Reviewed, UniProtKB/Swiss-Prot Q92597 (NDRG1_HUMAN)

Names and origin

Protein names

Recommended name:
    Protein NDRG1
Alternative name(s):
    N-myc downstream-regulated gene 1 protein
    Differentiation-related gene 1 protein
      Short name=DRG-1
    Reducing agents and tunicamycin-responsive protein
      Short name=RTP
    Nickel-specific induction protein Cap43
    Rit42

Gene names

Name:	NDRG1
Synonyms:	CAP43, DRG1, RTP

Organism

Homo sapiens (Human) [Complete proteome]

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	May have a growth inhibitory role. Ref.11
Subcellular location	Cytoplasm. Nucleus. Cell membrane. Note: Whereas in prostate epithelium and placental chorion it is located in both the cytoplasm and the nucleus, nuclear staining is not observed in colon epithelium cells. Instead its localization changes from the cytoplasm to the plasma membrane during differentiation of colon carcinoma cell lines in vitro.
Tissue specificity	Ubiquitous; expressed most prominently in placental membranes and prostate, kidney, small intestine, and ovary tissues. Reduced expression in adenocarcinomas compared to normal tissues. In colon, prostate and placental membranes, the cells that border the lumen show the highest expression.
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 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.
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.13
Sequence similarities	Belongs to the NDRG family.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Membrane Nucleus
Coding sequence diversity	Polymorphism
Disease	Charcot-Marie-Tooth disease Neuropathy
Domain	Repeat
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	response to metal ion Ref.3 Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from direct assay. Source: HPA cytoskeleton Inferred from direct assay. Source: HPA nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ACSL3	O95573	1	EBI-716486,EBI-1190822
ACTG1	P63261	1	EBI-716486,EBI-351292
AP1M2	Q9Y6Q5-1	1	EBI-716486,EBI-752259
AP2M1	Q96CW1	1	EBI-716486,EBI-297683
ATP1A1	P05023	1	EBI-716486,EBI-358778
CANX	P27824	2	EBI-716486,EBI-355947
CLTC	Q00610	1	EBI-716486,EBI-354967
CNDP2	Q96KP4	1	EBI-716486,EBI-1190734
COPB2	P35606	1	EBI-716486,EBI-1056534
CTNNB1	P35222-1	1	EBI-716486,EBI-491563
DARS	P14868	1	EBI-716486,EBI-358730
DDX1	Q92499	1	EBI-716486,EBI-358474
DDX5	P17844	1	EBI-716486,EBI-351962
DLST	P36957	1	EBI-716486,EBI-351007
EEF1G	P26641	1	EBI-716486,EBI-351467
EEF2	P13639	1	EBI-716486,EBI-352560
EIF2S3	P41091	1	EBI-716486,EBI-1054228
EIF3E	P60228	1	EBI-716486,EBI-347740
EWSR1	Q01844	1	EBI-716486,EBI-739737
FASN	P49327	1	EBI-716486,EBI-356658
HNRNPF	P52597	1	EBI-716486,EBI-352986
HNRNPH1	P31943	1	EBI-716486,EBI-351590
HNRNPU	Q00839	1	EBI-716486,EBI-351126
HSD17B4	P51659	1	EBI-716486,EBI-358398
HSP90AA1	P07900	1	EBI-716486,EBI-296047
HSPA5	P11021	1	EBI-716486,EBI-354921
ILF3	Q12906-5	1	EBI-716486,EBI-288405
KIF5B	P33176	1	EBI-716486,EBI-355878
LDHA	P00338-1	1	EBI-716486,EBI-681495
MAOA	P21397	1	EBI-716486,EBI-1190845
MME	P08473	1	EBI-716486,EBI-353759
NCL	P19338	1	EBI-716486,EBI-352553
PABPC1	P11940	1	EBI-716486,EBI-81531
PKM2	P14618	1	EBI-716486,EBI-353408
PPP2R2A	P63151	1	EBI-716486,EBI-1048931
PSMC2	P35998	1	EBI-716486,EBI-359710
PSMC3	P17980	1	EBI-716486,EBI-359720
PSMD2	Q13200	1	EBI-716486,EBI-357648
RPL24	P83731	1	EBI-716486,EBI-353146
RPL3	P39023	1	EBI-716486,EBI-1056348
RPL4	P36578	1	EBI-716486,EBI-348313
RPN2	P04844	1	EBI-716486,EBI-719731
RPS16	P62249	1	EBI-716486,EBI-352480
RPS20	P60866	1	EBI-716486,EBI-353105
RPS26	P62854	1	EBI-716486,EBI-353438
RPS3	P23396	1	EBI-716486,EBI-351193
RPS6	P62753	1	EBI-716486,EBI-356625
RPS8	P62241	1	EBI-716486,EBI-351811
RPS9	P46781	1	EBI-716486,EBI-351206
RUVBL2	Q9Y230	1	EBI-716486,EBI-352939
SEC23A	Q15436	1	EBI-716486,EBI-81088
SHMT2	P34897	1	EBI-716486,EBI-352908
SLC25A6	P12236	1	EBI-716486,EBI-356254
TARS	P26639	1	EBI-716486,EBI-1042683
TLE3	Q04726-1	1	EBI-716486,EBI-1052074
UPF1	Q92900	1	EBI-716486,EBI-373471
VCP	P55072	1	EBI-716486,EBI-355164
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.12
	Modified residue	326	1	Phosphoserine Ref.14 Ref.17
	Modified residue	328	1	Phosphothreonine Ref.14 Ref.17 Ref.21
	Modified residue	330	1	Phosphoserine Ref.12 Ref.14 Ref.17 Ref.21 Ref.15 Ref.19
	Modified residue	332	1	Phosphoserine Ref.17 Ref.19
	Modified residue	333	1	Phosphoserine Ref.17 Ref.21 Ref.19
	Modified residue	335	1	Phosphothreonine Ref.17 Ref.19
	Modified residue	336	1	Phosphoserine Ref.12 Ref.17
	Modified residue	346	1	Phosphothreonine By similarity
	Modified residue	362	1	Phosphoserine By similarity
	Modified residue	364	1	Phosphoserine Ref.17 Ref.19
	Modified residue	366	1	Phosphothreonine Ref.16
	Modified residue	375	1	Phosphothreonine Ref.17
Natural variations
	Natural variant	67	1	M → V: dbSNP rs2233319.		VAR_050234
	Natural variant	111	1	M → L: dbSNP rs2233328.		VAR_050235
Experimental info
	Sequence conflict	145	1	I → T in CAA63430. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q92597-1 [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

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]. 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].
[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: 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].
[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.
[12]	"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: Epithelium.
[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: 10831399] [Abstract] Cited for: INVOLVEMENT IN CMT4D.
[14]	"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: Epithelium.
[15]	"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: Epithelium.
[16]	"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.
[17]	"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.
[18]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[19]	"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.
[20]	"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.
[21]	"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: T-cell.
+	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. NP_006087.2.
UniGene	Hs.372914 Hs.618002
3D structure databases
SMR	Q92597. Positions 31-311.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q92597. 63 interactions.
STRING	Q92597.
Protein family/group databases
MEROPS	S33.988.
PTM databases
PhosphoSite	Q92597.
Proteomic databases
PRIDE	Q92597.
Genome annotation databases
Ensembl	ENST00000323851; ENSP00000319977; ENSG00000104419; Homo sapiens. [Genome view] ENST00000414097; ENSP00000404854; ENSG00000104419; Homo sapiens. [Genome view]
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.
Orphanet	99950. Charcot-Marie-Tooth disease, type 4D.
PharmGKB	PA31482.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG15489.
HOGENOM	HBG445737.
HOVERGEN	Q92597.
InParanoid	Q92597.
OMA	QEFDVQE.
OrthoDB	EOG9QNQFK.
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 Resources
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:	February 9, 2010
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.