Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1

Preferred order of sections

Names and origin

Protein names

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

Gene names

Name:	PPIP5K1
Synonyms:	HISPPD2A, VIP1

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	1477 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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 activity	ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate. ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate = ADP + 1D-myo-inositol diphosphate tetrakisphosphate (isomeric configuration unknown). ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate = ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate (isomeric configuration unknown).
Subcellular location	Cytoplasm › cytosol By similarity. Cell membrane By similarity. Note: Relocalizes to the plasma membrane upon activation of the PtdIns 3-kinase pathway By similarity.
Domain	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 similarities	Belongs to the histidine acid phosphatase family. VIP1 subfamily.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Membrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	inositol metabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytosol Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW acid phosphatase activity Inferred from electronic annotation. Source: InterPro diphosphoinositol-pentakisphosphate kinase activity Inferred from sequence or structural similarity. Source: UniProtKB inositol hexakisphosphate 1-kinase activity Inferred from electronic annotation. Source: EC inositol hexakisphosphate 3-kinase activity Inferred from electronic annotation. Source: EC inositol hexakisphosphate 5-kinase activity Inferred from sequence or structural similarity. Source: UniProtKB inositol-1,3,4,5,6-pentakisphosphate kinase activity Inferred from sequence or structural similarity. Source: UniProtKB kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1477

1477

Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1

PRO_0000315687

Regions

Nucleotide binding

248 – 251

4

ATP By similarity

Nucleotide binding

257 – 259

3

ATP By similarity

Nucleotide binding

332 – 334

3

ATP By similarity

Region

64 – 65

2

Substrate binding By similarity

Region

224 – 225

2

Substrate binding By similarity

Region

337 – 340

4

Substrate binding By similarity

Region

382 – 453

72

Polyphosphoinositide-binding domain By similarity

Sites

Binding site

145

1

ATP By similarity

Binding site

198

1

ATP By similarity

Binding site

205

1

ATP By similarity

Binding site

224

1

ATP By similarity

Binding site

259

1

Substrate By similarity

Binding site

273

1

Substrate By similarity

Binding site

275

1

ATP By similarity

Binding site

320

1

ATP By similarity

Amino acid modifications

Modified residue

1148

1

Phosphoserine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

A7Z050 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: DF692A0B30BB1EB4
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FASTA

1,477

163,665

        10         20         30         40         50         60 
MWSLPASEGE SATAHFFLGA GDEGLGTRGL GMRPEESDSE LLEDEEDEVP PEPQIIVGIC 

        70         80         90        100        110        120 
AMTKKSKSKP MTQILERLCR FDYLTVIILG EDVILNEPVE NWPSCHCLIS FHSKGFPLDK 

       130        140        150        160        170        180 
AVAYSKLRNP FLINDLAMQY YIQDRREVYR ILQEEGIDLP RYAVLNRDPA RPEECNLIEG 

       190        200        210        220        230        240 
EDQVEVNGAV FPKPFVEKPV SAEDHNVYIY YPSSAGGGSQ RLFRKIGSRS SVYSPESSVR 

       250        260        270        280        290        300 
KTGSYIYEEF MPTDGTDVKV YTVGPDYAHA EARKSPALDG KVERDSEGKE IRYPVMLTAM 

       310        320        330        340        350        360 
EKLVARKVCV AFKQTVCGFD LLRANGHSFV CDVNGFSFVK NSMKYYDDCA KILGNTIMRE 

       370        380        390        400        410        420 
LAPQFQIPWS IPMEAEDIPI VPTTSGTMME LRCVIAIIRH GDRTPKQKMK MEVTHPRFFS 

       430        440        450        460        470        480 
LFEKHGGYKT GKLKLKRPEQ LQEVLDITRL LLAELEKEPG GEIEEKTGKL EQLKSVLEMY 

       490        500        510        520        530        540 
GHFSGINRKV QLTYYPHGVK ASNEGQDTQR EALAPSLLLV LKWGGELTPA GRVQAEELGR 

       550        560        570        580        590        600 
AFRCMYPGGQ GDYAGFPGCG LLRLHSTFRH DLKIYASDEG RVQMTAAAFA KGLLALEGEL 

       610        620        630        640        650        660 
TPILVQMVKS ANMNGLLDSD GDSLSSCQHR VKARLHHILQ QDAPFGPEDY NQLAPTGSTS 

       670        680        690        700        710        720 
LLSSMAVIQN PVKVCDQVFD LIENLTHQIR ERMQDPKSVD LQLYHSETLE LMLQRWSKLE 

       730        740        750        760        770        780 
RDFRQKSGRY DISKIPDIYD CVKYDVQHNG SLGLQGTAEL LRLSKALADV VIPQEYGISR 

       790        800        810        820        830        840 
EEKLEIAVGF CLPLLRKILL DLQRTHEDES VNKLHPLYSR GVLSPGRHVR TRLYFTSESH 

       850        860        870        880        890        900 
VHSLLSVFRY GGLLDETKDT QWQRALAYLS AISELNYMTQ IVIMLYEDNT RDPLSEERFH 

       910        920        930        940        950        960 
VELHFSPGVK GVEEEGSAPT GCGFRPASSE NEERKADQGS VEDLCPGKAS DEPDRALQTS 

       970        980        990       1000       1010       1020 
PLPSEGPGLP KRSPLIRNRK AGSMEVLSET SSSRPGGHRL FSSSRPPTEM KQSGLGSQCT 

      1030       1040       1050       1060       1070       1080 
GLFSTTVLGG SSSAPNLQDY ARSQGKKLPP ASLKHRDELL FVPAVKRFSV SFAKHPTNGF 

      1090       1100       1110       1120       1130       1140 
EGCSMVPTIY PLETLHNALS LRQVSEFLSR VCQRHTEAQA QASAALFDSM HSNQASDSPF 

      1150       1160       1170       1180       1190       1200 
SPPRTLHSPT LQLQQRSEKP PWYSSGPSST VSSAGPSSPT AVDGNCPFGF SDQPSVSSHV 

      1210       1220       1230       1240       1250       1260 
TEEYQGLGLL QEAPGSGAQE PPLEGQQEPF EQNQSPQEPP VETKKPCQEV AEEVSQPCQD 

      1270       1280       1290       1300       1310       1320 
IPEEVNQPCQ QVSDICQPCE ENHDDVDQTC QEVPQISQPC EDASQLYQKV SKEVCELCQN 

      1330       1340       1350       1360       1370       1380 
SEEVNQPCQG VPVEIGRLVH GFPVGVGGLA QEVLGEVGRP TQEIPEELSQ SCQEFSVDIG 

      1390       1400       1410       1420       1430       1440 
RLAQEASAIN LLSPDTPEVD NPPLEFPGEG ALQAQEVSEW VKQQQSYVVP ELIDQLSREE 

      1450       1460       1470 
VPQVQCPPSN ANPQSQSLAP DQNAPLPPAT CDSSFSH

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References

[1]	NIH - Mammalian Gene Collection (MGC) project Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Brain cortex.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC153248 mRNA. Translation: AAI53249.1.
IPI	IPI00868635.
RefSeq	NP_001098824.1. NM_001105354.1.
UniGene	Bt.27184.
3D structure databases
ProteinModelPortal	A7Z050.
ModBase	Search...
Protein-protein interaction databases
STRING	9913.ENSBTAP00000018635.
Proteomic databases
PRIDE	A7Z050.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSBTAT00000018635; ENSBTAP00000018635; ENSBTAG00000014005.
GeneID	510684.
KEGG	bta:510684.
Organism-specific databases
CTD	9677.
Phylogenomic databases
eggNOG	NOG245915.
GeneTree	ENSGT00390000009048.
HOGENOM	HOG000177917.
HOVERGEN	HBG108657.
InParanoid	A7Z050.
KO	K13024.
OMA	DSMHSNQ.
OrthoDB	EOG41VK25.
Family and domain databases
InterPro	IPR000560. His_Pase_superF_clade-2. [Graphical view]
Pfam	PF00328. His_Phos_2. 1 hit. [Graphical view]
PROSITE	PS00616. HIS_ACID_PHOSPHAT_1. 1 hit. PS00778. HIS_ACID_PHOSPHAT_2. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	20869569.

Entry information

Entry name

VIP1_BOVIN

Accession

Primary (citable) accession number: A7Z050

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	October 23, 2007
Last modified:	May 1, 2013
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents