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Q14642 (I5P1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Type I inositol 1,4,5-trisphosphate 5-phosphatase

Short name=5PTase
EC=3.1.3.56
Gene names
Name:INPP5A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length412 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Major isoenzyme hydrolyzing the calcium-mobilizing second messenger Ins(1,4,5)P3, this is a signal-terminating reaction.

Catalytic activity

D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate.

1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate.

Subcellular location

Membrane; Lipid-anchor.

Tissue specificity

Brain; high level in Purkinje cells.

Sequence similarities

Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase type I family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PLEKP085674EBI-8670520,EBI-2565501

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 409409Type I inositol 1,4,5-trisphosphate 5-phosphatase
PRO_0000209719
Propeptide410 – 4123Removed in mature form Potential
PRO_0000396780

Amino acid modifications

Modified residue4091Cysteine methyl ester Potential
Lipidation4081S-palmitoyl cysteine Potential
Lipidation4091S-farnesyl cysteine Potential

Natural variations

Natural variant451K → R.
Corresponds to variant rs1133400 [ dbSNP | Ensembl ].
VAR_034006

Experimental info

Sequence conflict152 – 17221PQDYF…RTRWC → RRLLPRVQMVKKRLHPDEVV in CAA83500. Ref.5
Sequence conflict247 – 2515CTKAT → SAKPP in CAA83500. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q14642 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: F55C0DFDDA01A850

FASTA41247,820
        10         20         30         40         50         60 
MAGKAAAPGT AVLLVTANVG SLFDDPENLQ KNWLREFYQV VHTHKPHFMA LHCQEFGGKN 

        70         80         90        100        110        120 
YEASMSHVDK FVKELLSSDA MKEYNRARVY LDENYKSQEH FTALGSFYFL HESLKNIYQF 

       130        140        150        160        170        180 
DFKAKKYRKV AGKEIYSDTL ESTPMLEKEK FPQDYFPECK WSRKGFIRTR WCIADCAFDL 

       190        200        210        220        230        240 
VNIHLFHDAS NLVAWETSPS VYSGIRHKAL GYVLDRIIDQ RFEKVSYFVF GDFNFRLDSK 

       250        260        270        280        290        300 
SVVETLCTKA TMQTVRAADT NEVVKLIFRE SDNDRKVMLQ LEKKLFDYFN QEVFRDNNGT 

       310        320        330        340        350        360 
ALLEFDKELS VFKDRLYELD ISFPPSYPYS EDARQGEQYM NTRCPAWCDR ILMSPSAKEL 

       370        380        390        400        410 
VLRSESEEKV VTYDHIGPNV CMGDHKPVFL AFRIMPGAGK PHAHVHKCCV VQ 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of human brain type I inositol 1,4,5-trisphosphate 5-phosphatase. High levels of mRNA in cerebellar Purkinje cells."
de Smedt F., Verjans B., Mailleux P., Erneux C.
FEBS Lett. 347:69-72(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"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].
[3]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. expand/collapse author list , 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].
[4]"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].
[5]"Characterization of a cDNA encoding the 43-kDa membrane-associated inositol-polyphosphate 5-phosphatase."
Laxminarayan K.M., Chan B.K., Tetaz T., Bird P.I., Mitchell C.A.
J. Biol. Chem. 269:17305-17310(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 49-412.
Tissue: Placenta.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X77567 mRNA. Translation: CAA54676.1.
AL392043, AL356603, AL451069 Genomic DNA. Translation: CAI39945.1.
AL451069, AL392043, AL356603 Genomic DNA. Translation: CAI14121.1.
AL356603, AL451069, AL392043 Genomic DNA. Translation: CAI40942.1.
CH471211 Genomic DNA. Translation: EAW61306.1.
CH471211 Genomic DNA. Translation: EAW61307.1.
BC096280 mRNA. Translation: AAH96280.1.
Z31695 mRNA. Translation: CAA83500.1.
CCDSCCDS7669.2.
PIRS45721.
RefSeqNP_005530.3. NM_005539.3.
UniGeneHs.523360.
Hs.715308.

3D structure databases

ProteinModelPortalQ14642.
SMRQ14642. Positions 13-56, 159-238.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109844. 3 interactions.
IntActQ14642. 1 interaction.
STRING9606.ENSP00000357583.

Chemistry

BindingDBQ14642.
ChEMBLCHEMBL4243.

PTM databases

PhosphoSiteQ14642.

Polymorphism databases

DMDM3122245.

Proteomic databases

MaxQBQ14642.
PaxDbQ14642.
PRIDEQ14642.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368594; ENSP00000357583; ENSG00000068383.
GeneID3632.
KEGGhsa:3632.
UCSCuc001llp.3. human.

Organism-specific databases

CTD3632.
GeneCardsGC10P134351.
HGNCHGNC:6076. INPP5A.
HPAHPA012285.
MIM600106. gene.
neXtProtNX_Q14642.
PharmGKBPA29884.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG288675.
HOGENOMHOG000006583.
HOVERGENHBG006102.
InParanoidQ14642.
KOK01106.
OMAQGRQYMN.
OrthoDBEOG70GMFC.
PhylomeDBQ14642.
TreeFamTF314246.

Enzyme and pathway databases

BioCycMetaCyc:HS00936-MONOMER.
BRENDA3.1.3.56. 2681.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ14642.
BgeeQ14642.
CleanExHS_INPP5A.
GenevestigatorQ14642.

Family and domain databases

Gene3D3.60.10.10. 1 hit.
InterProIPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
[Graphical view]
PfamPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
SMARTSM00128. IPPc. 1 hit.
[Graphical view]
SUPFAMSSF56219. SSF56219. 3 hits.
ProtoNetSearch...

Other

GeneWikiINPP5A.
GenomeRNAi3632.
NextBio14213.
PROQ14642.
SOURCESearch...

Entry information

Entry nameI5P1_HUMAN
AccessionPrimary (citable) accession number: Q14642
Secondary accession number(s): D3DXI3, Q14640, Q5JSF1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 112 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