Q92597 (NDRG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein NDRG1

Alternative name(s):
Differentiation-related gene 1 protein
Short name=DRG-1
N-myc downstream-regulated gene 1 protein
Nickel-specific induction protein Cap43
Reducing agents and tunicamycin-responsive protein
Short name=RTP
Rit42

Gene names

Name:	NDRG1
Synonyms:	CAP43, DRG1, RTP

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	394 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.11 Ref.15 Ref.16 Ref.18 Ref.23
Subunit structure	Interacts with RAB4A (membrane-bound form); the interaction involves NDRG1 in vesicular recycling of CDH1. Ref.18 Ref.23
Subcellular location	Cytoplasm › cytosol. Cytoplasm › cytoskeleton › 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. Ref.2 Ref.13 Ref.14 Ref.15 Ref.22 Ref.23 Ref.29
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. Ref.1 Ref.2 Ref.3 Ref.14
Induction	By homocysteine, 2-mercaptoethanol, tunicamycin in endothelial cells. Induced approximately 20-fold during in vitro differentiation of the colon carcinoma cell lines HT29-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. Ref.1 Ref.2 Ref.3 Ref.4 Ref.11 Ref.22
Post-translational modification	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. Ref.13 Ref.17 Ref.19 Ref.20 Ref.21 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29
Involvement in disease	Defects in NDRG1 are the cause of Charcot-Marie-Tooth disease type 4D (CMT4D) [MIM:601455]; also known as hereditary motor and sensory neuropathy Lom type (HMSNL). CMT4D is a recessive form of Charcot-Marie-Tooth disease, the most common inherited disorder of the peripheral nervous system. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathy and primary peripheral axonal neuropathy. Demyelinating CMT 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. Ref.12
Sequence similarities	Belongs to the NDRG family.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Cytoskeleton Membrane Microtubule Nucleus
Coding sequence diversity	Polymorphism
Disease	Charcot-Marie-Tooth disease Neuropathy
Domain	Repeat
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	DNA damage response, signal transduction by p53 class mediator Inferred from expression pattern Ref.11. Source: UniProtKB cellular response to hypoxia Inferred from expression pattern. Source: UniProtKB positive regulation of spindle checkpoint Inferred from direct assay Ref.15. Source: UniProtKB response to metal ion Traceable author statement. Source: ProtInc
Cellular component	cell-cell adherens junction Inferred from direct assay Ref.14. Source: UniProtKB centrosome Inferred from direct assay Ref.15. Source: UniProtKB cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule Inferred from direct assay Ref.15. Source: UniProtKB nucleus Inferred from direct assay Ref.11. Source: UniProtKB perinuclear region of cytoplasm Inferred from direct assay Ref.23. Source: UniProtKB plasma membrane Inferred from direct assay Ref.14. Source: UniProtKB recycling endosome membrane Inferred from direct assay Ref.23. Source: UniProtKB
Molecular function	Rab GTPase binding Inferred from direct assay Ref.23. Source: UniProtKB cadherin binding Inferred from direct assay Ref.23. Source: UniProtKB gamma-tubulin binding Inferred from direct assay Ref.15. Source: UniProtKB microtubule binding Inferred from direct assay Ref.15. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CANX	P27824	2	EBI-716486,EBI-355947
XRCC6	P12956	2	EBI-716486,EBI-353208

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 394	394	Protein NDRG1		PRO_0000159573
Regions
	Repeat	339 – 348	10	1
	Repeat	349 – 358	10	2
	Repeat	359 – 368	10	3
	Region	339 – 368	30	3 X 10 AA tandem repeats of G-T-R-S-R-S-H-T-S-E
Amino acid modifications
	Modified residue	2	1	Phosphoserine By similarity
	Modified residue	319	1	Phosphoserine Ref.17
	Modified residue	326	1	Phosphoserine Ref.19 Ref.24
	Modified residue	328	1	Phosphothreonine Ref.19 Ref.24 Ref.28
	Modified residue	330	1	Phosphoserine; by SGK1 Ref.17 Ref.19 Ref.20 Ref.24 Ref.25 Ref.28
	Modified residue	332	1	Phosphoserine; by SGK1 Ref.24 Ref.25
	Modified residue	333	1	Phosphoserine Ref.24 Ref.25 Ref.28
	Modified residue	335	1	Phosphothreonine Ref.24 Ref.25
	Modified residue	336	1	Phosphoserine Ref.17 Ref.24
	Modified residue	346	1	Phosphothreonine; by SGK1 Ref.27
	Modified residue	356	1	Phosphothreonine; by SGK1 Ref.27
	Modified residue	362	1	Phosphoserine By similarity
	Modified residue	364	1	Phosphoserine; by SGK1 Ref.24 Ref.25 Ref.26
	Modified residue	366	1	Phosphothreonine Ref.21 Ref.27
	Modified residue	375	1	Phosphothreonine Ref.24
Natural variations
	Natural variant	67	1	M → V. Corresponds to variant rs2233319 [ dbSNP | Ensembl ].		VAR_050234
	Natural variant	111	1	M → L. Corresponds to variant rs2233328 [ dbSNP | Ensembl ].		VAR_050235
Experimental info
	Sequence conflict	145	1	I → T in CAA63430. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q92597 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 4C816B9C85E3756F	FASTA	394	42,835
	10 20 30 40 50 60 MSREMQDVDL AEVKPLVEKG ETITGLLQEF DVQEQDIETL HGSVHVTLCG TPKGNRPVIL 70 80 90 100 110 120 TYHDIGMNHK TCYNPLFNYE DMQEITQHFA VCHVDAPGQQ DGAASFPAGY MYPSMDQLAE 130 140 150 160 170 180 MLPGVLQQFG LKSIIGMGTG AGAYILTRFA LNNPEMVEGL VLINVNPCAE GWMDWAASKI 190 200 210 220 230 240 SGWTQALPDM VVSHLFGKEE MQSNVEVVHT YRQHIVNDMN PGNLHLFINA YNSRRDLEIE 250 260 270 280 290 300 RPMPGTHTVT LQCPALLVVG DSSPAVDAVV ECNSKLDPTK TTLLKMADCG GLPQISQPAK 310 320 330 340 350 360 LAEAFKYFVQ GMGYMPSASM TRLMRSRTAS GSSVTSLDGT RSRSHTSEGT RSRSHTSEGT 370 380 390 RSRSHTSEGA HLDITPNSGA AGNSAGPKSM EVSC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Homocysteine-respondent genes in vascular endothelial cells identified by differential display analysis. GRP78/BiP and novel genes." Kokame K., Kato H., Miyata T. J. Biol. Chem. 271:29659-29665(1996) [PubMed: 8939898] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, TISSUE SPECIFICITY. Tissue: Umbilical vein endothelial cell.
[2]	"A novel gene which is up-regulated during colon epithelial cell differentiation and down-regulated in colorectal neoplasms." 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. Lab. Invest. 77:85-92(1997) [PubMed: 9251681] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[3]	"Cap43, a novel gene specifically induced by Ni2+ compounds." Zhou D., Salnikow K., Costa M. Cancer Res. 58:2182-2189(1998) [PubMed: 9605764] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION. Tissue: Lung.
[4]	"Differential expression of the RTP/Drg1/Ndr1 gene product in proliferating and growth arrested cells." Piquemal D., Joulia D., Balaguer P., Basset A., Marti J., Commes T. Biochim. Biophys. Acta 1450:364-373(1999) [PubMed: 10395947] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
[5]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[7]	"DNA sequence and analysis of human chromosome 8." 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. Nature 439:331-335(2006) [PubMed: 16421571] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.
[9]	Angelicheva D., Kalaydjieva L. Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-21. Tissue: Brain.
[10]	Lubec G., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 4-19; 54-70; 133-148; 199-212; 286-300; 307-322; 328-341 AND 364-388, MASS SPECTROMETRY. Tissue: Fetal brain cortex.
[11]	"Inhibition of tumor cell growth by RTP/rit42 and its responsiveness to p53 and DNA damage." Kurdistani S.K., Arizti P., Reimer C.L., Sugrue M.M., Aaronson S.A., Lee S.W. Cancer Res. 58:4439-4444(1998) [PubMed: 9766676] [Abstract] Cited for: FUNCTION, INDUCTION.
[12]	"N-myc downstream-regulated gene 1 is mutated in hereditary motor and sensory neuropathy-Lom." 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. Am. J. Hum. Genet. 67:47-58(2000) [PubMed: 10831399] [Abstract] Cited for: INVOLVEMENT IN CMT4D.
[13]	"Phosphorylation of RTP, an ER stress-responsive cytoplasmic protein." Agarwala K.L., Kokame K., Kato H., Miyata T. Biochem. Biophys. Res. Commun. 272:641-647(2000) [PubMed: 10860807] [Abstract] Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION.
[14]	"Expression of NDRG1, a differentiation-related gene, in human tissues." Lachat P., Shaw P., Gebhard S., van Belzen N., Chaubert P., Bosman F.T. Histochem. Cell Biol. 118:399-408(2002) [PubMed: 12432451] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[15]	"Function of Drg1/Rit42 in p53-dependent mitotic spindle checkpoint." Kim K.T., Ongusaha P.P., Hong Y.K., Kurdistani S.K., Nakamura M., Lu K.P., Lee S.W. J. Biol. Chem. 279:38597-38602(2004) [PubMed: 15247272] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[16]	"NDRG1 is necessary for p53-dependent apoptosis." Stein S., Thomas E.K., Herzog B., Westfall M.D., Rocheleau J.V., Jackson R.S. II, Wang M., Liang P. J. Biol. Chem. 279:48930-48940(2004) [PubMed: 15377670] [Abstract] Cited for: FUNCTION.
[17]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319; SER-330 AND SER-336, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"NDRG1 interacts with APO A-I and A-II and is a functional candidate for the HDL-C QTL on 8q24." Hunter M., Angelicheva D., Tournev I., Ingley E., Chan D.C., Watts G.F., Kremensky I., Kalaydjieva L. Biochem. Biophys. Res. Commun. 332:982-992(2005) [PubMed: 15922294] [Abstract] Cited for: INTERACTION WITH APOA1; APOA2; PRA1 AND RTN1, POSSIBLE FUNCTION.
[19]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326; THR-328 AND SER-330, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line." Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S. Electrophoresis 28:2027-2034(2007) [PubMed: 17487921] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-366, MASS SPECTROMETRY. Tissue: Prostate cancer.
[22]	"Hypoxia increases cytoplasmic expression of NDRG1, but is insufficient for its membrane localization in human hepatocellular carcinoma." Sibold S., Roh V., Keogh A., Studer P., Tiffon C., Angst E., Vorburger S.A., Weimann R., Candinas D., Stroka D. FEBS Lett. 581:989-994(2007) [PubMed: 17316623] [Abstract] Cited for: SUBCELLULAR LOCATION, INDUCTION.
[23]	"The N-Myc down regulated Gene1 (NDRG1) is a Rab4a effector involved in vesicular recycling of E-cadherin." Kachhap S.K., Faith D., Qian D.Z., Shabbeer S., Galloway N.L., Pili R., Denmeade S.R., DeMarzo A.M., Carducci M.A. PLoS ONE 2:E844-E844(2007) [PubMed: 17786215] [Abstract] Cited for: INTERACTION WITH RAB4A, SUBCELLULAR LOCATION, FUNCTION.
[24]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326; THR-328; SER-330; SER-332; SER-333; THR-335; SER-336; SER-364 AND THR-375, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[25]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330; SER-332; SER-333; THR-335 AND SER-364, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[26]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, MASS SPECTROMETRY.
[27]	"SGK1 activity in Na+ absorbing airway epithelial cells monitored by assaying NDRG1-Thr346/356/366 phosphorylation." Inglis S.K., Gallacher M., Brown S.G., McTavish N., Getty J., Husband E.M., Murray J.T., Wilson S.M. Pflugers Arch. 457:1287-1301(2009) [PubMed: 18787837] [Abstract] Cited for: PHOSPHORYLATION AT THR-346; THR-356 AND THR-366.
[28]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-328; SER-330 AND SER-333, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[29]	"Phosphorylation of NDRG1 is temporally and spatially controlled during the cell cycle." McCaig C., Potter L., Abramczyk O., Murray J.T. Biochem. Biophys. Res. Commun. 411:227-234(2011) [PubMed: 21708134] [Abstract] Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION.
[30]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	D87953 mRNA. Translation: BAA13505.1. X92845 mRNA. Translation: CAA63430.1. AF004162 mRNA. Translation: AAC13419.1. AF186190 Genomic DNA. No translation available. CR456842 mRNA. Translation: CAG33123.1. AK126924 mRNA. Translation: BAG54400.1. AF192304 Genomic DNA. No translation available. BC003175 mRNA. Translation: AAH03175.1. AF230380 mRNA. Translation: AAF71305.1.
IPI	IPI00022078.
RefSeq	NP_001128714.1. NM_001135242.1. NP_006087.2. NM_006096.3.
UniGene	Hs.372914. Hs.618002.
3D structure databases
ProteinModelPortal	Q92597.
SMR	Q92597. Positions 32-316.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q92597. 64 interactions.
STRING	Q92597.
Protein family/group databases
MEROPS	S33.988.
PTM databases
PhosphoSite	Q92597.
Polymorphism databases
DMDM	6166568.
Proteomic databases
PRIDE	Q92597.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000323851; ENSP00000319977; ENSG00000104419. ENST00000414097; ENSP00000404854; ENSG00000104419.
GeneID	10397.
KEGG	hsa:10397.
UCSC	uc003yug.1. human.
Organism-specific databases
CTD	10397.
GeneCards	GC08M134318.
H-InvDB	HIX0019763.
HGNC	HGNC:7679. NDRG1.
HPA	HPA006881.
MIM	601455. phenotype. 605262. gene.
neXtProt	NX_Q92597.
Orphanet	99950. Charcot-Marie-Tooth disease type 4D.
PharmGKB	PA31482.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG15489.
GeneTree	ENSGT00390000001874.
HOGENOM	HBG445737.
HOVERGEN	HBG052591.
InParanoid	Q92597.
OMA	QEQDIET.
PhylomeDB	Q92597.
Enzyme and pathway databases
Pathway_Interaction_DB	hif1_tfpathway. HIF-1-alpha transcription factor network.
Gene expression databases
ArrayExpress	Q92597.
Bgee	Q92597.
CleanEx	HS_DRG1. HS_NDRG1.
Genevestigator	Q92597.
GermOnline	ENSG00000104419. Homo sapiens.
Family and domain databases
InterPro	IPR004142. Ndr. [Graphical view]
PANTHER	PTHR11034. Ndr. 1 hit.
Pfam	PF03096. Ndr. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	39394.
SOURCE	Search...

Entry information

Entry name

NDRG1_HUMAN

Accession

Primary (citable) accession number: Q92597
Secondary accession number(s): O15207 , Q6IBG2, Q9NYR6, Q9UK29

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	February 1, 1997
Last modified:	January 25, 2012
This is version 117 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.