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UniProtKB/Swiss-Prot entry Q92597

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NDRG1_HUMAN
Primary accession number Q92597
Secondary accession numbers O15207 Q9NYR6 Q9UK29
Integrated into Swiss-Prot on July 15, 1999
Sequence was last modified on February 1, 1997 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 81)
Name and origin of the protein
Protein name Protein NDRG1
Synonyms N-myc downstream-regulated gene 1 protein
Differentiation-related gene 1 protein
DRG-1
Reducing agents and tunicamycin-responsive protein
RTP
Nickel-specific induction protein Cap43
Rit42
Gene name
Name: NDRG1
Synonyms: CAP43, DRG1, RTP
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Umbilical vein endothelial cell;
DOI=10.1074/jbc.271.47.29659; PubMed=8939898 [NCBI, ExPASy, EBI, Israel, Japan]
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].
PubMed=9251681 [NCBI, ExPASy, EBI, Israel, Japan]
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].
TISSUE=Lung;
PubMed=9605764 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1016/S0167-4889(99)00056-7; PubMed=10395947 [NCBI, ExPASy, EBI, Israel, Japan]
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 GENOMIC DNA].
DOI=10.1038/nature04406; PubMed=16421571 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[7]
 NUCLEOTIDE SEQUENCE [MRNA] OF 1-21.
TISSUE=Brain;
Angelicheva D., Kalaydjieva L.;
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[8]
 FUNCTION.
PubMed=9766676 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319; SER-330 AND SER-336, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[10]
 INVOLVEMENT IN CMT4D.
DOI=10.1086/302978; PubMed=10831399 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[11]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326; THR-328 AND SER-330, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[12]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[13]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-366, AND MASS SPECTROMETRY.
DOI=10.1002/elps.200600782; PubMed=17487921 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D87953; BAA13505.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X92845; CAA63430.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF004162; AAC13419.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF186190; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
AF192304; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
BC003175; AAH03175.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF230380; AAF71305.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_006087.2; -.
UniGene Hs.372914
3D structure databases
ModBase Q92597.
Protein-protein interaction databases
IntAct Q92597; -.
Protein family/group databases
MEROPS S33.988; -.
PTM databases
PhosphoSite Q92597; -.
Organism-specific databases
H-InvDB HIX0019763; -.
HGNC HGNC:7679; NDRG1.
GenAtlas NDRG1.
HPA HPA006881; -.
MIM 601455; phenotype. [NCBI / EBI]
605262; gene. [NCBI / EBI]
Orphanet 64749; Charcot-Marie-Tooth disease, type 4.
99950; Charcot-Marie-Tooth disease, type 4D.
PharmGKB PA31482; -.
GeneCards Q92597.
Gene expression databases
ArrayExpress Q92597; -.
CleanEx HS_DRG1; -.
HS_NDRG1; -.
GermOnline ENSG00000104419; Homo sapiens.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0010038; Biological process: response to metal ion (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR004142; Ndr.
Graphical view of domain structure.
PANTHER PTHR11034; Ndr; 1.
Pfam PF03096; Ndr; 1.
Pfam graphical view of domain structure.
BLOCKS Q92597.
Genome annotation databases
Ensembl ENSG00000104419; Homo sapiens. [Contig view]
GeneID 10397; -.
KEGG hsa:10397; -.
Phylogenomic databases
HOGENOM Q92597; -.
HOVERGEN Q92597; -.
Other
SOURCE NDRG1; Homo sapiens.
ProtoNet Q92597.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell membrane; Charcot-Marie-Tooth disease; Cytoplasm; Membrane; Nucleus; Phosphoprotein; Repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   394  394     Protein NDRG1. PRO_0000159573
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. 
MOD_RES   319   319        Phosphoserine. 
MOD_RES   326   326        Phosphoserine. 
MOD_RES   328   328        Phosphothreonine. 
MOD_RES   330   330        Phosphoserine. 
MOD_RES   335   335        Phosphothreonine (By similarity). 
MOD_RES   336   336        Phosphoserine. 
MOD_RES   366   366        Phosphothreonine. 
CONFLICT   145   145        I -> T (in Ref. 2; CAA63430). 
Sequence information
Length: 394 AA [This is the length of the unprocessed precursor] Molecular weight: 42835 Da [This is the MW of the unprocessed precursor] CRC64: 4C816B9C85E3756F [This is a checksum on the sequence] 
        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
Q92597 in FASTA format

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