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Protein

72 kDa inositol polyphosphate 5-phosphatase

Gene

INPP5E

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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, and phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 4-phosphate. 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.1 Publication

Enzyme regulationi

Active in the presence of octyl-glucoside or Triton X-100, but completely inhibited by CTAB.1 Publication

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. organelle organization Source: Reactome
  3. phosphatidylinositol biosynthetic process Source: Reactome
  4. phosphatidylinositol dephosphorylation Source: Ensembl
  5. phospholipid metabolic process Source: Reactome
  6. 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:3.1.3.361 Publication)
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 3 Publications. Golgi apparatusGolgi stack membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cell projectionruffle By similarity. Cytoplasm By similarity
Note: Peripheral membrane protein associated with Golgi stacks.By similarity

GO - Cellular componenti

  1. axoneme Source: UniProtKB
  2. cytoskeleton Source: UniProtKB-KW
  3. cytosol Source: Reactome
  4. Golgi cisterna membrane Source: UniProtKB-SubCell
  5. plasma membrane Source: UniProtKB-SubCell
  6. primary cilium Source: Reactome
  7. ruffle Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Involvement in diseasei

Joubert syndrome 11 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:213300
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 micropenis1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn 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.

See also OMIM:610156

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi641 – 6411C → A: Abolishes farnesylation-dependent interaction with PDE6D. 1 Publication

Keywords - Diseasei

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

Organism-specific databases

MIMi213300. phenotype.
610156. phenotype.
Orphaneti475. Joubert syndrome.
1454. Joubert syndrome with hepatic defect.
220493. Joubert syndrome with ocular defect.
75858. MORM syndrome.
PharmGKBiPA164741785.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 64164172 kDa inositol polyphosphate 5-phosphatase1 PublicationPRO_0000209747Add
BLAST
Propeptidei642 – 6443Removed in mature form1 PublicationPRO_0000431688

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei99 – 991Phosphoserine1 Publication
Modified residuei641 – 6411Cysteine methyl ester1 Publication
Lipidationi641 – 6411S-farnesyl cysteine1 Publication

Keywords - PTMi

Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

MaxQBiQ9NRR6.
PaxDbiQ9NRR6.
PRIDEiQ9NRR6.

PTM databases

DEPODiQ9NRR6.
PhosphoSiteiQ9NRR6.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9NRR6.
CleanExiHS_INPP5E.
ExpressionAtlasiQ9NRR6. baseline.
GenevestigatoriQ9NRR6.

Interactioni

Subunit structurei

Interacts (when prenylated) with PDE6D; this is important for normal location in cilia.1 Publication

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 – 2937Combined sources
Beta strandi298 – 30710Combined sources
Helixi319 – 3224Combined sources
Beta strandi332 – 3409Combined sources
Helixi345 – 35612Combined sources
Beta strandi360 – 3689Combined sources
Beta strandi371 – 3788Combined sources
Helixi379 – 3846Combined sources
Beta strandi389 – 39911Combined sources
Beta strandi402 – 41312Combined sources
Beta strandi416 – 4249Combined sources
Helixi432 – 44514Combined sources
Beta strandi450 – 4523Combined sources
Helixi457 – 4593Combined sources
Helixi465 – 4673Combined sources
Beta strandi468 – 47710Combined sources
Beta strandi482 – 4843Combined sources
Helixi486 – 4938Combined sources
Helixi501 – 5055Combined sources
Helixi509 – 5157Combined sources
Beta strandi518 – 5203Combined sources
Beta strandi540 – 5434Combined sources
Beta strandi556 – 5649Combined sources
Beta strandi567 – 5759Combined sources
Beta strandi581 – 5844Combined sources
Beta strandi587 – 5948Combined sources
Helixi611 – 62313Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XSWX-ray1.90A/B275-623[»]
ProteinModelPortaliQ9NRR6.
SMRiQ9NRR6. Positions 282-623.
ModBaseiSearch...
MobiDBiSearch...

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.
GeneTreeiENSGT00760000119075.
HOGENOMiHOG000231541.
HOVERGENiHBG052132.
InParanoidiQ9NRR6.
KOiK01099.
OMAiSCSPPCL.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

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

        10         20         30         40         50
MPSKAENLRP SEPAPQPPEG RTLQGQLPGA PPAQRAGSPP DAPGSESPAL
60 70 80 90 100
ACSTPATPSG EDPPARAAPI APRPPARPRL ERALSLDDKG WRRRRFRGSQ
110 120 130 140 150
EDLEARNGTS PSRGSVQSEG PGAPAHSCSP PCLSTSLQEI PKSRGVLSSE
160 170 180 190 200
RGSPSSGGNP LSGVASSSPN LPHRDAAVAG SSPRLPSLLP PRPPPALSLD
210 220 230 240 250
IASDSLRTAN KVDSDLADYK LRAQPLLVRA HSSLGPGRPR SPLACDDCSL
260 270 280 290 300
RSAKSSFSLL APIRSKDVRS RSYLEGSLLA SGALLGADEL ARYFPDRNVA
310 320 330 340 350
LFVATWNMQG QKELPPSLDE FLLPAEADYA QDLYVIGVQE GCSDRREWET
360 370 380 390 400
RLQETLGPHY VLLSSAAHGV LYMSLFIRRD LIWFCSEVEC STVTTRIVSQ
410 420 430 440 450
IKTKGALGIS FTFFGTSFLF ITSHFTSGDG KVAERLLDYT RTVQALVLPR
460 470 480 490 500
NVPDTNPYRS SAADVTTRFD EVFWFGDFNF RLSGGRTVVD ALLCQGLVVD
510 520 530 540 550
VPALLQHDQL IREMRKGSIF KGFQEPDIHF LPSYKFDIGK DTYDSTSKQR
560 570 580 590 600
TPSYTDRVLY RSRHKGDICP VSYSSCPGIK TSDHRPVYGL FRVKVRPGRD
610 620 630 640
NIPLAAGKFD RELYLLGIKR RISKEIQRQQ ALQSQNSSTI CSVS
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.Several sequencing problems.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti345 – 3451R → T in AAF81404 (PubMed:10764818).Curated

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. 1 PublicationVSP_009799Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2XSWX-ray1.90A/B275-623[»]
ProteinModelPortaliQ9NRR6.
SMRiQ9NRR6. Positions 282-623.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121159. 1 interaction.
STRINGi9606.ENSP00000360777.

PTM databases

DEPODiQ9NRR6.
PhosphoSiteiQ9NRR6.

Polymorphism databases

DMDMi212276439.

Proteomic databases

MaxQBiQ9NRR6.
PaxDbiQ9NRR6.
PRIDEiQ9NRR6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi56623.
GeneCardsiGC09M139323.
GeneReviewsiINPP5E.
H-InvDBHIX0125641.
HGNCiHGNC:21474. INPP5E.
MIMi213300. phenotype.
610156. phenotype.
613037. gene.
neXtProtiNX_Q9NRR6.
Orphaneti475. Joubert syndrome.
1454. Joubert syndrome with hepatic defect.
220493. Joubert syndrome with ocular defect.
75858. MORM syndrome.
PharmGKBiPA164741785.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5411.
GeneTreeiENSGT00760000119075.
HOGENOMiHOG000231541.
HOVERGENiHBG052132.
InParanoidiQ9NRR6.
KOiK01099.
OMAiSCSPPCL.
OrthoDBiEOG70KGPF.
PhylomeDBiQ9NRR6.
TreeFamiTF323475.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiINPP5E. human.
GenomeRNAii56623.
NextBioi62067.
PROiQ9NRR6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NRR6.
CleanExiHS_INPP5E.
ExpressionAtlasiQ9NRR6. baseline.
GenevestigatoriQ9NRR6.

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.
ProtoNetiSearch...

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, CATALYTIC ACTIVITY, ENZYME REGULATION, 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. Cited for: INTERACTION WITH PDE6D, SUBCELLULAR LOCATION, ISOPRENYLATION AT CYS-641, MUTAGENESIS OF CYS-641.
  10. "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: March 4, 2015
This is version 113 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.