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Q9UNW1 (MINP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Multiple inositol polyphosphate phosphatase 1

EC=3.1.3.62
Alternative name(s):
2,3-bisphosphoglycerate 3-phosphatase
Short name=2,3-BPG phosphatase
EC=3.1.3.80
Inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase
Short name=Ins(1,3,4,5)P(4) 3-phosphatase
Gene names
Name:MINPP1
Synonyms:MIPP
ORF Names:UNQ900/PRO1917
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length487 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as a phosphoinositide 5- and phosphoinositide 6-phosphatase and regulates cellular levels of inositol pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6). Also acts as a 2,3-bisphosphoglycerate 3-phosphatase, by mediating the dephosphorylation of 2,3-bisphosphoglycerate (2,3-BPG) to produce phospho-D-glycerate without formation of 3-phosphoglycerate. May play a role in bone development (endochondral ossification). Ref.10

Catalytic activity

Myo-inositol hexakisphosphate + H2O = myo-inositol pentakisphosphate (mixed isomers) + phosphate. Ref.10

2,3-bisphospho-D-glycerate + H2O = 2-phospho-D-glycerate + phosphate. Ref.10

Subcellular location

Endoplasmic reticulum lumen By similarity.

Tissue specificity

Widely expressed with highest levels in kidney, liver and placenta. Ref.1

Involvement in disease

Defects in MINPP1 may be involved in follicular thyroid tumors development.

Sequence similarities

Belongs to the histidine acid phosphatase family. MINPP1 subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=0.61 mM for 2,3-bisphosphoglycerate Ref.10

Vmax=15.8 nmol/min/mg enzyme with 2,3-bisphospho-D-glycerate as substrate

Sequence caution

The sequence BAD93056.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UNW1-1)

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: Q9UNW1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     279-312: DLIQVAFFTCSFDLAIKGVKSPWCDVFDIDDAKV → GLSQFLLQSSSSLVMQRLFFHCFLSWATSKTRNP
     313-487: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9UNW1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     279-284: DLIQVA → GIRIFK
     285-487: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q9UNW1-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-213: MLRAPGCLLR...PGLPPPDVAD → MCLFQLCGLVRY
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 By similarity
Chain31 – 487457Multiple inositol polyphosphate phosphatase 1
PRO_0000019582

Regions

Motif484 – 4874Prevents secretion from ER Potential

Sites

Active site891 Potential

Amino acid modifications

Glycosylation2421N-linked (GlcNAc...) Ref.9
Glycosylation4811N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 213213MLRAP…PDVAD → MCLFQLCGLVRY in isoform 4.
VSP_044569
Alternative sequence279 – 31234DLIQV…DDAKV → GLSQFLLQSSSSLVMQRLFF HCFLSWATSKTRNP in isoform 2.
VSP_014552
Alternative sequence279 – 2846DLIQVA → GIRIFK in isoform 3.
VSP_014553
Alternative sequence285 – 487203Missing in isoform 3.
VSP_014554
Alternative sequence313 – 487175Missing in isoform 2.
VSP_014555
Natural variant411S → L in a follicular thyroid carcinoma; somatic mutation. Ref.12
VAR_022836
Natural variant2701Q → R in a follicular thyroid adenoma. Ref.12
VAR_022837

Experimental info

Mutagenesis891H → A: Strong reduction of 2,3-bisphosphoglycerate 3-phosphatase activity. Ref.10
Mutagenesis3701H → A: Greatly diminishes phosphatase activity. Ref.1
Sequence conflict811V → A in CAB43673. Ref.3
Sequence conflict1111A → P in AAD02437. Ref.2
Sequence conflict1321A → R in AAD02437. Ref.2
Sequence conflict156 – 1572QL → HV in AAD02437. Ref.2
Sequence conflict3441F → S in CAB43673. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 89B8F347885B320A

FASTA48755,051
        10         20         30         40         50         60 
MLRAPGCLLR TSVAPAAALA AALLSSLARC SLLEPRDPVA SSLSPYFGTK TRYEDVNPVL 

        70         80         90        100        110        120 
LSGPEAPWRD PELLEGTCTP VQLVALIRHG TRYPTVKQIR KLRQLHGLLQ ARGSRDGGAS 

       130        140        150        160        170        180 
STGSRDLGAA LADWPLWYAD WMDGQLVEKG RQDMRQLALR LASLFPALFS RENYGRLRLI 

       190        200        210        220        230        240 
TSSKHRCMDS SAAFLQGLWQ HYHPGLPPPD VADMEFGPPT VNDKLMRFFD HCEKFLTEVE 

       250        260        270        280        290        300 
KNATALYHVE AFKTGPEMQN ILKKVAATLQ VPVNDLNADL IQVAFFTCSF DLAIKGVKSP 

       310        320        330        340        350        360 
WCDVFDIDDA KVLEYLNDLK QYWKRGYGYT INSRSSCTLF QDIFQHLDKA VEQKQRSQPI 

       370        380        390        400        410        420 
SSPVILQFGH AETLLPLLSL MGYFKDKEPL TAYNYKKQMH RKFRSGLIVP YASNLIFVLY 

       430        440        450        460        470        480 
HCENAKTPKE QFRVQMLLNE KVLPLAYSQE TVSFYEDLKN HYKDILQSCQ TSEECELARA 


NSTSDEL 

« Hide

Isoform 2 [UniParc].

Checksum: DC950F3E7144F13B
Show »

FASTA31234,661
Isoform 3 [UniParc].

Checksum: 0F4BC3ED1B4BFF67
Show »

FASTA28431,475
Isoform 4 [UniParc].

Checksum: B48950FD3549CEEB
Show »

FASTA28633,100

References

« Hide 'large scale' references
[1]"The human and rat forms of multiple inositol polyphosphate phosphatase: functional homology with a histidine acid phosphatase up-regulated during endochondral ossification."
Caffrey J.J., Hidaka K., Matsuda M., Hirata M., Shears S.B.
FEBS Lett. 442:99-104(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, MUTAGENESIS OF HIS-370.
[2]"Multiple inositol polyphosphate phosphatase: evolution as a distinct group within the histidine phosphatase family and chromosomal localization of the human and mouse genes to chromosomes 10q23 and 19."
Chi H., Tiller G.E., Dasouki M.J., Romano P.R., Wang J., O'keefe R.J., Puzas J.E., Rosier R.N., Reynolds P.R.
Genomics 56:324-336(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"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. expand/collapse author list , 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] (ISOFORM 1).
Tissue: Brain.
[4]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"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. expand/collapse author list , 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 4).
Tissue: Thalamus.
[6]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Brain.
[7]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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 1).
Tissue: Brain.
[9]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-242.
Tissue: Plasma.
[10]"Dephosphorylation of 2,3-bisphosphoglycerate by MIPP expands the regulatory capacity of the Rapoport-Luebering glycolytic shunt."
Cho J., King J.S., Qian X., Harwood A.J., Shears S.B.
Proc. Natl. Acad. Sci. U.S.A. 105:5998-6003(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS 2,3-BISPHOSPHOGLYCERATE 3-PHOSPHATASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-89.
[11]"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].
[12]"Somatic mutation and germline variants of MINPP1, a phosphatase gene located in proximity to PTEN on 10q23.3, in follicular thyroid carcinomas."
Gimm O., Chi H., Dahia P.L., Perren A., Hinze R., Komminoth P., Dralle H., Reynolds P.R., Eng C.
J. Clin. Endocrinol. Metab. 86:1801-1805(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FOLLICULAR THYROID CARCINOMA LEU-41, VARIANT FOLLICULAR THYROID ADENOMA ARG-270.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF084943 mRNA. Translation: AAD09751.1.
AF084944 mRNA. Translation: AAD09752.1.
AF046914 mRNA. Translation: AAD02437.1.
AL050356 mRNA. Translation: CAB43673.1.
AY358938 mRNA. Translation: AAQ89297.1.
AK309176 mRNA. No translation available.
AB209819 mRNA. Translation: BAD93056.1. Different initiation.
AL355334, AL138767 Genomic DNA. Translation: CAH73423.1.
AL138767, AL355334 Genomic DNA. Translation: CAI16030.1.
AL355334, AL138767 Genomic DNA. Translation: CAH73422.1.
AL138767, AL355334 Genomic DNA. Translation: CAI16029.1.
BC032504 mRNA. Translation: AAH32504.1.
CCDSCCDS53551.1. [Q9UNW1-2]
CCDS53552.1. [Q9UNW1-4]
CCDS7384.1. [Q9UNW1-1]
RefSeqNP_001171588.1. NM_001178117.1. [Q9UNW1-2]
NP_001171589.1. NM_001178118.1. [Q9UNW1-4]
NP_004888.2. NM_004897.4. [Q9UNW1-1]
UniGeneHs.121260.

3D structure databases

ProteinModelPortalQ9UNW1.
SMRQ9UNW1. Positions 79-455.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114932. 1 interaction.
STRING9606.ENSP00000361064.

PTM databases

PhosphoSiteQ9UNW1.

Polymorphism databases

DMDM68565617.

Proteomic databases

MaxQBQ9UNW1.
PaxDbQ9UNW1.
PeptideAtlasQ9UNW1.
PRIDEQ9UNW1.

Protocols and materials databases

DNASU9562.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371994; ENSP00000361062; ENSG00000107789. [Q9UNW1-2]
ENST00000371996; ENSP00000361064; ENSG00000107789. [Q9UNW1-1]
ENST00000536010; ENSP00000437823; ENSG00000107789. [Q9UNW1-4]
GeneID9562.
KEGGhsa:9562.
UCSCuc001keu.3. human. [Q9UNW1-1]
uc001kev.3. human. [Q9UNW1-2]

Organism-specific databases

CTD9562.
GeneCardsGC10P089264.
HGNCHGNC:7102. MINPP1.
HPAHPA026859.
MIM605391. gene.
neXtProtNX_Q9UNW1.
PharmGKBPA30820.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG260296.
HOGENOMHOG000113591.
HOVERGENHBG052872.
InParanoidQ9UNW1.
KOK03103.
OMAADMEFGP.
OrthoDBEOG7992QC.
PhylomeDBQ9UNW1.
TreeFamTF324072.

Enzyme and pathway databases

BioCycMetaCyc:HS03025-MONOMER.
BRENDA3.1.3.62. 2681.
ReactomeREACT_111217. Metabolism.
SABIO-RKQ9UNW1.

Gene expression databases

ArrayExpressQ9UNW1.
BgeeQ9UNW1.
CleanExHS_MINPP1.
GenevestigatorQ9UNW1.

Family and domain databases

Gene3D3.40.50.1240. 1 hit.
InterProIPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
IPR016274. Histidine_acid_Pase_euk.
[Graphical view]
PfamPF00328. His_Phos_2. 1 hit.
[Graphical view]
PIRSFPIRSF000894. Acid_phosphatase. 1 hit.
SUPFAMSSF53254. SSF53254. 1 hit.
PROSITEPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMINPP1. human.
GeneWikiMINPP1.
GenomeRNAi9562.
NextBio35863.
PROQ9UNW1.
SOURCESearch...

Entry information

Entry nameMINP1_HUMAN
AccessionPrimary (citable) accession number: Q9UNW1
Secondary accession number(s): F5H683 expand/collapse secondary AC list , O95172, O95286, Q59EJ2, Q9UGA3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM