Reviewed, UniProtKB/Swiss-Prot Q9UNW1 (MINP1_HUMAN)

Names and origin

Protein names

Recommended name:
    Multiple inositol polyphosphate phosphatase 1
    EC=3.1.3.62
Alternative name(s):
    Inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase
    Ins(1,3,4,5)P(4) 3-phosphatase

Gene names

Name:	MINPP1
Synonyms:	MIPP
ORF Names:	UNQ900/PRO1917

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	487 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	Acts as a phosphoinositide 5- and phosphoinositide 6-phosphatase and regulates cellular levels of inositol pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6) By similarity. May play a role in bone development (endochondral ossification).
Catalytic activity	Myo-inositol hexakisphosphate + H2O = myo-inositol pentakisphosphate (mixed isomers) + phosphate.
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.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Signal
Molecular function	Hydrolase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	bone mineralization Ref.1 Non-traceable author statement. Source: UniProtKB polyphosphate metabolic process Ref.2 Traceable author statement. Source: ProtInc
Cellular component	endoplasmic reticulum Ref.2 Traceable author statement. Source: ProtInc endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acid phosphatase activity Inferred from electronic annotation. Source: InterPro bisphosphoglycerate 3-phosphatase activity Inferred from direct assay. Source: UniProtKB multiple inositol-polyphosphate phosphatase activity Inferred from electronic annotation. Source: EC phosphohistidine phosphatase activity Ref.2 Traceable author statement. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 3 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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 30	30	By similarity
	Chain	31 – 487	457	Multiple inositol polyphosphate phosphatase 1		PRO_0000019582
Regions
	Motif	484 – 487	4	Prevents secretion from ER Potential
Sites
	Active site	89	1	Potential
Amino acid modifications
	Glycosylation	242	1	N-linked (GlcNAc...) Ref.8
	Glycosylation	481	1	N-linked (GlcNAc...) Potential
Natural variations
	Alternative sequence	279 – 312	34	DLIQV…DDAKV → GLSQFLLQSSSSLVMQRLFF HCFLSWATSKTRNP in isoform 2.		VSP_014552
	Alternative sequence	279 – 284	6	DLIQVA → GIRIFK in isoform 3.		VSP_014553
	Alternative sequence	285 – 487	203	Missing in isoform 3.		VSP_014554
	Alternative sequence	313 – 487	175	Missing in isoform 2.		VSP_014555
	Natural variant	41	1	S → L in a follicular thyroid carcinoma; somatic mutation. Ref.10		VAR_022836
	Natural variant	270	1	Q → R in a follicular thyroid adenoma. Ref.10		VAR_022837
Experimental info
	Mutagenesis	370	1	H → A: Greatly diminishes phosphatase activity. Ref.1
	Sequence conflict	81	1	V → A in CAB43673. Ref.3
	Sequence conflict	111	1	A → P in AAD02437. Ref.2
	Sequence conflict	132	1	A → R in AAD02437. Ref.2
	Sequence conflict	156 – 157	2	QL → HV in AAD02437. Ref.2
	Sequence conflict	344	1	F → S in CAB43673. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 89B8F347885B320A	FASTA	487	55,051
	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
	Isoform 2. Checksum: DC950F3E7144F13B	FASTA	312	34,661
	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 VPVNDLNAGL SQFLLQSSSS LVMQRLFFHC 310 FLSWATSKTR NP
	Isoform 3. Checksum: 0F4BC3ED1B4BFF67	FASTA	284	31,475
	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 KNATALYHVE AFKTGPEMQN ILKKVAATLQ VPVNDLNAGI RIFK

References

	« Hide 'large scale' referencesShow '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: 9923613] [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: 10087200] [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. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed: 11230166] [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. , 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: 12975309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]	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.
[6]	"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. , 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: 15164054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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 1). Tissue: Brain.
[8]	"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: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-242, MASS SPECTROMETRY. Tissue: Plasma.
[9]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[10]	"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: 11297621] [Abstract] Cited for: VARIANT FOLLICULAR THYROID CARCINOMA LEU-41, VARIANT FOLLICULAR THYROID ADENOMA ARG-270.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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. 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.
IPI	IPI00028553. IPI00293748. IPI00607763.
RefSeq	NP_004888.2.
UniGene	Hs.121260
3D structure databases
ModBase	Search...
Proteomic databases
PeptideAtlas	Q9UNW1.
PRIDE	Q9UNW1.
Genome annotation databases
Ensembl	ENSG00000107789. Homo sapiens. [Contig view]
GeneID	9562.
KEGG	hsa:9562.
Organism-specific databases
GeneCards	GC10P089254.
HGNC	HGNC:7102. MINPP1.
MIM	605391. gene.
PharmGKB	PA30820.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q9UNW1.
HOVERGEN	Q9UNW1.
OMA	Q9UNW1. QKQRSQP.
Enzyme and pathway databases
BRENDA	3.1.3.62. 247.
Gene expression databases
ArrayExpress	Q9UNW1.
Bgee	Q9UNW1.
CleanEx	HS_MINPP1.
GermOnline	ENSG00000107789. Homo sapiens.
Family and domain databases
InterPro	IPR000886. ER_targeting_sequence. IPR000560. Histidine_acid_Pase. IPR016274. Histidine_acid_Pase_euk. [Graphical view]
Pfam	PF00328. Acid_phosphat_A. 1 hit. [Graphical view]
PIRSF	PIRSF000894. Acid_phosphatase. 1 hit.
PROSITE	PS00014. ER_TARGET. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	35863.
SOURCE	Search...

Entry information

Entry name

MINP1_HUMAN

Accession

Primary (citable) accession number: Q9UNW1
Secondary accession number(s): O95172 , O95286, Q59EJ2, Q9UGA3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2005
Last sequence update:	May 1, 2000
Last modified:	June 16, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)