NDE1_HUMAN
ID NDE1_HUMAN Reviewed; 335 AA.
AC Q9NXR1; Q49AQ2;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Nuclear distribution protein nudE homolog 1;
DE Short=NudE;
GN Name=NDE1; Synonyms=NUDE;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta, 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 [4]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=12556484; DOI=10.1128/mcb.23.4.1239-1250.2003;
RA Yan X., Li F., Liang Y., Shen Y., Zhao X., Huang Q., Zhu X.;
RT "Human Nudel and NudE as regulators of cytoplasmic dynein in poleward
RT protein transport along the mitotic spindle.";
RL Mol. Cell. Biol. 23:1239-1250(2003).
RN [5]
RP INTERACTION WITH DYNACTIN; TUBULIN GAMMA; PAFAH1B1; PCM1 AND PCNT.
RX PubMed=16291865; DOI=10.1091/mbc.e05-04-0360;
RA Guo J., Yang Z., Song W., Chen Q., Wang F., Zhang Q., Zhu X.;
RT "Nudel contributes to microtubule anchoring at the mother centriole and is
RT involved in both dynein-dependent and -independent centrosomal protein
RT assembly.";
RL Mol. Biol. Cell 17:680-689(2006).
RN [6]
RP INTERACTION WITH ZNF365, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND
RP MUTAGENESIS OF THR-191; THR-215; THR-228; THR-243; THR-246 AND SER-282.
RX PubMed=16682949; DOI=10.1038/sj.onc.1209637;
RA Hirohashi Y., Wang Q., Liu Q., Li B., Du X., Zhang H., Furuuchi K.,
RA Masuda K., Sato N., Greene M.I.;
RT "Centrosomal proteins Nde1 and Su48 form a complex regulated by
RT phosphorylation.";
RL Oncogene 25:6048-6055(2006).
RN [7]
RP FUNCTION, INTERACTION WITH CENPF, AND SUBCELLULAR LOCATION.
RX PubMed=17600710; DOI=10.1016/j.cub.2007.05.077;
RA Vergnolle M.A.S., Taylor S.S.;
RT "Cenp-F links kinetochores to Ndel1/Nde1/Lis1/dynein microtubule motor
RT complexes.";
RL Curr. Biol. 17:1173-1179(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211; THR-215; THR-228;
RP SER-231; SER-239; THR-243; THR-246 AND SER-282, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PALMITOYLATION AT CYS-274 BY ZDHHC2; ZDHHC3 AND ZDHHC7.
RX PubMed=19927128; DOI=10.1038/emboj.2009.325;
RA Shmueli A., Segal M., Sapir T., Tsutsumi R., Noritake J., Bar A.,
RA Sapoznik S., Fukata Y., Orr I., Fukata M., Reiner O.;
RT "Ndel1 palmitoylation: a new mean to regulate cytoplasmic dynein
RT activity.";
RL EMBO J. 29:107-119(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-243; THR-246 AND SER-282, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INVOLVEMENT IN
RP LIS4.
RX PubMed=21529752; DOI=10.1016/j.ajhg.2011.03.019;
RA Bakircioglu M., Carvalho O.P., Khurshid M., Cox J.J., Tuysuz B., Barak T.,
RA Yilmaz S., Caglayan O., Dincer A., Nicholas A.K., Quarrell O.,
RA Springell K., Karbani G., Malik S., Gannon C., Sheridan E., Crosier M.,
RA Lisgo S.N., Lindsay S., Bilguvar K., Gergely F., Gunel M., Woods C.G.;
RT "The essential role of centrosomal NDE1 in human cerebral cortex
RT neurogenesis.";
RL Am. J. Hum. Genet. 88:523-535(2011).
RN [13]
RP INVOLVEMENT IN LIS4.
RX PubMed=21529751; DOI=10.1016/j.ajhg.2011.04.003;
RA Alkuraya F.S., Cai X., Emery C., Mochida G.H., Al-Dosari M.S., Felie J.M.,
RA Hill R.S., Barry B.J., Partlow J.N., Gascon G.G., Kentab A., Jan M.,
RA Shaheen R., Feng Y., Walsh C.A.;
RT "Human mutations in NDE1 cause extreme microcephaly with lissencephaly.";
RL Am. J. Hum. Genet. 88:536-547(2011).
RN [14]
RP ERRATUM OF PUBMED:21529751.
RA Alkuraya F.S., Cai X., Emery C., Mochida G.H., Al-Dosari M.S., Felie J.M.,
RA Hill R.S., Barry B.J., Partlow J.N., Gascon G.G., Kentab A., Jan M.,
RA Shaheen R., Feng Y., Walsh C.A.;
RL Am. J. Hum. Genet. 88:677-677(2011).
RN [15]
RP INVOLVEMENT IN MHAC.
RX PubMed=22526350; DOI=10.1007/s10048-012-0326-9;
RA Guven A., Gunduz A., Bozoglu T.M., Yalcinkaya C., Tolun A.;
RT "Novel NDE1 homozygous mutation resulting in microhydranencephaly and not
RT microlyssencephaly.";
RL Neurogenetics 13:189-194(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211; SER-231; SER-239;
RP SER-282 AND SER-309, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Required for centrosome duplication and formation and
CC function of the mitotic spindle. Essential for the development of the
CC cerebral cortex. May regulate the production of neurons by controlling
CC the orientation of the mitotic spindle during division of cortical
CC neuronal progenitors of the proliferative ventricular zone of the
CC brain. Orientation of the division plane perpendicular to the layers of
CC the cortex gives rise to two proliferative neuronal progenitors whereas
CC parallel orientation of the division plane yields one proliferative
CC neuronal progenitor and a post-mitotic neuron. A premature shift
CC towards a neuronal fate within the progenitor population may result in
CC an overall reduction in the final number of neurons and an increase in
CC the number of neurons in the deeper layers of the cortex.
CC {ECO:0000269|PubMed:17600710, ECO:0000269|PubMed:21529752}.
CC -!- SUBUNIT: Self-associates. Interacts with CNTRL, LIS1, dynein, SLMAP and
CC TCP1 (By similarity). Interacts with CENPF, dynactin, tubulin gamma,
CC PAFAH1B1, PCM1 and PCNT. Interacts with ZNF365. {ECO:0000250,
CC ECO:0000269|PubMed:16291865, ECO:0000269|PubMed:16682949,
CC ECO:0000269|PubMed:17600710}.
CC -!- INTERACTION:
CC Q9NXR1; Q9NRI5: DISC1; NbExp=4; IntAct=EBI-941227, EBI-529989;
CC Q9NXR1; Q9NXR1: NDE1; NbExp=5; IntAct=EBI-941227, EBI-941227;
CC Q9NXR1; Q9GZM8: NDEL1; NbExp=2; IntAct=EBI-941227, EBI-928842;
CC Q9NXR1; P62258: YWHAE; NbExp=2; IntAct=EBI-941227, EBI-356498;
CC Q9NXR1; Q70YC5: ZNF365; NbExp=3; IntAct=EBI-941227, EBI-941182;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome. Chromosome, centromere,
CC kinetochore. Cytoplasm, cytoskeleton, spindle. Cleavage furrow.
CC Note=Localizes to the interphase and S phase centrosome. During
CC mitosis, partially associated with the mitotic spindle. Concentrates at
CC the plus ends of microtubules coincident with kinetochores in metaphase
CC and anaphase in a CENPF-dependent manner. Also localizes to the
CC cleavage furrow during cytokinesis. manner. Also localizes to the
CC cleavage furrow during cytokinesis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NXR1-2; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NXR1-1; Sequence=VSP_059512;
CC -!- TISSUE SPECIFICITY: Expressed in the neuroepithelium throughout the
CC developing brain, including the cerebral cortex and cerebellum.
CC {ECO:0000269|PubMed:21529752}.
CC -!- PTM: Phosphorylated in mitosis. Phosphorylated in vitro by CDC2.
CC Phosphorylation at Thr-246 is essential for the G2/M transition (By
CC similarity). {ECO:0000250}.
CC -!- DISEASE: Lissencephaly 4 (LIS4) [MIM:614019]: A neurodevelopmental
CC disorder characterized by lissencephaly, severe brain atrophy, extreme
CC microcephaly, and profound intellectual disability.
CC {ECO:0000269|PubMed:21529751, ECO:0000269|PubMed:21529752}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Microhydranencephaly (MHAC) [MIM:605013]: A severe
CC neurodevelopmental disorder characterized by microcephaly, severe motor
CC and intellectual disability, spasticity, and brain malformations that
CC include gross dilation of the ventricles with complete absence of the
CC cerebral hemispheres or severe delay in their development.
CC {ECO:0000269|PubMed:22526350}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the nudE family. {ECO:0000305}.
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DR EMBL; AK000108; BAA90949.1; -; mRNA.
DR EMBL; AC026401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF001548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001421; AAH01421.1; -; mRNA.
DR EMBL; BC033900; AAH33900.1; -; mRNA.
DR CCDS; CCDS10564.1; -. [Q9NXR1-2]
DR RefSeq; NP_001137451.1; NM_001143979.1. [Q9NXR1-2]
DR RefSeq; NP_060138.1; NM_017668.2. [Q9NXR1-2]
DR RefSeq; XP_016878838.1; XM_017023349.1. [Q9NXR1-1]
DR RefSeq; XP_016878845.1; XM_017023356.1. [Q9NXR1-1]
DR PDB; 7E1T; X-ray; 2.45 A; C/D=98-168.
DR PDBsum; 7E1T; -.
DR AlphaFoldDB; Q9NXR1; -.
DR SMR; Q9NXR1; -.
DR BioGRID; 120175; 116.
DR IntAct; Q9NXR1; 50.
DR MINT; Q9NXR1; -.
DR STRING; 9606.ENSP00000379643; -.
DR GlyGen; Q9NXR1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NXR1; -.
DR MetOSite; Q9NXR1; -.
DR PhosphoSitePlus; Q9NXR1; -.
DR SwissPalm; Q9NXR1; -.
DR BioMuta; NDE1; -.
DR DMDM; 108860813; -.
DR EPD; Q9NXR1; -.
DR jPOST; Q9NXR1; -.
DR MassIVE; Q9NXR1; -.
DR MaxQB; Q9NXR1; -.
DR PaxDb; Q9NXR1; -.
DR PeptideAtlas; Q9NXR1; -.
DR PRIDE; Q9NXR1; -.
DR ProteomicsDB; 83120; -. [Q9NXR1-1]
DR ProteomicsDB; 83121; -. [Q9NXR1-2]
DR Antibodypedia; 11751; 283 antibodies from 31 providers.
DR DNASU; 54820; -.
DR Ensembl; ENST00000396354.6; ENSP00000379642.1; ENSG00000072864.16. [Q9NXR1-2]
DR Ensembl; ENST00000396355.5; ENSP00000379643.1; ENSG00000072864.16. [Q9NXR1-2]
DR Ensembl; ENST00000631844.1; ENSP00000488199.1; ENSG00000275911.3. [Q9NXR1-2]
DR Ensembl; ENST00000631923.1; ENSP00000488050.1; ENSG00000275911.3. [Q9NXR1-2]
DR Ensembl; ENST00000674554.1; ENSP00000502635.1; ENSG00000072864.16. [Q9NXR1-2]
DR Ensembl; ENST00000674888.1; ENSP00000501936.1; ENSG00000072864.16. [Q9NXR1-2]
DR Ensembl; ENST00000675926.1; ENSP00000502354.1; ENSG00000072864.16. [Q9NXR1-2]
DR Ensembl; ENST00000675951.1; ENSP00000502160.1; ENSG00000072864.16. [Q9NXR1-2]
DR GeneID; 54820; -.
DR KEGG; hsa:54820; -.
DR MANE-Select; ENST00000396354.6; ENSP00000379642.1; NM_017668.3; NP_060138.1.
DR CTD; 54820; -.
DR DisGeNET; 54820; -.
DR GeneCards; NDE1; -.
DR HGNC; HGNC:17619; NDE1.
DR HPA; ENSG00000072864; Low tissue specificity.
DR MalaCards; NDE1; -.
DR MIM; 605013; phenotype.
DR MIM; 609449; gene.
DR MIM; 614019; phenotype.
DR neXtProt; NX_Q9NXR1; -.
DR OpenTargets; ENSG00000072864; -.
DR Orphanet; 2177; Hydranencephaly.
DR Orphanet; 89844; Lissencephaly syndrome, Norman-Roberts type.
DR Orphanet; 443162; NDE1-related microhydranencephaly.
DR PharmGKB; PA128394673; -.
DR VEuPathDB; HostDB:ENSG00000072864; -.
DR eggNOG; KOG1853; Eukaryota.
DR GeneTree; ENSGT00390000000111; -.
DR HOGENOM; CLU_057872_1_0_1; -.
DR InParanoid; Q9NXR1; -.
DR OMA; CERPATL; -.
DR PhylomeDB; Q9NXR1; -.
DR TreeFam; TF325693; -.
DR PathwayCommons; Q9NXR1; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; Q9NXR1; -.
DR SIGNOR; Q9NXR1; -.
DR BioGRID-ORCS; 54820; 329 hits in 1082 CRISPR screens.
DR ChiTaRS; NDE1; human.
DR GeneWiki; NDE1; -.
DR GenomeRNAi; 54820; -.
DR Pharos; Q9NXR1; Tbio.
DR PRO; PR:Q9NXR1; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9NXR1; protein.
DR Bgee; ENSG00000072864; Expressed in colonic epithelium and 104 other tissues.
DR ExpressionAtlas; Q9NXR1; baseline and differential.
DR Genevisible; Q9NXR1; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0031616; C:spindle pole centrosome; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0051298; P:centrosome duplication; ISS:UniProtKB.
DR GO; GO:0051642; P:centrosome localization; IBA:GO_Central.
DR GO; GO:0021987; P:cerebral cortex development; IMP:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; IBA:GO_Central.
DR GO; GO:0051303; P:establishment of chromosome localization; IMP:UniProtKB.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:UniProtKB.
DR GO; GO:0007020; P:microtubule nucleation; IBA:GO_Central.
DR GO; GO:0007100; P:mitotic centrosome separation; IBA:GO_Central.
DR GO; GO:0007405; P:neuroblast proliferation; IEA:Ensembl.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:0047496; P:vesicle transport along microtubule; IBA:GO_Central.
DR InterPro; IPR033494; NUDE.
DR InterPro; IPR006964; NUDE_dom.
DR PANTHER; PTHR10921; PTHR10921; 1.
DR Pfam; PF04880; NUDE_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division; Centromere;
KW Chromosome; Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein;
KW Differentiation; Kinetochore; Lipoprotein; Lissencephaly; Microtubule;
KW Mitosis; Neurogenesis; Palmitate; Phosphoprotein; Reference proteome.
FT CHAIN 1..335
FT /note="Nuclear distribution protein nudE homolog 1"
FT /id="PRO_0000240202"
FT REGION 1..93
FT /note="Self-association"
FT /evidence="ECO:0000250"
FT REGION 88..156
FT /note="Interaction with PAFAH1B1"
FT /evidence="ECO:0000250"
FT REGION 167..290
FT /note="Interaction with CENPF"
FT /evidence="ECO:0000250"
FT REGION 181..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 18..188
FT /evidence="ECO:0000255"
FT COMPBIAS 197..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 215
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 228
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 231
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 243
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 246
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT LIPID 274
FT /note="S-palmitoyl cysteine; by ZDHHC2, ZDHHC3 and ZDHHC7"
FT /evidence="ECO:0000269|PubMed:19927128"
FT VAR_SEQ 318..335
FT /note="DTSCRWLSKSTTRSSSSC -> GKRLEFGKPPSHMSSSPLPSAQGVVKMLL
FT (in isoform 2)"
FT /id="VSP_059512"
FT MUTAGEN 191
FT /note="T->E: Loss of centrosomal localization and reduced
FT ZNF365-binding; when associated with E-215; E-228; E-243;
FT E-246 and E-282."
FT /evidence="ECO:0000269|PubMed:16682949"
FT MUTAGEN 191
FT /note="T->V: Retained on spindle poles during mitosis, no
FT loss of phosphorylation in vivo and increased ZNF365-
FT binding; when associated with V-215; V-228; V-243; V-246
FT and A-282."
FT /evidence="ECO:0000269|PubMed:16682949"
FT MUTAGEN 215
FT /note="T->E: Loss of centrosomal localization and reduced
FT ZNF365-binding; when associated with E-191; E-228; E-243;
FT E-246 and E-282."
FT /evidence="ECO:0000269|PubMed:16682949"
FT MUTAGEN 215
FT /note="T->V: Retained on spindle poles during mitosis, no
FT loss of phosphorylation in vivo and increased ZNF365-
FT binding; when associated with V-191; V-228; V-243; V-246
FT and A-282."
FT /evidence="ECO:0000269|PubMed:16682949"
FT MUTAGEN 228
FT /note="T->E: Loss of centrosomal localization and reduced
FT ZNF365-binding; when associated with E-191; E-215; E-243;
FT E-246 and E-282."
FT /evidence="ECO:0000269|PubMed:16682949"
FT MUTAGEN 228
FT /note="T->V: Retained on spindle poles during mitosis, no
FT loss of phosphorylation in vivo and increased ZNF365-
FT binding; when associated with V-191; V-215; V-243; V-246
FT and A-282."
FT /evidence="ECO:0000269|PubMed:16682949"
FT MUTAGEN 243
FT /note="T->E: Loss of centrosomal localization and reduced
FT ZNF365-binding; when associated with E-191; E-215; E-228;
FT E-246 and E-282."
FT /evidence="ECO:0000269|PubMed:16682949"
FT MUTAGEN 243
FT /note="T->V: Retained on spindle poles during mitosis, no
FT loss of phosphorylation in vivo and increased ZNF365-
FT binding; when associated with V-191; V-215; V-228; V-246
FT and A-282."
FT /evidence="ECO:0000269|PubMed:16682949"
FT MUTAGEN 246
FT /note="T->E: Loss of centrosomal localization and reduced
FT ZNF365-binding; when associated with E-191; E-215; E-228;
FT E-243 and E-282."
FT /evidence="ECO:0000269|PubMed:16682949"
FT MUTAGEN 246
FT /note="T->V: Retained on spindle poles during mitosis, no
FT loss of phosphorylation in vivo and increased ZNF365-
FT binding; when associated with V-191; V-215; V-228; V-243
FT and A-282."
FT /evidence="ECO:0000269|PubMed:16682949"
FT MUTAGEN 282
FT /note="S->A: Retained on spindle poles during mitosis, no
FT loss of phosphorylation in vivo and increased ZNF365-
FT binding; when associated with V-191; V-215; V-228; V-243
FT and V-246."
FT /evidence="ECO:0000269|PubMed:16682949"
FT MUTAGEN 282
FT /note="S->E: Loss of centrosomal localization and reduced
FT ZNF365-binding; when associated with E-191; E-215; E-228;
FT E-243 and E-246."
FT /evidence="ECO:0000269|PubMed:16682949"
FT CONFLICT 191
FT /note="T -> I (in Ref. 3; AAH33900)"
FT /evidence="ECO:0000305"
FT HELIX 99..129
FT /evidence="ECO:0007829|PDB:7E1T"
SQ SEQUENCE 335 AA; 37721 MW; FC0BDD8BB90324B8 CRC64;
MEDSGKTFSS EEEEANYWKD LAMTYKQRAE NTQEELREFQ EGSREYEAEL ETQLQQIETR
NRDLLSENNR LRMELETIKE KFEVQHSEGY RQISALEDDL AQTKAIKDQL QKYIRELEQA
NDDLERAKRA TIMSLEDFEQ RLNQAIERNA FLESELDEKE NLLESVQRLK DEARDLRQEL
AVQQKQEKPR TPMPSSVEAE RTDTAVQATG SVPSTPIAHR GPSSSLNTPG SFRRGLDDST
GGTPLTPAAR ISALNIVGDL LRKVGALESK LASCRNLVYD QSPNRTGGPA SGRSSKNRDG
GERRPSSTSV PLGDKGLDTS CRWLSKSTTR SSSSC
