Q9BQG2 (NUD12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Peroxisomal NADH pyrophosphatase NUDT12
EC=3.6.1.22

Alternative name(s):
Nucleoside diphosphate-linked moiety X motif 12
Short name=Nudix motif 12

Gene names

Name:

NUDT12

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	462 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Hydrolyzes NAD(P)H to NMNH and AMP (2',5'-ADP), and diadenosine diphosphate to AMP. Has also activity towards NAD(P)+, ADP-ribose and diadenosine triphosphate. May act to regulate the concentration of peroxisomal nicotinamide nucleotide cofactors required for oxidative metabolism in this organelle. Ref.5
Catalytic activity	NAD+ + H2O = AMP + NMN. Ref.5
Cofactor	Magnesium or manganese By similarity.
Subcellular location	Peroxisome Ref.5.
Sequence similarities	Belongs to the Nudix hydrolase family. NudC subfamily. Contains 3 ANK repeats. Contains 1 nudix hydrolase domain.
Biophysicochemical properties	Kinetic parameters: KM=11 µM for NADH Ref.5 KM=16 µM for NADPH KM=190 µM for NAD pH dependence: Optimum pH is 8-9.

Ontologies

Keywords
Cellular component	Peroxisome
Coding sequence diversity	Polymorphism
Domain	ANK repeat Repeat
Ligand	Magnesium Manganese Metal-binding NAD NADP
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	NAD catabolic process Inferred from direct assay Ref.5. Source: UniProtKB NADP catabolic process Inferred from direct assay Ref.5. Source: UniProtKB
Cellular_component	nucleus Inferred from direct assay. Source: LIFEdb peroxisome Inferred from direct assay Ref.5. Source: UniProtKB
Molecular_function	NAD+ diphosphatase activity Inferred from direct assay Ref.5. Source: UniProtKB NADH pyrophosphatase activity Inferred from direct assay Ref.5. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 462	462	Peroxisomal NADH pyrophosphatase NUDT12		PRO_0000056956
Regions
	Repeat	11 – 40	30	ANK 1
	Repeat	45 – 74	30	ANK 2
	Repeat	78 – 98	21	ANK 3
	Domain	319 – 453	135	Nudix hydrolase
	Motif	355 – 376	22	Nudix box
	Motif	460 – 462	3	Microbody targeting signal Probable
Sites
	Metal binding	370	1	Magnesium or manganese By similarity
	Metal binding	374	1	Magnesium or manganese By similarity
Natural variations
	Natural variant	129	1	K → E. Corresponds to variant rs35903418 [ dbSNP | Ensembl ].		VAR_034157
	Natural variant	235	1	I → V. Corresponds to variant rs34468716 [ dbSNP | Ensembl ].		VAR_034158
Experimental info
	Mutagenesis	460 – 462	3	Missing: Abolishes localization to peroxisomes. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q9BQG2 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 1A470B93707DB1D5	FASTA	462	52,076
	10 20 30 40 50 60 MSSVKRSLKQ EIVTQFHCSA AEGDIAKLTG ILSHSPSLLN ETSENGWTAL MYAARNGHPE 70 80 90 100 110 120 IVQFLLEKGC DRSIVNKSRQ TALDIAVFWG YKHIANLLAT AKGGKKPWFL TNEVEECENY 130 140 150 160 170 180 FSKTLLDRKS EKRNNSDWLL AKESHPATVF ILFSDLNPLV TLGGNKESFQ QPEVRLCQLN 190 200 210 220 230 240 YTDIKDYLAQ PEKITLIFLG VELEIKDKLL NYAGEVPREE EDGLVAWFAL GIDPIAAEEF 250 260 270 280 290 300 KQRHENCYFL HPPMPALLQL KEKEAGVVAQ ARSVLAWHSR YKFCPTCGNA TKIEEGGYKR 310 320 330 340 350 360 LCLKEDCPSL NGVHNTSYPR VDPVVIMQVI HPDGTKCLLG RQKRFPPGMF TCLAGFIEPG 370 380 390 400 410 420 ETIEDAVRRE VEEESGVKVG HVQYVACQPW PMPSSLMIGC LALAVSTEIK VDKNEIEDAR 430 440 450 460 WFTREQVLDV LTKGKQQAFF VPPSRAIAHQ LIKHWIRINP NL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Amygdala.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Trachea.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Eye and Ovary.
[5]	"Mammalian NADH diphosphatases of the Nudix family: cloning and characterization of the human peroxisomal NUDT12 protein." Abdelraheim S.R., Spiller D.G., McLennan A.G. Biochem. J. 374:329-335(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, MUTAGENESIS OF 460-PRO--LEU-462.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL136592 mRNA. Translation: CAB66527.1. AK098066 mRNA. Translation: BAG53574.1. CH471086 Genomic DNA. Translation: EAW49073.1. BC026748 mRNA. Translation: AAH26748.1. BC041099 mRNA. Translation: AAH41099.1.
IPI	IPI00027778.
RefSeq	NP_113626.1. NM_031438.2.
UniGene	Hs.434289.
3D structure databases
ProteinModelPortal	Q9BQG2.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000230792.
PTM databases
PhosphoSite	Q9BQG2.
Polymorphism databases
DMDM	68565930.
Proteomic databases
PaxDb	Q9BQG2.
PRIDE	Q9BQG2.
Protocols and materials databases
DNASU	83594.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000230792; ENSP00000230792; ENSG00000112874.
GeneID	83594.
KEGG	hsa:83594.
UCSC	uc003koi.3. human.
Organism-specific databases
CTD	83594.
GeneCards	GC05M102912.
HGNC	HGNC:18826. NUDT12.
HPA	HPA045449.
MIM	609232. gene.
neXtProt	NX_Q9BQG2.
PharmGKB	PA38699.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG2816.
HOGENOM	HOG000247937.
HOVERGEN	HBG054394.
InParanoid	Q9BQG2.
KO	K03426.
OMA	EEGGYKR.
OrthoDB	EOG43XV3B.
PhylomeDB	Q9BQG2.
Gene expression databases
ArrayExpress	Q9BQG2.
Bgee	Q9BQG2.
CleanEx	HS_NUDT12.
Genevestigator	Q9BQG2.
GermOnline	ENSG00000112874. Homo sapiens.
Family and domain databases
Gene3D	1.25.40.20. 1 hit. 3.90.79.10. 1 hit.
InterPro	IPR002110. Ankyrin_rpt. IPR020683. Ankyrin_rpt-contain_dom. IPR015375. NADH_PPase-like_N. IPR020084. NUDIX_hydrolase_CS. IPR000086. NUDIX_hydrolase_dom. IPR015797. NUDIX_hydrolase_dom-like. IPR015376. Znr_NADH_PPase. [Graphical view]
Pfam	PF12796. Ank_2. 1 hit. PF00293. NUDIX. 1 hit. PF09296. NUDIX-like. 1 hit. PF09297. zf-NADH-PPase. 1 hit. [Graphical view]
SMART	SM00248. ANK. 3 hits. [Graphical view]
SUPFAM	SSF48403. ANK. 1 hit. SSF55811. NUDIX_hydrolase. 1 hit.
PROSITE	PS50297. ANK_REP_REGION. 1 hit. PS50088. ANK_REPEAT. 1 hit. PS51462. NUDIX. 1 hit. PS00893. NUDIX_BOX. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	83594.
NextBio	72525.
SOURCE	Search...

Entry information

Entry name

NUD12_HUMAN

Accession

Primary (citable) accession number: Q9BQG2
Secondary accession number(s): B3KUW2, Q8TAL7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 103 of the entry and version 1 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.