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Q969T7 (5NT3B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
7-methylguanosine phosphate-specific 5'-nucleotidase

Short name=7-methylguanosine nucleotidase
EC=3.1.3.91
Alternative name(s):
Cytosolic 5'-nucleotidase 3B
Cytosolic 5'-nucleotidase III-like protein
Short name=cN-III-like protein
EC=3.1.3.5
N(7)-methylguanylate 5'-phosphatase
Gene names
Name:NT5C3B
Synonyms:NT5C3L
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length300 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Specifically hydrolyzes 7-methylguanosine monophosphate (m7GMP) to 7-methylguanosine and inorganic phosphate. The specific activity for m7GMP may protect cells against undesired salvage of m7GMP and its incorporation into nucleic acids. Also has weak activity for CMP. UMP and purine nucleotides are poor substrates. Ref.6

Catalytic activity

N(7)-methyl-GMP + H2O = N(7)-methyl-guanosine + phosphate. Ref.6

CMP + H2O = cytidine + phosphate. Ref.6

A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate. Ref.6

Subunit structure

Monomer. Ref.6

Subcellular location

Cytoplasm Potential.

Sequence similarities

Belongs to the pyrimidine 5'-nucleotidase family.

Biophysicochemical properties

Kinetic parameters:

kcat is 0.24 sec(-1) with m7GMP. kcat is 7 sec(-1) with CMP. kcat is 0.07 sec(-1) with GMP. kcat is 0.04 sec(-1) with AMP. kcat is 6.2 sec(-1) with UMP.

KM=7.8 µM for m7GMP Ref.6

KM=79 µM for CMP

KM=355 µM for GMP

KM=456 µM for AMP

KM=439 µM for UMP

Vmax=0.41 µmol/min/mg enzyme with m7GMP as substrate

Vmax=12 µmol/min/mg enzyme with CMP as substrate

Vmax=0.13 µmol/min/mg enzyme with GMP as substrate

Vmax=0.07 µmol/min/mg enzyme with AMP as substrate

Vmax=10.7 µmol/min/mg enzyme with UMP as substrate

Ontologies

Keywords
   Biological processNucleotide metabolism
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandMagnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnucleotide metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function5'-nucleotidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

nucleotide binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 20706999. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MLH1P406923EBI-2932564,EBI-744248

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q969T7-1)

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: Q969T7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3003007-methylguanosine phosphate-specific 5'-nucleotidase
PRO_0000328948

Regions

Region156 – 1572Substrate binding By similarity

Sites

Active site411Nucleophile By similarity
Active site431Proton donor By similarity
Metal binding411Magnesium By similarity
Metal binding431Magnesium; via carbonyl oxygen By similarity
Metal binding2301Magnesium By similarity
Binding site2051Substrate By similarity

Amino acid modifications

Modified residue2561N6-acetyllysine Ref.4

Natural variations

Alternative sequence1 – 88Missing in isoform 2.
VSP_046297
Natural variant2091A → V. Ref.2 Ref.3
Corresponds to variant rs1046403 [ dbSNP | Ensembl ].
VAR_042582
Natural variant2131S → C. Ref.2 Ref.3
Corresponds to variant rs1046404 [ dbSNP | Ensembl ].
VAR_042583

Sequences

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

Last modified April 3, 2013. Version 4.
Checksum: 3E221583153381F8

FASTA30034,389
        10         20         30         40         50         60 
MAEEVSTLMK ATVLMRQPGR VQEIVGALRK GGGDRLQVIS DFDMTLSRFA YNGKRCPSSY 

        70         80         90        100        110        120 
NILDNSKIIS EECRKELTAL LHHYYPIEID PHRTVKEKLP HMVEWWTKAH NLLCQQKIQK 

       130        140        150        160        170        180 
FQIAQVVRES NAMLREGYKT FFNTLYHNNI PLFIFSAGIG DILEEIIRQM KVFHPNIHIV 

       190        200        210        220        230        240 
SNYMDFNEDG FLQGFKGQLI HTYNKNSSAC ENSGYFQQLE GKTNVILLGD SIGDLTMADG 

       250        260        270        280        290        300 
VPGVQNILKI GFLNDKVEER RERYMDSYDI VLEKDETLDV VNGLLQHILC QGVQLEMQGP 

« Hide

Isoform 2 [UniParc].

Checksum: 8ACC59D5F25E629A
Show »

FASTA29233,528

References

« Hide 'large scale' references
[1]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS VAL-209 AND CYS-213.
[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 2), VARIANTS VAL-209 AND CYS-213.
Tissue: Liver, Lung and Testis.
[4]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-256, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[5]"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].
[6]"Identification of Drosophila and Human 7-Methyl GMP-specific Nucleotidases."
Buschmann J., Moritz B., Jeske M., Lilie H., Schierhorn A., Wahle E.
J. Biol. Chem. 288:2441-2451(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC091172 Genomic DNA. No translation available.
CH471152 Genomic DNA. Translation: EAW60771.1.
BC013742 mRNA. Translation: AAH13742.2.
BC014132 mRNA. Translation: AAH14132.2.
BC016971 mRNA. Translation: AAH16971.2.
BC067788 mRNA. Translation: AAH67788.1.
CCDSCCDS11410.2. [Q969T7-1]
RefSeqNP_443167.4. NM_052935.4. [Q969T7-1]
UniGeneHs.237536.

3D structure databases

ProteinModelPortalQ969T7.
SMRQ969T7. Positions 18-289.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ969T7. 1 interaction.
STRING9606.ENSP00000269534.

PTM databases

PhosphoSiteQ969T7.

Polymorphism databases

DMDM476007845.

Proteomic databases

MaxQBQ969T7.
PaxDbQ969T7.
PRIDEQ969T7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000269534; ENSP00000269534; ENSG00000141698. [Q969T7-2]
ENST00000435506; ENSP00000389948; ENSG00000141698. [Q969T7-1]
ENST00000569139; ENSP00000454620; ENSG00000260753. [Q969T7-1]
GeneID115024.
KEGGhsa:115024.
UCSCuc002hxy.4. human. [Q969T7-1]

Organism-specific databases

CTD115024.
GeneCardsGC17M039982.
HGNCHGNC:28300. NT5C3B.
HPAHPA030786.
neXtProtNX_Q969T7.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG266578.
HOVERGENHBG059750.
InParanoidQ969T7.
KOK01081.
OMANDKVEEQ.
TreeFamTF314663.

Enzyme and pathway databases

SABIO-RKQ969T7.

Gene expression databases

ArrayExpressQ969T7.
BgeeQ969T7.
CleanExHS_NT5C3L.
GenevestigatorQ969T7.

Family and domain databases

Gene3D3.40.50.1000. 2 hits.
InterProIPR023214. HAD-like_dom.
IPR006434. Pyrimidine_nucleotidase_eu.
[Graphical view]
PANTHERPTHR13045. PTHR13045. 1 hit.
PfamPF05822. UMPH-1. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 1 hit.
TIGRFAMsTIGR01544. HAD-SF-IE. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi115024.
NextBio13644547.
PROQ969T7.

Entry information

Entry name5NT3B_HUMAN
AccessionPrimary (citable) accession number: Q969T7
Secondary accession number(s): A8MWB9, C9JKC4, Q7L3B7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: April 3, 2013
Last modified: July 9, 2014
This is version 107 of the entry and version 4 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

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 17

Human chromosome 17: entries, gene names and cross-references to MIM