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Q9NRR6

- INP5E_HUMAN

UniProt

Q9NRR6 - INP5E_HUMAN

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Protein

72 kDa inositol polyphosphate 5-phosphatase

Gene
INPP5E
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Enzyme regulationi

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

GO - Molecular functioni

  1. inositol-polyphosphate 5-phosphatase activity Source: UniProtKB
  2. phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity Source: UniProtKB-EC

GO - Biological processi

  1. inositol phosphate dephosphorylation Source: Ensembl
  2. phosphatidylinositol biosynthetic process Source: Reactome
  3. phosphatidylinositol dephosphorylation Source: Ensembl
  4. phospholipid metabolic process Source: Reactome
  5. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:HS09270-MONOMER.
ReactomeiREACT_120836. Synthesis of PIPs at the Golgi membrane.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:INPP5E
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:21474. INPP5E.

Subcellular locationi

Cytoplasmcytoskeletoncilium axoneme. Golgi apparatusGolgi stack membrane; Peripheral membrane protein; Cytoplasmic side By similarity
Note: Peripheral membrane protein associated with Golgi stacks By similarity.2 Publications

GO - Cellular componenti

  1. axoneme Source: UniProtKB
  2. cytoskeleton Source: UniProtKB-KW
  3. cytosol Source: Reactome
  4. Golgi cisterna membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cilium, Cytoplasm, Cytoskeleton, Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Joubert syndrome 1 (JBTS1) [MIM:213300]: A disorder presenting with cerebellar ataxia, oculomotor apraxia, hypotonia, neonatal breathing abnormalities and psychomotor delay. Neuroradiologically, it is characterized by cerebellar vermian hypoplasia/aplasia, thickened and reoriented superior cerebellar peduncles, and an abnormally large interpeduncular fossa, giving the appearance of a molar tooth on transaxial slices (molar tooth sign). Additional variable features include retinal dystrophy and renal disease.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti378 – 3781R → C in JBTS1; slightly reduced activity. 1 Publication
VAR_063012
Natural varianti435 – 4351R → Q in JBTS1; severe reduction of activity. 1 Publication
VAR_063013
Natural varianti512 – 5121R → W in JBTS1; associated with W-515; severe reduction of activity. 1 Publication
VAR_063014
Natural varianti515 – 5151R → W in JBTS1; associated with W-512; severe reduction of activity. 1 Publication
VAR_063015
Natural varianti563 – 5631R → H in JBTS1; slightly reduced activity. 1 Publication
VAR_063016
Natural varianti580 – 5801K → E in JBTS1; severe reduction of activity. 1 Publication
VAR_063017
Mental retardation, truncal obesity, retinal dystrophy, and micropenis (MORMS) [MIM:610156]: An autosomal recessive disorder characterized by moderate mental retardation, truncal obesity, congenital non-progressive retinal dystrophy, and micropenis in males. The phenotype is similar to Bardet-Biedl syndrome and Cohen syndrome Distinguishing features are the age of onset, the non-progressive nature of the visual impairment, lack of dysmorphic facies, skin or gingival infection, microcephaly, mottled retina, polydactyly, and testicular anomalies.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication

Keywords - Diseasei

Ciliopathy, Disease mutation, Joubert syndrome, Mental retardation, Obesity

Organism-specific databases

MIMi213300. phenotype.
610156. phenotype.
Orphaneti475. Joubert syndrome.
220493. Joubert syndrome with ocular defect.
75858. MORM syndrome.
PharmGKBiPA164741785.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 64464472 kDa inositol polyphosphate 5-phosphatasePRO_0000209747Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei99 – 991Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9NRR6.
PRIDEiQ9NRR6.

PTM databases

PhosphoSiteiQ9NRR6.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiQ9NRR6.
BgeeiQ9NRR6.
CleanExiHS_INPP5E.
GenevestigatoriQ9NRR6.

Interactioni

Protein-protein interaction databases

BioGridi121159. 1 interaction.
STRINGi9606.ENSP00000360777.

Structurei

Secondary structure

1
644
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi287 – 2937
Beta strandi298 – 30710
Helixi319 – 3224
Beta strandi332 – 3409
Helixi345 – 35612
Beta strandi360 – 3689
Beta strandi371 – 3788
Helixi379 – 3846
Beta strandi389 – 39911
Beta strandi402 – 41312
Beta strandi416 – 4249
Helixi432 – 44514
Beta strandi450 – 4523
Helixi457 – 4593
Helixi465 – 4673
Beta strandi468 – 47710
Beta strandi482 – 4843
Helixi486 – 4938
Helixi501 – 5055
Helixi509 – 5157
Beta strandi518 – 5203
Beta strandi540 – 5434
Beta strandi556 – 5649
Beta strandi567 – 5759
Beta strandi581 – 5844
Beta strandi587 – 5948
Helixi611 – 62313

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XSWX-ray1.90A/B275-623[»]
ProteinModelPortaliQ9NRR6.
SMRiQ9NRR6. Positions 282-623.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati10 – 1341
Repeati15 – 1842
Repeati28 – 3143
Repeati39 – 4244
Repeati55 – 5845
Repeati69 – 7136
Repeati72 – 7437
Repeati75 – 7848
Repeati121 – 12449
Repeati169 – 172410
Repeati183 – 185311
Repeati190 – 193412
Repeati236 – 239413

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni10 – 24223313 X 4 AA repeats of P-X-X-PAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi92 – 976Poly-Arg

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5411.
HOGENOMiHOG000231541.
HOVERGENiHBG052132.
InParanoidiQ9NRR6.
KOiK01099.
OMAiAVKYSSC.
OrthoDBiEOG70KGPF.
PhylomeDBiQ9NRR6.
TreeFamiTF323475.

Family and domain databases

Gene3Di3.60.10.10. 1 hit.
InterProiIPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
[Graphical view]
PfamiPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
SMARTiSM00128. IPPc. 1 hit.
[Graphical view]
SUPFAMiSSF56219. SSF56219. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NRR6-1) [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

MPSKAENLRP SEPAPQPPEG RTLQGQLPGA PPAQRAGSPP DAPGSESPAL    50
ACSTPATPSG EDPPARAAPI APRPPARPRL ERALSLDDKG WRRRRFRGSQ 100
EDLEARNGTS PSRGSVQSEG PGAPAHSCSP PCLSTSLQEI PKSRGVLSSE 150
RGSPSSGGNP LSGVASSSPN LPHRDAAVAG SSPRLPSLLP PRPPPALSLD 200
IASDSLRTAN KVDSDLADYK LRAQPLLVRA HSSLGPGRPR SPLACDDCSL 250
RSAKSSFSLL APIRSKDVRS RSYLEGSLLA SGALLGADEL ARYFPDRNVA 300
LFVATWNMQG QKELPPSLDE FLLPAEADYA QDLYVIGVQE GCSDRREWET 350
RLQETLGPHY VLLSSAAHGV LYMSLFIRRD LIWFCSEVEC STVTTRIVSQ 400
IKTKGALGIS FTFFGTSFLF ITSHFTSGDG KVAERLLDYT RTVQALVLPR 450
NVPDTNPYRS SAADVTTRFD EVFWFGDFNF RLSGGRTVVD ALLCQGLVVD 500
VPALLQHDQL IREMRKGSIF KGFQEPDIHF LPSYKFDIGK DTYDSTSKQR 550
TPSYTDRVLY RSRHKGDICP VSYSSCPGIK TSDHRPVYGL FRVKVRPGRD 600
NIPLAAGKFD RELYLLGIKR RISKEIQRQQ ALQSQNSSTI CSVS 644
Length:644
Mass (Da):70,205
Last modified:November 4, 2008 - v2
Checksum:i5B6CFB75CD0ADC9A
GO
Isoform 2 (identifier: Q9NRR6-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:610
Mass (Da):66,193
Checksum:i093CCDE3EBB9DD9A
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti201 – 2011I → M.
Corresponds to variant rs36064831 [ dbSNP | Ensembl ].
VAR_047078
Natural varianti378 – 3781R → C in JBTS1; slightly reduced activity. 1 Publication
VAR_063012
Natural varianti435 – 4351R → Q in JBTS1; severe reduction of activity. 1 Publication
VAR_063013
Natural varianti512 – 5121R → W in JBTS1; associated with W-515; severe reduction of activity. 1 Publication
VAR_063014
Natural varianti515 – 5151R → W in JBTS1; associated with W-512; severe reduction of activity. 1 Publication
VAR_063015
Natural varianti563 – 5631R → H in JBTS1; slightly reduced activity. 1 Publication
VAR_063016
Natural varianti580 – 5801K → E in JBTS1; severe reduction of activity. 1 Publication
VAR_063017

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei346 – 37934Missing in isoform 2. VSP_009799Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti345 – 3451R → T in AAF81404. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS7000.1. [Q9NRR6-1]
RefSeqiNP_063945.2. NM_019892.4. [Q9NRR6-1]
XP_006717250.1. XM_006717187.1. [Q9NRR6-2]
UniGeneiHs.120998.

Genome annotation databases

EnsembliENST00000371712; ENSP00000360777; ENSG00000148384. [Q9NRR6-1]
GeneIDi56623.
KEGGihsa:56623.
UCSCiuc004cho.3. human. [Q9NRR6-1]

Polymorphism databases

DMDMi212276439.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS7000.1. [Q9NRR6-1 ]
RefSeqi NP_063945.2. NM_019892.4. [Q9NRR6-1 ]
XP_006717250.1. XM_006717187.1. [Q9NRR6-2 ]
UniGenei Hs.120998.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2XSW X-ray 1.90 A/B 275-623 [» ]
ProteinModelPortali Q9NRR6.
SMRi Q9NRR6. Positions 282-623.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121159. 1 interaction.
STRINGi 9606.ENSP00000360777.

PTM databases

PhosphoSitei Q9NRR6.

Polymorphism databases

DMDMi 212276439.

Proteomic databases

PaxDbi Q9NRR6.
PRIDEi Q9NRR6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000371712 ; ENSP00000360777 ; ENSG00000148384 . [Q9NRR6-1 ]
GeneIDi 56623.
KEGGi hsa:56623.
UCSCi uc004cho.3. human. [Q9NRR6-1 ]

Organism-specific databases

CTDi 56623.
GeneCardsi GC09M139323.
GeneReviewsi INPP5E.
H-InvDB HIX0125641.
HGNCi HGNC:21474. INPP5E.
MIMi 213300. phenotype.
610156. phenotype.
613037. gene.
neXtProti NX_Q9NRR6.
Orphaneti 475. Joubert syndrome.
220493. Joubert syndrome with ocular defect.
75858. MORM syndrome.
PharmGKBi PA164741785.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5411.
HOGENOMi HOG000231541.
HOVERGENi HBG052132.
InParanoidi Q9NRR6.
KOi K01099.
OMAi AVKYSSC.
OrthoDBi EOG70KGPF.
PhylomeDBi Q9NRR6.
TreeFami TF323475.

Enzyme and pathway databases

BioCyci MetaCyc:HS09270-MONOMER.
Reactomei REACT_120836. Synthesis of PIPs at the Golgi membrane.

Miscellaneous databases

GenomeRNAii 56623.
NextBioi 62067.
PROi Q9NRR6.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NRR6.
Bgeei Q9NRR6.
CleanExi HS_INPP5E.
Genevestigatori Q9NRR6.

Family and domain databases

Gene3Di 3.60.10.10. 1 hit.
InterProi IPR005135. Endo/exonuclease/phosphatase.
IPR000300. IPPc.
[Graphical view ]
Pfami PF03372. Exo_endo_phos. 1 hit.
[Graphical view ]
SMARTi SM00128. IPPc. 1 hit.
[Graphical view ]
SUPFAMi SSF56219. SSF56219. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. 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] (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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  7. "INPP5E mutations cause primary cilium signaling defects, ciliary instability and ciliopathies in human and mouse."
    Jacoby M., Cox J.J., Gayral S., Hampshire D.J., Ayub M., Blockmans M., Pernot E., Kisseleva M.V., Compere P., Schiffmann S.N., Gergely F., Riley J.H., Perez-Morga D., Woods C.G., Schurmans S.
    Nat. Genet. 41:1027-1031(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INVOLVEMENT IN MORMS.
  8. Cited for: SUBCELLULAR LOCATION, VARIANTS JBTS1 CYS-378; GLN-435; TRP-512; TRP-515; HIS-563 AND GLU-580, CHARACTERIZATION OF VARIANTS JBTS1 CYS-378; GLN-435; TRP-512; TRP-515; HIS-563 AND GLU-580.
  9. "Crystal structure of human INPP5E."
    Structural genomics consortium (SGC)
    Submitted (NOV-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 275-623.

Entry informationi

Entry nameiINP5E_HUMAN
AccessioniPrimary (citable) accession number: Q9NRR6
Secondary accession number(s): Q15734, Q6PIV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: November 4, 2008
Last modified: September 3, 2014
This is version 107 of the entry and version 2 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 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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