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 27-MAR-2024, entry version 182. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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. DR PDB; 7E1T; X-ray; 2.45 A; C/D=98-168. DR PDBsum; 7E1T; -. DR AlphaFoldDB; Q9NXR1; -. DR SMR; Q9NXR1; -. DR BioGRID; 120175; 128. DR IntAct; Q9NXR1; 51. 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; 9606-ENSP00000379643; -. DR PeptideAtlas; Q9NXR1; -. DR ProteomicsDB; 83120; -. [Q9NXR1-1] DR ProteomicsDB; 83121; -. [Q9NXR1-2] DR Pumba; Q9NXR1; -. DR Antibodypedia; 11751; 319 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 AGR; HGNC:17619; -. 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; AMRRTPI; -. DR OrthoDB; 2910907at2759; -. 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; 347 hits in 1160 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 105 other cell types or tissues. DR ExpressionAtlas; Q9NXR1; baseline and differential. 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: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 Gene3D; 6.10.250.1080; -; 1. DR InterPro; IPR033494; NUDE. DR InterPro; IPR006964; NUDE_dom. DR PANTHER; PTHR10921; NUCLEAR DISTRIBUTION PROTEIN NUDE HOMOLOG 1; 1. DR PANTHER; PTHR10921:SF2; NUCLEAR DISTRIBUTION PROTEIN NUDE HOMOLOG 1; 1. DR Pfam; PF04880; NUDE_C; 1. DR Genevisible; Q9NXR1; HS. 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 FT ZNF365-binding; when associated with V-215; V-228; V-243; FT V-246 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 FT ZNF365-binding; when associated with V-191; V-228; V-243; FT V-246 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 FT ZNF365-binding; when associated with V-191; V-215; V-243; FT V-246 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 FT ZNF365-binding; when associated with V-191; V-215; V-228; FT V-246 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 FT ZNF365-binding; when associated with V-191; V-215; V-228; FT V-243 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 FT ZNF365-binding; when associated with V-191; V-215; V-228; FT V-243 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 //