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Q5RDF1

- VIP1_PONAB

UniProt

Q5RDF1 - VIP1_PONAB

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Protein
Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1
Gene
PPIP5K1, HISPPD2A, VIP1
Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 5 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. Activated when cells are exposed to hyperosmotic stress 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 sitei145 – 1451ATP By similarity
Binding sitei198 – 1981ATP By similarity
Binding sitei205 – 2051ATP By similarity
Binding sitei224 – 2241ATP By similarity
Binding sitei259 – 2591Substrate By similarity
Binding sitei273 – 2731Substrate By similarity
Binding sitei275 – 2751ATP By similarity
Binding sitei320 – 3201ATP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi248 – 2514ATP By similarity
Nucleotide bindingi257 – 2593ATP By similarity
Nucleotide bindingi332 – 3343ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. acid phosphatase activity Source: InterPro
  3. diphosphoinositol-pentakisphosphate kinase activity Source: UniProtKB
  4. inositol hexakisphosphate 1-kinase activity Source: UniProtKB-EC
  5. inositol hexakisphosphate 3-kinase activity Source: UniProtKB-EC
  6. inositol hexakisphosphate 5-kinase activity Source: UniProtKB
  7. inositol-1,3,4,5,6-pentakisphosphate 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 1 (EC:2.7.4.21, EC:2.7.4.24)
Alternative name(s):
Diphosphoinositol pentakisphosphate kinase 1
Histidine acid phosphatase domain-containing protein 2A
InsP6 and PP-IP5 kinase 1
VIP1 homolog
Gene namesi
Name:PPIP5K1
Synonyms:HISPPD2A, VIP1
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

Subcellular locationi

Cytoplasmcytosol By similarity. Cell membrane By similarity
Note: Relocalizes to the plasma membrane upon activation of the PtdIns 3-kinase pathway By similarity.

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14091409Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1
PRO_0000315690Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1128 – 11281Phosphoserine By similarity

Keywords - PTMi

Phosphoprotein

Structurei

3D structure databases

ProteinModelPortaliQ5RDF1.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni64 – 652Substrate binding By similarity
Regioni224 – 2252Substrate binding By similarity
Regioni337 – 3404Substrate binding By similarity
Regioni382 – 45372Polyphosphoinositide-binding domain By similarity
Add
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

HOGENOMiHOG000177917.
HOVERGENiHBG108657.
InParanoidiQ5RDF1.

Family and domain databases

Gene3Di3.40.50.1240. 4 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.

Q5RDF1-1 [UniParc]FASTAAdd to Basket

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MWSLTASEGE STTAHFFLGA GDEGLGTRGI GMRPEESDSE LLEDEEDEVP     50
PEPQIIVGIC AMTKKSKSKP MTQILERLCR FDYLTVIILG EDVILNEPVE 100
NWPSCHCLIS FHSKGFPLDK AVAYSKLRNP FLINDLAMQY YIQDRREVYR 150
ILQEEGIDLP RYAVLNRDPA RPEECNLIEG EDQVEVNGAV FPKPFVEKPV 200
SAEDHNVYIY YPSSAGGGSQ RLFRKIGSRS SVYSPESIVR KTGSYIYEEF 250
MPTDGTDVKV YAVGPDYAHA EARKSPALDG KVERDSEGKE IRYPVMLTAM 300
EKLVARKVCV AFRQTVCGFD LLRANGHSFV CDVNGFSFVK NSMKYYDDCA 350
KILGNTIMRE LAPQFQIPWS IPTEAEDIPI VPTTSGTMME LRCVIAIIRH 400
GDRTPKQKMK MEVKHPRFFA LFEKHGGYKT GKLKLKRPEQ LQEVLDITRL 450
LLAELEKEPG GEIEEKTGKL EQLKSVLEMY GHFSGINRKV QSTYYPHGVK 500
ASNEGQDPQR ETLAPSLLLV LKWGGELTPA GRVQAEELGR AFRCMYPGGQ 550
GDYAGFPGCG LLRLHSTFRH DLKIYASDEG RVQMTAAAFA KGLLALEGEL 600
TPILVQMVKS ANMNGLLDSD GDSLSSCQHR VKARLHHILQ QDAPFGPEDY 650
DELAPTRSTS LLNSMTVIQN PVKVCDQVFA LIENLTHQIR ERMQDPRSVD 700
LQLYHSETLE LMLQRWSKLE RDFRQKSGRY DISKIPDIYD CVKYDVQHNG 750
SLGLQGAAEL LRLSKALADV VIPQEYGISR EEKLEIAVGF CLPLLRKILL 800
DLQRTHEDES VNKLHPLESH VHSLLSVFRY GGLLDETQDA QWQRALDYLS 850
AISELNYMTQ IVIMLYEDNT QDPLSEERFH VELHFSPGVK GVEEEGSAPA 900
GCGFRPASSE NEEMKTNEGS MENLCPGKAS DEPDRALQTS PQPPEGPGLP 950
RRSPLIRNRK AGSMEVLSET SSSRPGGYRL FSSSRPPTEM KQSGLGSQCT 1000
GLFSTTVLGG SFSAPNLQDY ARSHGKKLPP ASLKHRDELL FVPAVKRFSV 1050
SFAKHPTNGF EGCSMVPTIY PLETLHNALS LHQVSEFLSR VCQRHTDAQA 1100
QASAALFDSM HSSQASDNPF SPPRTLHSPP LQLQQRSEKP PWYSSGPSST 1150
VSSAGPSSPT TVDGNSQFGF SDQPSLNSHV AEEHQGLGLL LETPGSGAQE 1200
LSIEGEQELF EPNQSPQVPP VETSQPYEEV SQPCQEVPDI SQPCQDISEA 1250
LSQPCQEVPD ISQQCQENHD NGNHTCQEVP HISQPCQKSS QLCQKVSEEV 1300
CQLCLENSEE VSQPCQGVSV EVGKLVHKFH VGVGSLVQET LVEVGSPAEE 1350
IPEEVIQPYQ GFSVEVGRLA QEASAINLLS QGIPEIDKPS QEFPEEIDLQ 1400
AQEVPEEIN 1409
Length:1,409
Mass (Da):156,514
Last modified:December 21, 2004 - v1
Checksum:iEDFDB8AF4D0BED96
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR857961 mRNA. Translation: CAH90206.1.
UniGeneiPab.17834.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR857961 mRNA. Translation: CAH90206.1 .
UniGenei Pab.17834.

3D structure databases

ProteinModelPortali Q5RDF1.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOGENOMi HOG000177917.
HOVERGENi HBG108657.
InParanoidi Q5RDF1.

Family and domain databases

Gene3Di 3.40.50.1240. 4 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 nameiVIP1_PONAB
AccessioniPrimary (citable) accession number: Q5RDF1
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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