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   27-MAR-2024, entry version 198.
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; 298.
DR   IntAct; Q9Y266; 137.
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; 9606-ENSP00000319664; -.
DR   PeptideAtlas; Q9Y266; -.
DR   ProteomicsDB; 85671; -.
DR   Pumba; Q9Y266; -.
DR   TopDownProteomics; Q9Y266; -.
DR   Antibodypedia; 30707; 439 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   AGR; HGNC:8045; -.
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; QDGPRIQ; -.
DR   OrthoDB; 141208at2759; -.
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; 689 hits in 1165 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 208 other cell types or tissues.
DR   ExpressionAtlas; Q9Y266; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
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 chromosome alignment; 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   CDD; cd06492; p23_mNUDC_like; 1.
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:SF3; NUCLEAR MIGRATION PROTEIN NUDC; 1.
DR   PANTHER; PTHR12356; NUCLEAR MOVEMENT PROTEIN NUDC; 1.
DR   Pfam; PF04969; CS; 1.
DR   Pfam; PF16273; NuDC; 1.
DR   Pfam; PF14050; Nudc_N; 1.
DR   SUPFAM; SSF49764; HSP20-like chaperones; 1.
DR   PROSITE; PS51203; CS; 1.
DR   Genevisible; Q9Y266; HS.
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
//