiki A., Wynshaw-Boris A., Hirotsune S.;
RT "Complete loss of Ndel1 results in neuronal migration defects and early
RT embryonic lethality.";
RL Mol. Cell. Biol. 25:7812-7827(2005).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=15797709; DOI=10.1016/j.mcn.2004.11.003;
RA Brandon N.J., Schurov I., Camargo L.M., Handford E.J., Duran-Jimeniz B.,
RA Hunt P., Millar J.K., Porteous D.J., Shearman M.S., Whiting P.J.;
RT "Subcellular targeting of DISC1 is dependent on a domain independent from
RT the Nudel binding site.";
RL Mol. Cell. Neurosci. 28:613-624(2005).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215 AND THR-219, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215 AND THR-219, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [18]
RP FUNCTION, AND INTERACTION WITH PLEKHM1.
RX PubMed=27777970; DOI=10.1172/jci.insight.86330;
RA Fujiwara T., Ye S., Castro-Gomes T., Winchell C.G., Andrews N.W.,
RA Voth D.E., Varughese K.I., Mackintosh S.G., Feng Y., Pavlos N.,
RA Nakamura T., Manolagas S.C., Zhao H.;
RT "PLEKHM1/DEF8/RAB7 complex regulates lysosome positioning and bone
RT homeostasis.";
RL JCI Insight 1:E86330-E86330(2016).
CC -!- FUNCTION: Required for organization of the cellular microtubule array
CC and microtubule anchoring at the centrosome. May regulate microtubule
CC organization at least in part by targeting the microtubule severing
CC protein KATNA1 to the centrosome. Also positively regulates the
CC activity of the minus-end directed microtubule motor protein dynein.
CC May enhance dynein-mediated microtubule sliding by targeting dynein to
CC the microtubule plus ends. Required for several dynein- and
CC microtubule-dependent processes such as the maintenance of Golgi
CC integrity, the centripetal motion of secretory vesicles and the
CC coupling of the nucleus and centrosome. Also required during brain
CC development for the migration of newly formed neurons from the
CC ventricular/subventricular zone toward the cortical plate. Plays a
CC role, together with DISC1, in the regulation of neurite outgrowth.
CC Required for mitosis in some cell types but appears to be dispensible
CC for mitosis in cortical neuronal progenitors, which instead requires
CC NDE1. Facilitates the polymerization of neurofilaments from the
CC individual subunits NEFH and NEFL. Positively regulates lysosome
CC peripheral distribution and ruffled border formation in osteoclasts
CC (PubMed:27777970). {ECO:0000269|PubMed:12796778,
CC ECO:0000269|PubMed:15208636, ECO:0000269|PubMed:15473966,
CC ECO:0000269|PubMed:16107726, ECO:0000269|PubMed:16203747,
CC ECO:0000269|PubMed:27777970}.
CC -!- SUBUNIT: Interacts with PLEKHM1 (via N- and C-terminus)
CC (PubMed:27777970). Interacts with dynactin, PCM1 and PCNT. Interacts
CC (via C-terminus) with CENPF (By similarity). Self-associates. Interacts
CC with DISC1, dynein, tubulin gamma, KATNA1, KATNB1, microtubules,
CC PAFAHB1 and YWHAE. Interacts directly with NEFL and indirectly with
CC NEFH. Interacts with ZNF365 (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:27777970}.
CC -!- INTERACTION:
CC Q9ERR1; Q9ERR1: Ndel1; NbExp=3; IntAct=EBI-646668, EBI-646668;
CC Q9ERR1; P63005: Pafah1b1; NbExp=9; IntAct=EBI-646668, EBI-917499;
CC Q9ERR1; P62259: Ywhae; NbExp=7; IntAct=EBI-646668, EBI-356480;
CC Q9ERR1; Q9NRI5: DISC1; Xeno; NbExp=2; IntAct=EBI-646668, EBI-529989;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome. Chromosome, centromere,
CC kinetochore {ECO:0000250}. Cytoplasm, cytoskeleton, spindle.
CC Note=Localizes to the kinetochore in a CENPF-dependent manner.
CC Colocalizes with DISC1 in the perinuclear region, including the
CC centrosome (By similarity). Localizes to the interphase centrosome and
CC the mitotic spindle. Localizes to the cell body of the motor neurons
CC and colocalizes with assembled neurofilaments within axonal processes.
CC Localizes to the microtubules of the manchette in elongated spermatids.
CC Localizes to the interphase centrosome and the mitotic spindle.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ERR1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ERR1-2; Sequence=VSP_019311;
CC -!- TISSUE SPECIFICITY: Expressed in brain, liver, lung and testis (at
CC protein level). Expressed in brain, epididymis, eye, heart, kidney,
CC large intestine, liver, ovary, pancreas, prostate, skeletal muscle,
CC smooth muscle, spleen, submaxillary gland, testis, thymus and thyroid.
CC Within the brain expression is pronounced in the cortex, hippocampus,
CC olfactory bulb, striatum, thalamic and hypothalamic structures and in
CC the molecular layer of the cerebellum. Largely excluded from cortical
CC progenitor cells which express NDE1. {ECO:0000269|PubMed:11163259,
CC ECO:0000269|PubMed:11163260, ECO:0000269|PubMed:11231056,
CC ECO:0000269|PubMed:15147871}.
CC -!- DEVELOPMENTAL STAGE: Expression in the brain is detectable from 7 dpc,
CC rises at 15 dpc and 17 dpc and peaks at P5. Enriched in the developing
CC cortex, particularly in neuroblasts of the ventricular zone and
CC postmitotic migrating cortical plate neurons. Interaction with DISC1 in
CC the brain is developmentally regulated, peaking at 17 dpc and
CC decreasing at P16 so as to be undetectable in the adult brain.
CC Expressed in the testis from P12, when zygotene spermatocytes first
CC appear, and expression subsequently rises at P27.
CC {ECO:0000269|PubMed:11163260, ECO:0000269|PubMed:11231056,
CC ECO:0000269|PubMed:15147871, ECO:0000269|PubMed:15473966,
CC ECO:0000269|PubMed:15473967}.
CC -!- PTM: Phosphorylated by CDK1 and MAPK1 (By similarity). Phosphorylated
CC in mitosis. Phosphorylated by CDK5. Phosphorylation by CDK5 promotes
CC interaction with KATNA1 and YWHAE. {ECO:0000250,
CC ECO:0000269|PubMed:11163259, ECO:0000269|PubMed:12796778,
CC ECO:0000269|PubMed:16203747}.
CC -!- PTM: Palmitoylation at Cys-273 reduces affinity for dynein.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nudE family. {ECO:0000305}.
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DR EMBL; AF290472; AAG10061.1; -; mRNA.
DR EMBL; AF323918; AAG42496.1; -; mRNA.
DR EMBL; AK011168; BAB27443.1; -; mRNA.
DR EMBL; AL603662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021434; AAH21434.1; -; mRNA.
DR EMBL; BC046796; AAH46796.1; -; mRNA.
DR CCDS; CCDS24870.1; -. [Q9ERR1-1]
DR RefSeq; NP_076157.2; NM_023668.2. [Q9ERR1-1]
DR PDB; 5YI4; NMR; -; A=238-284.
DR PDB; 6KZJ; X-ray; 1.50 A; B/C=238-284.
DR PDBsum; 5YI4; -.
DR PDBsum; 6KZJ; -.
DR AlphaFoldDB; Q9ERR1; -.
DR SMR; Q9ERR1; -.
DR BioGRID; 219922; 50.
DR DIP; DIP-29553N; -.
DR IntAct; Q9ERR1; 24.
DR MINT; Q9ERR1; -.
DR STRING; 10090.ENSMUSP00000018880; -.
DR iPTMnet; Q9ERR1; -.
DR PhosphoSitePlus; Q9ERR1; -.
DR SwissPalm; Q9ERR1; -.
DR EPD; Q9ERR1; -.
DR MaxQB; Q9ERR1; -.
DR PaxDb; Q9ERR1; -.
DR PeptideAtlas; Q9ERR1; -.
DR PRIDE; Q9ERR1; -.
DR ProteomicsDB; 252795; -. [Q9ERR1-1]
DR ProteomicsDB; 252796; -. [Q9ERR1-2]
DR Antibodypedia; 12558; 511 antibodies from 38 providers.
DR DNASU; 83431; -.
DR Ensembl; ENSMUST00000018880; ENSMUSP00000018880; ENSMUSG00000018736. [Q9ERR1-1]
DR Ensembl; ENSMUST00000101017; ENSMUSP00000098579; ENSMUSG00000018736. [Q9ERR1-2]
DR Ensembl; ENSMUST00000108672; ENSMUSP00000104312; ENSMUSG00000018736. [Q9ERR1-2]
DR GeneID; 83431; -.
DR KEGG; mmu:83431; -.
DR UCSC; uc007joc.3; mouse. [Q9ERR1-1]
DR CTD; 81565; -.
DR MGI; MGI:1932915; Ndel1.
DR VEuPathDB; HostDB:ENSMUSG00000018736; -.
DR eggNOG; KOG1853; Eukaryota.
DR GeneTree; ENSGT00390000000111; -.
DR HOGENOM; CLU_057872_0_0_1; -.
DR InParanoid; Q9ERR1; -.
DR OMA; EVEALKX; -.
DR OrthoDB; 1082224at2759; -.
DR PhylomeDB; Q9ERR1; -.
DR TreeFam; TF325693; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 83431; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Ndel1; mouse.
DR PRO; PR:Q9ERR1; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9ERR1; protein.
DR Bgee; ENSMUSG00000018736; Expressed in seminal vesicle and 291 other tissues.
DR Genevisible; Q9ERR1; MM.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0043203; C:axon hillock; IDA:MGI.
DR GO; GO:0044297; C:cell body; ISO:MGI.
DR GO; GO:0031252; C:cell leading edge; IDA:MGI.
DR GO; GO:0090724; C:central region of growth cone; ISO:MGI.
DR GO; GO:0005813; C:centrosome; IDA:CAFA.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005871; C:kinesin complex; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005875; C:microtubule associated complex; IDA:MGI.
DR GO; GO:0005815; C:microtubule organizing center; IGI:MGI.
DR GO; GO:0060053; C:neurofilament cytoskeleton; IDA:MGI.
DR GO; GO:0005635; C:nuclear envelope; ISS:MGI.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR GO; GO:0043014; F:alpha-tubulin binding; IDA:MGI.
DR GO; GO:0048487; F:beta-tubulin binding; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR GO; GO:0070012; F:oligopeptidase activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; IDA:MGI.
DR GO; GO:0016477; P:cell migration; IMP:MGI.
DR GO; GO:0021955; P:central nervous system neuron axonogenesis; IMP:MGI.
DR GO; GO:0051642; P:centrosome localization; IMP:MGI.
DR GO; GO:0021799; P:cerebral cortex radially oriented cell migration; IMP:DFLAT.
DR GO; GO:0007059; P:chromosome segregation; ISO:MGI.
DR GO; GO:0051303; P:establishment of chromosome localization; IBA:GO_Central.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IBA:GO_Central.
DR GO; GO:0001833; P:inner cell mass cell proliferation; IMP:MGI.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA:CAFA.
DR GO; GO:0032418; P:lysosome localization; IMP:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IGI:MGI.
DR GO; GO:0007020; P:microtubule nucleation; IBA:GO_Central.
DR GO; GO:0007100; P:mitotic centrosome separation; IMP:MGI.
DR GO; GO:0060052; P:neurofilament cytoskeleton organization; IMP:MGI.
DR GO; GO:0001764; P:neuron migration; IGI:MGI.
DR GO; GO:0031175; P:neuron projection development; ISO:MGI.
DR GO; GO:1990138; P:neuron projection extension; IGI:MGI.
DR GO; GO:0051081; P:nuclear membrane disassembly; ISS:MGI.
DR GO; GO:0045773; P:positive regulation of axon extension; ISO:MGI.
DR GO; GO:0048680; P:positive regulation of axon regeneration; ISO:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:1900029; P:positive regulation of ruffle assembly; IMP:UniProtKB.
DR GO; GO:0140650; P:radial glia-guided pyramidal neuron migration; IGI:MGI.
DR GO; GO:0033157; P:regulation of intracellular protein transport; ISO:MGI.
DR GO; GO:0010975; P:regulation of neuron projection development; IMP:UniProtKB.
DR GO; GO:0008090; P:retrograde axonal transport; IDA:MGI.
DR GO; GO:0047496; P:vesicle transport along microtubule; IGI:MGI.
DR InterPro; IPR033493; NDEL1.
DR InterPro; IPR033494; NUDE.
DR InterPro; IPR006964; NUDE_dom.
DR PANTHER; PTHR10921; PTHR10921; 1.
DR PANTHER; PTHR10921:SF0; PTHR10921:SF0; 1.
DR Pfam; PF04880; NUDE_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Centromere; Chromosome; Coiled coil;
KW Cytoplasm; Cytoskeleton; Developmental protein; Differentiation;
KW Kinetochore; Lipoprotein; Microtubule; Neurogenesis; Palmitate;
KW Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..345
FT /note="Nuclear distribution protein nudE-like 1"
FT /id="PRO_0000240212"
FT REGION 56..166
FT /note="Self-association"
FT REGION 64..189
FT /note="Interaction with KATNB1"
FT /evidence="ECO:0000269|PubMed:16203747"
FT REGION 114..133
FT /note="Required for interaction with PAFAH1B1"
FT /evidence="ECO:0000250"
FT REGION 175..345
FT /note="Interaction with CENPF"
FT /evidence="ECO:0000250"
FT REGION 189..256
FT /note="Interaction with YWHAE"
FT /evidence="ECO:0000269|PubMed:12796778"
FT REGION 191..345
FT /note="Interaction with NEFL"
FT /evidence="ECO:0000269|PubMed:15208636"
FT REGION 195..256
FT /note="Interaction with KATNA1"
FT /evidence="ECO:0000269|PubMed:16203747"
FT REGION 217..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..280
FT /note="Interaction with DISC1"
FT /evidence="ECO:0000250"
FT REGION 256..291
FT /note="Required for localization to the centrosome and
FT interaction with dynein, dynactin, tubulin gamma, PCM1 and
FT PCNT"
FT /evidence="ECO:0000250"
FT REGION 314..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 28..190
FT /evidence="ECO:0000255"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 219
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9GZM8"
FT MOD_RES 242
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q9GZM8"
FT MOD_RES 245
FT /note="Phosphothreonine; by CDK1 and MAPK1"
FT /evidence="ECO:0000250|UniProtKB:Q9GZM8"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q78PB6"
FT LIPID 273
FT /note="S-palmitoyl cysteine; by ZDHHC2, ZDHHC3 and ZDHHC7"
FT /evidence="ECO:0000250"
FT VAR_SEQ 316..345
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_019311"
FT MUTAGEN 198
FT /note="S->A: Reduces phosphorylation by CDK5 and impairs
FT interaction with YWHAE. Impairs interaction with KATNA1;
FT when associated with A-219 and A-231."
FT /evidence="ECO:0000269|PubMed:12796778,
FT ECO:0000269|PubMed:16203747"
FT MUTAGEN 219
FT /note="T->A: Reduces phosphorylation by CDK5 and impairs
FT interaction with YWHAE. Impairs interaction with KATNA1;
FT when associated with A-198 and A-231."
FT /evidence="ECO:0000269|PubMed:12796778,
FT ECO:0000269|PubMed:16203747"
FT MUTAGEN 231
FT /note="S->A: Reduces phosphorylation by CDK5 and impairs
FT interaction with YWHAE. Impairs interaction with KATNA1;
FT when associated with A-198 and A-219."
FT /evidence="ECO:0000269|PubMed:12796778,
FT ECO:0000269|PubMed:16203747"
FT MUTAGEN 266
FT /note="L->A: Impairs interaction with DISC1."
FT /evidence="ECO:0000269|PubMed:14962739"
FT MUTAGEN 267
FT /note="E->A: Impairs interaction with DISC1."
FT /evidence="ECO:0000269|PubMed:14962739"
FT CONFLICT 302
FT /note="E -> K (in Ref. 1; AAG10061)"
FT /evidence="ECO:0000305"
FT HELIX 246..272
FT /evidence="ECO:0007829|PDB:6KZJ"
SQ 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
