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Q5XHF8

- VIP2_XENLA

UniProt

Q5XHF8 - VIP2_XENLA

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Protein

Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2

Gene

ppip5k2

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).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 – 1481ATPBy similarity
Binding sitei201 – 2011ATPBy similarity
Binding sitei208 – 2081ATPBy similarity
Binding sitei227 – 2271ATPBy similarity
Binding sitei262 – 2621SubstrateBy similarity
Binding sitei276 – 2761SubstrateBy similarity
Binding sitei278 – 2781ATPBy similarity
Binding sitei323 – 3231ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi251 – 2544ATPBy similarity
Nucleotide bindingi260 – 2623ATPBy similarity
Nucleotide bindingi335 – 3373ATPBy 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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni67 – 682Substrate bindingBy similarity
Regioni227 – 2282Substrate bindingBy similarity
Regioni340 – 3434Substrate bindingBy similarity
Regioni385 – 45672Polyphosphoinositide-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.
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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSVSATENDV PRFFVGCEES DELLDQSKPE NLDNLYEHTE DEEDEEDDEY
60 70 80 90 100
DSPPERQIVV GICAMAKKSK SKPMKEILER LSLFKYITVV IFEEEVILNE
110 120 130 140 150
TVENWPLCDC LISFHSKGFL LDKAVAYAKL RNPFVINDLN LQYQIQDRRE
160 170 180 190 200
VYRILTNEGI MLPRYAVLNR DPNKPEECNL IEGEDHVEVN GEIFQKPFVE
210 220 230 240 250
KPVSAEDHNV YIYYPTSAGG GSQRLFRKIG SRSSVYSPES SVRKTGSYIY
260 270 280 290 300
EEFMPTDGTD VKVYTVGPDY AHAEARKSPA LDGKVERDSE GKEVRYPVIL
310 320 330 340 350
NAREKLIAWK VCLAFKQTVC GFDLLRASGQ SYVCDVNGFS FVKNSMKYYD
360 370 380 390 400
DCAKILGNII MRELAPVFHI PWSIPLEAED IPIVPTTSGT KMELRCVIAV
410 420 430 440 450
IRHGDRTPKQ KMKMEVRHQR FFDLFEKYHG YKTGKIKLKK PKQLQEVLDI
460 470 480 490 500
ARQLLVELGQ NNDSEIEESK AKLEQLKTVL EMYGHFSGIN RKVQLTYLPH
510 520 530 540 550
GCPKTSSEEE DCRREEPSLL LVLKWGGELT PAGRVQAEEL GRAFRCMYPG
560 570 580 590 600
GQGDYAGFPG CGLLRLHSTY RHDLKIYASD EGRVQMTAAA FAKGLLALEG
610 620 630 640 650
ELTPILVQMV KSANMNGLLD SDSDSLSSCQ HRVKARLHEI LQRDRDFSSE
660 670 680 690 700
DFEKLSPTGS VSQIKSMHFI KNPVKTCDKV YSLIQSLTSQ IRQRMEDPKF
710 720 730 740 750
ADIQLYHSET LELMLRRWSK LEKDFKTKNG RYDISKIPDI YDCIKYDVQH
760 770 780 790 800
NCSLKLENTM ELYRLSKALA DIVIPQEYGI SRPEKLEIAK GYCTPLVRKI
810 820 830 840 850
RSDLQRTQDD DTVNKLHPLY SRGVMSPERH VRTRLYFTSE SHVHSLLSIL
860 870 880 890 900
RFGALCDETK DEQWKRAMDY LNVVSELNYM TQIVIMLYED PNKDVSSEER
910 920 930 940 950
FHVELHFSPG AKGCEEDKNL PSGFGYRPAS QENESSKKHT HANDSDEDLG
960 970 980 990 1000
VCRRDEPDRA LVMFKPMVSD PIHIHRKSPL PRSRKIGSVE VLSDNNSHLR
1010 1020 1030 1040 1050
TARLLEQKHI GLGFELYSMV PSICPLETLH NSLSLKQVDE FLSAVAAPSS
1060 1070 1080 1090 1100
DYQMDTPTAS PSTPGFYTYV GGRKISLNTY TPTKILPPLF PVSTDVEMSD
1110 1120 1130
SVFQSCSSTS MVPGLAGSAD NTERNHQAQD D
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: October 1, 2014
This is version 55 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