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Q6ZQB6 (VIP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Short name=mmVIP2
Gene names
Name:Ppip5k2
Synonyms:Hisppd1, Kiaa0433, Vip2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1129 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. Ref.5

Catalytic activity

ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate. Ref.5

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. Ref.5

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. Ref.5

ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate.

Subcellular location

Cytoplasmcytosol 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.

Biophysicochemical properties

Kinetic parameters:

KM=0.23 µM for InsP6 Ref.5

KM=0.54 µM for InsP7

Vmax=1.70 nmol/min/mg enzyme with InsP6 as substrate

Vmax=5.23 nmol/min/mg enzyme with InsP7 as substrate

Sequence caution

The sequence BAC97950.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6ZQB6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q6ZQB6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     545-545: Missing.
     1051-1129: SSMATRSSPG...EPKKSTGKKR → CMEFTFIVT
Note: No experimental confirmation available.
Isoform 3 (identifier: Q6ZQB6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11291129Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2
PRO_0000315693

Regions

Nucleotide binding243 – 2464ATP By similarity
Nucleotide binding252 – 2543ATP By similarity
Nucleotide binding327 – 3293ATP By similarity
Region59 – 602Substrate binding By similarity
Region219 – 2202Substrate binding By similarity
Region332 – 3354Substrate binding By similarity
Region377 – 44872Polyphosphoinositide-binding domain By similarity

Sites

Binding site1401ATP By similarity
Binding site1931ATP By similarity
Binding site2001ATP By similarity
Binding site2191ATP By similarity
Binding site2541Substrate By similarity
Binding site2681Substrate By similarity
Binding site2701ATP By similarity
Binding site3151ATP By similarity

Amino acid modifications

Modified residue441Phosphoserine By similarity
Modified residue10581Phosphoserine By similarity

Natural variations

Alternative sequence1 – 66Missing in isoform 3.
VSP_041618
Alternative sequence5451Missing in isoform 2.
VSP_030637
Alternative sequence1051 – 112979SSMAT…TGKKR → CMEFTFIVT in isoform 2.
VSP_030638

Experimental info

Sequence conflict1971A → V in BAE38567. Ref.1
Sequence conflict5821A → T in AAH53396. Ref.4
Sequence conflict7291I → V in AAH53396. Ref.4
Sequence conflict10351S → P in AAH53396. Ref.4
Sequence conflict11091K → M in BAC97950. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: A563826CC0085E3C

FASTA1,129128,427
        10         20         30         40         50         60 
MSNSRKMSEP PRFFVGPEDA EINPGNYRRF FHHAEEEEEE EDESPPERQI VVGICSMAKK 

        70         80         90        100        110        120 
SKSKPMKEIL ERISLFKYIT VVVFEEEIIL NEPVENWPLC DCLISFHSKG FPLDKAVAYA 

       130        140        150        160        170        180 
KLRNPFVIND LNMQYLIQDR RDVYSILQAE GILLPRYAIL NRDPNNPKEC NLIEGEDHVE 

       190        200        210        220        230        240 
VNGEVFQKPF VEKPVSAEDH NVYIYYPTSA GGGSQRLFRK IGSRSSVYSP ESNVRKTGSY 

       250        260        270        280        290        300 
IYEEFMPTDG TDVKVYTVGP DYAHAEARKS PALDGKVERD SEGKEVRYPV ILNAREKLIA 

       310        320        330        340        350        360 
WKVCLAFKQT VCGFDLLRAN GQSYVCDVNG FSFVKNSMKY YDDCAKILGN IVMRELAPQF 

       370        380        390        400        410        420 
HIPWSIPLEA EDIPIVPTTS GTMMELRCVI AVIRHGDRTP KQKMKMEVRH QKFFDLFEKC 

       430        440        450        460        470        480 
DGYKSGKLKL KKPKQLQEVL DIARQLLMEL GQNNDSEIEE NKSKLEQLKT VLEMYGHFSG 

       490        500        510        520        530        540 
INRKVQLTYL PHGCPKTSSE EEDNRREEPS LLLVLKWGGE LTPAGRVQAE ELGRAFRCMY 

       550        560        570        580        590        600 
PGGQGDYAGF PGCGLLRLHS TYRHDLKIYA SDEGRVQMTA AAFAKGLLAL EGELTPILVQ 

       610        620        630        640        650        660 
MVKSANMNGL LDSDSDSLSS CQQRVKARLH EILQKDRDFT AEDYEKLTPS GSISVIKSMH 

       670        680        690        700        710        720 
LIKNPVKTCD KVYSLIQSLT SQIRYRMEDP KSADIQLYHS ETLELMLRRW SKLEKDFKTK 

       730        740        750        760        770        780 
NGRYDISKIP DIYDCIKYDV QHNGSLKLEN TMELYRLSKA LADIVIPQEY GITKAEKLEI 

       790        800        810        820        830        840 
AKGYCTPLVR KIRSDLQRTQ DDDTVNKLHP VYSRGVLSPE RHVRTRLYFT SESHVHSLLS 

       850        860        870        880        890        900 
ILRYGALCDD SKDEQWKRAM DYLNVVNELN YMTQIVIMLY EDPNKDLSSE ERFHVELHFS 

       910        920        930        940        950        960 
PGAKGCEEDK NLPSGYGYRP ASRENEGRRS LKTDDDEPHT SKRDEVDRAV MLFKPLVSEP 

       970        980        990       1000       1010       1020 
IHIHRKSPLP RSRKITANEV VSENANYLRT PRNLVEQKQN PTVGFELYSM VPSICPLETL 

      1030       1040       1050       1060       1070       1080 
HNALFLKQVD DFLASIASPS TEVLRKVPEM SSMATRSSPG MRRKISLNTY TPTKILPTPP 

      1090       1100       1110       1120 
AALKSSKASS KAAAGGPSQA MAPHTSSRKK SINSKTEGHE PKKSTGKKR 

« Hide

Isoform 2 [UniParc].

Checksum: EAD1A1398DB250E7
Show »

FASTA1,058121,181
Isoform 3 [UniParc].

Checksum: 7B7941A5E5AB948F
Show »

FASTA1,123127,723

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Embryonic tail.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Lung and Spinal cord.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Strain: C57BL/6J.
Tissue: Egg.
[5]"Cloning and characterization of two human VIP1-like inositol hexakisphosphate and diphosphoinositol pentakisphosphate kinases."
Fridy P.C., Otto J.C., Dollins D.E., York J.D.
J. Biol. Chem. 282:30754-30762(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[6]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK129140 mRNA. Translation: BAC97950.1. Different initiation.
AK138622 mRNA. Translation: BAE23724.1.
AK166095 mRNA. Translation: BAE38567.1.
AC099860 Genomic DNA. No translation available.
AC162298 Genomic DNA. No translation available.
BC053396 mRNA. Translation: AAH53396.1.
CCDSCCDS35678.1. [Q6ZQB6-1]
RefSeqNP_776121.4. NM_173760.5. [Q6ZQB6-1]
UniGeneMm.220817.
Mm.417682.

3D structure databases

ProteinModelPortalQ6ZQB6.
SMRQ6ZQB6. Positions 48-366.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ6ZQB6.

Proteomic databases

MaxQBQ6ZQB6.
PaxDbQ6ZQB6.
PRIDEQ6ZQB6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000042509; ENSMUSP00000043401; ENSMUSG00000040648. [Q6ZQB6-3]
ENSMUST00000171129; ENSMUSP00000132889; ENSMUSG00000040648. [Q6ZQB6-3]
GeneID227399.
KEGGmmu:227399.
UCSCuc007cfk.2. mouse. [Q6ZQB6-1]
uc007cfl.1. mouse. [Q6ZQB6-2]

Organism-specific databases

CTD23262.
MGIMGI:2142810. Ppip5k2.
RougeSearch...

Phylogenomic databases

eggNOGNOG245915.
GeneTreeENSGT00390000009048.
HOGENOMHOG000177917.
HOVERGENHBG108657.
KOK13024.
OrthoDBEOG77M8MT.

Gene expression databases

ArrayExpressQ6ZQB6.
BgeeQ6ZQB6.
CleanExMM_HISPPD1.
GenevestigatorQ6ZQB6.

Family and domain databases

Gene3D3.40.50.1240. 4 hits.
InterProIPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
[Graphical view]
PfamPF00328. His_Phos_2. 1 hit.
[Graphical view]
SUPFAMSSF53254. SSF53254. 3 hits.
PROSITEPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio378596.
PROQ6ZQB6.
SOURCESearch...

Entry information

Entry nameVIP2_MOUSE
AccessionPrimary (citable) accession number: Q6ZQB6
Secondary accession number(s): E9PVE9 expand/collapse secondary AC list , Q3TM75, Q3UUA3, Q7TPU4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 74 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot