P50583 (AP4A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	NUDT2
Synonyms:	APAH1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	147 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Asymmetrically hydrolyzes Ap4A to yield AMP and ATP. Plays a major role in maintaining homeostasis.
Catalytic activity	P1,P(4)-bis(5'-guanosyl) tetraphosphate + H2O = GTP + GMP.
Cofactor	Divalent ions By similarity.
Sequence similarities	Belongs to the Nudix hydrolase family. Contains 1 nudix hydrolase domain.

Ontologies

Keywords
Ligand	GTP-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	induction of apoptosis Inferred from sequence or structural similarity. Source: UniProtKB nucleobase-containing compound metabolic process Traceable author statement. Source: ProtInc
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity Inferred from sequence or structural similarity. Source: UniProtKB bis(5'-nucleosyl)-tetraphosphatase (symmetrical) activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 147

146

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

PRO_0000057102

Regions

Domain

1 – 139

139

Nudix hydrolase

Motif

43 – 64

22

Nudix box

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.5

Secondary structure

1

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147

Helix Strand Turn

Details...

Beta strand

4 – 13

10

Beta strand

19 – 21

3

Beta strand

23 – 31

9

Turn

32 – 35

4

Beta strand

41 – 44

4

Beta strand

47 – 49

3

Helix

51 – 62

12

Helix

67 – 69

3

Beta strand

70 – 72

3

Beta strand

79 – 81

3

Turn

84 – 86

3

Beta strand

90 – 99

10

Beta strand

111 – 117

7

Helix

119 – 126

8

Helix

129 – 143

15

Sequences

	Sequence		Length	Mass (Da)
	P50583 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 3599B12719F94AB8	FASTA	147	16,829
	10 20 30 40 50 60 MALRACGLII FRRCLIPKVD NNAIEFLLLQ ASDGIHHWTP PKGHVEPGED DLETALRETQ 70 80 90 100 110 120 EEAGIEAGQL TIIEGFKREL NYVARNKPKT VIYWLAEVKD YDVEIRLSHE HQAYRWLGLE 130 140 EACQLAQFKE MKAALQEGHQ FLCSIEA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human diadenosine 5',5''-P1,P4-tetraphosphate pyrophosphohydrolase is a member of the MutT family of nucleotide pyrophosphatases." Thorne N.M.H., Hankin S., Wilkinson M.C., Nunez C., Barraclough R., McLennan A.G. Biochem. J. 311:717-721(1995) [PubMed: 7487923] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver and Spleen.
[2]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed: 15164053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	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. , 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pancreas.
[5]	McLennan A.G. Submitted (JAN-1997) to UniProtKB Cited for: ACETYLATION AT ALA-2.
[6]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]	"Structure and substrate-binding mechanism of human Ap4A hydrolase." Swarbrick J.D., Buyya S., Gunawardana D., Gayler K.R., McLennan A.G., Gooley P.R. J. Biol. Chem. 280:8471-8481(2005) [PubMed: 15596429] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U30313 mRNA. Translation: AAC50277.1.
AL356494 Genomic DNA. Translation: CAI15964.1.
CH471071 Genomic DNA. Translation: EAW58461.1.
CH471071 Genomic DNA. Translation: EAW58462.1.
CH471071 Genomic DNA. Translation: EAW58463.1.
BC004926 mRNA. Translation: AAH04926.1.

IPI

IPI00221231.

PIR

S60111.

RefSeq

NP_001152.1. NM_001161.4.
NP_001231319.1. NM_001244390.1.
NP_671701.1. NM_147172.2.
NP_671702.1. NM_147173.2.

UniGene

Hs.493767.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1XSA	NMR	-	A	1-147	[»]
1XSB	NMR	-	A	1-147	[»]
1XSC	NMR	-	A	1-147	[»]

ProteinModelPortal

P50583.

SMR

P50583. Positions 1-147.

ModBase

Search...

Protein-protein interaction databases

STRING

P50583.

Polymorphism databases

DMDM

1703326.

Proteomic databases

PeptideAtlas

P50583.

PRIDE

P50583.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000337747; ENSP00000338397; ENSG00000164978.
ENST00000346365; ENSP00000344187; ENSG00000164978.
ENST00000379154; ENSP00000368451; ENSG00000164978.
ENST00000379155; ENSP00000368452; ENSG00000164978.
ENST00000379158; ENSP00000368455; ENSG00000164978.
ENST00000407581; ENSP00000384512; ENSG00000164978.

GeneID

318.

KEGG

hsa:318.

UCSC

uc003zub.1. human.

Organism-specific databases

CTD

318.

GeneCards

GC09P034329.

H-InvDB

HIX0007990.

HGNC

HGNC:8049. NUDT2.

HPA

CAB004684.

MIM

602852. gene.

neXtProt

NX_P50583.

PharmGKB

PA31833.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG17445.

GeneTree

ENSGT00390000002416.

HOGENOM

HBG741910.

HOVERGEN

HBG002853.

InParanoid

P50583.

OMA

RRRLIPK.

OrthoDB

EOG4FTW20.

PhylomeDB

P50583.

Gene expression databases

ArrayExpress

P50583.

Bgee

P50583.

CleanEx

HS_NUDT2.

Genevestigator

P50583.

GermOnline

ENSG00000164978. Homo sapiens.

Family and domain databases

InterPro

IPR020084. NUDIX_hydrolase_CS.
IPR000086. NUDIX_hydrolase_dom.
IPR015797. NUDIX_hydrolase_dom-like.
IPR003565. Tetra_PHTase.
[Graphical view]

Gene3D

G3DSA:3.90.79.10. NUDIX_hydrolase. 1 hit.

KO

K01518.

Pfam

PF00293. NUDIX. 1 hit.
[Graphical view]

PRINTS

PR01405. TETRPHPHTASE.

SUPFAM

SSF55811. NUDIX_hydrolase. 1 hit.

PROSITE

PS51462. NUDIX. 1 hit.
PS00893. NUDIX_BOX. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

1299.

SOURCE

Search...

Entry information

Entry name

AP4A_HUMAN

Accession

Primary (citable) accession number: P50583
Secondary accession number(s): D3DRM0, Q5T589

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 105 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.