O95861 (BPNT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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) [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	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 Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	3'-phosphoadenosine 5'-phosphosulfate metabolic process Traceable author statement. Source: Reactome nervous system development Traceable author statement Ref.1. Source: ProtInc phosphatidylinositol phosphorylation Inferred from electronic annotation. Source: InterPro xenobiotic metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	3'(2'),5'-bisphosphate nucleotidase activity Traceable author statement Ref.1. Source: ProtInc inositol-1,4-bisphosphate 1-phosphatase activity Inferred from electronic annotation. Source: Compara magnesium ion binding Inferred from electronic annotation. Source: Compara
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

119 – 122

4

Substrate binding

Region

195 – 198

4

Substrate binding

Sites

Metal binding

74

1

Magnesium 1

Metal binding

117

1

Magnesium 1

Metal binding

117

1

Magnesium 2

Metal binding

119

1

Magnesium 1; via carbonyl oxygen

Metal binding

120

1

Magnesium 2

Metal binding

247

1

Magnesium 2

Binding site

74

1

Substrate By similarity

Binding site

247

1

Substrate

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.5

Sequence conflict

260

1

G → S in CAB65115. Ref.2

Secondary structure

1

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308

Helix Strand Turn

Details...

Helix

7 – 32

26

Beta strand

38 – 42

5

Beta strand

45 – 47

3

Helix

49 – 65

17

Beta strand

70 – 75

6

Helix

84 – 86

3

Helix

93 – 96

4

Helix

102 – 104

3

Helix

109 – 111

3

Beta strand

112 – 120

9

Helix

122 – 126

5

Helix

130 – 132

3

Beta strand

134 – 141

8

Beta strand

144 – 152

9

Turn

153 – 158

6

Beta strand

167 – 172

6

Turn

173 – 175

3

Beta strand

176 – 180

5

Beta strand

191 – 194

4

Beta strand

196 – 198

3

Helix

201 – 208

8

Beta strand

213 – 217

5

Helix

221 – 229

9

Beta strand

234 – 238

5

Helix

245 – 257

13

Beta strand

261 – 263

3

Beta strand

284 – 289

6

Helix

291 – 295

5

Helix

300 – 305

6

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 [UniParc]. 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] [Europe PMC] [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]	"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] (ISOFORM 1).
[4]	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].
[5]	"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). Tissue: Skeletal muscle.
[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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]	"Human 3'(2'), 5'-bisphosphate nucleotidase 1 (BPNT1) in complex with AMP, PO4 and magnesium." Structural genomics consortium (SGC) Submitted (APR-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 6-308 IN COMPLEX WITH MAGNESIUM IONS AND AMP.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF125042 mRNA. Translation: AAD17329.1.
AJ249339 mRNA. Translation: CAB65115.1.
AK291943 mRNA. Translation: BAF84632.1.
CH471100 Genomic DNA. Translation: EAW93306.1.
CH471100 Genomic DNA. Translation: EAW93308.1.
BC017801 mRNA. Translation: AAH17801.1.

IPI

IPI00410214.
IPI00410215.

RefSeq

NP_006076.4. NM_006085.4.

UniGene

Hs.406134.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

O95861.

ModBase

Search...

Protein-protein interaction databases

IntAct

O95861. 1 interaction.

STRING

9606.ENSP00000318852.

PTM databases

PhosphoSite

O95861.

2D gel databases

REPRODUCTION-2DPAGE

IPI00410214.

Proteomic databases

PaxDb

O95861.

PRIDE

O95861.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000322067; ENSP00000318852; ENSG00000162813.
ENST00000469520; ENSP00000446828; ENSG00000162813.

GeneID

10380.

KEGG

hsa:10380.

UCSC

uc001hma.3. human.

Organism-specific databases

CTD

10380.

GeneCards

GC01M220230.

H-InvDB

HIX0001601.

HGNC

HGNC:1096. BPNT1.

HPA

HPA048461.

MIM

604053. gene.

neXtProt

NX_O95861.

PharmGKB

PA25407.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0483.

HOGENOM

HOG000293205.

HOVERGEN

HBG050719.

KO

K01082.

OMA

AHAYVFA.

OrthoDB

EOG4GXFND.

Enzyme and pathway databases

BRENDA

3.1.3.7. 2681.

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

O95861.

Bgee

O95861.

CleanEx

HS_BPNT1.

Genevestigator

O95861.

GermOnline

ENSG00000162813. Homo sapiens.

Family and domain databases

InterPro

IPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]

PANTHER

PTHR20854. PTHR20854. 1 hit.

Pfam

PF00459. Inositol_P. 1 hit.
[Graphical view]

PROSITE

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

ProtoNet

Search...

Other

EvolutionaryTrace

O95861.

GenomeRNAi

10380.

NextBio

39323.

SOURCE

Search...

Entry information

Entry name

BPNT1_HUMAN

Accession

Primary (citable) accession number: O95861
Secondary accession number(s): A8K7C8 , D3DTA9, Q8WVL5, Q9UGJ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 106 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.