Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9UN36 (NDRG2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 NDRG2
Alternative name(s):
N-myc downstream-regulated gene 2 protein
Protein Syld709613
Gene names
Name:NDRG2
Synonyms:KIAA1248, SYLD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length371 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Contributes to the regulation of the Wnt signaling pathway. Down-regulates CTNNB1-mediated transcriptional activation of target genes, such as CCND1, and may thereby act as tumor suppressor. May be involved in dendritic cell and neuron differentiation. Ref.3 Ref.15 Ref.21

Subunit structure

Interacts with CTNNB1. Ref.21

Subcellular location

Cytoplasm. Cytoplasmperinuclear region. Cell projectiongrowth cone By similarity. Note: In neurons, seems to concentrate at axonal growth cone. Perinuclear in neurons By similarity. Ref.1 Ref.13

Tissue specificity

Highly expressed in brain, heart, skeletal muscle and salivary gland, and moderately in kidney and liver. Expressed in dendritic cells, but not in other blood cells. Expression levels are low in pancreatic and liver cancer tissues; absent in meningioma. Expressed in low-grade gliomas but present at low levels in glioblastoma. Isoform 1 and isoform 2 are present in brain neurons and up-regulated in Alzheimer disease (at protein level). Ref.1 Ref.2 Ref.3 Ref.12 Ref.13 Ref.14 Ref.15

Developmental stage

Specifically expressed during dendritic cell differentiation (in vitro). Expression is low in fetal brain and increases during brain postnatal development. Ref.12 Ref.13

Sequence similarities

Belongs to the NDRG family.

Caution

Has some similarity to hydrolases, but lacks the conserved Ser-His-Asp catalytic triad. Has no hydrolase activity towards p-nitrophenylbutyrate (in vitro).

Sequence caution

The sequence BAA86562.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence CAD62350.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
Wnt signaling pathway
   Cellular componentCell projection
Cytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseTumor suppressor
   Molecular functionDevelopmental protein
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of ERK1 and ERK2 cascade

Inferred from electronic annotation. Source: Ensembl

negative regulation of cytokine production

Inferred from electronic annotation. Source: Ensembl

negative regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of platelet-derived growth factor production

Inferred from electronic annotation. Source: Ensembl

regulation of vascular endothelial growth factor production

Inferred from electronic annotation. Source: Ensembl

substantia nigra development

Inferred from expression pattern PubMed 22926577. Source: UniProt

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: LIFEdb

centrosome

Inferred from direct assay. Source: HPA

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Non-traceable author statement Ref.2. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708PubMed 23376485. Source: UniProt

growth cone

Inferred from electronic annotation. Source: UniProtKB-SubCell

microtubule organizing center

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 21217774PubMed 23068607. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ESR1P033722EBI-3895741,EBI-78473
RABAC1Q9UI147EBI-8084503,EBI-712367

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UN36-1)

Also known as: NDRG2ins;

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: Q9UN36-2)

Also known as: NDRG2var;

The sequence of this isoform differs from the canonical sequence as follows:
     26-39: Missing.
Isoform 3 (identifier: Q9UN36-3)

The sequence of this isoform differs from the canonical sequence as follows:
     262-272: Missing.
Isoform 4 (identifier: Q9UN36-4)

The sequence of this isoform differs from the canonical sequence as follows:
     26-39: Missing.
     157-185: Missing.
Isoform 5 (identifier: Q9UN36-5)

The sequence of this isoform differs from the canonical sequence as follows:
     26-39: Missing.
     272-287: Missing.
Isoform 6 (identifier: Q9UN36-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MENGGSMQATM
     26-39: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.17
Chain2 – 371370Protein NDRG2
PRO_0000159575

Amino acid modifications

Modified residue21N-acetylalanine Ref.17 Ref.20
Modified residue3261Phosphoserine By similarity
Modified residue3281Phosphoserine Ref.18
Modified residue3301Phosphothreonine By similarity
Modified residue3321Phosphoserine Ref.18
Modified residue3341Phosphothreonine By similarity
Modified residue3351Phosphoserine By similarity
Modified residue3381Phosphoserine Ref.16 Ref.18
Modified residue3481Phosphothreonine Ref.18
Modified residue3501Phosphoserine By similarity
Modified residue3571Phosphothreonine By similarity

Natural variations

Alternative sequence11M → MENGGSMQATM in isoform 6.
VSP_054583
Alternative sequence26 – 3914Missing in isoform 2, isoform 4, isoform 5 and isoform 6.
VSP_003417
Alternative sequence157 – 18529Missing in isoform 4.
VSP_019007
Alternative sequence262 – 27211Missing in isoform 3.
VSP_003418
Alternative sequence272 – 28716Missing in isoform 5.
VSP_019008
Natural variant451T → S.
Corresponds to variant rs36007455 [ dbSNP | Ensembl ].
VAR_050236
Natural variant481G → V. Ref.11
Corresponds to variant rs11552412 [ dbSNP | Ensembl ].
VAR_026572

Experimental info

Mutagenesis1861L → D: Decreased interaction with CTNNB1. Abolishes down-regulation of Wnt signaling. Ref.21
Sequence conflict541V → A in AAL08624. Ref.2
Sequence conflict1231Q → E in AAH93038. Ref.11
Sequence conflict1721D → G in AAK50340. Ref.3
Sequence conflict2501D → N in AAL08624. Ref.2
Sequence conflict2821Q → R in AAH93038. Ref.11
Sequence conflict2961Q → R in AAK50340. Ref.3
Sequence conflict3061A → V in AAL08624. Ref.2

Secondary structure

.................................................. 371
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (NDRG2ins) [UniParc].

Last modified January 23, 2002. Version 2.
Checksum: 7B49B0B12BD3F595

FASTA37140,798
        10         20         30         40         50         60 
MAELQEVQIT EEKPLLPGQT PEAAKEAELA ARILLDQGQT HSVETPYGSV TFTVYGTPKP 

        70         80         90        100        110        120 
KRPAILTYHD VGLNYKSCFQ PLFQFEDMQE IIQNFVRVHV DAPGMEEGAP VFPLGYQYPS 

       130        140        150        160        170        180 
LDQLADMIPC VLQYLNFSTI IGVGVGAGAY ILARYALNHP DTVEGLVLIN IDPNAKGWMD 

       190        200        210        220        230        240 
WAAHKLTGLT SSIPEMILGH LFSQEELSGN SELIQKYRNI ITHAPNLDNI ELYWNSYNNR 

       250        260        270        280        290        300 
RDLNFERGGD ITLRCPVMLV VGDQAPHEDA VVECNSKLDP TQTSFLKMAD SGGQPQLTQP 

       310        320        330        340        350        360 
GKLTEAFKYF LQGMGYMASS CMTRLSRSRT ASLTSAASVD GNRSRSRTLS QSSESGTLSS 

       370 
GPPGHTMEVS C 

« Hide

Isoform 2 (NDRG2var) [UniParc].

Checksum: DD793CDC7173704A
Show »

FASTA35739,289
Isoform 3 [UniParc].

Checksum: CB10621C98F95CED
Show »

FASTA36039,679
Isoform 4 [UniParc].

Checksum: 3B2E97F79C3E2875
Show »

FASTA32836,052
Isoform 5 [UniParc].

Checksum: 0A213AAB643816C8
Show »

FASTA34137,497
Isoform 6 [UniParc].

Checksum: 26CE96CF6F63D0D6
Show »

FASTA36740,297

References

« Hide 'large scale' references
[1]"Characterization of the human NDRG gene family: a newly identified member, NDRG4, is specifically expressed in brain and heart."
Zhou R.-H., Kokame K., Tsukamoto Y., Yutani C., Kato H., Miyata T.
Genomics 73:86-97(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[2]"Characterization and expression of three novel differentiation-related genes belong to the human NDRG gene family."
Qu X., Zhai Y., Wei H., Zhang C., Xing G., Yu Y., He F.
Mol. Cell. Biochem. 229:35-44(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[3]"N-Myc downstream-regulated gene 2 (NDRG2) inhibits glioblastoma cell proliferation."
Deng Y., Yao L., Chau L., Ng S.S.-M., Peng Y., Liu X., Au W.-S., Wang J., Li F., Ji S., Han H., Nie X., Li Q., Kung H.-F., Leung S.-Y., Lin M.C.-M.
Int. J. Cancer 106:342-347(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), TISSUE SPECIFICITY, FUNCTION.
Tissue: Brain.
[4]"Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[5]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Amygdala.
[6]"Full-length cDNA libraries and normalization."
Li W.B., Gruber C., Jessee J., Polayes D.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
Tissue: Neuroblastoma.
[7]"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 AND 6).
Tissue: Cerebellum and Small intestine.
[8]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Hippocampus.
[9]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]"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] (ISOFORMS 2 AND 3), VARIANT VAL-48.
Tissue: Brain.
[12]"Expression and regulation of NDRG2 (N-myc downstream regulated gene 2) during the differentiation of dendritic cells."
Choi S.-C., Kim K.D., Kim J.-T., Kim J.-W., Yoon D.-Y., Choe Y.-K., Chang Y.-S., Paik S.-G., Lim J.-S.
FEBS Lett. 553:413-418(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[13]"NDRG2: a novel Alzheimer's disease associated protein."
Mitchelmore C., Buechmann-Moller S., Rask L., West M.J., Troncoso J.C., Jensen N.A.
Neurobiol. Dis. 16:48-58(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION.
[14]"NDRG2 expression and mutation in human liver and pancreatic cancers."
Hu X.-L., Liu X.-P., Lin S.-X., Deng Y.-C., Liu N., Li X., Yao L.-B.
World J. Gastroenterol. 10:3518-3521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[15]"Integrative genomic analysis identifies NDRG2 as a candidate tumor suppressor gene frequently inactivated in clinically aggressive meningioma."
Lusis E.A., Watson M.A., Chicoine M.R., Lyman M., Roerig P., Reifenberger G., Gutmann D.H., Perry A.
Cancer Res. 65:7121-7126(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, FUNCTION.
[16]"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-338, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[18]"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 SER-328; SER-332; SER-338 AND THR-348, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[19]"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].
[20]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Crystal structure of the human N-Myc downstream-regulated gene 2 protein provides insight into its role as a tumor suppressor."
Hwang J., Kim Y., Kang H.B., Jaroszewski L., Deacon A.M., Lee H., Choi W.C., Kim K.J., Kim C.H., Kang B.S., Lee J.O., Oh T.K., Kim J.W., Wilson I.A., Kim M.H.
J. Biol. Chem. 286:12450-12460(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 40-318, FUNCTION, INTERACTION WITH CTNNB1, MUTAGENESIS OF LEU-186, ABSENCE OF HYDROLASE ACTIVITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF304051 mRNA. Translation: AAL08624.1.
AF159092 mRNA. Translation: AAD43131.2.
AY028430 Genomic DNA. Translation: AAK50340.1.
AB033074 mRNA. Translation: BAA86562.1. Different initiation.
AL136574 mRNA. Translation: CAB66509.1.
BX247987 mRNA. Translation: CAD62321.1.
BX248031 mRNA. Translation: CAD62350.1. Different initiation.
AK096999 mRNA. Translation: BAG53405.1.
AK293514 mRNA. Translation: BAG56997.1.
CR749252 mRNA. Translation: CAH18108.1.
AL161668 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW66423.1.
CH471078 Genomic DNA. Translation: EAW66422.1.
CH471078 Genomic DNA. Translation: EAW66424.1.
CH471078 Genomic DNA. Translation: EAW66425.1.
CH471078 Genomic DNA. Translation: EAW66426.1.
CH471078 Genomic DNA. Translation: EAW66427.1.
CH471078 Genomic DNA. Translation: EAW66428.1.
CH471078 Genomic DNA. Translation: EAW66429.1.
CH471078 Genomic DNA. Translation: EAW66430.1.
BC010458 mRNA. Translation: AAH10458.1.
BC011240 mRNA. Translation: AAH11240.1.
BC093038 mRNA. Translation: AAH93038.1.
CCDSCCDS61384.1. [Q9UN36-3]
CCDS9564.1. [Q9UN36-2]
CCDS9565.1. [Q9UN36-1]
RefSeqNP_001269140.1. NM_001282211.1. [Q9UN36-6]
NP_001269141.1. NM_001282212.1. [Q9UN36-5]
NP_001269142.1. NM_001282213.1. [Q9UN36-2]
NP_001269143.1. NM_001282214.1. [Q9UN36-2]
NP_001269144.1. NM_001282215.1. [Q9UN36-3]
NP_001269145.1. NM_001282216.1.
NP_057334.1. NM_016250.2. [Q9UN36-2]
NP_963293.1. NM_201535.1. [Q9UN36-1]
NP_963294.1. NM_201536.1. [Q9UN36-2]
NP_963831.1. NM_201537.1. [Q9UN36-1]
NP_963832.1. NM_201538.1. [Q9UN36-2]
NP_963833.1. NM_201539.1. [Q9UN36-1]
NP_963834.1. NM_201540.1. [Q9UN36-1]
NP_963835.1. NM_201541.1. [Q9UN36-2]
UniGeneHs.525205.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2XMQX-ray2.81A/B/C40-318[»]
2XMRX-ray2.00A/B/C40-318[»]
2XMSX-ray2.15A40-318[»]
ProteinModelPortalQ9UN36.
SMRQ9UN36. Positions 38-318.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121520. 2 interactions.
IntActQ9UN36. 3 interactions.
MINTMINT-3082604.

PTM databases

PhosphoSiteQ9UN36.

Polymorphism databases

DMDM20141615.

Proteomic databases

MaxQBQ9UN36.
PaxDbQ9UN36.
PRIDEQ9UN36.

Protocols and materials databases

DNASU57447.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000298684; ENSP00000298684; ENSG00000165795. [Q9UN36-4]
ENST00000298687; ENSP00000298687; ENSG00000165795. [Q9UN36-1]
ENST00000350792; ENSP00000344620; ENSG00000165795. [Q9UN36-2]
ENST00000360463; ENSP00000353649; ENSG00000165795. [Q9UN36-2]
ENST00000397844; ENSP00000380943; ENSG00000165795. [Q9UN36-5]
ENST00000397847; ENSP00000380945; ENSG00000165795. [Q9UN36-3]
ENST00000397851; ENSP00000380949; ENSG00000165795. [Q9UN36-1]
ENST00000397853; ENSP00000380951; ENSG00000165795. [Q9UN36-1]
ENST00000397855; ENSP00000380953; ENSG00000165795. [Q9UN36-4]
ENST00000397856; ENSP00000380954; ENSG00000165795. [Q9UN36-5]
ENST00000397858; ENSP00000380956; ENSG00000165795. [Q9UN36-1]
ENST00000403829; ENSP00000385889; ENSG00000165795.
ENST00000553503; ENSP00000452306; ENSG00000165795. [Q9UN36-2]
ENST00000554143; ENSP00000452006; ENSG00000165795. [Q9UN36-2]
ENST00000555158; ENSP00000452038; ENSG00000165795. [Q9UN36-2]
ENST00000556147; ENSP00000451712; ENSG00000165795. [Q9UN36-1]
GeneID57447.
KEGGhsa:57447.
UCSCuc001vyt.3. human. [Q9UN36-1]
uc001vyu.3. human. [Q9UN36-4]
uc001vyv.3. human. [Q9UN36-2]
uc001vzc.3. human. [Q9UN36-5]
uc010aig.3. human. [Q9UN36-3]

Organism-specific databases

CTD57447.
GeneCardsGC14M021484.
HGNCHGNC:14460. NDRG2.
HPACAB017491.
HPA002896.
HPA003590.
MIM605272. gene.
neXtProtNX_Q9UN36.
PharmGKBPA31483.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG310435.
HOVERGENHBG052591.
InParanoidQ9UN36.
OMAFQFGDMQ.
OrthoDBEOG7KH9JS.
PhylomeDBQ9UN36.
TreeFamTF313168.

Gene expression databases

ArrayExpressQ9UN36.
BgeeQ9UN36.
GenevestigatorQ9UN36.

Family and domain databases

Gene3D3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR004142. NDRG.
[Graphical view]
PANTHERPTHR11034. PTHR11034. 1 hit.
PfamPF03096. Ndr. 1 hit.
[Graphical view]
SUPFAMSSF53474. SSF53474. 1 hit.
ProtoNetSearch...

Other

ChiTaRSNDRG2. human.
EvolutionaryTraceQ9UN36.
GeneWikiNDRG2.
GenomeRNAi57447.
NextBio35471146.
PROQ9UN36.
SOURCESearch...

Entry information

Entry nameNDRG2_HUMAN
AccessionPrimary (citable) accession number: Q9UN36
Secondary accession number(s): B3KUE3 expand/collapse secondary AC list , B4DE86, B7WP11, B7WPD5, D3DS07, D3DS10, Q567T1, Q68DW2, Q86U08, Q86U46, Q96FD3, Q96FT0, Q96JU0, Q96PN0, Q9BQH5, Q9ULH2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 23, 2002
Last modified: July 9, 2014
This is version 120 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 14

Human chromosome 14: entries, gene names and cross-references to MIM