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Q9BT40 (INP5K_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inositol polyphosphate 5-phosphatase K

EC=3.1.3.56
Alternative name(s):
Skeletal muscle and kidney-enriched inositol phosphatase
Gene names
Name:INPP5K
Synonyms:PPS, SKIP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length448 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inositol 5-phosphatase which acts on inositol 1,4,5-trisphosphate, inositol 1,3,4,5-tetrakisphosphate, phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. Has 6-fold higher affinity for phosphatidylinositol 4,5-bisphosphate than for inositol 1,4,5-trisphosphate. May negatively regulate assembly of the actin cytoskeleton. Ref.1

Catalytic activity

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

Subcellular location

Endoplasmic reticulum. Note: Following stimulation with EGF, translocates to membrane ruffles. Ref.6

Tissue specificity

Ubiquitously expressed with highest levels in skeletal muscle, heart and kidney. Ref.1

Sequence similarities

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

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

actin cytoskeleton organization

Non-traceable author statement Ref.1. Source: UniProtKB

cellular response to cAMP

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to epidermal growth factor stimulus

Inferred from direct assay PubMed 21712384. Source: UniProtKB

cellular response to hormone stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to insulin stimulus

Inferred from direct assay PubMed 12556481. Source: UniProtKB

cellular response to tumor necrosis factor

Inferred from direct assay PubMed 21712384. Source: UniProtKB

dephosphorylation

Inferred from direct assay PubMed 18573875. Source: GOC

glucose homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

inositol phosphate dephosphorylation

Inferred from direct assay Ref.6. Source: MGI

negative regulation by host of viral transcription

Inferred from direct assay PubMed 18774950. Source: UniProtKB

negative regulation of MAP kinase activity

Inferred from direct assay PubMed 12556481. Source: UniProtKB

negative regulation of calcium ion transport

Inferred from direct assay PubMed 12556481. Source: UniProtKB

negative regulation of dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of glucose transport

Inferred from direct assay PubMed 12556481. Source: UniProtKB

negative regulation of glycogen (starch) synthase activity

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of glycogen biosynthetic process

Inferred from direct assay PubMed 12556481. Source: UniProtKB

negative regulation of insulin receptor signaling pathway

Inferred from direct assay PubMed 12556481. Source: UniProtKB

negative regulation of peptidyl-serine phosphorylation

Inferred from direct assay PubMed 12556481. Source: UniProtKB

negative regulation of peptidyl-threonine phosphorylation

Inferred from direct assay PubMed 12556481. Source: UniProtKB

negative regulation of protein kinase B signaling

Inferred from direct assay PubMed 12556481. Source: UniProtKB

negative regulation of protein kinase activity

Inferred from direct assay PubMed 12556481. Source: UniProtKB

negative regulation of protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of protein targeting to membrane

Inferred from direct assay PubMed 12556481. Source: UniProtKB

negative regulation of single stranded viral RNA replication via double stranded DNA intermediate

Inferred from direct assay PubMed 18774950. Source: UniProtKB

negative regulation of stress fiber assembly

Inferred from direct assay PubMed 12556481. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol biosynthetic process

Traceable author statement. Source: Reactome

phosphatidylinositol dephosphorylation

Inferred from direct assay PubMed 12556481. Source: UniProtKB

phospholipid metabolic process

Traceable author statement. Source: Reactome

positive regulation of renal water transport

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of urine volume

Inferred from sequence or structural similarity. Source: UniProtKB

protein targeting to plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of glycogen biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

ruffle assembly

Inferred from direct assay PubMed 12556481. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from direct assay Ref.1PubMed 21712384. Source: UniProtKB

endoplasmic reticulum

Inferred from direct assay PubMed 18774950. Source: UniProtKB

membrane

Inferred from direct assay Ref.6. Source: MGI

neuron projection

Inferred from direct assay Ref.1. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 18774950. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 18774950PubMed 21712384. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 12556481PubMed 21712384. Source: UniProtKB

ruffle

Inferred from direct assay Ref.6. Source: MGI

ruffle membrane

Inferred from direct assay PubMed 12556481. Source: UniProtKB

trans-Golgi network

Inferred from direct assay PubMed 12556481. Source: UniProtKB

   Molecular_functioninositol bisphosphate phosphatase activity

Inferred from direct assay PubMed 18573875. Source: MGI

inositol trisphosphate phosphatase activity

Inferred from direct assay PubMed 18573875. Source: MGI

inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

inositol-1,4,5-trisphosphate 5-phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

inositol-polyphosphate 5-phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

lipid phosphatase activity

Non-traceable author statement Ref.1. Source: UniProtKB

phosphatidylinositol phosphate 5-phosphatase activity

Inferred from mutant phenotype PubMed 18774950. Source: UniProtKB

phosphatidylinositol trisphosphate phosphatase activity

Inferred from direct assay PubMed 12556481. Source: UniProtKB

phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity

Inferred from direct assay PubMed 21712384. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 21712384. Source: UniProtKB

vasopressin receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LNX1Q8TBB13EBI-749162,EBI-739832

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 (identifier: Q9BT40-1)

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 Ref.1 (identifier: Q9BT40-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-76: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 448448Inositol polyphosphate 5-phosphatase K
PRO_0000209727

Regions

Region16 – 318303Catalytic Potential
Region321 – 448128Required for ruffle localization Ref.6

Natural variations

Alternative sequence1 – 7676Missing in isoform 2. Ref.1
VSP_050612
Natural variant3151S → F in a breast cancer sample; somatic mutation. Ref.7
VAR_036497

Experimental info

Mutagenesis3491Y → A or F: No effect on EGF-induced ruffle localization. Ref.6
Mutagenesis3611D → A: Significant decrease in EGF-induced ruffle localization. Ref.6
Mutagenesis3621W → A: Significant decrease in EGF-induced ruffle localization. Ref.6
Mutagenesis3761Y → A or F: No effect on EGF-induced ruffle localization. Ref.6
Sequence conflict1201T → A in AAB03214. Ref.5
Sequence conflict4161S → R in BAA92340. Ref.1
Sequence conflict4161S → R in BAA92341. Ref.1
Sequence conflict4161S → R in BAA92342. Ref.1
Sequence conflict4161S → R in AAB03214. Ref.5
Sequence conflict4261S → R in BAA92340. Ref.1
Sequence conflict4261S → R in BAA92341. Ref.1
Sequence conflict4261S → R in BAA92342. Ref.1
Sequence conflict4261S → R in AAB03214. Ref.5

Sequences

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

Last modified October 17, 2006. Version 3.
Checksum: 46FAA48C6E2EEAD4

FASTA44851,090
        10         20         30         40         50         60 
MSSRKLSGPK GRRLSIHVVT WNVASAAPPL DLSDLLQLNN RNLNLDIYVI GLQELNSGII 

        70         80         90        100        110        120 
SLLSDAAFND SWSSFLMDVL SPLSFIKVSH VRMQGILLLV FAKYQHLPYI QILSTKSTPT 

       130        140        150        160        170        180 
GLFGYWGNKG GVNICLKLYG YYVSIINCHL PPHISNNYQR LEHFDRILEM QNCEGRDIPN 

       190        200        210        220        230        240 
ILDHDLIIWF GDMNFRIEDF GLHFVRESIK NRCYGGLWEK DQLSIAKKHD PLLREFQEGR 

       250        260        270        280        290        300 
LLFPPTYKFD RNSNDYDTSE KKRKPAWTDR ILWRLKRQPC AGPDTPIPPA SHFSLSLRGY 

       310        320        330        340        350        360 
SSHMTYGISD HKPVSGTFDL ELKPLVSAPL IVLMPEDLWT VENDMMVSYS STSDFPSSPW 

       370        380        390        400        410        420 
DWIGLYKVGL RDVNDYVSYA WVGDSKVSCS DNLNQVYIDI SNIPTTEDEF LLCYYSNSLR 

       430        440 
SVVGISRPFQ IPPGSLREDP LGEAQPQI 

« Hide

Isoform 2 [UniParc].

Checksum: E257B4890DCD44F3
Show »

FASTA37242,784

References

« Hide 'large scale' references
[1]"Identification and characterization of a novel inositol polyphosphate 5-phosphatase."
Ijuin T., Mochizuki Y., Fukami K., Funaki M., Asano T., Takenawa T.
J. Biol. Chem. 275:10870-10875(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY.
Tissue: Testis.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain and Thymus.
[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] (ISOFORM 1).
Tissue: Eye.
[5]Nussbaum R.L.
Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 120-448.
Tissue: Brain.
[6]"Identification of a novel domain in two mammalian inositol-polyphosphate 5-phosphatases that mediates membrane ruffle localization. The inositol 5-phosphatase SKIP localizes to the endoplasmic reticulum and translocates to membrane ruffles following epidermal growth factor stimulation."
Gurung R., Tan A., Ooms L.M., McGrath M.J., Huysmans R.D., Munday A.D., Prescott M., Whisstock J.C., Mitchell C.A.
J. Biol. Chem. 278:11376-11385(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-349; ASP-361; TRP-362 AND TYR-376.
[7]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] PHE-315.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB036829 mRNA. Translation: BAA92340.1.
AB036830 mRNA. Translation: BAA92341.1.
AB036831 Genomic DNA. Translation: BAA92342.1.
AK312585 mRNA. Translation: BAG35479.1.
AK312844 mRNA. Translation: BAG35697.1.
CH471108 Genomic DNA. Translation: EAW90614.1.
CH471108 Genomic DNA. Translation: EAW90615.1.
CH471108 Genomic DNA. Translation: EAW90618.1.
BC004362 mRNA. Translation: AAH04362.1.
U45973 mRNA. Translation: AAB03214.1.
CCDSCCDS11004.1. [Q9BT40-1]
CCDS11005.1. [Q9BT40-2]
RefSeqNP_001129114.1. NM_001135642.1. [Q9BT40-2]
NP_057616.2. NM_016532.3. [Q9BT40-1]
NP_570122.1. NM_130766.2. [Q9BT40-2]
XP_005256740.1. XM_005256683.1. [Q9BT40-2]
XP_006721608.1. XM_006721545.1. [Q9BT40-2]
UniGeneHs.632238.

3D structure databases

ProteinModelPortalQ9BT40.
SMRQ9BT40. Positions 20-323.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119720. 17 interactions.
IntActQ9BT40. 13 interactions.
MINTMINT-1445023.
STRING9606.ENSP00000254712.

PTM databases

PhosphoSiteQ9BT40.

Polymorphism databases

DMDM116242791.

Proteomic databases

MaxQBQ9BT40.
PaxDbQ9BT40.
PRIDEQ9BT40.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000320345; ENSP00000318476; ENSG00000132376. [Q9BT40-2]
ENST00000406424; ENSP00000385177; ENSG00000132376. [Q9BT40-2]
ENST00000421807; ENSP00000413937; ENSG00000132376. [Q9BT40-1]
GeneID51763.
KEGGhsa:51763.
UCSCuc002fsq.3. human. [Q9BT40-1]

Organism-specific databases

CTD51763.
GeneCardsGC17M001397.
HGNCHGNC:33882. INPP5K.
HPAHPA031044.
MIM607875. gene.
neXtProtNX_Q9BT40.
PharmGKBPA164720951.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5411.
HOGENOMHOG000046051.
HOVERGENHBG082135.
InParanoidQ9BT40.
KOK01106.
OMAGLYGYWG.
PhylomeDBQ9BT40.
TreeFamTF317034.

Enzyme and pathway databases

BioCycMetaCyc:HS05626-MONOMER.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ9BT40.
BgeeQ9BT40.
CleanExHS_INPP5K.
GenevestigatorQ9BT40.

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. 1 hit.
ProtoNetSearch...

Other

GeneWikiSKIP.
GenomeRNAi51763.
NextBio55878.
PROQ9BT40.
SOURCESearch...

Entry information

Entry nameINP5K_HUMAN
AccessionPrimary (citable) accession number: Q9BT40
Secondary accession number(s): B2R6I2 expand/collapse secondary AC list , B2R750, D3DTH8, Q15733, Q9NPJ5, Q9P2R5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2003
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 113 of the entry and version 3 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 17

Human chromosome 17: entries, gene names and cross-references to MIM