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Q15735 (PI5PA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A

EC=3.1.3.56
Alternative name(s):
Inositol polyphosphate 5-phosphatase J
Gene names
Name:INPP5J
Synonyms:PIB5PA, PIPP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1006 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Inositol 5-phosphatase, which converts inositol 1,4,5-trisphosphate to inositol 1,4-bisphosphate. Also converts phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 4-phosphate and inositol 1,3,4,5-tetrakisphosphate to inositol 1,3,4-trisphosphate in vitro. May be involved in modulation of the function of inositol and phosphatidylinositol polyphosphate-binding proteins that are present at membranes ruffles By similarity.

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

Cytoplasm By similarity. Note: Predominantly localized to membrane ruffles By similarity.

Domain

The 5 Arg-Ser-Xaa-Ser-Xaa-Xaa (RSXSXX) motifs may constitute binding sites for the 14-3-3 protein.

Sequence similarities

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

Sequence caution

The sequence AAD15618.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
SH3-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processinositol phosphate metabolic process

Traceable author statement. Source: Reactome

negative regulation of microtubule polymerization

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron projection development

Inferred from electronic annotation. Source: Ensembl

negative regulation of peptidyl-serine phosphorylation

Inferred from electronic annotation. Source: Ensembl

phosphatidylinositol biosynthetic process

Traceable author statement. Source: Reactome

phosphatidylinositol dephosphorylation

Inferred from electronic annotation. Source: InterPro

phospholipid metabolic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 12536145. Source: MGI

cytosol

Traceable author statement. Source: Reactome

dendritic shaft

Inferred from electronic annotation. Source: Ensembl

growth cone

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: Ensembl

ruffle

Inferred from direct assay PubMed 12536145. Source: MGI

   Molecular_functioninositol-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

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

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15735-1)

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: Q15735-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-367: Missing.
Isoform 3 (identifier: Q15735-3)

The sequence of this isoform differs from the canonical sequence as follows:
     56-423: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10061006Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A
PRO_0000209738

Regions

Region425 – 728304Catalytic Potential
Region729 – 840112Required for ruffle localization By similarity
Motif102 – 1076RSXSXX motif 1
Motif345 – 3506SH3-binding Potential
Motif350 – 3556RSXSXX motif 2
Motif874 – 8796RSXSXX motif 3
Motif885 – 8906RSXSXX motif 4
Motif911 – 9166RSXSXX motif 5
Compositional bias122 – 371250Pro-rich
Compositional bias840 – 93798Ser-rich

Natural variations

Alternative sequence1 – 367367Missing in isoform 2.
VSP_007296
Alternative sequence56 – 423368Missing in isoform 3.
VSP_021017
Natural variant3331S → I.
Corresponds to variant rs12485025 [ dbSNP | Ensembl ].
VAR_028107

Experimental info

Sequence conflict610 – 6123SYD → ARG Ref.5
Sequence conflict6621V → A in BAC86611. Ref.1
Sequence conflict7911W → R in AAI09289. Ref.4

Sequences

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

Last modified October 17, 2006. Version 3.
Checksum: ADB6382AA33E15AC

FASTA1,006107,197
        10         20         30         40         50         60 
MEGQSSRGSR RPGTRAGLGS LPMPQGVAQT GAPSKVDSSF QLPAKKNAAL GPSEPRLALA 

        70         80         90        100        110        120 
PVGPRAAMSA SSEGPRLALA SPRPILAPLC TPEGQKTATA HRSSSLAPTS VGQLVMSASA 

       130        140        150        160        170        180 
GPKPPPATTG SVLAPTSLGL VMPASAGPRS PPVTLGPNLA PTSRDQKQEP PASVGPKPTL 

       190        200        210        220        230        240 
AASGLSLALA SEEQPPELPS TPSPVPSPVL SPTQEQALAP ASTASGAASV GQTSARKRDA 

       250        260        270        280        290        300 
PAPRPLPASE GHLQPPAQTS GPTGSPPCIQ TSPDPRLSPS FRARPEALHS SPEDPVLPRP 

       310        320        330        340        350        360 
PQTLPLDVGQ GPSEPGTHSP GLLSPTFRPG APSGQTVPPP LPKPPRSPSR SPSHSPNRSP 

       370        380        390        400        410        420 
CVPPAPDMAL PRLGTQSTGP GRCLSPNLQA QEAPAPVTTS SSTSTLSSSP WSAQPTWKSD 

       430        440        450        460        470        480 
PGFRITVVTW NVGTAMPPDD VTSLLHLGGG DDSDGADMIA IGLQEVNSML NKRLKDALFT 

       490        500        510        520        530        540 
DQWSELFMDA LGPFNFVLVS SVRMQGVILL LFAKYYHLPF LRDVQTDCTR TGLGGYWGNK 

       550        560        570        580        590        600 
GGVSVRLAAF GHMLCFLNCH LPAHMDKAEQ RKDNFQTILS LQQFQGPGAQ GILDHDLVFW 

       610        620        630        640        650        660 
FGDLNFRIES YDLHFVKFAI DSDQLHQLWE KDQLNMAKNT WPILKGFQEG PLNFAPTFKF 

       670        680        690        700        710        720 
DVGTNKYDTS AKKRKPAWTD RILWKVKAPG GGPSPSGRKS HRLQVTQHSY RSHMEYTVSD 

       730        740        750        760        770        780 
HKPVAAQFLL QFAFRDDMPL VRLEVADEWV RPEQAVVRYR METVFARSSW DWIGLYRVGF 

       790        800        810        820        830        840 
RHCKDYVAYV WAKHEDVDGN TYQVTFSEES LPKGHGDFIL GYYSHNHSIL IGITEPFQIS 

       850        860        870        880        890        900 
LPSSELASSS TDSSGTSSEG EDDSTLELLA PKSRSPSPGK SKRHRSRSPG LARFPGLALR 

       910        920        930        940        950        960 
PSSRERRGAS RSPSPQSRRL SRVAPDRSSN GSSRGSSEEG PSGLPGPWAF PPAVPRSLGL 

       970        980        990       1000 
LPALRLETVD PGGGGSWGPD REALAPNSLS PSPQGHRGLE EGGLGP 

« Hide

Isoform 2 [UniParc].

Checksum: 3ED5CD8BBB3398D0
Show »

FASTA63970,464
Isoform 3 [UniParc].

Checksum: 3F8ECF77ECC71C26
Show »

FASTA63870,239

References

« Hide 'large scale' references
[1]"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 2 AND 3).
Tissue: Cerebellum, Heart and Spleen.
[2]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[5]Nussbaum R.L.
Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 610-1006.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK092859 mRNA. Translation: BAG52616.1.
AK095944 mRNA. Translation: BAC04657.1.
AK126610 mRNA. Translation: BAC86611.1.
AC005005 Genomic DNA. Translation: AAD15618.1. Sequence problems.
CH471095 Genomic DNA. Translation: EAW59936.1.
BC109288 mRNA. Translation: AAI09289.1.
U45975 mRNA. Translation: AAB03216.1.
CCDSCCDS46687.1. [Q15735-3]
CCDS63453.1. [Q15735-1]
CCDS63455.1. [Q15735-2]
RefSeqNP_001002837.1. NM_001002837.2. [Q15735-3]
NP_001271214.1. NM_001284285.1. [Q15735-1]
NP_001271217.1. NM_001284288.1. [Q15735-2]
NP_001271218.1. NM_001284289.1. [Q15735-2]
UniGeneHs.517549.

3D structure databases

ProteinModelPortalQ15735.
SMRQ15735. Positions 423-728.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000384534.

PTM databases

PhosphoSiteQ15735.

Polymorphism databases

DMDM116242713.

Proteomic databases

MaxQBQ15735.
PaxDbQ15735.
PRIDEQ15735.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000331075; ENSP00000333262; ENSG00000185133. [Q15735-1]
ENST00000400294; ENSP00000383150; ENSG00000185133. [Q15735-2]
ENST00000404390; ENSP00000384534; ENSG00000185133. [Q15735-3]
ENST00000405300; ENSP00000384596; ENSG00000185133. [Q15735-2]
GeneID27124.
KEGGhsa:27124.
UCSCuc003ajs.4. human. [Q15735-1]
uc003ajt.4. human. [Q15735-3]

Organism-specific databases

CTD27124.
GeneCardsGC22P031518.
HGNCHGNC:8956. INPP5J.
HPAHPA034539.
MIM606481. gene.
neXtProtNX_Q15735.
PharmGKBPA164720918.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5411.
HOGENOMHOG000046051.
HOVERGENHBG082135.
InParanoidQ15735.
KOK01106.
OMANIYQVTF.
OrthoDBEOG789CB4.
PhylomeDBQ15735.
TreeFamTF317034.

Enzyme and pathway databases

BioCycMetaCyc:HS11950-MONOMER.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ15735.
BgeeQ15735.
CleanExHS_INPP5J.
GenevestigatorQ15735.

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

GeneWikiPIB5PA.
GenomeRNAi27124.
NextBio49824.
PROQ15735.
SOURCESearch...

Entry information

Entry namePI5PA_HUMAN
AccessionPrimary (citable) accession number: Q15735
Secondary accession number(s): B3KS54 expand/collapse secondary AC list , Q32M61, Q6ZTH6, Q8N902, Q9UDT9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 30, 2003
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 125 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 22

Human chromosome 22: entries, gene names and cross-references to MIM