Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q92597

- NDRG1_HUMAN

UniProt

Q92597 - NDRG1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Protein NDRG1

Gene

NDRG1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Molecular functioni

  1. cadherin binding Source: UniProtKB
  2. gamma-tubulin binding Source: UniProtKB
  3. microtubule binding Source: UniProtKB
  4. Rab GTPase binding Source: UniProtKB

GO - Biological processi

  1. cell death Source: UniProtKB-KW
  2. cellular response to hypoxia Source: UniProtKB
  3. DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
  4. mast cell activation Source: Ensembl
  5. peripheral nervous system myelin maintenance Source: Ensembl
  6. positive regulation of spindle checkpoint Source: UniProtKB
  7. response to metal ion Source: ProtInc
Complete GO annotation...

Protein family/group databases

MEROPSiS33.988.

Names & Taxonomyi

Protein namesi
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 namesi
Name:NDRG1
Synonyms:CAP43, DRG1, RTP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:7679. NDRG1.

Subcellular locationi

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.

GO - Cellular componenti

  1. cell-cell adherens junction Source: UniProtKB
  2. centrosome Source: UniProtKB
  3. cytoplasm Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProt
  5. microtubule Source: UniProtKB
  6. microtubule cytoskeleton Source: HPA
  7. nucleus Source: UniProtKB
  8. perinuclear region of cytoplasm Source: UniProtKB
  9. plasma membrane Source: UniProtKB
  10. recycling endosome membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Microtubule, Nucleus

Pathology & Biotechi

Involvement in diseasei

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 CMT4.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Keywords - Diseasei

Charcot-Marie-Tooth disease, Neurodegeneration, Neuropathy

Organism-specific databases

MIMi601455. phenotype.
Orphaneti99950. Charcot-Marie-Tooth disease type 4D.
PharmGKBiPA31482.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 394393Protein NDRG1PRO_0000159573Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei326 – 3261Phosphoserine1 Publication
Modified residuei328 – 3281Phosphothreonine; by SGK12 Publications
Modified residuei330 – 3301Phosphoserine; by SGK14 Publications
Modified residuei332 – 3321Phosphoserine; by SGK1
Modified residuei333 – 3331Phosphoserine3 Publications
Modified residuei336 – 3361Phosphoserine1 Publication
Modified residuei346 – 3461Phosphothreonine; by SGK12 Publications
Modified residuei356 – 3561Phosphothreonine; by SGK12 Publications
Modified residuei364 – 3641Phosphoserine; by SGK11 Publication
Modified residuei366 – 3661Phosphothreonine; by SGK12 Publications
Modified residuei375 – 3751Phosphothreonine1 Publication

Post-translational modificationi

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.8 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ92597.
PaxDbiQ92597.
PRIDEiQ92597.

PTM databases

PhosphoSiteiQ92597.

Expressioni

Tissue specificityi

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.4 Publications

Inductioni

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.6 Publications

Gene expression databases

BgeeiQ92597.
CleanExiHS_DRG1.
HS_NDRG1.
ExpressionAtlasiQ92597. baseline and differential.
GenevestigatoriQ92597.

Organism-specific databases

HPAiHPA006881.

Interactioni

Subunit structurei

Interacts with RAB4A (membrane-bound form); the interaction involves NDRG1 in vesicular recycling of CDH1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CANXP278242EBI-716486,EBI-355947
XRCC6P129562EBI-716486,EBI-353208

Protein-protein interaction databases

BioGridi115669. 86 interactions.
IntActiQ92597. 64 interactions.
MINTiMINT-4999487.
STRINGi9606.ENSP00000319977.

Structurei

3D structure databases

ProteinModelPortaliQ92597.
SMRiQ92597. Positions 35-311.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati339 – 348101
Repeati349 – 358102
Repeati359 – 368103

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni339 – 368303 X 10 AA tandem repeats of G-T-R-S-R-S-H-T-S-EAdd
BLAST

Sequence similaritiesi

Belongs to the NDRG family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG310435.
GeneTreeiENSGT00390000001874.
HOGENOMiHOG000230891.
HOVERGENiHBG052591.
InParanoidiQ92597.
KOiK18266.
OMAiTLHGSIH.
OrthoDBiEOG7KH9JS.
PhylomeDBiQ92597.
TreeFamiTF313168.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR004142. NDRG.
[Graphical view]
PANTHERiPTHR11034. PTHR11034. 1 hit.
PfamiPF03096. Ndr. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q92597-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSREMQDVDL AEVKPLVEKG ETITGLLQEF DVQEQDIETL HGSVHVTLCG
60 70 80 90 100
TPKGNRPVIL TYHDIGMNHK TCYNPLFNYE DMQEITQHFA VCHVDAPGQQ
110 120 130 140 150
DGAASFPAGY MYPSMDQLAE MLPGVLQQFG LKSIIGMGTG AGAYILTRFA
160 170 180 190 200
LNNPEMVEGL VLINVNPCAE GWMDWAASKI SGWTQALPDM VVSHLFGKEE
210 220 230 240 250
MQSNVEVVHT YRQHIVNDMN PGNLHLFINA YNSRRDLEIE RPMPGTHTVT
260 270 280 290 300
LQCPALLVVG DSSPAVDAVV ECNSKLDPTK TTLLKMADCG GLPQISQPAK
310 320 330 340 350
LAEAFKYFVQ GMGYMPSASM TRLMRSRTAS GSSVTSLDGT RSRSHTSEGT
360 370 380 390
RSRSHTSEGT RSRSHTSEGA HLDITPNSGA AGNSAGPKSM EVSC
Length:394
Mass (Da):42,835
Last modified:February 1, 1997 - v1
Checksum:i4C816B9C85E3756F
GO
Isoform 2 (identifier: Q92597-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:328
Mass (Da):35,521
Checksum:iB8065321A684117C
GO
Isoform 3 (identifier: Q92597-3) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:313
Mass (Da):33,650
Checksum:i33AA0F4A954887BE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti145 – 1451I → T in CAA63430. (PubMed:9251681)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti67 – 671M → V.
Corresponds to variant rs2233319 [ dbSNP | Ensembl ].
VAR_050234
Natural varianti111 – 1111M → L.
Corresponds to variant rs2233328 [ dbSNP | Ensembl ].
VAR_050235

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8181Missing in isoform 3. 1 PublicationVSP_045037Add
BLAST
Alternative sequencei1 – 6666Missing in isoform 2. 1 PublicationVSP_045038Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34945.1. [Q92597-1]
CCDS59112.1. [Q92597-3]
CCDS59113.1. [Q92597-2]
RefSeqiNP_001128714.1. NM_001135242.1. [Q92597-1]
NP_001245361.1. NM_001258432.1. [Q92597-2]
NP_001245362.1. NM_001258433.1. [Q92597-3]
NP_006087.2. NM_006096.3. [Q92597-1]
UniGeneiHs.372914.
Hs.618002.

Genome annotation databases

EnsembliENST00000323851; ENSP00000319977; ENSG00000104419. [Q92597-1]
ENST00000414097; ENSP00000404854; ENSG00000104419. [Q92597-1]
ENST00000522476; ENSP00000427894; ENSG00000104419. [Q92597-2]
ENST00000537882; ENSP00000437443; ENSG00000104419. [Q92597-3]
GeneIDi10397.
KEGGihsa:10397.
UCSCiuc003yuf.1. human. [Q92597-1]

Polymorphism databases

DMDMi6166568.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS34945.1. [Q92597-1 ]
CCDS59112.1. [Q92597-3 ]
CCDS59113.1. [Q92597-2 ]
RefSeqi NP_001128714.1. NM_001135242.1. [Q92597-1 ]
NP_001245361.1. NM_001258432.1. [Q92597-2 ]
NP_001245362.1. NM_001258433.1. [Q92597-3 ]
NP_006087.2. NM_006096.3. [Q92597-1 ]
UniGenei Hs.372914.
Hs.618002.

3D structure databases

ProteinModelPortali Q92597.
SMRi Q92597. Positions 35-311.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115669. 86 interactions.
IntActi Q92597. 64 interactions.
MINTi MINT-4999487.
STRINGi 9606.ENSP00000319977.

Protein family/group databases

MEROPSi S33.988.

PTM databases

PhosphoSitei Q92597.

Polymorphism databases

DMDMi 6166568.

Proteomic databases

MaxQBi Q92597.
PaxDbi Q92597.
PRIDEi Q92597.

Protocols and materials databases

DNASUi 10397.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000323851 ; ENSP00000319977 ; ENSG00000104419 . [Q92597-1 ]
ENST00000414097 ; ENSP00000404854 ; ENSG00000104419 . [Q92597-1 ]
ENST00000522476 ; ENSP00000427894 ; ENSG00000104419 . [Q92597-2 ]
ENST00000537882 ; ENSP00000437443 ; ENSG00000104419 . [Q92597-3 ]
GeneIDi 10397.
KEGGi hsa:10397.
UCSCi uc003yuf.1. human. [Q92597-1 ]

Organism-specific databases

CTDi 10397.
GeneCardsi GC08M134249.
GeneReviewsi NDRG1.
HGNCi HGNC:7679. NDRG1.
HPAi HPA006881.
MIMi 601455. phenotype.
605262. gene.
neXtProti NX_Q92597.
Orphaneti 99950. Charcot-Marie-Tooth disease type 4D.
PharmGKBi PA31482.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG310435.
GeneTreei ENSGT00390000001874.
HOGENOMi HOG000230891.
HOVERGENi HBG052591.
InParanoidi Q92597.
KOi K18266.
OMAi TLHGSIH.
OrthoDBi EOG7KH9JS.
PhylomeDBi Q92597.
TreeFami TF313168.

Miscellaneous databases

ChiTaRSi NDRG1. human.
GeneWikii NDRG1.
GenomeRNAii 10397.
NextBioi 39394.
PROi Q92597.
SOURCEi Search...

Gene expression databases

Bgeei Q92597.
CleanExi HS_DRG1.
HS_NDRG1.
ExpressionAtlasi Q92597. baseline and differential.
Genevestigatori Q92597.

Family and domain databases

Gene3Di 3.40.50.1820. 1 hit.
InterProi IPR029058. AB_hydrolase.
IPR004142. NDRG.
[Graphical view ]
PANTHERi PTHR11034. PTHR11034. 1 hit.
Pfami PF03096. Ndr. 1 hit.
[Graphical view ]
SUPFAMi SSF53474. SSF53474. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. 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. 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.

Entry informationi

Entry nameiNDRG1_HUMAN
AccessioniPrimary (citable) accession number: Q92597
Secondary accession number(s): B3KR80
, B7Z446, O15207, Q6IBG2, Q9NYR6, Q9UK29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: February 1, 1997
Last modified: October 29, 2014
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3