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Protein NDRG1 (Differentiation-related gene 1 protein) (DRG-1) (N-myc downstream-regulated gene 1 protein) (Nickel-specific induction protein Cap43) (Reducing agents and tunicamycin-responsive protein) (RTP) (Rit42)

 NDRG1_HUMAN             Reviewed;         394 AA.
Q92597; B3KR80; B7Z446; O15207; Q6IBG2; Q9NYR6; Q9UK29;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
25-OCT-2017, entry version 172.
RecName: Full=Protein NDRG1;
AltName: Full=Differentiation-related gene 1 protein;
Short=DRG-1;
AltName: Full=N-myc downstream-regulated gene 1 protein;
AltName: Full=Nickel-specific induction protein Cap43;
AltName: Full=Reducing agents and tunicamycin-responsive protein;
Short=RTP;
AltName: Full=Rit42;
Name=NDRG1; Synonyms=CAP43, DRG1, RTP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, AND TISSUE
SPECIFICITY.
TISSUE=Umbilical vein endothelial cell;
PubMed=8939898; DOI=10.1074/jbc.271.47.29659;
Kokame K., Kato H., Miyata T.;
"Homocysteine-respondent genes in vascular endothelial cells
identified by differential display analysis. GRP78/BiP and novel
genes.";
J. Biol. Chem. 271:29659-29665(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=9251681;
van Belzen N., Dinjens W.N.M., Diesveld M.P.G., Groen N.A.,
van der Made A.C.J., Nozawa Y., Vlietstra R., Trapman J., Bosman F.T.;
"A novel gene which is up-regulated during colon epithelial cell
differentiation and down-regulated in colorectal neoplasms.";
Lab. Invest. 77:85-92(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
INDUCTION.
TISSUE=Lung;
PubMed=9605764;
Zhou D., Salnikow K., Costa M.;
"Cap43, a novel gene specifically induced by Ni2+ compounds.";
Cancer Res. 58:2182-2189(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INDUCTION.
PubMed=10395947; DOI=10.1016/S0167-4889(99)00056-7;
Piquemal D., Joulia D., Balaguer P., Basset A., Marti J., Commes T.;
"Differential expression of the RTP/Drg1/Ndr1 gene product in
proliferating and growth arrested cells.";
Biochim. Biophys. Acta 1450:364-373(1999).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Brain, and Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-21 (ISOFORM 1).
TISSUE=Brain;
Angelicheva D., Kalaydjieva L.;
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[11]
PROTEIN SEQUENCE OF 4-19; 54-70; 133-148; 199-212; 286-300; 307-322;
328-341 AND 364-388, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[12]
FUNCTION, AND INDUCTION.
PubMed=9766676;
Kurdistani S.K., Arizti P., Reimer C.L., Sugrue M.M., Aaronson S.A.,
Lee S.W.;
"Inhibition of tumor cell growth by RTP/rit42 and its responsiveness
to p53 and DNA damage.";
Cancer Res. 58:4439-4444(1998).
[13]
INVOLVEMENT IN CMT4D.
PubMed=10831399; DOI=10.1086/302978;
Kalaydjieva L., Gresham D., Gooding R., Heather L., Baas F.,
de Jonge R., Blechschmidt K., Angelicheva D., Chandler D., Worsley P.,
Rosenthal A., King R.H.M., Thomas P.K.;
"N-myc downstream-regulated gene 1 is mutated in hereditary motor and
sensory neuropathy-Lom.";
Am. J. Hum. Genet. 67:47-58(2000).
[14]
PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
PubMed=10860807; DOI=10.1006/bbrc.2000.2833;
Agarwala K.L., Kokame K., Kato H., Miyata T.;
"Phosphorylation of RTP, an ER stress-responsive cytoplasmic
protein.";
Biochem. Biophys. Res. Commun. 272:641-647(2000).
[15]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=12432451; DOI=10.1007/s00418-002-0460-9;
Lachat P., Shaw P., Gebhard S., van Belzen N., Chaubert P.,
Bosman F.T.;
"Expression of NDRG1, a differentiation-related gene, in human
tissues.";
Histochem. Cell Biol. 118:399-408(2002).
[16]
PHOSPHORYLATION AT THR-328; SER-330; THR-346; THR-356 AND THR-366.
PubMed=15461589; DOI=10.1042/BJ20041057;
Murray J.T., Campbell D.G., Morrice N., Auld G.C., Shpiro N.,
Marquez R., Peggie M., Bain J., Bloomberg G.B., Grahammer F., Lang F.,
Wulff P., Kuhl D., Cohen P.;
"Exploitation of KESTREL to identify NDRG family members as
physiological substrates for SGK1 and GSK3.";
Biochem. J. 384:477-488(2004).
[17]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15247272; DOI=10.1074/jbc.M400781200;
Kim K.T., Ongusaha P.P., Hong Y.K., Kurdistani S.K., Nakamura M.,
Lu K.P., Lee S.W.;
"Function of Drg1/Rit42 in p53-dependent mitotic spindle checkpoint.";
J. Biol. Chem. 279:38597-38602(2004).
[18]
FUNCTION.
PubMed=15377670; DOI=10.1074/jbc.M400386200;
Stein S., Thomas E.K., Herzog B., Westfall M.D., Rocheleau J.V.,
Jackson R.S. II, Wang M., Liang P.;
"NDRG1 is necessary for p53-dependent apoptosis.";
J. Biol. Chem. 279:48930-48940(2004).
[19]
INTERACTION WITH APOA1; APOA2; PRA1 AND RTN1, AND POSSIBLE FUNCTION.
PubMed=15922294; DOI=10.1016/j.bbrc.2005.05.050;
Hunter M., Angelicheva D., Tournev I., Ingley E., Chan D.C.,
Watts G.F., Kremensky I., Kalaydjieva L.;
"NDRG1 interacts with APO A-I and A-II and is a functional candidate
for the HDL-C QTL on 8q24.";
Biochem. Biophys. Res. Commun. 332:982-992(2005).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330 AND SER-333, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Prostate cancer;
PubMed=17487921; DOI=10.1002/elps.200600782;
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
"Toward a global characterization of the phosphoproteome in prostate
cancer cells: identification of phosphoproteins in the LNCaP cell
line.";
Electrophoresis 28:2027-2034(2007).
[23]
SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=17316623; DOI=10.1016/j.febslet.2007.01.080;
Sibold S., Roh V., Keogh A., Studer P., Tiffon C., Angst E.,
Vorburger S.A., Weimann R., Candinas D., Stroka D.;
"Hypoxia increases cytoplasmic expression of NDRG1, but is
insufficient for its membrane localization in human hepatocellular
carcinoma.";
FEBS Lett. 581:989-994(2007).
[24]
INTERACTION WITH RAB4A, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=17786215; DOI=10.1371/journal.pone.0000844;
Kachhap S.K., Faith D., Qian D.Z., Shabbeer S., Galloway N.L.,
Pili R., Denmeade S.R., DeMarzo A.M., Carducci M.A.;
"The N-Myc down regulated Gene1 (NDRG1) is a Rab4a effector involved
in vesicular recycling of E-cadherin.";
PLoS ONE 2:E844-E844(2007).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326; SER-330; SER-333;
SER-336; SER-364 AND THR-375, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[26]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[27]
PHOSPHORYLATION AT THR-346; THR-356 AND THR-366.
PubMed=18787837; DOI=10.1007/s00424-008-0587-1;
Inglis S.K., Gallacher M., Brown S.G., McTavish N., Getty J.,
Husband E.M., Murray J.T., Wilson S.M.;
"SGK1 activity in Na+ absorbing airway epithelial cells monitored by
assaying NDRG1-Thr346/356/366 phosphorylation.";
Pflugers Arch. 457:1287-1301(2009).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-328 AND SER-330, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[30]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[31]
PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
PubMed=21708134; DOI=10.1016/j.bbrc.2011.06.092;
McCaig C., Potter L., Abramczyk O., Murray J.T.;
"Phosphorylation of NDRG1 is temporally and spatially controlled
during the cell cycle.";
Biochem. Biophys. Res. Commun. 411:227-234(2011).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; THR-328; SER-330;
SER-333; SER-336; SER-364; THR-366 AND THR-375, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-328; SER-332 AND
SER-333, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Stress-responsive protein involved in hormone responses,
cell growth, and differentiation. Acts as a tumor suppressor in
many cell types. Necessary but not sufficient for p53/TP53-
mediated caspase activation and apoptosis. Has a role in cell
trafficking, notably of the Schwann cell, and is necessary for the
maintenance and development of the peripheral nerve myelin sheath.
Required for vesicular recycling of CDH1 and TF. May also function
in lipid trafficking. Protects cells from spindle disruption
damage. Functions in p53/TP53-dependent mitotic spindle
checkpoint. Regulates microtubule dynamics and maintains euploidy.
{ECO:0000269|PubMed:15247272, ECO:0000269|PubMed:15377670,
ECO:0000269|PubMed:17786215, ECO:0000269|PubMed:9766676}.
-!- SUBUNIT: Interacts with RAB4A (membrane-bound form); the
interaction involves NDRG1 in vesicular recycling of CDH1.
{ECO:0000269|PubMed:15922294, ECO:0000269|PubMed:17786215}.
-!- INTERACTION:
Q9Y3D8:AK6; NbExp=3; IntAct=EBI-10278703, EBI-2896123;
P27824:CANX; NbExp=2; IntAct=EBI-716486, EBI-355947;
P12956:XRCC6; NbExp=2; IntAct=EBI-716486, EBI-353208;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome. Nucleus. Cell membrane.
Note=Mainly cytoplasmic but differentially localized to other
regions. Associates with the plasma membrane in intestinal
epithelia and lactating mammary gland. Translocated to the nucleus
in a p53/TP53-dependent manner. In prostate epithelium and
placental chorion, located in both the cytoplasm and in the
nucleus. No nuclear localization in colon epithelium cells. In
intestinal mucosa, prostate and renal cortex, located
predominantly adjacent to adherens junctions. Cytoplasmic with
granular staining in proximal tubular cells of the kidney and
salivary gland ducts. Recruits to the membrane of
recycling/sorting and late endosomes via binding to
phosphatidylinositol 4-phosphate. Associates with microtubules.
Colocalizes with TUBG1 in the centrosome. Cytoplasmic location
increased with hypoxia. Phosphorylated form found associated with
centromeres during S-phase of mitosis and with the plasma
membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q92597-1; Sequence=Displayed;
Name=2;
IsoId=Q92597-2; Sequence=VSP_045038;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q92597-3; Sequence=VSP_045037;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous; expressed most prominently in
placental membranes and prostate, kidney, small intestine, and
ovary tissues. Also expressed in heart, brain, skeletal muscle,
lung, liver and pancreas. Low levels in peripheral blood
leukocytes and in tissues of the immune system. Expressed mainly
in epithelial cells. Also found in Schwann cells of peripheral
neurons. Reduced expression in adenocarcinomas compared to normal
tissues. In colon, prostate and placental membranes, the cells
that border the lumen show the highest expression.
{ECO:0000269|PubMed:12432451, ECO:0000269|PubMed:8939898,
ECO:0000269|PubMed:9251681, ECO:0000269|PubMed:9605764}.
-!- INDUCTION: By homocysteine, 2-mercaptoethanol, tunicamycin in
endothelial cells. Induced approximately 20-fold during in vitro
differentiation of the colon carcinoma cell lines HT-29-D4 and
Caco-2. Induced by oxidative stress in colon cancers. Decreased
expression in colon adenomas and adenocarcinomas. Induced by
nickel compounds in all tested cell lines. The primary signal for
its induction is an elevation of free intracellular calcium ion
caused by nickel ion exposure. Okadaic acid, a serine/threonine
phosphatase inhibitor, induced its expression more rapidly and
more efficiently than nickel. {ECO:0000269|PubMed:10395947,
ECO:0000269|PubMed:17316623, ECO:0000269|PubMed:8939898,
ECO:0000269|PubMed:9251681, ECO:0000269|PubMed:9605764,
ECO:0000269|PubMed:9766676}.
-!- PTM: Under stress conditions, phosphorylated in the C-terminal on
many serine and threonine residues. Phosphorylated in vitro by
PKA. Phosphorylation enhanced by increased intracellular cAMP
levels. Homocysteine induces dephosphorylation. Phosphorylation by
SGK1 is cell cycle dependent. {ECO:0000269|PubMed:10860807,
ECO:0000269|PubMed:15461589, ECO:0000269|PubMed:18787837,
ECO:0000269|PubMed:21708134}.
-!- DISEASE: Charcot-Marie-Tooth disease 4D (CMT4D) [MIM:601455]: A
recessive demyelinating form of Charcot-Marie-Tooth disease, a
disorder of the peripheral nervous system, characterized by
progressive weakness and atrophy, initially of the peroneal
muscles and later of the distal muscles of the arms. Charcot-
Marie-Tooth disease is classified in two main groups on the basis
of electrophysiologic properties and histopathology: primary
peripheral demyelinating neuropathies (designated CMT1 when they
are dominantly inherited) and primary peripheral axonal
neuropathies (CMT2). Demyelinating neuropathies are characterized
by severely reduced nerve conduction velocities (less than 38
m/sec), segmental demyelination and remyelination with onion bulb
formations on nerve biopsy, slowly progressive distal muscle
atrophy and weakness, absent deep tendon reflexes, and hollow
feet. By convention autosomal recessive forms of demyelinating
Charcot-Marie-Tooth disease are designated CMT4.
{ECO:0000269|PubMed:10831399}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the NDRG family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/NDRG1ID41512ch8q24.html";
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EMBL; D87953; BAA13505.1; -; mRNA.
EMBL; X92845; CAA63430.1; -; mRNA.
EMBL; AF004162; AAC13419.1; -; mRNA.
EMBL; AF186190; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CR456842; CAG33123.1; -; mRNA.
EMBL; AK091147; BAG52292.1; -; mRNA.
EMBL; AK126924; BAG54400.1; -; mRNA.
EMBL; AK296794; BAH12432.1; -; mRNA.
EMBL; AF192304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471060; EAW92164.1; -; Genomic_DNA.
EMBL; BC003175; AAH03175.1; -; mRNA.
EMBL; AF230380; AAF71305.1; -; mRNA.
CCDS; CCDS34945.1; -. [Q92597-1]
CCDS; CCDS59112.1; -. [Q92597-3]
CCDS; CCDS59113.1; -. [Q92597-2]
RefSeq; NP_001128714.1; NM_001135242.1. [Q92597-1]
RefSeq; NP_001245361.1; NM_001258432.1. [Q92597-2]
RefSeq; NP_001245362.1; NM_001258433.1. [Q92597-3]
RefSeq; NP_006087.2; NM_006096.3. [Q92597-1]
UniGene; Hs.372914; -.
UniGene; Hs.618002; -.
ProteinModelPortal; Q92597; -.
SMR; Q92597; -.
BioGrid; 115669; 111.
IntAct; Q92597; 66.
MINT; MINT-4999487; -.
STRING; 9606.ENSP00000319977; -.
ESTHER; human-NDRG1; Ndr_family.
MEROPS; S33.988; -.
iPTMnet; Q92597; -.
PhosphoSitePlus; Q92597; -.
SwissPalm; Q92597; -.
BioMuta; NDRG1; -.
DMDM; 6166568; -.
EPD; Q92597; -.
MaxQB; Q92597; -.
PaxDb; Q92597; -.
PeptideAtlas; Q92597; -.
PRIDE; Q92597; -.
TopDownProteomics; Q92597-1; -. [Q92597-1]
DNASU; 10397; -.
Ensembl; ENST00000323851; ENSP00000319977; ENSG00000104419. [Q92597-1]
Ensembl; ENST00000414097; ENSP00000404854; ENSG00000104419. [Q92597-1]
Ensembl; ENST00000522476; ENSP00000427894; ENSG00000104419. [Q92597-2]
Ensembl; ENST00000537882; ENSP00000437443; ENSG00000104419. [Q92597-3]
GeneID; 10397; -.
KEGG; hsa:10397; -.
UCSC; uc003yug.3; human. [Q92597-1]
CTD; 10397; -.
DisGeNET; 10397; -.
EuPathDB; HostDB:ENSG00000104419.14; -.
GeneCards; NDRG1; -.
GeneReviews; NDRG1; -.
HGNC; HGNC:7679; NDRG1.
HPA; HPA006881; -.
MalaCards; NDRG1; -.
MIM; 601455; phenotype.
MIM; 605262; gene.
neXtProt; NX_Q92597; -.
OpenTargets; ENSG00000104419; -.
Orphanet; 99950; Charcot-Marie-Tooth disease type 4D.
PharmGKB; PA31482; -.
eggNOG; KOG2931; Eukaryota.
eggNOG; ENOG410XSPF; LUCA.
GeneTree; ENSGT00390000001874; -.
HOGENOM; HOG000230891; -.
HOVERGEN; HBG052591; -.
InParanoid; Q92597; -.
KO; K18266; -.
OMA; NNVEVVH; -.
OrthoDB; EOG091G09VW; -.
PhylomeDB; Q92597; -.
TreeFam; TF313168; -.
Reactome; R-HSA-6803205; TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain.
SIGNOR; Q92597; -.
ChiTaRS; NDRG1; human.
GeneWiki; NDRG1; -.
GenomeRNAi; 10397; -.
PRO; PR:Q92597; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000104419; -.
CleanEx; HS_DRG1; -.
CleanEx; HS_NDRG1; -.
ExpressionAtlas; Q92597; baseline and differential.
Genevisible; Q92597; HS.
GO; GO:0005913; C:cell-cell adherens junction; IDA:UniProtKB.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005874; C:microtubule; IDA:UniProtKB.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
GO; GO:0045296; F:cadherin binding; IDA:UniProtKB.
GO; GO:0043015; F:gamma-tubulin binding; IDA:UniProtKB.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0017137; F:Rab GTPase binding; IDA:UniProtKB.
GO; GO:0071456; P:cellular response to hypoxia; IEP:UniProtKB.
GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IEP:UniProtKB.
GO; GO:0045576; P:mast cell activation; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0032287; P:peripheral nervous system myelin maintenance; IEA:Ensembl.
GO; GO:0090232; P:positive regulation of spindle checkpoint; IDA:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; TAS:Reactome.
GO; GO:0010038; P:response to metal ion; TAS:ProtInc.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR004142; NDRG.
InterPro; IPR030693; NDRG1.
PANTHER; PTHR11034; PTHR11034; 1.
PANTHER; PTHR11034:SF18; PTHR11034:SF18; 1.
Pfam; PF03096; Ndr; 1.
SUPFAM; SSF53474; SSF53474; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell membrane;
Charcot-Marie-Tooth disease; Complete proteome; Cytoplasm;
Cytoskeleton; Direct protein sequencing; Membrane; Microtubule;
Neurodegeneration; Neuropathy; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 394 Protein NDRG1.
/FTId=PRO_0000159573.
REPEAT 339 348 1.
REPEAT 349 358 2.
REPEAT 359 368 3.
REGION 339 368 3 X 10 AA tandem repeats of G-T-R-S-R-S-
H-T-S-E.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 319 319 Phosphoserine.
{ECO:0000250|UniProtKB:Q62433}.
MOD_RES 326 326 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 328 328 Phosphothreonine; by SGK1.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:15461589}.
MOD_RES 330 330 Phosphoserine; by SGK1.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:15461589}.
MOD_RES 332 332 Phosphoserine; by SGK1.
{ECO:0000244|PubMed:24275569}.
MOD_RES 333 333 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 335 335 Phosphothreonine.
{ECO:0000250|UniProtKB:Q62433}.
MOD_RES 336 336 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 340 340 Phosphothreonine.
{ECO:0000250|UniProtKB:Q62433}.
MOD_RES 342 342 Phosphoserine.
{ECO:0000250|UniProtKB:Q62433}.
MOD_RES 346 346 Phosphothreonine; by SGK1.
{ECO:0000269|PubMed:15461589,
ECO:0000269|PubMed:18787837}.
MOD_RES 352 352 Phosphoserine.
{ECO:0000250|UniProtKB:Q6JE36}.
MOD_RES 356 356 Phosphothreonine; by SGK1.
{ECO:0000269|PubMed:15461589,
ECO:0000269|PubMed:18787837}.
MOD_RES 362 362 Phosphoserine.
{ECO:0000250|UniProtKB:Q6JE36}.
MOD_RES 364 364 Phosphoserine; by SGK1.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 366 366 Phosphothreonine; by SGK1.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:15461589,
ECO:0000269|PubMed:18787837}.
MOD_RES 375 375 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 81 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045037.
VAR_SEQ 1 66 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045038.
VARIANT 67 67 M -> V (in dbSNP:rs2233319).
/FTId=VAR_050234.
VARIANT 111 111 M -> L (in dbSNP:rs2233328).
/FTId=VAR_050235.
CONFLICT 145 145 I -> T (in Ref. 2; CAA63430).
{ECO:0000305}.
SEQUENCE 394 AA; 42835 MW; 4C816B9C85E3756F CRC64;
MSREMQDVDL AEVKPLVEKG ETITGLLQEF DVQEQDIETL HGSVHVTLCG TPKGNRPVIL
TYHDIGMNHK TCYNPLFNYE DMQEITQHFA VCHVDAPGQQ DGAASFPAGY MYPSMDQLAE
MLPGVLQQFG LKSIIGMGTG AGAYILTRFA LNNPEMVEGL VLINVNPCAE GWMDWAASKI
SGWTQALPDM VVSHLFGKEE MQSNVEVVHT YRQHIVNDMN PGNLHLFINA YNSRRDLEIE
RPMPGTHTVT LQCPALLVVG DSSPAVDAVV ECNSKLDPTK TTLLKMADCG GLPQISQPAK
LAEAFKYFVQ GMGYMPSASM TRLMRSRTAS GSSVTSLDGT RSRSHTSEGT RSRSHTSEGT
RSRSHTSEGA HLDITPNSGA AGNSAGPKSM EVSC


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