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Q5REW0

- VIP2_PONAB

UniProt

Q5REW0 - VIP2_PONAB

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Protein

Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2

Gene
PPIP5K2, HISPPD1, VIP2
Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

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.

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 – 1341ATP By similarity
Binding sitei187 – 1871ATP By similarity
Binding sitei194 – 1941ATP By similarity
Binding sitei213 – 2131ATP By similarity
Binding sitei248 – 2481Substrate By similarity
Binding sitei262 – 2621Substrate By similarity
Binding sitei264 – 2641ATP By similarity
Binding sitei309 – 3091ATP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi237 – 2404ATP By similarity
Nucleotide bindingi246 – 2483ATP By similarity
Nucleotide bindingi321 – 3233ATP By 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
Complete GO annotation...

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
Complete GO annotation...

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 – 381Phosphoserine By similarity
Modified residuei1007 – 10071Phosphoserine By similarity
Modified residuei1017 – 10171Phosphoserine By similarity
Modified residuei1173 – 11731Phosphoserine By similarity

Keywords - PTMi

Phosphoprotein

Structurei

3D structure databases

ProteinModelPortaliQ5REW0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni53 – 542Substrate binding By similarity
Regioni213 – 2142Substrate binding By similarity
Regioni326 – 3294Substrate binding By similarity
Regioni371 – 44272Polyphosphoinositide-binding domain By 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.

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

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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: June 11, 2014
This is version 47 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

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