ID NDEL1_HUMAN Reviewed; 345 AA. AC Q9GZM8; B3KP93; D3DTS0; J3QT32; Q86T80; Q8TAR7; Q9UH50; DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 02-SEP-2026, entry version 190. DE RecName: Full=Nuclear distribution protein nudE-like 1; DE Short=Protein Nudel; DE AltName: Full=Mitosin-associated protein 1; GN Name=NDEL1; Synonyms=EOPA, MITAP1, NUDEL; 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 [MRNA] (ISOFORM 1), INTERACTION WITH DYNEIN AND RP PAFAH1B1, SUBCELLULAR LOCATION, PHOSPHORYLATION BY CDK5, AND MUTAGENESIS OF RP SER-198; THR-219 AND SER-231. RC TISSUE=Brain; 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 [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH RP PAFAH1B1, SUBCELLULAR LOCATION, PHOSPHORYLATION BY CDK1 AND MAPK1, AND RP MUTAGENESIS OF SER-198; THR-219; SER-231; SER-242 AND THR-245. 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PUTATIVE FUNCTION AS AN RP OLIGOPEPTIDASE, INTERACTION WITH DISC1, AND MUTAGENESIS OF CYS-273. RC TISSUE=Brain; RX PubMed=15728732; DOI=10.1073/pnas.0500330102; RA Hayashi M.A.F., Portaro F.C.V., Bastos M.F., Guerreiro J.R., Oliveira V., RA Gorrao S.S., Tambourgi D.V., Sant'Anna O.A., Whiting P.J., Camargo L.M., RA Konno K., Brandon N.J., de Camargo A.C.M.; RT "Inhibition of NUDEL (nuclear distribution element-like)-oligopeptidase RT activity by disrupted-in-schizophrenia 1."; RL Proc. Natl. Acad. Sci. U.S.A. 102:3828-3833(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 152-328 (ISOFORM 3). RC TISSUE=Caudate nucleus; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Spinal cord; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC 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 [9] RP INTERACTION WITH DISC1, AND SUBCELLULAR LOCATION. RX PubMed=12812986; DOI=10.1093/hmg/ddg162; RA Morris J.A., Kandpal G., Ma L., Austin C.P.; RT "DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated protein RT that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL: regulation and loss of RT interaction with mutation."; RL Hum. Mol. Genet. 12:1591-1608(2003). RN [10] RP INTERACTION WITH DISC1. RX PubMed=12506198; DOI=10.1073/pnas.0136913100; RA Ozeki Y., Tomoda T., Kleiderlein J., Kamiya A., Bord L., Fujii K., RA Okawa M., Yamada N., Hatten M.E., Snyder S.H., Ross C.A., Sawa A.; RT "Disrupted-in-Schizophrenia-1 (DISC-1): mutant truncation prevents binding RT to NudE-like (NUDEL) and inhibits neurite outgrowth."; RL Proc. Natl. Acad. Sci. U.S.A. 100:289-294(2003). RN [11] RP ERRATUM OF PUBMED:12506198. RA Ozeki Y., Tomoda T., Kleiderlein J., Kamiya A., Bord L., Fujii K., RA Okawa M., Yamada N., Hatten M.E., Snyder S.H., Ross C.A., Sawa A.; RL Proc. Natl. Acad. Sci. U.S.A. 101:13969-13969(2004). RN [12] RP FUNCTION, SELF-ASSOCIATION, INTERACTION WITH DYNACTIN; DYNEIN AND PAFAH1B1, RP AND SUBCELLULAR LOCATION. RX PubMed=14970193; DOI=10.1083/jcb.200308058; RA Liang Y., Yu W., Li Y., Yang Z., Yan X., Huang Q., Zhu X.; RT "Nudel functions in membrane traffic mainly through association with Lis1 RT and cytoplasmic dynein."; RL J. Cell Biol. 164:557-566(2004). RN [13] RP INTERACTION WITH DISC1. 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 [14] RP SELF-ASSOCIATION, AND INTERACTION WITH PAFAH1B1. RX PubMed=15572112; DOI=10.1016/j.neuron.2004.11.019; RA Tarricone C., Perrina F., Monzani S., Massimiliano L., Kim M.-H., RA Derewenda Z.S., Knapp S., Tsai L.-H., Musacchio A.; RT "Coupling PAF signaling to dynein regulation: structure of LIS1 in complex RT with PAF-acetylhydrolase."; RL Neuron 44:809-821(2004). RN [15] RP TISSUE SPECIFICITY. RX PubMed=16005531; DOI=10.1016/j.bbaexp.2005.06.001; RA Guerreiro J.R., Winnischofer S.M.B., Bastos M.F., Portaro F.C.V., RA Sogayar M.C., de Camargo A.C.M., Hayashi M.A.F.; RT "Cloning and characterization of the human and rabbit NUDEL-oligopeptidase RT promoters and their negative regulation."; RL Biochim. Biophys. Acta 1730:77-84(2005). RN [16] RP INTERACTION WITH KATNA1 AND KATNB1, SUBCELLULAR LOCATION, DEVELOPMENTAL RP STAGE, AND PHOSPHORYLATION. 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 [17] RP INTERACTION WITH DISC1, AND MUTAGENESIS OF LEU-266 AND GLU-267. RX PubMed=17035248; DOI=10.1093/hmg/ddl407; RA Kamiya A., Tomoda T., Chang J., Takaki M., Zhan C., Morita M., Cascio M.B., RA Elashvili S., Koizumi H., Takanezawa Y., Dickerson F., Yolken R., Arai H., RA Sawa A.; RT "DISC1-NDEL1/NUDEL protein interaction, an essential component for neurite RT outgrowth, is modulated by genetic variations of DISC1."; RL Hum. Mol. Genet. 15:3313-3323(2006). RN [18] RP FUNCTION, INTERACTION WITH DYNACTIN; TUBULIN GAMMA; PAFAH1B1; PCM1; PCNT, RP AND SUBCELLULAR LOCATION. 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 [19] RP INTERACTION WITH ZNF365. 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 [20] 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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; THR-219 AND THR-245, AND RP IDENTIFICATION BY MASS 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 [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [23] RP PALMITOYLATION AT CYS-273 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 [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; THR-219; SER-242 AND RP THR-245, AND 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 [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215 AND SER-231, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [26] RP FUNCTION, AND INTERACTION WITH RAB9A. RX PubMed=34793709; DOI=10.1016/j.str.2021.10.013; RA Zhang Y., Chen Z., Wang F., Sun H., Zhu X., Ding J., Zhang T.; RT "Nde1 is a Rab9 effector for loading late endosomes to cytoplasmic dynein RT motor complex."; RL Structure 30:386-395.e5(2022). 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 (By CC similarity). Plays a role, together with DISC1, in the regulation of CC neurite outgrowth (By similarity). May act as a RAB9A/B effector that CC tethers RAB9-associated late endosomes to the dynein motor for their CC retrograde transport to the trans-Golgi network (PubMed:34793709). CC {ECO:0000250|UniProtKB:Q78PB6, ECO:0000250|UniProtKB:Q9ERR1, CC ECO:0000269|PubMed:12556484, ECO:0000269|PubMed:14970193, CC ECO:0000269|PubMed:16291865, ECO:0000269|PubMed:17600710, CC ECO:0000269|PubMed:34793709}. CC -!- SUBUNIT: Interacts with PLEKHM1 (via N- and C-terminus) (By CC similarity). Interacts with YWHAE. Interacts directly with NEFL and CC indirectly with NEFH. Interacts with microtubules (By similarity). CC Self-associates. Interacts with DISC1, dynein, dynactin, tubulin gamma, CC KATNA1, KATNB1, PAFAH1B1, PCM1 and PCNT. Interacts (via C-terminus) CC with CENPF. Interacts with ZNF365. Interacts with GTP-bound RAB9A; the CC interaction may lead to RAB9A-dynein motor tethering (PubMed:34793709). CC {ECO:0000250, ECO:0000250|UniProtKB:Q9ERR1, CC ECO:0000269|PubMed:11163260, ECO:0000269|PubMed:12506198, CC ECO:0000269|PubMed:12556484, ECO:0000269|PubMed:12812986, CC ECO:0000269|PubMed:14962739, ECO:0000269|PubMed:14970193, CC ECO:0000269|PubMed:15572112, ECO:0000269|PubMed:15728732, CC ECO:0000269|PubMed:16203747, ECO:0000269|PubMed:16291865, CC ECO:0000269|PubMed:16682949, ECO:0000269|PubMed:17035248, CC ECO:0000269|PubMed:17600710, ECO:0000269|PubMed:34793709}. CC -!- INTERACTION: CC Q9GZM8; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-928842, EBI-742038; CC Q9GZM8; Q13155: AIMP2; NbExp=3; IntAct=EBI-928842, EBI-745226; CC Q9GZM8; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-928842, EBI-2548012; CC Q9GZM8; P35226: BMI1; NbExp=3; IntAct=EBI-928842, EBI-2341576; CC Q9GZM8; Q96GS4: BORCS6; NbExp=6; IntAct=EBI-928842, EBI-10193358; CC Q9GZM8; Q8WUW1: BRK1; NbExp=9; IntAct=EBI-928842, EBI-2837444; CC Q9GZM8; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-928842, EBI-10175300; CC Q9GZM8; Q9C0I3: CCSER1; NbExp=5; IntAct=EBI-928842, EBI-1104948; CC Q9GZM8; Q9H7U1: CCSER2; NbExp=6; IntAct=EBI-928842, EBI-714702; CC Q9GZM8; P49454: CENPF; NbExp=6; IntAct=EBI-928842, EBI-968343; CC Q9GZM8; Q66GS9: CEP135; NbExp=5; IntAct=EBI-928842, EBI-1046993; CC Q9GZM8; P28329-3: CHAT; NbExp=3; IntAct=EBI-928842, EBI-25837549; CC Q9GZM8; Q5SYC1: CLVS2; NbExp=3; IntAct=EBI-928842, EBI-12357161; CC Q9GZM8; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-928842, EBI-5453285; CC Q9GZM8; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-928842, EBI-742054; CC Q9GZM8; Q9NRI5: DISC1; NbExp=17; IntAct=EBI-928842, EBI-529989; CC Q9GZM8; Q9NRI5-1: DISC1; NbExp=4; IntAct=EBI-928842, EBI-15881455; CC Q9GZM8; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-928842, EBI-11988027; CC Q9GZM8; Q155Q3: DIXDC1; NbExp=6; IntAct=EBI-928842, EBI-1104700; CC Q9GZM8; O60941: DTNB; NbExp=3; IntAct=EBI-928842, EBI-740402; CC Q9GZM8; P22607: FGFR3; NbExp=3; IntAct=EBI-928842, EBI-348399; CC Q9GZM8; Q08379: GOLGA2; NbExp=3; IntAct=EBI-928842, EBI-618309; CC Q9GZM8; P06396: GSN; NbExp=3; IntAct=EBI-928842, EBI-351506; CC Q9GZM8; P01112: HRAS; NbExp=3; IntAct=EBI-928842, EBI-350145; CC Q9GZM8; Q16891-1: IMMT; NbExp=4; IntAct=EBI-928842, EBI-11614103; CC Q9GZM8; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-928842, EBI-2125614; CC Q9GZM8; Q6A162: KRT40; NbExp=5; IntAct=EBI-928842, EBI-10171697; CC Q9GZM8; Q9NS73-5: MBIP; NbExp=3; IntAct=EBI-928842, EBI-10182361; CC Q9GZM8; Q9P086: MED11; NbExp=3; IntAct=EBI-928842, EBI-394704; CC Q9GZM8; Q9NYP9: MIS18A; NbExp=5; IntAct=EBI-928842, EBI-1104552; CC Q9GZM8; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-928842, EBI-742948; CC Q9GZM8; O14777: NDC80; NbExp=4; IntAct=EBI-928842, EBI-715849; CC Q9GZM8; Q9NXR1: NDE1; NbExp=6; IntAct=EBI-928842, EBI-941227; CC Q9GZM8; Q9GZM8: NDEL1; NbExp=14; IntAct=EBI-928842, EBI-928842; CC Q9GZM8; Q7Z3B4: NUP54; NbExp=4; IntAct=EBI-928842, EBI-741048; CC Q9GZM8; P43034: PAFAH1B1; NbExp=7; IntAct=EBI-928842, EBI-720620; CC Q9GZM8; Q9HBI0: PARVG; NbExp=3; IntAct=EBI-928842, EBI-3921217; CC Q9GZM8; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-928842, EBI-79165; CC Q9GZM8; Q99959: PKP2; NbExp=4; IntAct=EBI-928842, EBI-702235; CC Q9GZM8; Q99959-2: PKP2; NbExp=3; IntAct=EBI-928842, EBI-10987518; CC Q9GZM8; P49023-2: PXN; NbExp=5; IntAct=EBI-928842, EBI-11954250; CC Q9GZM8; O75971: SNAPC5; NbExp=3; IntAct=EBI-928842, EBI-749483; CC Q9GZM8; O75971-2: SNAPC5; NbExp=3; IntAct=EBI-928842, EBI-12004298; CC Q9GZM8; Q9Y6A5: TACC3; NbExp=3; IntAct=EBI-928842, EBI-2554984; CC Q9GZM8; Q9Y228: TRAF3IP3; NbExp=6; IntAct=EBI-928842, EBI-765817; CC Q9GZM8; P14373: TRIM27; NbExp=10; IntAct=EBI-928842, EBI-719493; CC Q9GZM8; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-928842, EBI-741480; CC Q9GZM8; O75604: USP2; NbExp=6; IntAct=EBI-928842, EBI-743272; CC Q9GZM8; P23025: XPA; NbExp=6; IntAct=EBI-928842, EBI-295222; CC Q9GZM8; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-928842, EBI-14104088; CC Q9GZM8; P17014: ZNF12; NbExp=3; IntAct=EBI-928842, EBI-11278550; CC Q9GZM8; Q9UJW8: ZNF180; NbExp=4; IntAct=EBI-928842, EBI-10322527; CC Q9GZM8; P15622-3: ZNF250; NbExp=5; IntAct=EBI-928842, EBI-10177272; CC Q9GZM8; Q3ZCT1: ZNF260; NbExp=3; IntAct=EBI-928842, EBI-10241410; CC Q9GZM8; Q14C61: ZNF264; NbExp=3; IntAct=EBI-928842, EBI-2826570; CC Q9GZM8; P17036: ZNF3; NbExp=3; IntAct=EBI-928842, EBI-1640965; CC Q9GZM8; P13682: ZNF35; NbExp=3; IntAct=EBI-928842, EBI-11041653; CC Q9GZM8; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-928842, EBI-740727; CC Q9GZM8; P59923: ZNF445; NbExp=3; IntAct=EBI-928842, EBI-2849229; CC Q9GZM8; Q9ULM2: ZNF490; NbExp=6; IntAct=EBI-928842, EBI-1105370; CC Q9GZM8; Q6NX49: ZNF544; NbExp=5; IntAct=EBI-928842, EBI-2841978; CC Q9GZM8; Q68EA5: ZNF57; NbExp=3; IntAct=EBI-928842, EBI-8490788; CC Q9GZM8; Q7Z3I7: ZNF572; NbExp=3; IntAct=EBI-928842, EBI-10172590; CC Q9GZM8; Q96NL3: ZNF599; NbExp=6; IntAct=EBI-928842, EBI-8653994; CC Q9GZM8; Q6ZS27-3: ZNF662; NbExp=3; IntAct=EBI-928842, EBI-10255155; CC Q9GZM8; Q96C28: ZNF707; NbExp=3; IntAct=EBI-928842, EBI-748111; CC Q9GZM8; Q08AG5: ZNF844; NbExp=6; IntAct=EBI-928842, EBI-10225757; CC Q9GZM8; P63005: Pafah1b1; Xeno; NbExp=4; IntAct=EBI-928842, EBI-917499; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, CC microtubule organizing center, centrosome. Chromosome, centromere, CC kinetochore. Cytoplasm, cytoskeleton, spindle. Note=Localizes to the CC cell body of the motor neurons and colocalizes with assembled CC neurofilaments within axonal processes. Localizes to the microtubules CC of the manchette in elongated spermatids. Colocalizes with DISC1 in the CC perinuclear region, including the centrosome (By similarity). Localizes CC to the interphase centrosome and the mitotic spindle. Localizes to the CC kinetochore in a CENPF-dependent manner. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9GZM8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9GZM8-2; Sequence=VSP_019310; CC Name=3; CC IsoId=Q9GZM8-3; Sequence=VSP_047509; CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung, CC pancreas, placenta and skeletal muscle. {ECO:0000269|PubMed:16005531}. CC -!- DEVELOPMENTAL STAGE: Expression peaks in mitosis. CC {ECO:0000269|PubMed:16203747}. CC -!- PTM: Phosphorylated in mitosis. Can be phosphorylated by CDK1, CDK5 and CC MAPK1. Phosphorylation by CDK5 promotes interaction with KATNA1 and CC YWHAE. {ECO:0000269|PubMed:11163260, ECO:0000269|PubMed:12556484, CC ECO:0000269|PubMed:16203747}. CC -!- PTM: Palmitoylation at Cys-273 reduces affinity for dynein. CC {ECO:0000269|PubMed:19927128}. CC -!- SIMILARITY: Belongs to the nudE family. {ECO:0000305}. CC -!- CAUTION: Was originally thought to function as an oligopeptidase CC (NUDEL-oligopeptidase or endooligopeptidase A) which could regulate CC peptide levels relevant to brain function. CC {ECO:0000305|PubMed:15728732}. 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; AY004871; AAF97497.1; -; mRNA. DR EMBL; AF182078; AAG43425.1; -; mRNA. DR EMBL; AF217798; AAF24516.3; -; mRNA. DR EMBL; AK056014; BAG51605.1; -; mRNA. DR EMBL; DA256375; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AL832648; CAD89957.3; -; mRNA. DR EMBL; AC026130; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471108; EAW90051.1; -; Genomic_DNA. DR EMBL; CH471108; EAW90052.1; -; Genomic_DNA. DR EMBL; BC026101; AAH26101.1; -; mRNA. DR CCDS; CCDS11143.1; -. [Q9GZM8-1] DR CCDS; CCDS32564.1; -. [Q9GZM8-3] DR RefSeq; NP_001020750.1; NM_001025579.3. [Q9GZM8-3] DR RefSeq; NP_110435.1; NM_030808.5. [Q9GZM8-1] DR RefSeq; XP_047292817.1; XM_047436861.1. [Q9GZM8-1] DR RefSeq; XP_054173423.1; XM_054317448.1. [Q9GZM8-1] DR PDB; 2V66; X-ray; 2.10 A; B/C/D/E=58-168. DR AlphaFoldDB; Q9GZM8; -. DR SMR; Q9GZM8; -. DR BioGRID; 123527; 168. DR DIP; DIP-29554N; -. DR FunCoup; Q9GZM8; 1400. DR IntAct; Q9GZM8; 179. DR MINT; Q9GZM8; -. DR NDEx; IQUERY-CP-NDEL1; 5 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000333982; -. DR MoonDB; Q9GZM8; Predicted. DR GlyGen; Q9GZM8; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9GZM8; -. DR PhosphoSitePlus; Q9GZM8; -. DR SwissPalm; Q9GZM8; -. DR BioMuta; NDEL1; -. DR DMDM; 74725006; -. DR jPOST; Q9GZM8; -. DR MassIVE; Q9GZM8; -. DR PaxDb; 9606-ENSP00000333982; -. DR PeptideAtlas; Q9GZM8; -. DR ProteomicsDB; 80092; -. [Q9GZM8-1] DR ProteomicsDB; 80093; -. [Q9GZM8-2] DR Pumba; Q9GZM8; -. DR Antibodypedia; 12558; 509 antibodies from 40 providers. DR DNASU; 81565; -. DR Ensembl; ENST00000334527.12; ENSP00000333982.7; ENSG00000166579.17. [Q9GZM8-1] DR Ensembl; ENST00000402554.7; ENSP00000384963.3; ENSG00000166579.17. [Q9GZM8-3] DR Ensembl; ENST00000852238.1; ENSP00000522297.1; ENSG00000166579.17. [Q9GZM8-1] DR Ensembl; ENST00000852239.1; ENSP00000522298.1; ENSG00000166579.17. [Q9GZM8-1] DR Ensembl; ENST00000852243.1; ENSP00000522302.1; ENSG00000166579.17. [Q9GZM8-1] DR Ensembl; ENST00000852244.1; ENSP00000522303.1; ENSG00000166579.17. [Q9GZM8-1] DR Ensembl; ENST00000852246.1; ENSP00000522305.1; ENSG00000166579.17. [Q9GZM8-1] DR Ensembl; ENST00000852247.1; ENSP00000522306.1; ENSG00000166579.17. [Q9GZM8-1] DR Ensembl; ENST00000916784.1; ENSP00000586843.1; ENSG00000166579.17. [Q9GZM8-1] DR Ensembl; ENST00000916785.1; ENSP00000586844.1; ENSG00000166579.17. [Q9GZM8-1] DR Ensembl; ENST00000953597.1; ENSP00000623656.1; ENSG00000166579.17. [Q9GZM8-1] DR Ensembl; ENST00000953599.1; ENSP00000623658.1; ENSG00000166579.17. [Q9GZM8-1] DR Ensembl; ENST00000953600.1; ENSP00000623659.1; ENSG00000166579.17. [Q9GZM8-1] DR GeneID; 81565; -. DR KEGG; hsa:81565; -. DR MANE-Select; ENST00000334527.12; ENSP00000333982.7; NM_030808.5; NP_110435.1. DR UCSC; uc002gli.5; human. [Q9GZM8-1] DR AGR; HGNC:17620; -. DR ClinPGx; PA134887314; -. DR CTD; 81565; -. DR DisGeNET; 81565; -. DR GeneCards; NDEL1; -. DR HGNC; HGNC:17620; NDEL1. DR HPA; ENSG00000166579; Low tissue specificity. DR MIM; 607538; gene. DR OpenTargets; ENSG00000166579; -. DR VEuPathDB; HostDB:ENSG00000166579; -. DR eggNOG; KOG1853; Eukaryota. DR GeneTree; ENSGT00390000000111; -. DR HOGENOM; CLU_057872_1_0_1; -. DR InParanoid; Q9GZM8; -. DR OMA; KTYREHA; -. DR OrthoDB; 5877028at2759; -. DR PAN-GO; Q9GZM8; 13 GO annotations based on evolutionary models. DR PhylomeDB; Q9GZM8; -. DR PathwayCommons; Q9GZM8; -. 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-5663220; RHO GTPases Activate Formins. DR Reactome; R-HSA-68877; Mitotic Prometaphase. DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation. DR SignaLink; Q9GZM8; -. DR SIGNOR; Q9GZM8; -. DR Agora; ENSG00000166579; -. DR BioGRID-ORCS; 81565; 16 hits in 1164 CRISPR screens. DR CD-CODE; 232F8A39; P-body. DR CD-CODE; 8C2F96ED; Centrosome. DR CD-CODE; DEE660B4; Stress granule. DR ChiTaRS; NDEL1; human. DR EvolutionaryTrace; Q9GZM8; -. DR GeneWiki; NDEL1; -. DR GenomeRNAi; 81565; -. DR Pharos; Q9GZM8; Tbio. DR PRO; PR:Q9GZM8; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q9GZM8; protein. DR Bgee; ENSG00000166579; Expressed in adrenal tissue and 205 other cell types or tissues. DR ExpressionAtlas; Q9GZM8; baseline and differential. DR GO; GO:0043203; C:axon hillock; IEA:Ensembl. DR GO; GO:0031252; C:cell leading edge; IEA:Ensembl. DR GO; GO:0005813; C:centrosome; IBA:GO_Central. 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:0060053; C:neurofilament cytoskeleton; IEA:Ensembl. DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell. DR GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl. DR GO; GO:0043014; F:alpha-tubulin binding; IEA:Ensembl. DR GO; GO:0048487; F:beta-tubulin binding; IEA:Ensembl. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central. DR GO; GO:0016477; P:cell migration; IBA:GO_Central. DR GO; GO:0051642; P:centrosome localization; IBA:GO_Central. DR GO; GO:0021799; P:cerebral cortex radially oriented cell migration; IEA:Ensembl. DR GO; GO:0050000; P:chromosome localization; IBA:GO_Central. DR GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB. DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IBA:GO_Central. DR GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl. DR GO; GO:0032418; P:lysosome localization; ISS: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:0043547; P:positive regulation of GTPase activity; IMP:CACAO. DR GO; GO:1900029; P:positive regulation of ruffle assembly; ISS:UniProtKB. DR GO; GO:0033157; P:regulation of intracellular protein transport; IMP:CACAO. DR GO; GO:0010975; P:regulation of neuron projection development; IBA:GO_Central. 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:SF0; NUCLEAR DISTRIBUTION PROTEIN NUDE-LIKE 1; 1. DR Pfam; PF04880; NUDE_C; 1. DR PDBsum; 2V66; -. 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; Proteomics identification; Reference proteome; Transport. FT CHAIN 1..345 FT /note="Nuclear distribution protein nudE-like 1" FT /id="PRO_0000240210" FT REGION 56..166 FT /note="Self-association" FT /evidence="ECO:0000250" FT REGION 64..189 FT /note="Interaction with KATNB1" FT /evidence="ECO:0000250" FT REGION 114..133 FT /note="Required for interaction with PAFAH1B1" FT REGION 175..345 FT /note="Interaction with CENPF" FT /evidence="ECO:0000269|PubMed:17600710" FT REGION 189..256 FT /note="Interaction with YWHAE" FT /evidence="ECO:0000250" FT REGION 191..345 FT /note="Interaction with NEFL" FT /evidence="ECO:0000250" FT REGION 195..256 FT /note="Interaction with KATNA1" FT /evidence="ECO:0000250" FT REGION 241..280 FT /note="Interaction with DISC1" 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:0000269|PubMed:16291865" FT REGION 315..345 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 28..190 FT /evidence="ECO:0000255" FT COMPBIAS 329..339 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 215 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 219 FT /note="Phosphothreonine; by CDK1 and MAPK1" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 231 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 242 FT /note="Phosphoserine; by CDK1" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 245 FT /note="Phosphothreonine; by CDK1 and MAPK1" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" 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:0000269|PubMed:19927128" FT VAR_SEQ 316..345 FT /note="AVNGFDPAPPPPGLGSSRPSSAPGMLPLSV -> SSSSCAIRASRRRFSSSS FT ADLAGRGGGDGSIPAQHSTGASGKAPPPTLLLET (in isoform 2)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_019310" FT VAR_SEQ 316..345 FT /note="AVNGFDPAPPPPGLGSSRPSSAPGMLPLSV -> QEKVIFPTLFMGQ (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_047509" FT MUTAGEN 198 FT /note="S->A: Abrogates mitotic phosphorylation; when FT associated with V-219; A-231; A-242 and V-245. Abrogates FT phosphorylation by CDK5; when associated with A-219 and FT A-231." FT /evidence="ECO:0000269|PubMed:11163260, FT ECO:0000269|PubMed:12556484" FT MUTAGEN 198 FT /note="S->E: Enhances interaction with PAFAH1B1 and impairs FT centrosomal localization; when associated with E-219; FT E-231; E-242 and E-245." FT /evidence="ECO:0000269|PubMed:11163260, FT ECO:0000269|PubMed:12556484" FT MUTAGEN 219 FT /note="T->A: Abrogates phosphorylation by CDK5; when FT associated with A-198 and A-231." FT /evidence="ECO:0000269|PubMed:11163260, FT ECO:0000269|PubMed:12556484" FT MUTAGEN 219 FT /note="T->E: Enhances interaction with PAFAH1B1 and impairs FT centrosomal localization; when associated with E-198; FT E-231; E-242 and E-245." FT /evidence="ECO:0000269|PubMed:11163260, FT ECO:0000269|PubMed:12556484" FT MUTAGEN 219 FT /note="T->V: Abrogates mitotic phosphorylation; when FT associated with A-198; A-231; A-242 and V-245." FT /evidence="ECO:0000269|PubMed:11163260, FT ECO:0000269|PubMed:12556484" FT MUTAGEN 231 FT /note="S->A: Abrogates mitotic phosphorylation; when FT associated with A-198; V-219; A-242 and V-245. Abrogates FT phosphorylation by CDK5; when associated with A-198 and FT A-219." FT /evidence="ECO:0000269|PubMed:11163260, FT ECO:0000269|PubMed:12556484" FT MUTAGEN 231 FT /note="S->E: Enhances interaction with PAFAH1B1 and impairs FT centrosomal localization; when associated with E-198; FT E-219; E-242 and E-245." FT /evidence="ECO:0000269|PubMed:11163260, FT ECO:0000269|PubMed:12556484" FT MUTAGEN 242 FT /note="S->A: Abrogates mitotic phosphorylation; when FT associated with A-198; V-219; A-231 and V-245." FT /evidence="ECO:0000269|PubMed:12556484" FT MUTAGEN 242 FT /note="S->E: Enhances interaction with PAFAH1B1 and impairs FT centrosomal localization; when associated with E-198; FT E-219; E-231 and E-245." FT /evidence="ECO:0000269|PubMed:12556484" FT MUTAGEN 245 FT /note="T->E: Enhances interaction with PAFAH1B1 and impairs FT centrosomal localization; when associated with E-198; FT E-219; E-231 and E-242." FT /evidence="ECO:0000269|PubMed:12556484" FT MUTAGEN 245 FT /note="T->V: Abrogates mitotic phosphorylation; when FT associated with A-198; V-219; A-231 and A-242." FT /evidence="ECO:0000269|PubMed:12556484" FT MUTAGEN 266 FT /note="L->A: Abolishes interaction with DISC1; when FT associated with A-267." FT /evidence="ECO:0000269|PubMed:17035248" FT MUTAGEN 267 FT /note="E->A: Abolishes interaction with DISC1; when FT associated with A-266." FT /evidence="ECO:0000269|PubMed:17035248" FT MUTAGEN 273 FT /note="C->A: Abolishes oligopeptidase activity." FT /evidence="ECO:0000269|PubMed:15728732" FT CONFLICT 322 FT /note="P -> T (in Ref. 8; AAH26101)" FT /evidence="ECO:0000305" FT HELIX 59..165 FT /evidence="ECO:0007829|PDB:2V66" SQ SEQUENCE 345 AA; 38375 MW; E91EA053FCA315D7 CRC64; MDGEDIPDFS SLKEETAYWK ELSLKYKQSF QEARDELVEF QEGSRELEAE LEAQLVQAEQ RNRDLQADNQ RLKYEVEALK EKLEHQYAQS YKQVSVLEDD LSQTRAIKEQ LHKYVRELEQ ANDDLERAKR ATIVSLEDFE QRLNQAIERN AFLESELDEK ESLLVSVQRL KDEARDLRQE LAVRERQQEV TRKSAPSSPT LDCEKMDSAV QASLSLPATP VGKGTENTFP SPKAIPNGFG TSPLTPSARI SALNIVGDLL RKVGALESKL AACRNFAKDQ ASRKSYISGN VNCGVLNGNG TKFSRSGHTS FFDKGAVNGF DPAPPPPGLG SSRPSSAPGM LPLSV //