SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q5XHF8

- VIP2_XENLA

UniProt

Q5XHF8 - VIP2_XENLA

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2

Gene
ppip5k2, hisppd1, vip2
Organism
Xenopus laevis (African clawed frog)
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 sitei148 – 1481ATP By similarity
Binding sitei201 – 2011ATP By similarity
Binding sitei208 – 2081ATP By similarity
Binding sitei227 – 2271ATP By similarity
Binding sitei262 – 2621Substrate By similarity
Binding sitei276 – 2761Substrate By similarity
Binding sitei278 – 2781ATP By similarity
Binding sitei323 – 3231ATP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi251 – 2544ATP By similarity
Nucleotide bindingi260 – 2623ATP By similarity
Nucleotide bindingi335 – 3373ATP 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
OrganismiXenopus laevis (African clawed frog)
Taxonomic identifieri8355 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Organism-specific databases

XenbaseiXB-GENE-1000382. ppip5k2.

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 – 11311131Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2PRO_0000315695Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ5XHF8.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni67 – 682Substrate binding By similarity
Regioni227 – 2282Substrate binding By similarity
Regioni340 – 3434Substrate binding By similarity
Regioni385 – 45672Polyphosphoinositide-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.
KOiK13024.

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.

Q5XHF8-1 [UniParc]FASTAAdd to Basket

« Hide

MSVSATENDV PRFFVGCEES DELLDQSKPE NLDNLYEHTE DEEDEEDDEY     50
DSPPERQIVV GICAMAKKSK SKPMKEILER LSLFKYITVV IFEEEVILNE 100
TVENWPLCDC LISFHSKGFL LDKAVAYAKL RNPFVINDLN LQYQIQDRRE 150
VYRILTNEGI MLPRYAVLNR DPNKPEECNL IEGEDHVEVN GEIFQKPFVE 200
KPVSAEDHNV YIYYPTSAGG GSQRLFRKIG SRSSVYSPES SVRKTGSYIY 250
EEFMPTDGTD VKVYTVGPDY AHAEARKSPA LDGKVERDSE GKEVRYPVIL 300
NAREKLIAWK VCLAFKQTVC GFDLLRASGQ SYVCDVNGFS FVKNSMKYYD 350
DCAKILGNII MRELAPVFHI PWSIPLEAED IPIVPTTSGT KMELRCVIAV 400
IRHGDRTPKQ KMKMEVRHQR FFDLFEKYHG YKTGKIKLKK PKQLQEVLDI 450
ARQLLVELGQ NNDSEIEESK AKLEQLKTVL EMYGHFSGIN RKVQLTYLPH 500
GCPKTSSEEE DCRREEPSLL LVLKWGGELT PAGRVQAEEL GRAFRCMYPG 550
GQGDYAGFPG CGLLRLHSTY RHDLKIYASD EGRVQMTAAA FAKGLLALEG 600
ELTPILVQMV KSANMNGLLD SDSDSLSSCQ HRVKARLHEI LQRDRDFSSE 650
DFEKLSPTGS VSQIKSMHFI KNPVKTCDKV YSLIQSLTSQ IRQRMEDPKF 700
ADIQLYHSET LELMLRRWSK LEKDFKTKNG RYDISKIPDI YDCIKYDVQH 750
NCSLKLENTM ELYRLSKALA DIVIPQEYGI SRPEKLEIAK GYCTPLVRKI 800
RSDLQRTQDD DTVNKLHPLY SRGVMSPERH VRTRLYFTSE SHVHSLLSIL 850
RFGALCDETK DEQWKRAMDY LNVVSELNYM TQIVIMLYED PNKDVSSEER 900
FHVELHFSPG AKGCEEDKNL PSGFGYRPAS QENESSKKHT HANDSDEDLG 950
VCRRDEPDRA LVMFKPMVSD PIHIHRKSPL PRSRKIGSVE VLSDNNSHLR 1000
TARLLEQKHI GLGFELYSMV PSICPLETLH NSLSLKQVDE FLSAVAAPSS 1050
DYQMDTPTAS PSTPGFYTYV GGRKISLNTY TPTKILPPLF PVSTDVEMSD 1100
SVFQSCSSTS MVPGLAGSAD NTERNHQAQD D 1131
Length:1,131
Mass (Da):128,720
Last modified:November 23, 2004 - v1
Checksum:i4ADD5D46EC308E46
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC084099 mRNA. Translation: AAH84099.1.
RefSeqiNP_001088187.1. NM_001094718.1.
UniGeneiXl.18971.

Genome annotation databases

GeneIDi495012.
KEGGixla:495012.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BC084099 mRNA. Translation: AAH84099.1 .
RefSeqi NP_001088187.1. NM_001094718.1.
UniGenei Xl.18971.

3D structure databases

ProteinModelPortali Q5XHF8.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 495012.
KEGGi xla:495012.

Organism-specific databases

CTDi 23262.
Xenbasei XB-GENE-1000382. ppip5k2.

Phylogenomic databases

HOVERGENi HBG108657.
KOi K13024.

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. NIH - Xenopus Gene Collection (XGC) project
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Oocyte.

Entry informationi

Entry nameiVIP2_XENLA
AccessioniPrimary (citable) accession number: Q5XHF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 23, 2004
Last modified: June 11, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi