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Q5REW0

- VIP2_PONAB

UniProt

Q5REW0 - VIP2_PONAB

Protein

Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2

Gene

PPIP5K2

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 48 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
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    Functioni

    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.By similarity

    Catalytic activityi

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei134 – 1341ATPBy similarity
    Binding sitei187 – 1871ATPBy similarity
    Binding sitei194 – 1941ATPBy similarity
    Binding sitei213 – 2131ATPBy similarity
    Binding sitei248 – 2481SubstrateBy similarity
    Binding sitei262 – 2621SubstrateBy similarity
    Binding sitei264 – 2641ATPBy similarity
    Binding sitei309 – 3091ATPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi237 – 2404ATPBy similarity
    Nucleotide bindingi246 – 2483ATPBy similarity
    Nucleotide bindingi321 – 3233ATPBy similarity

    GO - Molecular functioni

    1. acid phosphatase activity Source: InterPro
    2. ATP binding Source: UniProtKB-KW
    3. diphosphoinositol-pentakisphosphate kinase activity Source: UniProtKB
    4. inositol-1,3,4,5,6-pentakisphosphate kinase activity Source: UniProtKB
    5. inositol hexakisphosphate 1-kinase activity Source: UniProtKB-EC
    6. inositol hexakisphosphate 3-kinase activity Source: UniProtKB-EC
    7. inositol hexakisphosphate 5-kinase activity Source: UniProtKB

    GO - Biological processi

    1. inositol metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:PPIP5K2
    Synonyms:HISPPD1, VIP2
    OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
    Taxonomic identifieri9601 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
    ProteomesiUP000001595: Unplaced

    Subcellular locationi

    Cytoplasmcytosol By similarity

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12441244Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2PRO_0000315694Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei38 – 381PhosphoserineBy similarity
    Modified residuei1007 – 10071PhosphoserineBy similarity
    Modified residuei1017 – 10171PhosphoserineBy similarity
    Modified residuei1173 – 11731PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ5REW0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni53 – 542Substrate bindingBy similarity
    Regioni213 – 2142Substrate bindingBy similarity
    Regioni326 – 3294Substrate bindingBy similarity
    Regioni371 – 44272Polyphosphoinositide-binding domainBy similarityAdd
    BLAST

    Domaini

    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.By similarity

    Sequence similaritiesi

    Phylogenomic databases

    HOVERGENiHBG108657.

    Family and domain databases

    Gene3Di3.40.50.1240. 3 hits.
    InterProiIPR000560. His_Pase_superF_clade-2.
    IPR029033. His_PPase_superfam.
    [Graphical view]
    PfamiPF00328. His_Phos_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF53254. SSF53254. 3 hits.
    PROSITEiPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q5REW0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEAPRFFVG PEDTEINPGN YRHFFHHADE DDEEEDDSPP ERQIVVGICS     50
    MAKKSKSKPM KEILERVSLF KYITVVVFEE EVILNEPVEN WPLCDCLISF 100
    HSKGFPLDKA VAYAKLRNPF VINDLNMQYL IQDRREVYSI LQAEGILLPR 150
    YAILNRDPNN PKECNLIEGE DHVEVNGEVF QKPFVEKPVS AEDHNVYIYY 200
    PTSAGGGSQR LFRKIGSRSS VYSPESNVRK TGSYIYEEFM PTDGTDVKVY 250
    TVGPDYAHAE ARKSPALDGK VERDSEGKEV RYPVILNARE KLIAWKVCLA 300
    FKQTVCGFDL LRANGQSYVC DVNGFSFVKN SMKYYDDCAK ILGNIVMREL 350
    APQFHIPWSI PLEAEDIPIV PTTSGTMMEL RCVIAVIRHG DRTPKQKMKM 400
    EVRHQKFFDL FEKCDGYKSG KLKLKKPKQL QEVLDIARQL LMELGQNNDS 450
    EIEENKPKLE QLKTVLEMYG HFFSGINRKV QLTYLPHGCP KTSSEEEDSR 500
    REEPSLLLVL KWGGELTPAG RVQAEELGRA FRCMYPGGQG DYAGFPGCGL 550
    LRLHSTYRHD LKIYASDEGR VQMTAAAFAK GLLALEGELT PILVQMVKSA 600
    NMNGLLDSDS DSLSSCQQRV KARLHEILQK DRDFTAEDYE ELTPSGSVSL 650
    IKSMHLIKNP VKTCDKVYSL IQSLTSQIRH RMEDPKSSDI QLYHSETLEL 700
    MLRRWSKLEK DFKAKNGRYD ISKIPDIYDC IKYDVQHNGS LKLENTMELY 750
    RLSKALADIV IPQEYGITKA EKLEIAKGYC TPLVRKIRSD LQRTQDDGTV 800
    NKLHPVYSRG VLSPERHVRT RLYFTSESHV HSLLSILRYG ALCNESKDEQ 850
    WKRAMDYLNV VNELNYMTQI VIMLYEDPNK DLSSEERFHV ELHFSPGAKG 900
    CEEDKNLPSG YGYRPASREN EGRRPSKIDN DDEPHTSKRD EVDRAVILFK 950
    PMVSEPIHIH RKSPLPRSRK MATNDEESPL SVSSPEGTGT WLHYTSGVGT 1000
    GRRRRRSGEQ ITSSPVSPKS LAFTSSIFGS WQQVVSENAN YLRTPRTLVE 1050
    QKQNPTVGSH CAGLFSTSVL GGSSSAPNLQ DYARTHRKKL TSSGCIDDAT 1100
    RGSAVKRFSI SFARHPTNGF ELYSMVPSIC PLETLHNALS LKQVDEFLAS 1150
    IASPSSDVPR KTAEISSTAL HSSPIMRKKV SLNTYTPAKI LPTPPATLKS 1200
    TKASSKPATS GPSSAVVPNT SSRKKNITSK TETHEHKKNT GKKK 1244
    Length:1,244
    Mass (Da):140,390
    Last modified:December 21, 2004 - v1
    Checksum:iCBB0901E63D33824
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR857406 mRNA. Translation: CAH89697.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR857406 mRNA. Translation: CAH89697.1 .

    3D structure databases

    ProteinModelPortali Q5REW0.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG108657.

    Family and domain databases

    Gene3Di 3.40.50.1240. 3 hits.
    InterProi IPR000560. His_Pase_superF_clade-2.
    IPR029033. His_PPase_superfam.
    [Graphical view ]
    Pfami PF00328. His_Phos_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53254. SSF53254. 3 hits.
    PROSITEi PS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

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

    Entry informationi

    Entry nameiVIP2_PONAB
    AccessioniPrimary (citable) accession number: Q5REW0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 48 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3