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Protein

5'(3')-deoxyribonucleotidase, cytosolic type

Gene

Nt5c

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

Functioni

Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides, with a preference for dUMP and dTMP, intermediate activity towards dGMP, and low activity towards dCMP and dAMP.1 Publication

Catalytic activityi

A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.

Cofactori

Mg2+1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei12 – 121NucleophileCurated
Metal bindingi12 – 121Magnesium
Active sitei14 – 141Proton donorCurated
Metal bindingi14 – 141Magnesium; via carbonyl oxygen
Binding sitei20 – 201Substrate
Binding sitei46 – 461Substrate
Binding sitei67 – 671Substrate
Binding sitei101 – 1011Substrate
Binding sitei136 – 1361Substrate
Metal bindingi147 – 1471Magnesium

GO - Molecular functioni

  • 5'-nucleotidase activity Source: MGI
  • metal ion binding Source: UniProtKB-KW
  • nucleotidase activity Source: MGI
  • phosphatase activity Source: MGI
  • pyrimidine nucleotide binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.1.3.34. 3474.
ReactomeiR-MMU-73621. Pyrimidine catabolism.
R-MMU-74259. Purine catabolism.
SABIO-RKQ9JM14.

Names & Taxonomyi

Protein namesi
Recommended name:
5'(3')-deoxyribonucleotidase, cytosolic type (EC:3.1.3.-)
Alternative name(s):
Cytosolic 5',3'-pyrimidine nucleotidase
Deoxy-5'-nucleotidase 1
Short name:
dNT-1
Gene namesi
Name:Nt5c
Synonyms:Dnt1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1354954. Nt5c.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • mitochondrion Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2002005'(3')-deoxyribonucleotidase, cytosolic typePRO_0000164372Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei102 – 1021PhosphothreonineCombined sources
Modified residuei184 – 1841PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9JM14.
MaxQBiQ9JM14.
PaxDbiQ9JM14.
PRIDEiQ9JM14.

2D gel databases

REPRODUCTION-2DPAGEIPI00124639.

PTM databases

iPTMnetiQ9JM14.
PhosphoSiteiQ9JM14.

Expressioni

Gene expression databases

BgeeiQ9JM14.
CleanExiMM_NT5C.
ExpressionAtlasiQ9JM14. baseline and differential.
GenevisibleiQ9JM14. MM.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

IntActiQ9JM14. 2 interactions.
MINTiMINT-1845792.
STRINGi10090.ENSMUSP00000021082.

Structurei

Secondary structure

1
200
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 148Combined sources
Turni15 – 173Combined sources
Helixi20 – 3112Combined sources
Helixi40 – 423Combined sources
Helixi48 – 558Combined sources
Helixi59 – 679Combined sources
Turni70 – 756Combined sources
Helixi82 – 909Combined sources
Beta strandi95 – 1017Combined sources
Turni108 – 1103Combined sources
Helixi111 – 12111Combined sources
Helixi124 – 1274Combined sources
Beta strandi130 – 1323Combined sources
Helixi136 – 1383Combined sources
Beta strandi142 – 1476Combined sources
Beta strandi159 – 1657Combined sources
Helixi168 – 1703Combined sources
Beta strandi179 – 1824Combined sources
Helixi189 – 1979Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JAOX-ray2.00A1-200[»]
2JARX-ray1.94A1-200[»]
ProteinModelPortaliQ9JM14.
SMRiQ9JM14. Positions 4-199.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JM14.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IHG0. Eukaryota.
ENOG410XQYS. LUCA.
GeneTreeiENSGT00390000011596.
HOGENOMiHOG000236944.
HOVERGENiHBG045599.
InParanoidiQ9JM14.
KOiK01081.
OMAiFTCCHNR.
OrthoDBiEOG7CRTQX.
PhylomeDBiQ9JM14.
TreeFamiTF331117.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
InterProiIPR010708. 5'(3')-deoxyribonucleotidase.
IPR023214. HAD-like_dom.
[Graphical view]
PfamiPF06941. NT5C. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9JM14-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVKRPVRVL VDMDGVLADF ESGLLQGFRR RFPEEPHVPL EQRRGFLANE
60 70 80 90 100
QYGALRPDLA EKVASVYESP GFFLNLEPIP GALDALREMN DMKDTEVFIC
110 120 130 140 150
TTPLLKYDHC VGEKYRWVEQ NLGPEFVERI ILTRDKTVVM GDLLIDDKDN
160 170 180 190 200
IQGLEETPSW EHILFTCCHN QHLALPPTRR RLLSWSDNWR GIIESKRASL
Length:200
Mass (Da):23,076
Last modified:October 1, 2000 - v1
Checksum:i5E5A3AFB0A214082
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF078840 mRNA. Translation: AAF36421.1.
AK007418 mRNA. Translation: BAB25027.1.
BC024368 mRNA. Translation: AAH24368.1.
BK000208 Genomic DNA. Translation: DAA00069.1.
CCDSiCCDS25637.1.
RefSeqiNP_056622.1. NM_015807.1.
UniGeneiMm.390379.

Genome annotation databases

EnsembliENSMUST00000021082; ENSMUSP00000021082; ENSMUSG00000020736.
GeneIDi50773.
KEGGimmu:50773.
UCSCiuc007mhu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF078840 mRNA. Translation: AAF36421.1.
AK007418 mRNA. Translation: BAB25027.1.
BC024368 mRNA. Translation: AAH24368.1.
BK000208 Genomic DNA. Translation: DAA00069.1.
CCDSiCCDS25637.1.
RefSeqiNP_056622.1. NM_015807.1.
UniGeneiMm.390379.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JAOX-ray2.00A1-200[»]
2JARX-ray1.94A1-200[»]
ProteinModelPortaliQ9JM14.
SMRiQ9JM14. Positions 4-199.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9JM14. 2 interactions.
MINTiMINT-1845792.
STRINGi10090.ENSMUSP00000021082.

PTM databases

iPTMnetiQ9JM14.
PhosphoSiteiQ9JM14.

2D gel databases

REPRODUCTION-2DPAGEIPI00124639.

Proteomic databases

EPDiQ9JM14.
MaxQBiQ9JM14.
PaxDbiQ9JM14.
PRIDEiQ9JM14.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021082; ENSMUSP00000021082; ENSMUSG00000020736.
GeneIDi50773.
KEGGimmu:50773.
UCSCiuc007mhu.1. mouse.

Organism-specific databases

CTDi30833.
MGIiMGI:1354954. Nt5c.

Phylogenomic databases

eggNOGiENOG410IHG0. Eukaryota.
ENOG410XQYS. LUCA.
GeneTreeiENSGT00390000011596.
HOGENOMiHOG000236944.
HOVERGENiHBG045599.
InParanoidiQ9JM14.
KOiK01081.
OMAiFTCCHNR.
OrthoDBiEOG7CRTQX.
PhylomeDBiQ9JM14.
TreeFamiTF331117.

Enzyme and pathway databases

BRENDAi3.1.3.34. 3474.
ReactomeiR-MMU-73621. Pyrimidine catabolism.
R-MMU-74259. Purine catabolism.
SABIO-RKQ9JM14.

Miscellaneous databases

EvolutionaryTraceiQ9JM14.
PROiQ9JM14.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JM14.
CleanExiMM_NT5C.
ExpressionAtlasiQ9JM14. baseline and differential.
GenevisibleiQ9JM14. MM.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
InterProiIPR010708. 5'(3')-deoxyribonucleotidase.
IPR023214. HAD-like_dom.
[Graphical view]
PfamiPF06941. NT5C. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mammalian 5'(3')-deoxyribonucleotidase, cDNA cloning, and overexpression of the enzyme in Escherichia coli and mammalian cells."
    Rampazzo C., Johansson M., Gallinaro L., Ferraro P., Hellman U., Karlsson A., Reichard P., Bianchi V.
    J. Biol. Chem. 275:5409-5415(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Strain: C57BL/6J.
  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].
    Strain: C57BL/6J.
    Tissue: Pancreas.
  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].
    Tissue: Mammary tumor.
  4. "Mouse cytosolic and mitochondrial deoxyribonucleotidases: cDNA cloning of the mitochondrial enzyme, gene structures, chromosomal mapping and comparison with the human orthologs."
    Rampazzo C., Kost-Alimova M., Ruzzenente B., Dumanski J.P., Bianchi V.
    Gene 294:109-117(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE STRUCTURE.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-102 AND SER-184, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  6. "Crystal structures of human and murine deoxyribonucleotidases: insights into recognition of substrates and nucleotide analogues."
    Wallden K., Rinaldo-Matthis A., Ruzzenente B., Rampazzo C., Bianchi V., Nordlund P.
    Biochemistry 46:13809-13818(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEXES WITH MAGNESIUM IONS; 2'-DEOXYURIDINE 5'-MONOPHOSPHATE AND 2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiNT5C_MOUSE
AccessioniPrimary (citable) accession number: Q9JM14
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 119 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, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.