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Q5REW0 (VIP2_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2

EC=2.7.4.21
EC=2.7.4.24
Alternative name(s):
Diphosphoinositol pentakisphosphate kinase 2
Histidine acid phosphatase domain-containing protein 1
InsP6 and PP-IP5 kinase 2
VIP1 homolog 2
Gene names
Name:PPIP5K2
Synonyms:HISPPD1, VIP2
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length1244 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Bifunctional inositol kinase that acts in concert with the IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and InsP8, regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, exocytosis, insulin signaling and neutrophil activation. Phosphorylates inositol hexakisphosphate (InsP6) at positions 1 or 3 to produce PP-InsP5 which is in turn phosphorylated by IP6Ks to produce (PP)2-InsP4. Alternatively, phosphorylates at position 1 or 3 PP-InsP5, produced by IP6Ks from InsP6, to produce (PP)2-InsP4 By similarity.

Catalytic activity

ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate.

ATP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate = ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate.

ATP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate = ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate.

ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate.

Subcellular location

Cytoplasmcytosol By similarity.

Domain

The polyphosphoinositide-binding domain mediates binding of PtdIns(3,4,5)P3 and InsP6. Despite its similarity with the phosphatase domain of histidine acid phosphatases, it has no phosphatase activity By similarity.

Sequence similarities

Belongs to the histidine acid phosphatase family. VIP1 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12441244Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2
PRO_0000315694

Regions

Nucleotide binding237 – 2404ATP By similarity
Nucleotide binding246 – 2483ATP By similarity
Nucleotide binding321 – 3233ATP By similarity
Region53 – 542Substrate binding By similarity
Region213 – 2142Substrate binding By similarity
Region326 – 3294Substrate binding By similarity
Region371 – 44272Polyphosphoinositide-binding domain By similarity

Sites

Binding site1341ATP By similarity
Binding site1871ATP By similarity
Binding site1941ATP By similarity
Binding site2131ATP By similarity
Binding site2481Substrate By similarity
Binding site2621Substrate By similarity
Binding site2641ATP By similarity
Binding site3091ATP By similarity

Amino acid modifications

Modified residue381Phosphoserine By similarity
Modified residue10071Phosphoserine By similarity
Modified residue10171Phosphoserine By similarity
Modified residue11731Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5REW0 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: CBB0901E63D33824

FASTA1,244140,390
        10         20         30         40         50         60 
MSEAPRFFVG PEDTEINPGN YRHFFHHADE DDEEEDDSPP ERQIVVGICS MAKKSKSKPM 

        70         80         90        100        110        120 
KEILERVSLF KYITVVVFEE EVILNEPVEN WPLCDCLISF HSKGFPLDKA VAYAKLRNPF 

       130        140        150        160        170        180 
VINDLNMQYL IQDRREVYSI LQAEGILLPR YAILNRDPNN PKECNLIEGE DHVEVNGEVF 

       190        200        210        220        230        240 
QKPFVEKPVS AEDHNVYIYY PTSAGGGSQR LFRKIGSRSS VYSPESNVRK TGSYIYEEFM 

       250        260        270        280        290        300 
PTDGTDVKVY TVGPDYAHAE ARKSPALDGK VERDSEGKEV RYPVILNARE KLIAWKVCLA 

       310        320        330        340        350        360 
FKQTVCGFDL LRANGQSYVC DVNGFSFVKN SMKYYDDCAK ILGNIVMREL APQFHIPWSI 

       370        380        390        400        410        420 
PLEAEDIPIV PTTSGTMMEL RCVIAVIRHG DRTPKQKMKM EVRHQKFFDL FEKCDGYKSG 

       430        440        450        460        470        480 
KLKLKKPKQL QEVLDIARQL LMELGQNNDS EIEENKPKLE QLKTVLEMYG HFFSGINRKV 

       490        500        510        520        530        540 
QLTYLPHGCP KTSSEEEDSR REEPSLLLVL KWGGELTPAG RVQAEELGRA FRCMYPGGQG 

       550        560        570        580        590        600 
DYAGFPGCGL LRLHSTYRHD LKIYASDEGR VQMTAAAFAK GLLALEGELT PILVQMVKSA 

       610        620        630        640        650        660 
NMNGLLDSDS DSLSSCQQRV KARLHEILQK DRDFTAEDYE ELTPSGSVSL IKSMHLIKNP 

       670        680        690        700        710        720 
VKTCDKVYSL IQSLTSQIRH RMEDPKSSDI QLYHSETLEL MLRRWSKLEK DFKAKNGRYD 

       730        740        750        760        770        780 
ISKIPDIYDC IKYDVQHNGS LKLENTMELY RLSKALADIV IPQEYGITKA EKLEIAKGYC 

       790        800        810        820        830        840 
TPLVRKIRSD LQRTQDDGTV NKLHPVYSRG VLSPERHVRT RLYFTSESHV HSLLSILRYG 

       850        860        870        880        890        900 
ALCNESKDEQ WKRAMDYLNV VNELNYMTQI VIMLYEDPNK DLSSEERFHV ELHFSPGAKG 

       910        920        930        940        950        960 
CEEDKNLPSG YGYRPASREN EGRRPSKIDN DDEPHTSKRD EVDRAVILFK PMVSEPIHIH 

       970        980        990       1000       1010       1020 
RKSPLPRSRK MATNDEESPL SVSSPEGTGT WLHYTSGVGT GRRRRRSGEQ ITSSPVSPKS 

      1030       1040       1050       1060       1070       1080 
LAFTSSIFGS WQQVVSENAN YLRTPRTLVE QKQNPTVGSH CAGLFSTSVL GGSSSAPNLQ 

      1090       1100       1110       1120       1130       1140 
DYARTHRKKL TSSGCIDDAT RGSAVKRFSI SFARHPTNGF ELYSMVPSIC PLETLHNALS 

      1150       1160       1170       1180       1190       1200 
LKQVDEFLAS IASPSSDVPR KTAEISSTAL HSSPIMRKKV SLNTYTPAKI LPTPPATLKS 

      1210       1220       1230       1240 
TKASSKPATS GPSSAVVPNT SSRKKNITSK TETHEHKKNT GKKK 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR857406 mRNA. Translation: CAH89697.1.

3D structure databases

ProteinModelPortalQ5REW0.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG108657.

Family and domain databases

InterProIPR000560. His_Pase_superF_clade-2.
[Graphical view]
PfamPF00328. His_Phos_2. 1 hit.
[Graphical view]
PROSITEPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameVIP2_PONAB
AccessionPrimary (citable) accession number: Q5REW0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families