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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

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).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 – 1341ATPBy similarity
Binding sitei187 – 1871ATPBy similarity
Binding sitei194 – 1941ATPBy similarity
Binding sitei213 – 2131ATPBy similarity
Binding sitei248 – 2481SubstrateBy similarity
Binding sitei262 – 2621SubstrateBy similarity
Binding sitei264 – 2641ATPBy similarity
Binding sitei309 – 3091ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi237 – 2404ATPBy similarity
Nucleotide bindingi246 – 2483ATPBy similarity
Nucleotide bindingi321 – 3233ATPBy 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 – 381PhosphoserineBy similarity
Modified residuei1007 – 10071PhosphoserineBy similarity
Modified residuei1017 – 10171PhosphoserineBy similarity
Modified residuei1173 – 11731PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Structurei

3D structure databases

ProteinModelPortaliQ5REW0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni53 – 542Substrate bindingBy similarity
Regioni213 – 2142Substrate bindingBy similarity
Regioni326 – 3294Substrate bindingBy similarity
Regioni371 – 44272Polyphosphoinositide-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.
InParanoidiQ5REW0.

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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        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

ProteinModelPortali Q5REW0.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG108657.
InParanoidi Q5REW0.

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: October 29, 2014
This is version 49 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