Reviewed, UniProtKB/Swiss-Prot O95861 (BPNT1_HUMAN)

Names and origin

Protein names

Recommended name:
    3'(2'),5'-bisphosphate nucleotidase 1
    EC=3.1.3.7
Alternative name(s):
    Bisphosphate 3'-nucleotidase 1
    PAP-inositol-1,4-phosphatase
      Short name=PIP

Gene names

Name:

BPNT1

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	308 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	Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. Has 1000-fold lower activity towards inositol 1,4-bisphosphate (Ins(1,4)P2) and inositol 1,3,4-trisphosphate (Ins(1,3,4)P3), but does not hydrolyze Ins1P, Ins(3,4)P2, Ins(1,3,4,5)P4 or InsP6. Ref.1
Catalytic activity	Adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate + phosphate.
Cofactor	Magnesium.
Enzyme regulation	Uncompetitive inhibition by micromolar concentrations of lithium. Competitive inhibition by inositol 1,4-bisphosphate. Ref.1
Tissue specificity	Highly expressed in kidney, liver, pancreas and heart. Detected at lower levels in brain, placenta, lung and skeletal muscle. Ref.1
Sequence similarities	Belongs to the inositol monophosphatase family.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Ligand	Lithium Magnesium Metal-binding
Molecular function	Hydrolase
PTM	Acetylation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	nervous system development Ref.1 Traceable author statement. Source: ProtInc nucleobase, nucleoside, nucleotide and nucleic acid metabolic process Ref.1 Traceable author statement. Source: ProtInc
Cellular component	cytosol Ref.1 Inferred from Experiment. Source: Reactome
Molecular function	3'(2'),5'-bisphosphate nucleotidase activity Ref.1 Inferred from Experiment. Source: Reactome inositol or phosphatidylinositol phosphatase activity Inferred from electronic annotation. Source: InterPro lithium ion binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O95861-1)

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: O95861-2)

The sequence of this isoform differs from the canonical sequence as follows:
     277-308: KHMNSAGVLATLRNYDYYASRVPESIKNALVP → SHRTWPKPDF...VIIYAYETDL

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 308	307	3'(2'),5'-bisphosphate nucleotidase 1		PRO_0000142527
Regions
	Region	195 – 198	4	Substrate binding By similarity
Sites
	Metal binding	74	1	Magnesium 1 By similarity
	Metal binding	117	1	Magnesium 1 By similarity
	Metal binding	117	1	Magnesium 2 By similarity
	Metal binding	119	1	Magnesium 1; via carbonyl oxygen By similarity
	Metal binding	120	1	Magnesium 2 By similarity
	Metal binding	247	1	Magnesium 2 By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
Natural variations
	Alternative sequence	277 – 308	32	KHMNS…NALVP → SHRTWPKPDFFRAQFFLESH SCFSRNFKNVSTPIKNIYDV IIYAYETDL in isoform 2.		VSP_009937
Experimental info
	Sequence conflict	221	1	A → V in AAH17801. Ref.3
	Sequence conflict	260	1	G → S in CAB65115. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: A5952F5E31C8CFCB	FASTA	308	33,392
	10 20 30 40 50 60 MASSNTVLMR LVASAYSIAQ KAGMIVRRVI AEGDLGIVEK TCATDLQTKA DRLAQMSICS 70 80 90 100 110 120 SLARKFPKLT IIGEEDLPSE EVDQELIEDS QWEEILKQPC PSQYSAIKEE DLVVWVDPLD 130 140 150 160 170 180 GTKEYTEGLL DNVTVLIGIA YEGKAIAGVI NQPYYNYEAG PDAVLGRTIW GVLGLGAFGF 190 200 210 220 230 240 QLKEVPAGKH IITTTRSHSN KLVTDCVAAM NPDAVLRVGG AGNKIIQLIE GKASAYVFAS 250 260 270 280 290 300 PGCKKWDTCA PEVILHAVGG KLTDIHGNVL QYHKDVKHMN SAGVLATLRN YDYYASRVPE SIKNALVP
	Isoform 2. Checksum: 87527CD609009E68	FASTA	325	35,744
	10 20 30 40 50 60 MASSNTVLMR LVASAYSIAQ KAGMIVRRVI AEGDLGIVEK TCATDLQTKA DRLAQMSICS 70 80 90 100 110 120 SLARKFPKLT IIGEEDLPSE EVDQELIEDS QWEEILKQPC PSQYSAIKEE DLVVWVDPLD 130 140 150 160 170 180 GTKEYTEGLL DNVTVLIGIA YEGKAIAGVI NQPYYNYEAG PDAVLGRTIW GVLGLGAFGF 190 200 210 220 230 240 QLKEVPAGKH IITTTRSHSN KLVTDCVAAM NPDAVLRVGG AGNKIIQLIE GKASAYVFAS 250 260 270 280 290 300 PGCKKWDTCA PEVILHAVGG KLTDIHGNVL QYHKDVSHRT WPKPDFFRAQ FFLESHSCFS 310 320 RNFKNVSTPI KNIYDVIIYA YETDL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of a mammalian lithium-sensitive bisphosphate 3'-nucleotidase inhibited by inositol 1,4-bisphosphate." Spiegelberg B.D., Xiong J.-P., Smith J.J., Gu R.F., York J.D. J. Biol. Chem. 274:13619-13628(1999) [PubMed: 10224133] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION, TISSUE SPECIFICITY.
[2]	"Hydrolysis of inositol-1,4-bisphosphate by human and yeast lithium sensitive 3'-phosphoadenosine 5'-phosphate nucleotidases." Yenush L., Gil-Mascarell M., Serrano R., Rodriguez P.L. Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: B-cell.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Skeletal muscle.
[4]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF125042 mRNA. Translation: AAD17329.1.
AJ249339 mRNA. Translation: CAB65115.1.
BC017801 mRNA. Translation: AAH17801.1.

IPI

IPI00410214.
IPI00410215.

RefSeq

NP_006076.4.

UniGene

Hs.406134

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2WEF	X-ray	1.80	A	6-308	[»]

SMR

O95861. Positions 5-308.

ModBase

Search...

Protein-protein interaction databases

IntAct

O95861. 2 interactions.

PTM databases

PhosphoSite

O95861.

2-D gel databases

REPRODUCTION-2DPAGE

IPI00410214.

Proteomic databases

PRIDE

O95861.

Genome annotation databases

Ensembl

ENSG00000162813. Homo sapiens. [Contig view]

GeneID

10380.

KEGG

hsa:10380.

Organism-specific databases

GeneCards

GC01M218297.

H-InvDB

HIX0001601.
HIX0044973.

HGNC

HGNC:1096. BPNT1.

MIM

604053. gene.

PharmGKB

PA25407.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

O95861.

OMA

O95861. GFQLKEA.

Enzyme and pathway databases

BRENDA

3.1.3.7. 247.

Gene expression databases

ArrayExpress

O95861.

Bgee

O95861.

CleanEx

HS_BPNT1.

GermOnline

ENSG00000162813. Homo sapiens.

Family and domain databases

InterPro

IPR000760. Inositol_P.
[Graphical view]

PANTHER

PTHR20854. Inositol_P. 1 hit.

Pfam

PF00459. Inositol_P. 1 hit.
[Graphical view]

PRINTS

PR00378. INOSPHPHTASE.

ProDom

PD023420. Inositol_P. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

39323.

SOURCE

Search...

Entry information

Entry name

BPNT1_HUMAN

Accession

Primary (citable) accession number: O95861
Secondary accession number(s): Q8WVL5, Q9UGJ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	May 1, 1999
Last modified:	June 16, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)