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Q9QYG0

- NDRG2_MOUSE

UniProt

Q9QYG0 - NDRG2_MOUSE

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Protein

Protein NDRG2

Gene

Ndrg2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

GO - Biological processi

  1. cell differentiation Source: UniProtKB-KW
  2. negative regulation of cytokine production Source: MGI
  3. negative regulation of ERK1 and ERK2 cascade Source: MGI
  4. negative regulation of smooth muscle cell proliferation Source: MGI
  5. regulation of platelet-derived growth factor production Source: MGI
  6. regulation of vascular endothelial growth factor production Source: MGI
  7. substantia nigra development Source: Ensembl
  8. Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Neurogenesis, Wnt signaling pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Protein NDRG2
Alternative name(s):
N-myc downstream-regulated gene 2 protein
Protein Ndr2
Gene namesi
Name:Ndrg2
Synonyms:Kiaa1248, Ndr2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:1352498. Ndrg2.

Subcellular locationi

Cytoplasm 2 Publications. Cytoplasmperinuclear region By similarity. Cell projectiongrowth cone By similarity
Note: In neurons, seems to concentrate at axonal growth cone. Perinuclear in neurons (By similarity).By similarity

GO - Cellular componenti

  1. cell projection Source: UniProtKB-KW
  2. centrosome Source: Ensembl
  3. cytoplasm Source: MGI
  4. extracellular vesicular exosome Source: Ensembl
  5. Golgi apparatus Source: Ensembl
  6. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 371370Protein NDRG2PRO_0000159576Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei326 – 3261Phosphoserine1 Publication
Modified residuei328 – 3281Phosphoserine2 Publications
Modified residuei330 – 3301Phosphothreonine; by SGK13 Publications
Modified residuei332 – 3321Phosphoserine; by PKC/PRKCQ or SGK14 Publications
Modified residuei334 – 3341Phosphothreonine1 Publication
Modified residuei335 – 3351Phosphoserine1 Publication
Modified residuei338 – 3381Phosphoserine1 Publication
Modified residuei348 – 3481Phosphothreonine; by PKB/AKT1 or SGK12 Publications
Modified residuei350 – 3501Phosphoserine1 Publication
Modified residuei357 – 3571Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9QYG0.
PaxDbiQ9QYG0.
PRIDEiQ9QYG0.

PTM databases

PhosphoSiteiQ9QYG0.

Expressioni

Tissue specificityi

Expressed at highest levels in brain, heart and liver, and at lower levels in kidney, colon, skeletal muscle, adrenal gland, ovary and uterus (at protein level).3 Publications

Developmental stagei

Expression is restricted to the developing heart at the stage of 9.5 dpc, and increases after 11.5 dpc as development of tissues and organs proceeds. Present in many developing tissues including heart, brain, lung, liver, gut, kidney, skeletal muscle, cartilage and epidermis (at protein level).2 Publications

Gene expression databases

BgeeiQ9QYG0.
CleanExiMM_NDRG2.
ExpressionAtlasiQ9QYG0. baseline and differential.
GenevestigatoriQ9QYG0.

Interactioni

Subunit structurei

Interacts with CTNNB1.By similarity

Protein-protein interaction databases

IntActiQ9QYG0. 3 interactions.
MINTiMINT-1854707.

Structurei

Secondary structure

1
371
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi40 – 456Combined sources
Beta strandi48 – 569Combined sources
Beta strandi64 – 685Combined sources
Helixi75 – 839Combined sources
Helixi86 – 927Combined sources
Beta strandi97 – 1015Combined sources
Turni103 – 1053Combined sources
Helixi121 – 1266Combined sources
Helixi128 – 1358Combined sources
Beta strandi140 – 1456Combined sources
Helixi147 – 15812Combined sources
Helixi160 – 1623Combined sources
Beta strandi163 – 1708Combined sources
Helixi178 – 18811Combined sources
Helixi193 – 2019Combined sources
Helixi204 – 2085Combined sources
Helixi212 – 22211Combined sources
Helixi227 – 23812Combined sources
Beta strandi245 – 2473Combined sources
Beta strandi257 – 2626Combined sources
Helixi268 – 27710Combined sources
Helixi280 – 2823Combined sources
Beta strandi283 – 2886Combined sources
Helixi295 – 2984Combined sources
Helixi300 – 31112Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2QMQX-ray1.70A40-313[»]
ProteinModelPortaliQ9QYG0.
SMRiQ9QYG0. Positions 39-313.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9QYG0.

Family & Domainsi

Sequence similaritiesi

Belongs to the NDRG family.Curated

Phylogenomic databases

eggNOGiNOG310435.
GeneTreeiENSGT00390000001874.
HOGENOMiHOG000230891.
HOVERGENiHBG052591.
InParanoidiQ9QYG0.
OMAiFQFGDMQ.
OrthoDBiEOG7KH9JS.
PhylomeDBiQ9QYG0.
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 (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9QYG0-1) [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
MAELQEVQIT EEKPLLPGQT PETAKEAELA ARILLDQGQT HSVETPYGSV
60 70 80 90 100
TFTVYGTPKP KRPAIFTYHD VGLNYKSCFQ PLFRFGDMQE IIQNFVRVHV
110 120 130 140 150
DAPGMEEGAP VFPLGYQYPS LDQLADMIPC ILQYLNFSTI IGVGVGAGAY
160 170 180 190 200
ILSRYALNHP DTVEGLVLIN IDPNAKGWMD WAAHKLTGLT SSIPDMILGH
210 220 230 240 250
LFSQEELSGN SELIQKYRGI IQHAPNLENI ELYWNSYNNR RDLNFERGGE
260 270 280 290 300
TTLKCPVMLV VGDQAPHEDA VVECNSKLDP TQTSFLKMAD SGGQPQLTQP
310 320 330 340 350
GKLTEAFKYF LQGMGYMASS CMTRLSRSRT ASLTSAASID GSRSRSRTLS
360 370
QSSESGTLPS GPPGHTMEVS C
Length:371
Mass (Da):40,789
Last modified:May 1, 2000 - v1
Checksum:iA5237C04278197B2
GO
Isoform 2 (identifier: Q9QYG0-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     26-39: Missing.

Show »
Length:357
Mass (Da):39,281
Checksum:iE6A9E286AD92E7AC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti253 – 2531L → P in BAE39998. (PubMed:16141072)Curated
Sequence conflicti347 – 3471R → S in BAE39998. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei26 – 3914Missing in isoform 2. 1 PublicationVSP_019009Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB033921 mRNA. Translation: BAA85882.1.
AK076514 mRNA. Translation: BAC36373.1.
AK154597 mRNA. Translation: BAE32700.1.
AK158900 mRNA. Translation: BAE34721.1.
AK168011 mRNA. Translation: BAE39998.1.
BC012963 mRNA. Translation: AAH12963.1.
AK173136 mRNA. Translation: BAD32414.1.
CCDSiCCDS27047.1. [Q9QYG0-1]
CCDS49486.1. [Q9QYG0-2]
RefSeqiNP_001139431.1. NM_001145959.1. [Q9QYG0-2]
NP_038892.1. NM_013864.2. [Q9QYG0-1]
XP_006519164.1. XM_006519101.1. [Q9QYG0-1]
XP_006519165.1. XM_006519102.1. [Q9QYG0-1]
XP_006519166.1. XM_006519103.1. [Q9QYG0-1]
XP_006519167.1. XM_006519104.1. [Q9QYG0-2]
XP_006519168.1. XM_006519105.1. [Q9QYG0-2]
XP_006534714.1. XM_006534651.1. [Q9QYG0-1]
XP_006534715.1. XM_006534652.1. [Q9QYG0-1]
XP_006534716.1. XM_006534653.1. [Q9QYG0-1]
XP_006534717.1. XM_006534654.1. [Q9QYG0-1]
XP_006534719.1. XM_006534656.1. [Q9QYG0-2]
UniGeneiMm.26722.

Genome annotation databases

EnsembliENSMUST00000004673; ENSMUSP00000004673; ENSMUSG00000004558. [Q9QYG0-1]
ENSMUST00000111632; ENSMUSP00000107259; ENSMUSG00000004558. [Q9QYG0-2]
GeneIDi29811.
KEGGimmu:29811.
UCSCiuc007tnk.2. mouse. [Q9QYG0-1]
uc007tnl.2. mouse. [Q9QYG0-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB033921 mRNA. Translation: BAA85882.1 .
AK076514 mRNA. Translation: BAC36373.1 .
AK154597 mRNA. Translation: BAE32700.1 .
AK158900 mRNA. Translation: BAE34721.1 .
AK168011 mRNA. Translation: BAE39998.1 .
BC012963 mRNA. Translation: AAH12963.1 .
AK173136 mRNA. Translation: BAD32414.1 .
CCDSi CCDS27047.1. [Q9QYG0-1 ]
CCDS49486.1. [Q9QYG0-2 ]
RefSeqi NP_001139431.1. NM_001145959.1. [Q9QYG0-2 ]
NP_038892.1. NM_013864.2. [Q9QYG0-1 ]
XP_006519164.1. XM_006519101.1. [Q9QYG0-1 ]
XP_006519165.1. XM_006519102.1. [Q9QYG0-1 ]
XP_006519166.1. XM_006519103.1. [Q9QYG0-1 ]
XP_006519167.1. XM_006519104.1. [Q9QYG0-2 ]
XP_006519168.1. XM_006519105.1. [Q9QYG0-2 ]
XP_006534714.1. XM_006534651.1. [Q9QYG0-1 ]
XP_006534715.1. XM_006534652.1. [Q9QYG0-1 ]
XP_006534716.1. XM_006534653.1. [Q9QYG0-1 ]
XP_006534717.1. XM_006534654.1. [Q9QYG0-1 ]
XP_006534719.1. XM_006534656.1. [Q9QYG0-2 ]
UniGenei Mm.26722.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2QMQ X-ray 1.70 A 40-313 [» ]
ProteinModelPortali Q9QYG0.
SMRi Q9QYG0. Positions 39-313.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9QYG0. 3 interactions.
MINTi MINT-1854707.

PTM databases

PhosphoSitei Q9QYG0.

Proteomic databases

MaxQBi Q9QYG0.
PaxDbi Q9QYG0.
PRIDEi Q9QYG0.

Protocols and materials databases

DNASUi 29811.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000004673 ; ENSMUSP00000004673 ; ENSMUSG00000004558 . [Q9QYG0-1 ]
ENSMUST00000111632 ; ENSMUSP00000107259 ; ENSMUSG00000004558 . [Q9QYG0-2 ]
GeneIDi 29811.
KEGGi mmu:29811.
UCSCi uc007tnk.2. mouse. [Q9QYG0-1 ]
uc007tnl.2. mouse. [Q9QYG0-2 ]

Organism-specific databases

CTDi 57447.
MGIi MGI:1352498. Ndrg2.
Rougei Search...

Phylogenomic databases

eggNOGi NOG310435.
GeneTreei ENSGT00390000001874.
HOGENOMi HOG000230891.
HOVERGENi HBG052591.
InParanoidi Q9QYG0.
OMAi FQFGDMQ.
OrthoDBi EOG7KH9JS.
PhylomeDBi Q9QYG0.
TreeFami TF313168.

Miscellaneous databases

ChiTaRSi NDRG2. mouse.
EvolutionaryTracei Q9QYG0.
NextBioi 306962.
PROi Q9QYG0.
SOURCEi Search...

Gene expression databases

Bgeei Q9QYG0.
CleanExi MM_NDRG2.
ExpressionAtlasi Q9QYG0. baseline and differential.
Genevestigatori Q9QYG0.

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. "Identification of new genes ndr2 and ndr3 which are related to Ndr1/RTP/Drg1 but show distinct tissue specificity and response to N-myc."
    Okuda T., Kondoh H.
    Biochem. Biophys. Res. Commun. 266:208-215(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Embryo.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J, DBA/2 and NOD.
    Tissue: Head and Visual cortex.
  3. "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).
    Strain: FVB/N.
    Tissue: Liver.
  4. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 62-84; 155-176 AND 278-287, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  5. "Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
    DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 64-371.
    Tissue: Thymus.
  6. "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-330; SER-332; THR-348 AND SER-350, TISSUE SPECIFICITY.
  7. "Akt mediates insulin-stimulated phosphorylation of Ndrg2: evidence for cross-talk with protein kinase C theta."
    Burchfield J.G., Lennard A.J., Narasimhan S., Hughes W.E., Wasinger V.C., Corthals G.L., Okuda T., Kondoh H., Biden T.J., Schmitz-Peiffer C.
    J. Biol. Chem. 279:18623-18632(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-332 AND THR-348, SUBCELLULAR LOCATION.
  8. Cited for: DEVELOPMENTAL STAGE.
  9. "Expression analysis of the NDRG2 gene in mouse embryonic and adult tissues."
    Hu X.-L., Liu X.-P., Deng Y.-C., Lin S.-X., Wu L., Zhang J., Wang L.-F., Wang X.-B., Li X., Shen L., Zhang Y.-Q., Yao L.-B.
    Cell Tissue Res. 325:67-76(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328; THR-330; SER-332; THR-334; SER-335; SER-338 AND THR-357, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326; SER-328; THR-330 AND SER-332, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "NDRG4 protein-deficient mice exhibit spatial learning deficits and vulnerabilities to cerebral ischemia."
    Yamamoto H., Kokame K., Okuda T., Nakajo Y., Yanamoto H., Miyata T.
    J. Biol. Chem. 286:26158-26165(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  13. "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 (1.7 ANGSTROMS) OF 40-313.

Entry informationi

Entry nameiNDRG2_MOUSE
AccessioniPrimary (citable) accession number: Q9QYG0
Secondary accession number(s): Q3TI48
, Q3TY42, Q3U3T5, Q69ZN2, Q8C661
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3