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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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.12 Ref.17 Ref.18 Ref.19 Ref.24
Subunit structure	Interacts with RAB4A (membrane-bound form); the interaction involves NDRG1 in vesicular recycling of CDH1. Ref.19 Ref.24
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.14 Ref.15 Ref.17 Ref.23 Ref.24 Ref.30
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.15
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. Ref.1 Ref.2 Ref.3 Ref.4 Ref.12 Ref.23
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.14 Ref.16 Ref.26 Ref.30
Involvement in 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13
Sequence similarities	Belongs to the NDRG family.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Cytoskeleton Membrane Microtubule Nucleus
Coding sequence diversity	Alternative splicing 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.12. Source: UniProtKB cellular response to hypoxia Inferred from expression pattern PubMed 20810912. Source: UniProtKB mast cell activation Inferred from electronic annotation. Source: Compara peripheral nervous system myelin maintenance Inferred from electronic annotation. Source: Compara positive regulation of spindle checkpoint Inferred from direct assay Ref.17. Source: UniProtKB response to metal ion Traceable author statement Ref.3. Source: ProtInc
Cellular_component	cell-cell adherens junction Inferred from direct assay Ref.15. Source: UniProtKB centrosome Inferred from direct assay Ref.17. Source: UniProtKB cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule Inferred from direct assay Ref.17. Source: UniProtKB nucleus Inferred from direct assay Ref.12. Source: UniProtKB perinuclear region of cytoplasm Inferred from direct assay Ref.24. Source: UniProtKB plasma membrane Inferred from direct assay Ref.15. Source: UniProtKB recycling endosome membrane Inferred from direct assay Ref.24. Source: UniProtKB
Molecular_function	Rab GTPase binding Inferred from direct assay Ref.24. Source: UniProtKB cadherin binding Inferred from direct assay Ref.24. Source: UniProtKB gamma-tubulin binding Inferred from direct assay Ref.17. Source: UniProtKB microtubule binding Inferred from direct assay Ref.17. 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

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q92597-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q92597-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-66: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q92597-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: Missing.

Note: No experimental confirmation available.

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	326	1	Phosphoserine Ref.25
	Modified residue	328	1	Phosphothreonine; by SGK1 Ref.16 Ref.27
	Modified residue	330	1	Phosphoserine; by SGK1 Ref.16 Ref.21 Ref.25 Ref.27
	Modified residue	332	1	Phosphoserine; by SGK1
	Modified residue	333	1	Phosphoserine Ref.21 Ref.25 Ref.28
	Modified residue	335	1	Phosphothreonine By similarity
	Modified residue	336	1	Phosphoserine Ref.25
	Modified residue	346	1	Phosphothreonine; by SGK1 Ref.16 Ref.26
	Modified residue	356	1	Phosphothreonine; by SGK1 Ref.16 Ref.26
	Modified residue	362	1	Phosphoserine By similarity
	Modified residue	364	1	Phosphoserine; by SGK1 Ref.25
	Modified residue	366	1	Phosphothreonine; by SGK1 Ref.16 Ref.26
	Modified residue	375	1	Phosphothreonine Ref.25
Natural variations
	Alternative sequence	1 – 81	81	Missing in isoform 3.		VSP_045037
	Alternative sequence	1 – 66	66	Missing in isoform 2.		VSP_045038
	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)
	Isoform 1 [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
	Isoform 2 [UniParc]. Checksum: B8065321A684117C	FASTA	328	35,521
	10 20 30 40 50 60 MNHKTCYNPL FNYEDMQEIT QHFAVCHVDA PGQQDGAASF PAGYMYPSMD QLAEMLPGVL 70 80 90 100 110 120 QQFGLKSIIG MGTGAGAYIL TRFALNNPEM VEGLVLINVN PCAEGWMDWA ASKISGWTQA 130 140 150 160 170 180 LPDMVVSHLF GKEEMQSNVE VVHTYRQHIV NDMNPGNLHL FINAYNSRRD LEIERPMPGT 190 200 210 220 230 240 HTVTLQCPAL LVVGDSSPAV DAVVECNSKL DPTKTTLLKM ADCGGLPQIS QPAKLAEAFK 250 260 270 280 290 300 YFVQGMGYMP SASMTRLMRS RTASGSSVTS LDGTRSRSHT SEGTRSRSHT SEGTRSRSHT 310 320 SEGAHLDITP NSGAAGNSAG PKSMEVSC
	Isoform 3 [UniParc]. Checksum: 33AA0F4A954887BE	FASTA	313	33,650
	10 20 30 40 50 60 MQEITQHFAV CHVDAPGQQD GAASFPAGYM YPSMDQLAEM LPGVLQQFGL KSIIGMGTGA 70 80 90 100 110 120 GAYILTRFAL NNPEMVEGLV LINVNPCAEG WMDWAASKIS GWTQALPDMV VSHLFGKEEM 130 140 150 160 170 180 QSNVEVVHTY RQHIVNDMNP GNLHLFINAY NSRRDLEIER PMPGTHTVTL QCPALLVVGD 190 200 210 220 230 240 SSPAVDAVVE CNSKLDPTKT TLLKMADCGG LPQISQPAKL AEAFKYFVQG MGYMPSASMT 250 260 270 280 290 300 RLMRSRTASG SSVTSLDGTR SRSHTSEGTR SRSHTSEGTR SRSHTSEGAH LDITPNSGAA 310 GNSAGPKSME VSC

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] (ISOFORM 1).
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3). Tissue: Brain and Tongue.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Kidney.
[10]	Angelicheva D., Kalaydjieva L. Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-21 (ISOFORM 1). Tissue: Brain.
[11]	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.
[12]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION.
[13]	"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] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN CMT4D.
[14]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION.
[15]	"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] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[16]	"Exploitation of KESTREL to identify NDRG family members as physiological substrates for SGK1 and GSK3." 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. Biochem. J. 384:477-488(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-328; SER-330; THR-346; THR-356 AND THR-366.
[17]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[18]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[19]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH APOA1; APOA2; PRA1 AND RTN1, POSSIBLE FUNCTION.
[20]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[21]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330 AND SER-333, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Prostate cancer.
[23]	"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] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INDUCTION.
[24]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RAB4A, SUBCELLULAR LOCATION, FUNCTION.
[25]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326; SER-330; SER-333; SER-336; SER-364 AND THR-375, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[26]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-346; THR-356 AND THR-366.
[27]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-328 AND SER-330, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[28]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." 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. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[29]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION.
+	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. AK091147 mRNA. Translation: BAG52292.1. AK126924 mRNA. Translation: BAG54400.1. AK296794 mRNA. Translation: BAH12432.1. AF192304 Genomic DNA. No translation available. CH471060 Genomic DNA. Translation: EAW92164.1. BC003175 mRNA. Translation: AAH03175.1. AF230380 mRNA. Translation: AAF71305.1.
IPI	IPI00022078. IPI00982468. IPI01011666.
RefSeq	NP_001128714.1. NM_001135242.1. NP_001245361.1. NM_001258432.1. NP_001245362.1. NM_001258433.1. NP_006087.2. NM_006096.3.
UniGene	Hs.372914. Hs.618002.
3D structure databases
ProteinModelPortal	Q92597.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q92597. 63 interactions.
STRING	9606.ENSP00000319977.
Protein family/group databases
MEROPS	S33.988.
PTM databases
PhosphoSite	Q92597.
Polymorphism databases
DMDM	6166568.
Proteomic databases
PaxDb	Q92597.
PRIDE	Q92597.
Protocols and materials databases
DNASU	10397.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000323851; ENSP00000319977; ENSG00000104419. ENST00000414097; ENSP00000404854; ENSG00000104419. ENST00000522476; ENSP00000427894; ENSG00000104419. ENST00000537882; ENSP00000437443; ENSG00000104419.
GeneID	10397.
KEGG	hsa:10397.
UCSC	uc003yuf.1. human.
Organism-specific databases
CTD	10397.
GeneCards	GC08M134249.
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	NOG310435.
HOGENOM	HOG000230891.
HOVERGEN	HBG052591.
InParanoid	Q92597.
OMA	LHGSIHV.
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. PTHR11034. 1 hit.
Pfam	PF03096. Ndr. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	NDRG1. human.
GenomeRNAi	10397.
NextBio	39394.
SOURCE	Search...

Entry information

Entry name

NDRG1_HUMAN

Accession

Primary (citable) accession number: Q92597
Secondary accession number(s): B3KR80 , B7Z446, O15207, Q6IBG2, Q9NYR6, Q9UK29

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 132 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.