Skip Header

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

Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2

Gene

PPIP5K2

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed-Annotation score: 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.By similarity
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.By similarity
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.By similarity
ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei134ATPBy similarity1
Binding sitei187ATPBy similarity1
Binding sitei194ATPBy similarity1
Binding sitei213ATPBy similarity1
Binding sitei248SubstrateBy similarity1
Binding sitei262SubstrateBy similarity1
Binding sitei264ATPBy similarity1
Binding sitei309ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi237 – 240ATPBy similarity4
Nucleotide bindingi246 – 248ATPBy similarity3
Nucleotide bindingi321 – 323ATPBy similarity3

GO - Molecular functioni

GO - Biological processi

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:2.7.4.21By similarity, EC:2.7.4.24By similarity)
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
Proteomesi
  • UP000001595 Componenti: Unplaced

Subcellular locationi

  • Cytoplasmcytosol By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003156941 – 1244Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2Add BLAST1244

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei38PhosphoserineBy similarity1
Modified residuei223PhosphoserineBy similarity1
Modified residuei1007PhosphoserineBy similarity1
Modified residuei1017PhosphoserineBy similarity1
Modified residuei1075PhosphoserineBy similarity1
Modified residuei1092PhosphoserineBy similarity1
Modified residuei1166PhosphoserineBy similarity1
Modified residuei1173PhosphoserineBy similarity1
Modified residuei1181PhosphoserineBy similarity1
Modified residuei1221PhosphoserineBy similarity1
Modified residuei1222PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Structurei

3D structure databases

ProteinModelPortaliQ5REW0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni53 – 54Substrate bindingBy similarity2
Regioni213 – 214Substrate bindingBy similarity2
Regioni326 – 329Substrate bindingBy similarity4
Regioni371 – 442Polyphosphoinositide-binding domainBy similarityAdd BLAST72

Domaini

The C-terminal acid phosphatase-like domain binds 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.
InParanoidiQ5REW0.

Family and domain databases

CDDicd07061. HP_HAP_like. 1 hit.
Gene3Di3.40.50.1240. 3 hits.
InterProiIPR033379. Acid_Pase_AS.
IPR000560. His_Pase_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

        10         20         30         40         50
MSEAPRFFVG PEDTEINPGN YRHFFHHADE DDEEEDDSPP ERQIVVGICS
60 70 80 90 100
MAKKSKSKPM KEILERVSLF KYITVVVFEE EVILNEPVEN WPLCDCLISF
110 120 130 140 150
HSKGFPLDKA VAYAKLRNPF VINDLNMQYL IQDRREVYSI LQAEGILLPR
160 170 180 190 200
YAILNRDPNN PKECNLIEGE DHVEVNGEVF QKPFVEKPVS AEDHNVYIYY
210 220 230 240 250
PTSAGGGSQR LFRKIGSRSS VYSPESNVRK TGSYIYEEFM PTDGTDVKVY
260 270 280 290 300
TVGPDYAHAE ARKSPALDGK VERDSEGKEV RYPVILNARE KLIAWKVCLA
310 320 330 340 350
FKQTVCGFDL LRANGQSYVC DVNGFSFVKN SMKYYDDCAK ILGNIVMREL
360 370 380 390 400
APQFHIPWSI PLEAEDIPIV PTTSGTMMEL RCVIAVIRHG DRTPKQKMKM
410 420 430 440 450
EVRHQKFFDL FEKCDGYKSG KLKLKKPKQL QEVLDIARQL LMELGQNNDS
460 470 480 490 500
EIEENKPKLE QLKTVLEMYG HFFSGINRKV QLTYLPHGCP KTSSEEEDSR
510 520 530 540 550
REEPSLLLVL KWGGELTPAG RVQAEELGRA FRCMYPGGQG DYAGFPGCGL
560 570 580 590 600
LRLHSTYRHD LKIYASDEGR VQMTAAAFAK GLLALEGELT PILVQMVKSA
610 620 630 640 650
NMNGLLDSDS DSLSSCQQRV KARLHEILQK DRDFTAEDYE ELTPSGSVSL
660 670 680 690 700
IKSMHLIKNP VKTCDKVYSL IQSLTSQIRH RMEDPKSSDI QLYHSETLEL
710 720 730 740 750
MLRRWSKLEK DFKAKNGRYD ISKIPDIYDC IKYDVQHNGS LKLENTMELY
760 770 780 790 800
RLSKALADIV IPQEYGITKA EKLEIAKGYC TPLVRKIRSD LQRTQDDGTV
810 820 830 840 850
NKLHPVYSRG VLSPERHVRT RLYFTSESHV HSLLSILRYG ALCNESKDEQ
860 870 880 890 900
WKRAMDYLNV VNELNYMTQI VIMLYEDPNK DLSSEERFHV ELHFSPGAKG
910 920 930 940 950
CEEDKNLPSG YGYRPASREN EGRRPSKIDN DDEPHTSKRD EVDRAVILFK
960 970 980 990 1000
PMVSEPIHIH RKSPLPRSRK MATNDEESPL SVSSPEGTGT WLHYTSGVGT
1010 1020 1030 1040 1050
GRRRRRSGEQ ITSSPVSPKS LAFTSSIFGS WQQVVSENAN YLRTPRTLVE
1060 1070 1080 1090 1100
QKQNPTVGSH CAGLFSTSVL GGSSSAPNLQ DYARTHRKKL TSSGCIDDAT
1110 1120 1130 1140 1150
RGSAVKRFSI SFARHPTNGF ELYSMVPSIC PLETLHNALS LKQVDEFLAS
1160 1170 1180 1190 1200
IASPSSDVPR KTAEISSTAL HSSPIMRKKV SLNTYTPAKI LPTPPATLKS
1210 1220 1230 1240
TKASSKPATS GPSSAVVPNT SSRKKNITSK TETHEHKKNT GKKK
Length:1,244
Mass (Da):140,390
Last modified:December 21, 2004 - v1
Checksum:iCBB0901E63D33824
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR857406 mRNA. Translation: CAH89697.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR857406 mRNA. Translation: CAH89697.1.

3D structure databases

ProteinModelPortaliQ5REW0.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG108657.
InParanoidiQ5REW0.

Family and domain databases

CDDicd07061. HP_HAP_like. 1 hit.
Gene3Di3.40.50.1240. 3 hits.
InterProiIPR033379. Acid_Pase_AS.
IPR000560. His_Pase_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]
ProtoNetiSearch...

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: November 2, 2016
This is version 60 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.