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Reviewed, UniProtKB/Swiss-Prot Q9NRR6 (INP5E_HUMAN)

Last modified November 3, 2009. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    72 kDa inositol polyphosphate 5-phosphatase
    EC=3.1.3.36
Alternative name(s):
    Phosphatidylinositol-4,5-bisphosphate 5-phosphatase
    Phosphatidylinositol polyphosphate 5-phosphatase type IV
Gene names
Name: INPP5E
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length644 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Converts phosphatidylinositol-3,4,5-triphosphate (PtdIns 3,4,5-P3) to PtdIns-P2. Specific for lipid substrates, inactive towards water soluble inositol phosphates. Ref.1

Catalytic activity

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

Subcellular location

Golgi apparatusGolgi stack membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Note: Peripheral membrane protein associated with Golgi stacks By similarity.

Tissue specificity

Detected in brain, heart, pancreas, testis and spleen. Ref.1

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.6 Ref.7

Miscellaneous

Active in the presence of octyl-glucoside or Triton X-100, but completely inhibited by CTAB.

Sequence similarities

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

Sequence caution

The sequence AAB03215.1 differs from that shown. Reason: Miscellaneous discrepancy. Several sequencing problems.

Ontologies

Keywords
   Biological processLipid metabolism
   Cellular componentGolgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processlipid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentinternal side of plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioninositol-polyphosphate 5-phosphatase activity Ref.1

Traceable author statement. Source: UniProtKB

phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NRR6-1)

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: Q9NRR6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     346-379: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 64464472 kDa inositol polyphosphate 5-phosphatase
PRO_0000209747

Regions

Repeat10 – 1341
Repeat15 – 1842
Repeat28 – 3143
Repeat39 – 4244
Repeat55 – 5845
Repeat69 – 7136
Repeat72 – 7437
Repeat75 – 7848
Repeat121 – 12449
Repeat169 – 172410
Repeat183 – 185311
Repeat190 – 193412
Repeat236 – 239413
Region10 – 24223313 X 4 AA repeats of P-X-X-P
Compositional bias92 – 976Poly-Arg

Amino acid modifications

Modified residue991Phosphoserine Ref.7
Modified residue1091Phosphothreonine Ref.6
Modified residue2411Phosphoserine By similarity

Natural variations

Alternative sequence346 – 37934Missing in isoform 2.
VSP_009799
Natural variant2011I → M: dbSNP rs36064831.
VAR_047078

Experimental info

Sequence conflict3451R → T in AAF81404. Ref.1

Sequences

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

Last modified November 4, 2008. Version 2.
Checksum: 5B6CFB75CD0ADC9A

FASTA64470,205
        10         20         30         40         50         60 
MPSKAENLRP SEPAPQPPEG RTLQGQLPGA PPAQRAGSPP DAPGSESPAL ACSTPATPSG 

        70         80         90        100        110        120 
EDPPARAAPI APRPPARPRL ERALSLDDKG WRRRRFRGSQ EDLEARNGTS PSRGSVQSEG 

       130        140        150        160        170        180 
PGAPAHSCSP PCLSTSLQEI PKSRGVLSSE RGSPSSGGNP LSGVASSSPN LPHRDAAVAG 

       190        200        210        220        230        240 
SSPRLPSLLP PRPPPALSLD IASDSLRTAN KVDSDLADYK LRAQPLLVRA HSSLGPGRPR 

       250        260        270        280        290        300 
SPLACDDCSL RSAKSSFSLL APIRSKDVRS RSYLEGSLLA SGALLGADEL ARYFPDRNVA 

       310        320        330        340        350        360 
LFVATWNMQG QKELPPSLDE FLLPAEADYA QDLYVIGVQE GCSDRREWET RLQETLGPHY 

       370        380        390        400        410        420 
VLLSSAAHGV LYMSLFIRRD LIWFCSEVEC STVTTRIVSQ IKTKGALGIS FTFFGTSFLF 

       430        440        450        460        470        480 
ITSHFTSGDG KVAERLLDYT RTVQALVLPR NVPDTNPYRS SAADVTTRFD EVFWFGDFNF 

       490        500        510        520        530        540 
RLSGGRTVVD ALLCQGLVVD VPALLQHDQL IREMRKGSIF KGFQEPDIHF LPSYKFDIGK 

       550        560        570        580        590        600 
DTYDSTSKQR TPSYTDRVLY RSRHKGDICP VSYSSCPGIK TSDHRPVYGL FRVKVRPGRD 

       610        620        630        640 
NIPLAAGKFD RELYLLGIKR RISKEIQRQQ ALQSQNSSTI CSVS 

« Hide

Isoform 2.

Checksum: 093CCDE3EBB9DD9A
Show »

FASTA61066,193

References

« Hide 'large scale' references
[1]"The isolation and characterization of a cDNA encoding phospholipid-specific inositol polyphosphate 5-phosphatase."
Kisseleva M.V., Wilson M.P., Majerus P.W.
J. Biol. Chem. 275:20110-20116(2000) [PubMed: 10764818] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY.
Tissue: Fetal brain.
[2]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed: 15164053] [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 (JUL-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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[5]Nussbaum R.L.
Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 469-644 (ISOFORM 1).
[6]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-109, MASS SPECTROMETRY.
[7]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF187891 mRNA. Translation: AAF81404.1.
AL592301 Genomic DNA. Translation: CAI13947.1.
CH471090 Genomic DNA. Translation: EAW88234.1.
BC028032 mRNA. Translation: AAH28032.1.
U45974 mRNA. Translation: AAB03215.1. Sequence problems.
IPIIPI00181799.
IPI00409719.
RefSeqNP_063945.2.
UniGeneHs.120998

3D structure databases

HSSPHSSP built from PDB template 1I9Z based on UniProtKB O43001.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9NRR6.

PTM databases

PhosphoSiteQ9NRR6.

Proteomic databases

PRIDEQ9NRR6.

Genome annotation databases

EnsemblENST00000371712; ENSP00000360777; ENSG00000148384; Homo sapiens. [Genome view]
ENST00000445731; ENSP00000402715; ENSG00000148384; Homo sapiens. [Genome view]
GeneID56623.
KEGGhsa:56623.
UCSCuc004cho.1. human.

Organism-specific databases

CTD56623.
GeneCardsGC09M138442.
HGNCHGNC:21474. INPP5E.
PharmGKBPA134890388.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ9NRR6.
HOVERGENQ9NRR6.
OMASGMISTS.

Enzyme and pathway databases

BRENDA3.1.3.36. 247.

Gene expression databases

ArrayExpressQ9NRR6.
BgeeQ9NRR6.
CleanExHS_INPP5E.
GenevestigatorQ9NRR6.
GermOnlineENSG00000148384. Homo sapiens.

Family and domain databases

InterProIPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
[Graphical view]
PfamPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
SMARTSM00128. IPPc. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameINP5E_HUMAN
AccessionPrimary (citable) accession number: Q9NRR6
Secondary accession number(s): Q15734, Q6PIV5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: November 4, 2008
Last modified: November 3, 2009
This is version 61 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents