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Protein

Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]

Gene

Nudt2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Asymmetrically hydrolyzes Ap4A to yield AMP and ATP. Plays a major role in maintaining homeostasis (By similarity).By similarity

Catalytic activityi

P1,P(4)-bis(5'-guanosyl) tetraphosphate + H2O = GTP + GMP.

Cofactori

a divalent metal cationBy similarityNote: Divalent metal ions.By similarity

GO - Molecular functioni

  • bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity Source: UniProtKB
  • GTP binding Source: UniProtKB-KW

GO - Biological processi

  • apoptotic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-3299685. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical] (EC:3.6.1.17)
Alternative name(s):
Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase
Short name:
Ap4A hydrolase
Short name:
Ap4Aase
Short name:
Diadenosine tetraphosphatase
Nucleoside diphosphate-linked moiety X motif 2
Short name:
Nudix motif 2
Gene namesi
Name:Nudt2
Synonyms:Apah1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1913651. Nudt2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 147146Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]PRO_0000057103Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP56380.
MaxQBiP56380.
PaxDbiP56380.
PeptideAtlasiP56380.
PRIDEiP56380.

PTM databases

iPTMnetiP56380.
PhosphoSiteiP56380.

Expressioni

Gene expression databases

BgeeiP56380.
GenevisibleiP56380. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000030154.

Structurei

3D structure databases

ProteinModelPortaliP56380.
SMRiP56380. Positions 4-147.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 139138Nudix hydrolasePROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi43 – 6422Nudix boxAdd
BLAST

Sequence similaritiesi

Belongs to the Nudix hydrolase family.Curated
Contains 1 nudix hydrolase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2839. Eukaryota.
COG0494. LUCA.
GeneTreeiENSGT00390000002416.
HOGENOMiHOG000261976.
HOVERGENiHBG002853.
InParanoidiP56380.
KOiK01518.
OMAiGKTIHKT.
OrthoDBiEOG7GBFZN.
PhylomeDBiP56380.
TreeFamiTF105958.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
IPR003565. Tetra_PHTase.
[Graphical view]
PfamiPF00293. NUDIX. 1 hit.
[Graphical view]
PRINTSiPR01405. TETRPHPHTASE.
SUPFAMiSSF55811. SSF55811. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P56380-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALRACGLII FRRHLIPKMD NSTIEFLLLQ ASDGIHHWTP PKGHVDPGEN
60 70 80 90 100
DLETALRETR EETGIEASQL TIIEGFRREL NYVARQKPKT VIYWLAEVKD
110 120 130 140
YNVEIRLSQE HQAYRWLGLE EACQLAQFKE MKATLQEGHQ FLCSTPA
Length:147
Mass (Da):16,989
Last modified:January 23, 2007 - v3
Checksum:iA634D19F1E8CCE34
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191M → V in BAB31399 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009933 mRNA. Translation: BAB26592.1.
AK018771 mRNA. Translation: BAB31399.1.
BC025153 mRNA. Translation: AAH25153.1.
CCDSiCCDS18061.1.
RefSeqiNP_079815.2. NM_025539.2.
XP_006538228.1. XM_006538165.2.
XP_011248384.1. XM_011250082.1.
XP_011248385.1. XM_011250083.1.
UniGeneiMm.28574.

Genome annotation databases

EnsembliENSMUST00000030154; ENSMUSP00000030154; ENSMUSG00000028443.
GeneIDi66401.
KEGGimmu:66401.
UCSCiuc008sis.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009933 mRNA. Translation: BAB26592.1.
AK018771 mRNA. Translation: BAB31399.1.
BC025153 mRNA. Translation: AAH25153.1.
CCDSiCCDS18061.1.
RefSeqiNP_079815.2. NM_025539.2.
XP_006538228.1. XM_006538165.2.
XP_011248384.1. XM_011250082.1.
XP_011248385.1. XM_011250083.1.
UniGeneiMm.28574.

3D structure databases

ProteinModelPortaliP56380.
SMRiP56380. Positions 4-147.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000030154.

PTM databases

iPTMnetiP56380.
PhosphoSiteiP56380.

Proteomic databases

EPDiP56380.
MaxQBiP56380.
PaxDbiP56380.
PeptideAtlasiP56380.
PRIDEiP56380.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030154; ENSMUSP00000030154; ENSMUSG00000028443.
GeneIDi66401.
KEGGimmu:66401.
UCSCiuc008sis.1. mouse.

Organism-specific databases

CTDi318.
MGIiMGI:1913651. Nudt2.

Phylogenomic databases

eggNOGiKOG2839. Eukaryota.
COG0494. LUCA.
GeneTreeiENSGT00390000002416.
HOGENOMiHOG000261976.
HOVERGENiHBG002853.
InParanoidiP56380.
KOiK01518.
OMAiGKTIHKT.
OrthoDBiEOG7GBFZN.
PhylomeDBiP56380.
TreeFamiTF105958.

Enzyme and pathway databases

ReactomeiR-MMU-3299685. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

PROiP56380.
SOURCEiSearch...

Gene expression databases

BgeeiP56380.
GenevisibleiP56380. MM.

Family and domain databases

Gene3Di3.90.79.10. 1 hit.
InterProiIPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
IPR003565. Tetra_PHTase.
[Graphical view]
PfamiPF00293. NUDIX. 1 hit.
[Graphical view]
PRINTSiPR01405. TETRPHPHTASE.
SUPFAMiSSF55811. SSF55811. 1 hit.
PROSITEiPS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: Cerebellum and Tongue.
  2. "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].
    Strain: FVB/N.
    Tissue: Kidney.
  3. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 5-12; 43-57; 61-77; 90-99 AND 116-129, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiAP4A_MOUSE
AccessioniPrimary (citable) accession number: P56380
Secondary accession number(s): Q9D2U6, Q9D6V2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.