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Protein

3'(2'),5'-bisphosphate nucleotidase 1

Gene

BPNT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 InsP6.1 Publication

Catalytic activityi

Adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate + phosphate.

Cofactori

Enzyme regulationi

Uncompetitive inhibition by micromolar concentrations of lithium. Competitive inhibition by inositol 1,4-bisphosphate.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi74 – 741Magnesium 1
Binding sitei74 – 741SubstrateBy similarity
Metal bindingi117 – 1171Magnesium 1
Metal bindingi117 – 1171Magnesium 2
Metal bindingi119 – 1191Magnesium 1; via carbonyl oxygen
Metal bindingi120 – 1201Magnesium 2
Metal bindingi247 – 2471Magnesium 2
Binding sitei247 – 2471Substrate

GO - Molecular functioni

  1. 3'(2'),5'-bisphosphate nucleotidase activity Source: ProtInc
  2. inositol-1,4-bisphosphate 1-phosphatase activity Source: Ensembl
  3. magnesium ion binding Source: Ensembl

GO - Biological processi

  1. 3'-phosphoadenosine 5'-phosphosulfate metabolic process Source: Reactome
  2. dephosphorylation Source: GOC
  3. nervous system development Source: ProtInc
  4. nucleobase-containing compound metabolic process Source: ProtInc
  5. phosphatidylinositol phosphorylation Source: InterPro
  6. small molecule metabolic process Source: Reactome
  7. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Lithium, Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.3.7. 2681.
ReactomeiREACT_6913. Cytosolic sulfonation of small molecules.

Names & Taxonomyi

Protein namesi
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 namesi
Name:BPNT1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:1096. BPNT1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25407.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 3083073'(2'),5'-bisphosphate nucleotidase 1PRO_0000142527Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei244 – 2441N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO95861.
PaxDbiO95861.
PRIDEiO95861.

2D gel databases

REPRODUCTION-2DPAGEIPI00410214.

PTM databases

DEPODiO95861.
PhosphoSiteiO95861.

Expressioni

Tissue specificityi

Highly expressed in kidney, liver, pancreas and heart. Detected at lower levels in brain, placenta, lung and skeletal muscle.1 Publication

Gene expression databases

BgeeiO95861.
CleanExiHS_BPNT1.
ExpressionAtlasiO95861. baseline and differential.
GenevestigatoriO95861.

Organism-specific databases

HPAiHPA048461.

Interactioni

Protein-protein interaction databases

BioGridi115653. 3 interactions.
IntActiO95861. 1 interaction.
MINTiMINT-5002343.
STRINGi9606.ENSP00000318852.

Structurei

Secondary structure

1
308
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 3226Combined sources
Beta strandi38 – 425Combined sources
Beta strandi45 – 473Combined sources
Helixi49 – 6517Combined sources
Beta strandi70 – 756Combined sources
Helixi84 – 863Combined sources
Helixi93 – 964Combined sources
Helixi102 – 1043Combined sources
Helixi109 – 1113Combined sources
Beta strandi112 – 1209Combined sources
Helixi122 – 1265Combined sources
Helixi130 – 1323Combined sources
Beta strandi134 – 1418Combined sources
Beta strandi144 – 1529Combined sources
Turni153 – 1586Combined sources
Beta strandi167 – 1726Combined sources
Turni173 – 1753Combined sources
Beta strandi176 – 1805Combined sources
Beta strandi191 – 1944Combined sources
Beta strandi196 – 1983Combined sources
Helixi201 – 2088Combined sources
Beta strandi213 – 2175Combined sources
Helixi221 – 2299Combined sources
Beta strandi234 – 2385Combined sources
Helixi245 – 25713Combined sources
Beta strandi261 – 2633Combined sources
Beta strandi284 – 2896Combined sources
Helixi291 – 2955Combined sources
Helixi300 – 3056Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WEFX-ray1.80A6-308[»]
ProteinModelPortaliO95861.
SMRiO95861. Positions 6-308.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO95861.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni119 – 1224Substrate binding
Regioni195 – 1984Substrate binding

Sequence similaritiesi

Belongs to the inositol monophosphatase family.Curated

Phylogenomic databases

eggNOGiCOG0483.
GeneTreeiENSGT00530000063462.
HOGENOMiHOG000293205.
HOVERGENiHBG050719.
KOiK01082.
OMAiINQPFYN.
OrthoDBiEOG7WQ7SQ.
PhylomeDBiO95861.
TreeFamiTF314300.

Family and domain databases

InterProiIPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]
PANTHERiPTHR20854. PTHR20854. 1 hit.
PfamiPF00459. Inositol_P. 1 hit.
[Graphical view]
PROSITEiPS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O95861-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MASSNTVLMR LVASAYSIAQ KAGMIVRRVI AEGDLGIVEK TCATDLQTKA
60 70 80 90 100
DRLAQMSICS SLARKFPKLT IIGEEDLPSE EVDQELIEDS QWEEILKQPC
110 120 130 140 150
PSQYSAIKEE DLVVWVDPLD GTKEYTEGLL DNVTVLIGIA YEGKAIAGVI
160 170 180 190 200
NQPYYNYEAG PDAVLGRTIW GVLGLGAFGF QLKEVPAGKH IITTTRSHSN
210 220 230 240 250
KLVTDCVAAM NPDAVLRVGG AGNKIIQLIE GKASAYVFAS PGCKKWDTCA
260 270 280 290 300
PEVILHAVGG KLTDIHGNVL QYHKDVKHMN SAGVLATLRN YDYYASRVPE

SIKNALVP
Length:308
Mass (Da):33,392
Last modified:May 1, 1999 - v1
Checksum:iA5952F5E31C8CFCB
GO
Isoform 2 (identifier: O95861-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:325
Mass (Da):35,744
Checksum:i87527CD609009E68
GO
Isoform 3 (identifier: O95861-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-55: Missing.

Show »
Length:253
Mass (Da):27,543
Checksum:i6253BEF5F96A25E1
GO
Isoform 4 (identifier: O95861-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     76-111: Missing.

Show »
Length:272
Mass (Da):29,189
Checksum:iFC6456F98BDED5AC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti221 – 2211A → V in AAH17801. (PubMed:15489334)Curated
Sequence conflicti260 – 2601G → S in CAB65115. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5555Missing in isoform 3. 1 PublicationVSP_054807Add
BLAST
Alternative sequencei76 – 11136Missing in isoform 4. 1 PublicationVSP_054808Add
BLAST
Alternative sequencei277 – 30832KHMNS…NALVP → SHRTWPKPDFFRAQFFLESH SCFSRNFKNVSTPIKNIYDV IIYAYETDL in isoform 2. 1 PublicationVSP_009937Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF125042 mRNA. Translation: AAD17329.1.
AJ249339 mRNA. Translation: CAB65115.1.
AK291943 mRNA. Translation: BAF84632.1.
AK298476 mRNA. Translation: BAG60687.1.
AK300777 mRNA. Translation: BAG62441.1.
AC103590 Genomic DNA. No translation available.
CH471100 Genomic DNA. Translation: EAW93306.1.
CH471100 Genomic DNA. Translation: EAW93308.1.
BC017801 mRNA. Translation: AAH17801.1.
CCDSiCCDS41469.1. [O95861-1]
CCDS65787.1. [O95861-3]
CCDS65788.1. [O95861-4]
RefSeqiNP_001273078.1. NM_001286149.1. [O95861-3]
NP_001273079.1. NM_001286150.1. [O95861-4]
NP_001273080.1. NM_001286151.1. [O95861-3]
NP_006076.4. NM_006085.5. [O95861-1]
XP_005273057.1. XM_005273000.2. [O95861-1]
UniGeneiHs.406134.

Genome annotation databases

EnsembliENST00000322067; ENSP00000318852; ENSG00000162813. [O95861-1]
ENST00000414869; ENSP00000410348; ENSG00000162813. [O95861-4]
ENST00000469520; ENSP00000446828; ENSG00000162813. [O95861-1]
ENST00000544404; ENSP00000444398; ENSG00000162813. [O95861-3]
GeneIDi10380.
KEGGihsa:10380.
UCSCiuc001hma.3. human. [O95861-1]
uc010puh.2. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF125042 mRNA. Translation: AAD17329.1.
AJ249339 mRNA. Translation: CAB65115.1.
AK291943 mRNA. Translation: BAF84632.1.
AK298476 mRNA. Translation: BAG60687.1.
AK300777 mRNA. Translation: BAG62441.1.
AC103590 Genomic DNA. No translation available.
CH471100 Genomic DNA. Translation: EAW93306.1.
CH471100 Genomic DNA. Translation: EAW93308.1.
BC017801 mRNA. Translation: AAH17801.1.
CCDSiCCDS41469.1. [O95861-1]
CCDS65787.1. [O95861-3]
CCDS65788.1. [O95861-4]
RefSeqiNP_001273078.1. NM_001286149.1. [O95861-3]
NP_001273079.1. NM_001286150.1. [O95861-4]
NP_001273080.1. NM_001286151.1. [O95861-3]
NP_006076.4. NM_006085.5. [O95861-1]
XP_005273057.1. XM_005273000.2. [O95861-1]
UniGeneiHs.406134.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2WEFX-ray1.80A6-308[»]
ProteinModelPortaliO95861.
SMRiO95861. Positions 6-308.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115653. 3 interactions.
IntActiO95861. 1 interaction.
MINTiMINT-5002343.
STRINGi9606.ENSP00000318852.

PTM databases

DEPODiO95861.
PhosphoSiteiO95861.

2D gel databases

REPRODUCTION-2DPAGEIPI00410214.

Proteomic databases

MaxQBiO95861.
PaxDbiO95861.
PRIDEiO95861.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000322067; ENSP00000318852; ENSG00000162813. [O95861-1]
ENST00000414869; ENSP00000410348; ENSG00000162813. [O95861-4]
ENST00000469520; ENSP00000446828; ENSG00000162813. [O95861-1]
ENST00000544404; ENSP00000444398; ENSG00000162813. [O95861-3]
GeneIDi10380.
KEGGihsa:10380.
UCSCiuc001hma.3. human. [O95861-1]
uc010puh.2. human.

Organism-specific databases

CTDi10380.
GeneCardsiGC01M220230.
H-InvDBHIX0001601.
HGNCiHGNC:1096. BPNT1.
HPAiHPA048461.
MIMi604053. gene.
neXtProtiNX_O95861.
PharmGKBiPA25407.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0483.
GeneTreeiENSGT00530000063462.
HOGENOMiHOG000293205.
HOVERGENiHBG050719.
KOiK01082.
OMAiINQPFYN.
OrthoDBiEOG7WQ7SQ.
PhylomeDBiO95861.
TreeFamiTF314300.

Enzyme and pathway databases

BRENDAi3.1.3.7. 2681.
ReactomeiREACT_6913. Cytosolic sulfonation of small molecules.

Miscellaneous databases

EvolutionaryTraceiO95861.
GenomeRNAii10380.
NextBioi35473949.
PROiO95861.
SOURCEiSearch...

Gene expression databases

BgeeiO95861.
CleanExiHS_BPNT1.
ExpressionAtlasiO95861. baseline and differential.
GenevestigatoriO95861.

Family and domain databases

InterProiIPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]
PANTHERiPTHR20854. PTHR20854. 1 hit.
PfamiPF00459. Inositol_P. 1 hit.
[Graphical view]
PROSITEiPS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] (ISOFORMS 1; 3 AND 4).
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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.
  7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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.

Entry informationi

Entry nameiBPNT1_HUMAN
AccessioniPrimary (citable) accession number: O95861
Secondary accession number(s): A8K7C8
, B4DPS5, B4DUS9, D3DTA9, Q8WVL5, Q9UGJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: May 1, 1999
Last modified: January 7, 2015
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.