NDRG2_HUMAN
ID NDRG2_HUMAN Reviewed; 371 AA.
AC Q9UN36; B3KUE3; B4DE86; B7WP11; B7WPD5; D3DS07; D3DS10; Q567T1; Q68DW2;
AC Q86U08; Q86U46; Q96FD3; Q96FT0; Q96JU0; Q96PN0; Q9BQH5; Q9ULH2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Protein NDRG2;
DE AltName: Full=N-myc downstream-regulated gene 2 protein;
DE AltName: Full=Protein Syld709613;
GN Name=NDRG2; Synonyms=KIAA1248, SYLD;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=11352569; DOI=10.1006/geno.2000.6496;
RA Zhou R.-H., Kokame K., Tsukamoto Y., Yutani C., Kato H., Miyata T.;
RT "Characterization of the human NDRG gene family: a newly identified member,
RT NDRG4, is specifically expressed in brain and heart.";
RL Genomics 73:86-97(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=11936845; DOI=10.1023/a:1017934810825;
RA Qu X., Zhai Y., Wei H., Zhang C., Xing G., Yu Y., He F.;
RT "Characterization and expression of three novel differentiation-related
RT genes belong to the human NDRG gene family.";
RL Mol. Cell. Biochem. 229:35-44(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), TISSUE SPECIFICITY,
RP AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=12845671; DOI=10.1002/ijc.11228;
RA Deng Y., Yao L., Chau L., Ng S.S.-M., Peng Y., Liu X., Au W.-S., Wang J.,
RA Li F., Ji S., Han H., Nie X., Li Q., Kung H.-F., Leung S.-Y., Lin M.C.-M.;
RT "N-Myc downstream-regulated gene 2 (NDRG2) inhibits glioblastoma cell
RT proliferation.";
RL Int. J. Cancer 106:342-347(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Amygdala;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
RC TISSUE=Neuroblastoma;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6).
RC TISSUE=Cerebellum, and Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Hippocampus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP VAL-48.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [12]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=14572661; DOI=10.1016/s0014-5793(03)01030-5;
RA Choi S.-C., Kim K.D., Kim J.-T., Kim J.-W., Yoon D.-Y., Choe Y.-K.,
RA Chang Y.-S., Paik S.-G., Lim J.-S.;
RT "Expression and regulation of NDRG2 (N-myc downstream regulated gene 2)
RT during the differentiation of dendritic cells.";
RL FEBS Lett. 553:413-418(2003).
RN [13]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=15207261; DOI=10.1016/j.nbd.2004.01.003;
RA Mitchelmore C., Buechmann-Moller S., Rask L., West M.J., Troncoso J.C.,
RA Jensen N.A.;
RT "NDRG2: a novel Alzheimer's disease associated protein.";
RL Neurobiol. Dis. 16:48-58(2004).
RN [14]
RP TISSUE SPECIFICITY.
RX PubMed=15526377; DOI=10.3748/wjg.v10.i23.3518;
RA Hu X.-L., Liu X.-P., Lin S.-X., Deng Y.-C., Liu N., Li X., Yao L.-B.;
RT "NDRG2 expression and mutation in human liver and pancreatic cancers.";
RL World J. Gastroenterol. 10:3518-3521(2004).
RN [15]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=16103061; DOI=10.1158/0008-5472.can-05-0043;
RA Lusis E.A., Watson M.A., Chicoine M.R., Lyman M., Roerig P.,
RA Reifenberger G., Gutmann D.H., Perry A.;
RT "Integrative genomic analysis identifies NDRG2 as a candidate tumor
RT suppressor gene frequently inactivated in clinically aggressive
RT meningioma.";
RL Cancer Res. 65:7121-7126(2005).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328; SER-332; SER-338 AND
RP THR-348, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-330; SER-332 AND SER-338, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20; SER-326; SER-328;
RP THR-330; SER-332; THR-334; SER-338 AND SER-344, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 40-318, FUNCTION, INTERACTION WITH
RP CTNNB1, MUTAGENESIS OF LEU-186, AND ABSENCE OF HYDROLASE ACTIVITY.
RX PubMed=21247902; DOI=10.1074/jbc.m110.170803;
RA Hwang J., Kim Y., Kang H.B., Jaroszewski L., Deacon A.M., Lee H.,
RA Choi W.C., Kim K.J., Kim C.H., Kang B.S., Lee J.O., Oh T.K., Kim J.W.,
RA Wilson I.A., Kim M.H.;
RT "Crystal structure of the human N-Myc downstream-regulated gene 2 protein
RT provides insight into its role as a tumor suppressor.";
RL J. Biol. Chem. 286:12450-12460(2011).
CC -!- FUNCTION: Contributes to the regulation of the Wnt signaling pathway.
CC Down-regulates CTNNB1-mediated transcriptional activation of target
CC genes, such as CCND1, and may thereby act as tumor suppressor. May be
CC involved in dendritic cell and neuron differentiation.
CC {ECO:0000269|PubMed:12845671, ECO:0000269|PubMed:16103061,
CC ECO:0000269|PubMed:21247902}.
CC -!- SUBUNIT: Interacts with CTNNB1. {ECO:0000269|PubMed:21247902}.
CC -!- INTERACTION:
CC Q9UN36; P03372: ESR1; NbExp=2; IntAct=EBI-3895741, EBI-78473;
CC Q9UN36-1; Q9UI14: RABAC1; NbExp=7; IntAct=EBI-8084503, EBI-712367;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region. Cell
CC projection, growth cone {ECO:0000250}. Note=In neurons, seems to
CC concentrate at axonal growth cone. Perinuclear in neurons (By
CC similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=NDRG2ins;
CC IsoId=Q9UN36-1; Sequence=Displayed;
CC Name=2; Synonyms=NDRG2var;
CC IsoId=Q9UN36-2; Sequence=VSP_003417;
CC Name=3;
CC IsoId=Q9UN36-3; Sequence=VSP_003418;
CC Name=4;
CC IsoId=Q9UN36-4; Sequence=VSP_003417, VSP_019007;
CC Name=5;
CC IsoId=Q9UN36-5; Sequence=VSP_003417, VSP_019008;
CC Name=6;
CC IsoId=Q9UN36-6; Sequence=VSP_054583, VSP_003417;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, heart, skeletal muscle
CC and salivary gland, and moderately in kidney and liver. Expressed in
CC dendritic cells, but not in other blood cells. Expression levels are
CC low in pancreatic and liver cancer tissues; absent in meningioma.
CC Expressed in low-grade gliomas but present at low levels in
CC glioblastoma. Isoform 1 and isoform 2 are present in brain neurons and
CC up-regulated in Alzheimer disease (at protein level).
CC {ECO:0000269|PubMed:11352569, ECO:0000269|PubMed:11936845,
CC ECO:0000269|PubMed:12845671, ECO:0000269|PubMed:14572661,
CC ECO:0000269|PubMed:15207261, ECO:0000269|PubMed:15526377,
CC ECO:0000269|PubMed:16103061}.
CC -!- DEVELOPMENTAL STAGE: Specifically expressed during dendritic cell
CC differentiation (in vitro). Expression is low in fetal brain and
CC increases during brain postnatal development.
CC {ECO:0000269|PubMed:14572661, ECO:0000269|PubMed:15207261}.
CC -!- SIMILARITY: Belongs to the NDRG family. {ECO:0000305}.
CC -!- CAUTION: Has some similarity to hydrolases, but lacks the conserved
CC Ser-His-Asp catalytic triad. Has no hydrolase activity towards p-
CC nitrophenylbutyrate (in vitro). {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86562.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD62350.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/NDRG2ID41513ch14q11.html";
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DR EMBL; AF304051; AAL08624.1; -; mRNA.
DR EMBL; AF159092; AAD43131.2; -; mRNA.
DR EMBL; AY028430; AAK50340.1; -; Genomic_DNA.
DR EMBL; AB033074; BAA86562.1; ALT_INIT; mRNA.
DR EMBL; AL136574; CAB66509.1; -; mRNA.
DR EMBL; BX247987; CAD62321.1; -; mRNA.
DR EMBL; BX248031; CAD62350.1; ALT_INIT; mRNA.
DR EMBL; AK096999; BAG53405.1; -; mRNA.
DR EMBL; AK293514; BAG56997.1; -; mRNA.
DR EMBL; CR749252; CAH18108.1; -; mRNA.
DR EMBL; AL161668; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW66423.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66422.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66424.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66425.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66426.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66427.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66428.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66429.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66430.1; -; Genomic_DNA.
DR EMBL; BC010458; AAH10458.1; -; mRNA.
DR EMBL; BC011240; AAH11240.1; -; mRNA.
DR EMBL; BC093038; AAH93038.1; -; mRNA.
DR CCDS; CCDS61384.1; -. [Q9UN36-3]
DR CCDS; CCDS61386.1; -. [Q9UN36-6]
DR CCDS; CCDS73613.1; -. [Q9UN36-5]
DR CCDS; CCDS9564.1; -. [Q9UN36-2]
DR CCDS; CCDS9565.1; -. [Q9UN36-1]
DR RefSeq; NP_001269140.1; NM_001282211.1. [Q9UN36-6]
DR RefSeq; NP_001269141.1; NM_001282212.1. [Q9UN36-5]
DR RefSeq; NP_001269142.1; NM_001282213.1. [Q9UN36-2]
DR RefSeq; NP_001269143.1; NM_001282214.1. [Q9UN36-2]
DR RefSeq; NP_001269144.1; NM_001282215.1. [Q9UN36-3]
DR RefSeq; NP_001269145.1; NM_001282216.1.
DR RefSeq; NP_001307258.1; NM_001320329.1. [Q9UN36-1]
DR RefSeq; NP_057334.1; NM_016250.2. [Q9UN36-2]
DR RefSeq; NP_963293.1; NM_201535.1. [Q9UN36-1]
DR RefSeq; NP_963294.1; NM_201536.1. [Q9UN36-2]
DR RefSeq; NP_963831.1; NM_201537.1. [Q9UN36-1]
DR RefSeq; NP_963832.1; NM_201538.1. [Q9UN36-2]
DR RefSeq; NP_963833.1; NM_201539.1. [Q9UN36-1]
DR RefSeq; NP_963834.1; NM_201540.1. [Q9UN36-1]
DR RefSeq; NP_963835.1; NM_201541.1. [Q9UN36-2]
DR RefSeq; XP_011535298.1; XM_011536996.2.
DR RefSeq; XP_011535299.1; XM_011536997.1.
DR RefSeq; XP_011535300.1; XM_011536998.1.
DR RefSeq; XP_011535301.1; XM_011536999.1.
DR RefSeq; XP_011535303.1; XM_011537001.1.
DR RefSeq; XP_011535304.1; XM_011537002.1.
DR PDB; 2XMQ; X-ray; 2.81 A; A/B/C=40-318.
DR PDB; 2XMR; X-ray; 2.00 A; A/B/C=40-318.
DR PDB; 2XMS; X-ray; 2.15 A; A=40-318.
DR PDBsum; 2XMQ; -.
DR PDBsum; 2XMR; -.
DR PDBsum; 2XMS; -.
DR AlphaFoldDB; Q9UN36; -.
DR SMR; Q9UN36; -.
DR BioGRID; 121520; 53.
DR IntAct; Q9UN36; 12.
DR MINT; Q9UN36; -.
DR STRING; 9606.ENSP00000451712; -.
DR ESTHER; human-NDRG2; Ndr_family.
DR iPTMnet; Q9UN36; -.
DR PhosphoSitePlus; Q9UN36; -.
DR SwissPalm; Q9UN36; -.
DR BioMuta; NDRG2; -.
DR DMDM; 20141615; -.
DR EPD; Q9UN36; -.
DR jPOST; Q9UN36; -.
DR MassIVE; Q9UN36; -.
DR MaxQB; Q9UN36; -.
DR PaxDb; Q9UN36; -.
DR PeptideAtlas; Q9UN36; -.
DR PRIDE; Q9UN36; -.
DR ProteomicsDB; 3929; -.
DR ProteomicsDB; 85243; -. [Q9UN36-1]
DR ProteomicsDB; 85244; -. [Q9UN36-2]
DR ProteomicsDB; 85245; -. [Q9UN36-3]
DR ProteomicsDB; 85246; -. [Q9UN36-4]
DR ProteomicsDB; 85247; -. [Q9UN36-5]
DR Antibodypedia; 142; 388 antibodies from 38 providers.
DR DNASU; 57447; -.
DR Ensembl; ENST00000298684.9; ENSP00000298684.5; ENSG00000165795.25. [Q9UN36-4]
DR Ensembl; ENST00000298687.9; ENSP00000298687.5; ENSG00000165795.25. [Q9UN36-1]
DR Ensembl; ENST00000350792.7; ENSP00000344620.3; ENSG00000165795.25. [Q9UN36-2]
DR Ensembl; ENST00000360463.7; ENSP00000353649.3; ENSG00000165795.25. [Q9UN36-2]
DR Ensembl; ENST00000397844.6; ENSP00000380943.2; ENSG00000165795.25. [Q9UN36-5]
DR Ensembl; ENST00000397847.6; ENSP00000380945.2; ENSG00000165795.25. [Q9UN36-3]
DR Ensembl; ENST00000397851.6; ENSP00000380949.2; ENSG00000165795.25. [Q9UN36-1]
DR Ensembl; ENST00000397853.7; ENSP00000380951.3; ENSG00000165795.25. [Q9UN36-1]
DR Ensembl; ENST00000397858.5; ENSP00000380956.1; ENSG00000165795.25. [Q9UN36-1]
DR Ensembl; ENST00000403829.7; ENSP00000385889.3; ENSG00000165795.25. [Q9UN36-6]
DR Ensembl; ENST00000553503.5; ENSP00000452306.1; ENSG00000165795.25. [Q9UN36-2]
DR Ensembl; ENST00000554143.5; ENSP00000452006.1; ENSG00000165795.25. [Q9UN36-2]
DR Ensembl; ENST00000555158.5; ENSP00000452038.1; ENSG00000165795.25. [Q9UN36-2]
DR Ensembl; ENST00000556147.6; ENSP00000451712.1; ENSG00000165795.25. [Q9UN36-1]
DR GeneID; 57447; -.
DR KEGG; hsa:57447; -.
DR MANE-Select; ENST00000556147.6; ENSP00000451712.1; NM_001320329.2; NP_001307258.1.
DR UCSC; uc001vyu.4; human. [Q9UN36-1]
DR CTD; 57447; -.
DR DisGeNET; 57447; -.
DR GeneCards; NDRG2; -.
DR HGNC; HGNC:14460; NDRG2.
DR HPA; ENSG00000165795; Tissue enhanced (brain, salivary gland, skeletal muscle).
DR MIM; 605272; gene.
DR neXtProt; NX_Q9UN36; -.
DR OpenTargets; ENSG00000165795; -.
DR PharmGKB; PA31483; -.
DR VEuPathDB; HostDB:ENSG00000165795; -.
DR eggNOG; KOG2931; Eukaryota.
DR GeneTree; ENSGT00950000182872; -.
DR InParanoid; Q9UN36; -.
DR OMA; KTCFQPL; -.
DR OrthoDB; 854690at2759; -.
DR PhylomeDB; Q9UN36; -.
DR TreeFam; TF313168; -.
DR PathwayCommons; Q9UN36; -.
DR SignaLink; Q9UN36; -.
DR SIGNOR; Q9UN36; -.
DR BioGRID-ORCS; 57447; 14 hits in 1079 CRISPR screens.
DR ChiTaRS; NDRG2; human.
DR EvolutionaryTrace; Q9UN36; -.
DR GeneWiki; NDRG2; -.
DR GenomeRNAi; 57447; -.
DR Pharos; Q9UN36; Tbio.
DR PRO; PR:Q9UN36; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9UN36; protein.
DR Bgee; ENSG00000165795; Expressed in right frontal lobe and 202 other tissues.
DR ExpressionAtlas; Q9UN36; baseline and differential.
DR Genevisible; Q9UN36; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; NAS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:LIFEdb.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0001818; P:negative regulation of cytokine production; IEA:Ensembl.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0090361; P:regulation of platelet-derived growth factor production; IEA:Ensembl.
DR GO; GO:0010574; P:regulation of vascular endothelial growth factor production; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
DR GO; GO:1990874; P:vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR004142; NDRG.
DR InterPro; IPR030690; NDRG2.
DR PANTHER; PTHR11034; PTHR11034; 1.
DR PANTHER; PTHR11034:SF17; PTHR11034:SF17; 1.
DR Pfam; PF03096; Ndr; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell projection;
KW Cytoplasm; Developmental protein; Differentiation; Neurogenesis;
KW Phosphoprotein; Reference proteome; Tumor suppressor;
KW Wnt signaling pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..371
FT /note="Protein NDRG2"
FT /id="PRO_0000441166"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 20
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 330
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 334
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYG0"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 348
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYG0"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYG0"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYG0"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYG0"
FT MOD_RES 357
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYG0"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYG0"
FT VAR_SEQ 1
FT /note="M -> MENGGSMQATM (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054583"
FT VAR_SEQ 26..39
FT /note="Missing (in isoform 2, isoform 4, isoform 5 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:10574462,
FT ECO:0000303|PubMed:12845671, ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005,
FT ECO:0000303|Ref.6"
FT /id="VSP_003417"
FT VAR_SEQ 157..185
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_019007"
FT VAR_SEQ 262..272
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_003418"
FT VAR_SEQ 272..287
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_019008"
FT VARIANT 45
FT /note="T -> S (in dbSNP:rs36007455)"
FT /id="VAR_050236"
FT VARIANT 48
FT /note="G -> V (in dbSNP:rs11552412)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_026572"
FT MUTAGEN 186
FT /note="L->D: Decreased interaction with CTNNB1. Abolishes
FT down-regulation of Wnt signaling."
FT /evidence="ECO:0000269|PubMed:21247902"
FT CONFLICT 54
FT /note="V -> A (in Ref. 2; AAL08624)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="Q -> E (in Ref. 11; AAH93038)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="D -> G (in Ref. 3; AAK50340)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="D -> N (in Ref. 2; AAL08624)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="Q -> R (in Ref. 11; AAH93038)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="Q -> R (in Ref. 3; AAK50340)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="A -> V (in Ref. 2; AAL08624)"
FT /evidence="ECO:0000305"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:2XMR"
FT STRAND 48..57
FT /evidence="ECO:0007829|PDB:2XMR"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:2XMR"
FT HELIX 75..78
FT /evidence="ECO:0007829|PDB:2XMR"
FT HELIX 80..84
FT /evidence="ECO:0007829|PDB:2XMR"
FT HELIX 86..92
FT /evidence="ECO:0007829|PDB:2XMR"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:2XMR"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:2XMR"
FT HELIX 128..135
FT /evidence="ECO:0007829|PDB:2XMR"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:2XMR"
FT HELIX 147..158
FT /evidence="ECO:0007829|PDB:2XMR"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:2XMR"
FT STRAND 163..170
FT /evidence="ECO:0007829|PDB:2XMR"
FT HELIX 178..187
FT /evidence="ECO:0007829|PDB:2XMR"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:2XMR"
FT HELIX 193..201
FT /evidence="ECO:0007829|PDB:2XMR"
FT HELIX 204..209
FT /evidence="ECO:0007829|PDB:2XMR"
FT HELIX 212..222
FT /evidence="ECO:0007829|PDB:2XMR"
FT HELIX 227..238
FT /evidence="ECO:0007829|PDB:2XMR"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:2XMR"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:2XMR"
FT HELIX 268..275
FT /evidence="ECO:0007829|PDB:2XMR"
FT TURN 280..282
FT /evidence="ECO:0007829|PDB:2XMR"
FT STRAND 283..288
FT /evidence="ECO:0007829|PDB:2XMR"
FT HELIX 295..298
FT /evidence="ECO:0007829|PDB:2XMR"
FT HELIX 300..314
FT /evidence="ECO:0007829|PDB:2XMR"
SQ SEQUENCE 371 AA; 40798 MW; 7B49B0B12BD3F595 CRC64;
MAELQEVQIT EEKPLLPGQT PEAAKEAELA ARILLDQGQT HSVETPYGSV TFTVYGTPKP
KRPAILTYHD VGLNYKSCFQ PLFQFEDMQE IIQNFVRVHV DAPGMEEGAP VFPLGYQYPS
LDQLADMIPC VLQYLNFSTI IGVGVGAGAY ILARYALNHP DTVEGLVLIN IDPNAKGWMD
WAAHKLTGLT SSIPEMILGH LFSQEELSGN SELIQKYRNI ITHAPNLDNI ELYWNSYNNR
RDLNFERGGD ITLRCPVMLV VGDQAPHEDA VVECNSKLDP TQTSFLKMAD SGGQPQLTQP
GKLTEAFKYF LQGMGYMASS CMTRLSRSRT ASLTSAASVD GNRSRSRTLS QSSESGTLSS
GPPGHTMEVS C
