NUDC_HUMAN
ID NUDC_HUMAN Reviewed; 331 AA.
AC Q9Y266; Q5QP31; Q5QP35; Q9H0N2; Q9Y2B6;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Nuclear migration protein nudC;
DE AltName: Full=Nuclear distribution protein C homolog;
GN Name=NUDC;
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], INDUCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=10210332; DOI=10.1016/s0301-472x(98)00074-5;
RA Miller B.A., Zhang M.-Y., Gocke C.D., De Souza C., Osmani A.H., Lynch C.,
RA Davies J., Bell L., Osmani S.A.;
RT "A homolog of the fungal nuclear migration gene nudC is involved in normal
RT and malignant human hematopoiesis.";
RL Exp. Hematol. 27:742-750(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10453739; DOI=10.1007/s004390050994;
RA Matsumoto N., Ledbetter D.H.;
RT "Molecular cloning and characterization of the human NUDC gene.";
RL Hum. Genet. 104:498-504(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pituitary;
RA Song H., Peng Y., Dai M., Huang Q., Mao Y., Zhang Q., Mao M., Fu G.,
RA Luo M., Chen J., Hu R.;
RT "Human MNUDC protein gene.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Periodontal ligament;
RA Yamamoto T., Takashiba S., Myokai F., Washio N., Nishimura F., Arai H.,
RA Murayama Y.;
RT "Unique genes expressed in fibroblasts of periodontal ligament.";
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Li N.G., Yu L., Tu Q., Fu Q., Wang X.K., Zhao S.Y.;
RT "Cloning and characterization of a novel human cDNA homology to murine SIG-
RT 92 mRNA.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, Kidney, Lung, and Skin;
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 FUNCTION, INTERACTION WITH PLK1, IDENTIFICATION IN A COMPLEX WITH DYNACTIN
RP AND DYNEIN, MUTAGENESIS OF SER-274 AND SER-326, AND PHOSPHORYLATION AT
RP SER-274 AND SER-326.
RX PubMed=12852857; DOI=10.1016/s1534-5807(03)00186-2;
RA Zhou T., Aumais J.P., Liu X., Yu-Lee L.-Y., Erikson R.L.;
RT "A role for Plk1 phosphorylation of NudC in cytokinesis.";
RL Dev. Cell 5:127-138(2003).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12679384; DOI=10.1242/jcs.00412;
RA Aumais J.P., Williams S.N., Luo W., Nishino M., Caldwell K.A.,
RA Caldwell G.A., Lin S.-H., Yu-Lee L.-Y.;
RT "Role for NudC, a dynein-associated nuclear movement protein, in mitosis
RT and cytokinesis.";
RL J. Cell Sci. 116:1991-2003(2003).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139 AND THR-145, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139 AND THR-145, 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 [13]
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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-239, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108; SER-139 AND THR-145, 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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP INTERACTION WITH DCDC1.
RX PubMed=22159412; DOI=10.1242/jcs.085407;
RA Kaplan A., Reiner O.;
RT "Linking cytoplasmic dynein and transport of Rab8 vesicles to the midbody
RT during cytokinesis by the doublecortin domain-containing 5 protein.";
RL J. Cell Sci. 124:3989-4000(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; THR-108; SER-136;
RP SER-139; THR-145; SER-259; SER-260; SER-277; SER-285 AND SER-298, 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 [20]
RP IDENTIFICATION BY 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).
RN [21]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH EML4.
RX PubMed=25789526; DOI=10.1080/15384101.2015.1026514;
RA Chen D., Ito S., Yuan H., Hyodo T., Kadomatsu K., Hamaguchi M., Senga T.;
RT "EML4 promotes the loading of NUDC to the spindle for mitotic
RT progression.";
RL Cell Cycle 14:1529-1539(2015).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Plays a role in neurogenesis and neuronal migration (By
CC similarity). Necessary for correct formation of mitotic spindles and
CC chromosome separation during mitosis (PubMed:12852857, PubMed:12679384,
CC PubMed:25789526). Necessary for cytokinesis and cell proliferation
CC (PubMed:12852857, PubMed:12679384). {ECO:0000250|UniProtKB:O35685,
CC ECO:0000269|PubMed:12679384, ECO:0000269|PubMed:12852857,
CC ECO:0000269|PubMed:25789526}.
CC -!- SUBUNIT: Interacts with PAFAH1B1 (By similarity). Interacts with PLK1
CC (PubMed:12852857). Part of a complex containing PLK1, NUDC, dynein and
CC dynactin (PubMed:12852857). Interacts with DCDC1 (PubMed:22159412).
CC Interacts with EML4 (via WD repeats) (PubMed:25789526).
CC {ECO:0000250|UniProtKB:O35685, ECO:0000269|PubMed:12852857,
CC ECO:0000269|PubMed:22159412, ECO:0000269|PubMed:25789526}.
CC -!- INTERACTION:
CC Q9Y266; Q86V38: ATN1; NbExp=3; IntAct=EBI-357298, EBI-11954292;
CC Q9Y266; P02489: CRYAA; NbExp=3; IntAct=EBI-357298, EBI-6875961;
CC Q9Y266; O60884: DNAJA2; NbExp=2; IntAct=EBI-357298, EBI-352957;
CC Q9Y266; Q8WVS4: DYNC2I1; NbExp=3; IntAct=EBI-357298, EBI-2556085;
CC Q9Y266; Q9UKT8: FBXW2; NbExp=2; IntAct=EBI-357298, EBI-914727;
CC Q9Y266; O14908-2: GIPC1; NbExp=3; IntAct=EBI-357298, EBI-25913156;
CC Q9Y266; Q8TC44: POC1B; NbExp=3; IntAct=EBI-357298, EBI-1176274;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus
CC {ECO:0000269|PubMed:10210332}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:25789526}. Midbody {ECO:0000269|PubMed:25789526}.
CC Note=In a filamentous pattern adjacent to the nucleus of migrating
CC cerebellar granule cells. Colocalizes with tubulin and dynein and with
CC the microtubule organizing center. Distributed throughout the cytoplasm
CC of non-migrating cells. A small proportion is nuclear, in a punctate
CC pattern. Localizes to the mitotic spindle in a EML4-dependent manner
CC (PubMed:25789526). {ECO:0000269|PubMed:23186163,
CC ECO:0000269|PubMed:25789526}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in fetal liver,
CC kidney, lung and brain. Highly expressed in adult pancreas, kidney,
CC skeletal muscle, liver, lung, placenta, prostate, brain and heart.
CC {ECO:0000269|PubMed:10210332, ECO:0000269|PubMed:10453739}.
CC -!- INDUCTION: Up-regulated in actively dividing hematopoietic precursor
CC cells. Up-regulated in cultured erythroleukemia TF-1 cells by
CC granulocyte-macrophage colony-stimulating factor. Strongly down-
CC regulated during maturation of erythroid precursor cells.
CC {ECO:0000269|PubMed:10210332}.
CC -!- PTM: Reversibly phosphorylated on serine residues during the M phase of
CC the cell cycle. Phosphorylation on Ser-274 and Ser-326 is necessary for
CC correct formation of mitotic spindles and chromosome separation during
CC mitosis. Phosphorylated by PLK and other kinases.
CC {ECO:0000269|PubMed:12852857}.
CC -!- SIMILARITY: Belongs to the nudC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA76628.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF130736; AAD30517.1; -; mRNA.
DR EMBL; AF125465; AAD39921.1; -; mRNA.
DR EMBL; AF100760; AAD43024.1; -; mRNA.
DR EMBL; AB019408; BAA76628.1; ALT_FRAME; mRNA.
DR EMBL; AF086922; AAP97152.1; -; mRNA.
DR EMBL; AL136725; CAB66659.1; -; mRNA.
DR EMBL; AL356390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002399; AAH02399.1; -; mRNA.
DR EMBL; BC003132; AAH03132.1; -; mRNA.
DR EMBL; BC006147; AAH06147.1; -; mRNA.
DR EMBL; BC007280; AAH07280.1; -; mRNA.
DR EMBL; BC015153; AAH15153.1; -; mRNA.
DR EMBL; BC021139; AAH21139.1; -; mRNA.
DR CCDS; CCDS292.1; -.
DR RefSeq; NP_006591.1; NM_006600.3.
DR PDB; 3QOR; X-ray; 1.75 A; A/B/C/D/E=158-274.
DR PDB; 7NDX; X-ray; 2.54 A; B=100-141.
DR PDBsum; 3QOR; -.
DR PDBsum; 7NDX; -.
DR AlphaFoldDB; Q9Y266; -.
DR SMR; Q9Y266; -.
DR BioGRID; 115950; 206.
DR IntAct; Q9Y266; 136.
DR MINT; Q9Y266; -.
DR STRING; 9606.ENSP00000319664; -.
DR DrugBank; DB12695; Phenethyl Isothiocyanate.
DR GlyGen; Q9Y266; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y266; -.
DR MetOSite; Q9Y266; -.
DR PhosphoSitePlus; Q9Y266; -.
DR SwissPalm; Q9Y266; -.
DR BioMuta; NUDC; -.
DR DMDM; 62287138; -.
DR EPD; Q9Y266; -.
DR jPOST; Q9Y266; -.
DR MassIVE; Q9Y266; -.
DR MaxQB; Q9Y266; -.
DR PaxDb; Q9Y266; -.
DR PeptideAtlas; Q9Y266; -.
DR PRIDE; Q9Y266; -.
DR ProteomicsDB; 85671; -.
DR TopDownProteomics; Q9Y266; -.
DR Antibodypedia; 30707; 406 antibodies from 37 providers.
DR DNASU; 10726; -.
DR Ensembl; ENST00000321265.10; ENSP00000319664.5; ENSG00000090273.14.
DR GeneID; 10726; -.
DR KEGG; hsa:10726; -.
DR MANE-Select; ENST00000321265.10; ENSP00000319664.5; NM_006600.4; NP_006591.1.
DR UCSC; uc001bng.3; human.
DR CTD; 10726; -.
DR DisGeNET; 10726; -.
DR GeneCards; NUDC; -.
DR HGNC; HGNC:8045; NUDC.
DR HPA; ENSG00000090273; Low tissue specificity.
DR MalaCards; NUDC; -.
DR MIM; 610325; gene.
DR neXtProt; NX_Q9Y266; -.
DR OpenTargets; ENSG00000090273; -.
DR PharmGKB; PA31827; -.
DR VEuPathDB; HostDB:ENSG00000090273; -.
DR eggNOG; KOG2265; Eukaryota.
DR GeneTree; ENSGT00940000155361; -.
DR HOGENOM; CLU_047332_1_0_1; -.
DR InParanoid; Q9Y266; -.
DR OMA; KPEDSIW; -.
DR OrthoDB; 1474731at2759; -.
DR PhylomeDB; Q9Y266; -.
DR TreeFam; TF300147; -.
DR PathwayCommons; Q9Y266; -.
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 Reactome; R-HSA-9696270; RND2 GTPase cycle.
DR SignaLink; Q9Y266; -.
DR SIGNOR; Q9Y266; -.
DR BioGRID-ORCS; 10726; 657 hits in 1085 CRISPR screens.
DR ChiTaRS; NUDC; human.
DR GeneWiki; NUDC; -.
DR GenomeRNAi; 10726; -.
DR Pharos; Q9Y266; Tbio.
DR PRO; PR:Q9Y266; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9Y266; protein.
DR Bgee; ENSG00000090273; Expressed in tendon of biceps brachii and 206 other tissues.
DR ExpressionAtlas; Q9Y266; baseline and differential.
DR Genevisible; Q9Y266; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005819; C:spindle; TAS:Reactome.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:UniProtKB.
DR GO; GO:0007097; P:nuclear migration; IEA:Ensembl.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR032572; NuDC.
DR InterPro; IPR037898; NudC_fam.
DR InterPro; IPR025934; NudC_N_dom.
DR PANTHER; PTHR12356; PTHR12356; 1.
DR Pfam; PF04969; CS; 1.
DR Pfam; PF16273; NuDC; 1.
DR Pfam; PF14050; Nudc_N; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS51203; CS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell cycle; Cell division; Coiled coil;
KW Cytoplasm; Cytoskeleton; Microtubule; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..331
FT /note="Nuclear migration protein nudC"
FT /id="PRO_0000057990"
FT DOMAIN 167..258
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT REGION 62..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..331
FT /note="Interaction with EML4"
FT /evidence="ECO:0000269|PubMed:25789526"
FT COILED 60..134
FT /evidence="ECO:0000255"
FT MOTIF 68..74
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 70..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 108
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 145
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 239
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 274
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000269|PubMed:12852857"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 326
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000269|PubMed:12852857"
FT MUTAGEN 274
FT /note="S->A: Abolishes phosphorylation by PLK1; when
FT associated with A-326."
FT /evidence="ECO:0000269|PubMed:12852857"
FT MUTAGEN 326
FT /note="S->A: Abolishes phosphorylation by PLK1; when
FT associated with A-274."
FT /evidence="ECO:0000269|PubMed:12852857"
FT CONFLICT 19
FT /note="Q -> H (in Ref. 4; BAA76628)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="T -> N (in Ref. 6; CAB66659)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="R -> I (in Ref. 4; BAA76628)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="E -> K (in Ref. 4; BAA76628)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="R -> K (in Ref. 4; BAA76628)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="H -> P (in Ref. 4; BAA76628)"
FT /evidence="ECO:0000305"
FT CONFLICT 149
FT /note="E -> V (in Ref. 6; CAB66659)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="L -> P (in Ref. 6; CAB66659)"
FT /evidence="ECO:0000305"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:7NDX"
FT HELIX 109..123
FT /evidence="ECO:0007829|PDB:7NDX"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:7NDX"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:3QOR"
FT STRAND 178..186
FT /evidence="ECO:0007829|PDB:3QOR"
FT HELIX 195..197
FT /evidence="ECO:0007829|PDB:3QOR"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:3QOR"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:3QOR"
FT STRAND 217..224
FT /evidence="ECO:0007829|PDB:3QOR"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:3QOR"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:3QOR"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:3QOR"
FT STRAND 240..251
FT /evidence="ECO:0007829|PDB:3QOR"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:3QOR"
SQ SEQUENCE 331 AA; 38243 MW; 34F591170F7594AF CRC64;
MGGEQEEERF DGMLLAMAQQ HEGGVQELVN TFFSFLRRKT DFFIGGEEGM AEKLITQTFS
HHNQLAQKTR REKRARQEAE RREKAERAAR LAKEAKSETS GPQIKELTDE EAERLQLEID
QKKDAENHEA QLKNGSLDSP GKQDTEEDEE EDEKDKGKLK PNLGNGADLP NYRWTQTLSE
LDLAVPFCVN FRLKGKDMVV DIQRRHLRVG LKGQPAIIDG ELYNEVKVEE SSWLIEDGKV
VTVHLEKINK MEWWSRLVSS DPEINTKKIN PENSKLSDLD SETRSMVEKM MYDQRQKSMG
LPTSDEQKKQ EILKKFMDQH PEMDFSKAKF N
