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Q92597 (NDRG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length394 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Cytoplasmcytosol. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. 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.31

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.27 Ref.31

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 componentCell membrane
Cytoplasm
Cytoskeleton
Membrane
Microtubule
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCharcot-Marie-Tooth disease
Neurodegeneration
Neuropathy
   DomainRepeat
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA 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: Ensembl

peripheral nervous system myelin maintenance

Inferred from electronic annotation. Source: Ensembl

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_componentcell-cell adherens junction

Inferred from direct assay Ref.15. Source: UniProtKB

centrosome

Inferred from direct assay Ref.17. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.12. Source: UniProtKB

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

microtubule

Inferred from direct assay Ref.17. Source: UniProtKB

microtubule cytoskeleton

Inferred from direct assay. Source: HPA

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_functionRab 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

CANXP278242EBI-716486,EBI-355947
XRCC6P129562EBI-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.26
Chain2 – 394393Protein NDRG1
PRO_0000159573

Regions

Repeat339 – 348101
Repeat349 – 358102
Repeat359 – 368103
Region339 – 368303 X 10 AA tandem repeats of G-T-R-S-R-S-H-T-S-E

Amino acid modifications

Modified residue21N-acetylserine Ref.26
Modified residue3261Phosphoserine Ref.25
Modified residue3281Phosphothreonine; by SGK1 Ref.16 Ref.28
Modified residue3301Phosphoserine; by SGK1 Ref.16 Ref.21 Ref.25 Ref.28
Modified residue3321Phosphoserine; by SGK1
Modified residue3331Phosphoserine Ref.21 Ref.25 Ref.29
Modified residue3361Phosphoserine Ref.25
Modified residue3461Phosphothreonine; by SGK1 Ref.16 Ref.27
Modified residue3561Phosphothreonine; by SGK1 Ref.16 Ref.27
Modified residue3641Phosphoserine; by SGK1 Ref.25
Modified residue3661Phosphothreonine; by SGK1 Ref.16 Ref.27
Modified residue3751Phosphothreonine Ref.25

Natural variations

Alternative sequence1 – 8181Missing in isoform 3.
VSP_045037
Alternative sequence1 – 6666Missing in isoform 2.
VSP_045038
Natural variant671M → V.
Corresponds to variant rs2233319 [ dbSNP | Ensembl ].
VAR_050234
Natural variant1111M → L.
Corresponds to variant rs2233328 [ dbSNP | Ensembl ].
VAR_050235

Experimental info

Sequence conflict1451I → T in CAA63430. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 4C816B9C85E3756F

FASTA39442,835
        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 

« Hide

Isoform 2 [UniParc].

Checksum: B8065321A684117C
Show »

FASTA32835,521
Isoform 3 [UniParc].

Checksum: 33AA0F4A954887BE
Show »

FASTA31333,650

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[26]"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] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-328 AND SER-330, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[29]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]"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.

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.
RefSeqNP_001128714.1. NM_001135242.1.
NP_001245361.1. NM_001258432.1.
NP_001245362.1. NM_001258433.1.
NP_006087.2. NM_006096.3.
UniGeneHs.372914.
Hs.618002.

3D structure databases

ProteinModelPortalQ92597.
SMRQ92597. Positions 35-311.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115669. 79 interactions.
IntActQ92597. 64 interactions.
MINTMINT-4999487.
STRING9606.ENSP00000319977.

Protein family/group databases

MEROPSS33.988.

PTM databases

PhosphoSiteQ92597.

Polymorphism databases

DMDM6166568.

Proteomic databases

PaxDbQ92597.
PRIDEQ92597.

Protocols and materials databases

DNASU10397.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000323851; ENSP00000319977; ENSG00000104419. [Q92597-1]
ENST00000414097; ENSP00000404854; ENSG00000104419. [Q92597-1]
ENST00000522476; ENSP00000427894; ENSG00000104419. [Q92597-2]
ENST00000537882; ENSP00000437443; ENSG00000104419. [Q92597-3]
GeneID10397.
KEGGhsa:10397.
UCSCuc003yuf.1. human. [Q92597-1]

Organism-specific databases

CTD10397.
GeneCardsGC08M134249.
HGNCHGNC:7679. NDRG1.
HPAHPA006881.
MIM601455. phenotype.
605262. gene.
neXtProtNX_Q92597.
Orphanet99950. Charcot-Marie-Tooth disease type 4D.
PharmGKBPA31482.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG310435.
HOGENOMHOG000230891.
HOVERGENHBG052591.
InParanoidQ92597.
OMATLHGSIH.
OrthoDBEOG7KH9JS.
PhylomeDBQ92597.
TreeFamTF313168.

Gene expression databases

ArrayExpressQ92597.
BgeeQ92597.
CleanExHS_DRG1.
HS_NDRG1.
GenevestigatorQ92597.

Family and domain databases

InterProIPR004142. Ndr.
[Graphical view]
PANTHERPTHR11034. PTHR11034. 1 hit.
PfamPF03096. Ndr. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNDRG1. human.
GeneWikiNDRG1.
GenomeRNAi10397.
NextBio39394.
PROQ92597.
SOURCESearch...

Entry information

Entry nameNDRG1_HUMAN
AccessionPrimary (citable) accession number: Q92597
Secondary accession number(s): B3KR80 expand/collapse secondary AC list , B7Z446, O15207, Q6IBG2, Q9NYR6, Q9UK29
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: February 1, 1997
Last modified: April 16, 2014
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM