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Protein

7-methylguanosine phosphate-specific 5'-nucleotidase

Gene

NT5C3B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

N(7)-methyl-GMP + H2O = N(7)-methyl-guanosine + phosphate.1 Publication
CMP + H2O = cytidine + phosphate.1 Publication
A 5'-ribonucleotide + H2O = a ribonucleoside + phosphate.1 Publication

Kineticsi

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.

  1. KM=7.8 µM for m7GMP1 Publication
  2. KM=79 µM for CMP1 Publication
  3. KM=355 µM for GMP1 Publication
  4. KM=456 µM for AMP1 Publication
  5. KM=439 µM for UMP1 Publication

Vmax=0.41 µmol/min/mg enzyme with m7GMP as substrate1 Publication

Vmax=12 µmol/min/mg enzyme with CMP as substrate1 Publication

Vmax=0.13 µmol/min/mg enzyme with GMP as substrate1 Publication

Vmax=0.07 µmol/min/mg enzyme with AMP as substrate1 Publication

Vmax=10.7 µmol/min/mg enzyme with UMP as substrate1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei41 – 411NucleophileBy similarity
Metal bindingi41 – 411MagnesiumBy similarity
Active sitei43 – 431Proton donorBy similarity
Metal bindingi43 – 431Magnesium; via carbonyl oxygenBy similarity
Binding sitei205 – 2051SubstrateBy similarity
Metal bindingi230 – 2301MagnesiumBy similarity

GO - Molecular functioni

  1. 5'-nucleotidase activity Source: UniProtKB-EC
  2. magnesium ion binding Source: InterPro
  3. nucleotide binding Source: UniProtKB-KW

GO - Biological processi

  1. nucleotide metabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

SABIO-RKQ969T7.

Names & Taxonomyi

Protein namesi
Recommended name:
7-methylguanosine phosphate-specific 5'-nucleotidase (EC:3.1.3.91)
Short name:
7-methylguanosine nucleotidase
Alternative name(s):
Cytosolic 5'-nucleotidase 3B
Cytosolic 5'-nucleotidase III-like protein (EC:3.1.3.5)
Short name:
cN-III-like protein
N(7)-methylguanylate 5'-phosphatase
Gene namesi
Name:NT5C3B
Synonyms:NT5C3L
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:28300. NT5C3B.

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3003007-methylguanosine phosphate-specific 5'-nucleotidasePRO_0000328948Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei256 – 2561N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ969T7.
PaxDbiQ969T7.
PRIDEiQ969T7.

PTM databases

DEPODiQ969T7.
PhosphoSiteiQ969T7.

Expressioni

Gene expression databases

BgeeiQ969T7.
CleanExiHS_NT5C3L.
ExpressionAtlasiQ969T7. baseline and differential.
GenevestigatoriQ969T7.

Organism-specific databases

HPAiHPA030786.

Interactioni

Subunit structurei

Monomer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MLH1P406923EBI-2932564,EBI-744248

Protein-protein interaction databases

IntActiQ969T7. 1 interaction.
STRINGi9606.ENSP00000269534.

Structurei

3D structure databases

ProteinModelPortaliQ969T7.
SMRiQ969T7. Positions 18-289.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni156 – 1572Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the pyrimidine 5'-nucleotidase family.Curated

Phylogenomic databases

eggNOGiNOG266578.
GeneTreeiENSGT00390000012959.
HOVERGENiHBG059750.
KOiK01081.
OMAiNDKVEEQ.
TreeFamiTF314663.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
InterProiIPR023214. HAD-like_dom.
IPR006434. Pyrimidine_nucleotidase_eu.
[Graphical view]
PANTHERiPTHR13045. PTHR13045. 1 hit.
PfamiPF05822. UMPH-1. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01544. HAD-SF-IE. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q969T7-1) [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
MAEEVSTLMK ATVLMRQPGR VQEIVGALRK GGGDRLQVIS DFDMTLSRFA
60 70 80 90 100
YNGKRCPSSY NILDNSKIIS EECRKELTAL LHHYYPIEID PHRTVKEKLP
110 120 130 140 150
HMVEWWTKAH NLLCQQKIQK FQIAQVVRES NAMLREGYKT FFNTLYHNNI
160 170 180 190 200
PLFIFSAGIG DILEEIIRQM KVFHPNIHIV SNYMDFNEDG FLQGFKGQLI
210 220 230 240 250
HTYNKNSSAC ENSGYFQQLE GKTNVILLGD SIGDLTMADG VPGVQNILKI
260 270 280 290 300
GFLNDKVEER RERYMDSYDI VLEKDETLDV VNGLLQHILC QGVQLEMQGP
Length:300
Mass (Da):34,389
Last modified:April 3, 2013 - v4
Checksum:i3E221583153381F8
GO
Isoform 2 (identifier: Q969T7-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:292
Mass (Da):33,528
Checksum:i8ACC59D5F25E629A
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti209 – 2091A → V.2 Publications
Corresponds to variant rs1046403 [ dbSNP | Ensembl ].
VAR_042582
Natural varianti213 – 2131S → C.2 Publications
Corresponds to variant rs1046404 [ dbSNP | Ensembl ].
VAR_042583

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 88Missing in isoform 2. 1 PublicationVSP_046297

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11410.2. [Q969T7-1]
RefSeqiNP_443167.4. NM_052935.4. [Q969T7-1]
UniGeneiHs.237536.

Genome annotation databases

EnsembliENST00000435506; ENSP00000389948; ENSG00000141698. [Q969T7-1]
GeneIDi115024.
KEGGihsa:115024.
UCSCiuc002hxy.4. human. [Q969T7-1]

Polymorphism databases

DMDMi476007845.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11410.2. [Q969T7-1]
RefSeqiNP_443167.4. NM_052935.4. [Q969T7-1]
UniGeneiHs.237536.

3D structure databases

ProteinModelPortaliQ969T7.
SMRiQ969T7. Positions 18-289.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ969T7. 1 interaction.
STRINGi9606.ENSP00000269534.

PTM databases

DEPODiQ969T7.
PhosphoSiteiQ969T7.

Polymorphism databases

DMDMi476007845.

Proteomic databases

MaxQBiQ969T7.
PaxDbiQ969T7.
PRIDEiQ969T7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000435506; ENSP00000389948; ENSG00000141698. [Q969T7-1]
GeneIDi115024.
KEGGihsa:115024.
UCSCiuc002hxy.4. human. [Q969T7-1]

Organism-specific databases

CTDi115024.
GeneCardsiGC17M039982.
HGNCiHGNC:28300. NT5C3B.
HPAiHPA030786.
neXtProtiNX_Q969T7.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG266578.
GeneTreeiENSGT00390000012959.
HOVERGENiHBG059750.
KOiK01081.
OMAiNDKVEEQ.
TreeFamiTF314663.

Enzyme and pathway databases

SABIO-RKQ969T7.

Miscellaneous databases

GenomeRNAii115024.
NextBioi13644547.
PROiQ969T7.

Gene expression databases

BgeeiQ969T7.
CleanExiHS_NT5C3L.
ExpressionAtlasiQ969T7. baseline and differential.
GenevestigatoriQ969T7.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
InterProiIPR023214. HAD-like_dom.
IPR006434. Pyrimidine_nucleotidase_eu.
[Graphical view]
PANTHERiPTHR13045. PTHR13045. 1 hit.
PfamiPF05822. UMPH-1. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01544. HAD-SF-IE. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry namei5NT3B_HUMAN
AccessioniPrimary (citable) accession number: Q969T7
Secondary accession number(s): A8MWB9, C9JKC4, Q7L3B7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: April 3, 2013
Last modified: January 7, 2015
This is version 110 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.