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Q6ZQB6

- VIP2_MOUSE

UniProt

Q6ZQB6 - VIP2_MOUSE

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Protein

Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2

Gene

Ppip5k2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein 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-InsP4.1 Publication

Catalytic activityi

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

Kineticsi

  1. KM=0.23 µM for InsP61 Publication
  2. KM=0.54 µM for InsP71 Publication

Vmax=1.70 nmol/min/mg enzyme with InsP6 as substrate1 Publication

Vmax=5.23 nmol/min/mg enzyme with InsP7 as substrate1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei140 – 1401ATPBy similarity
Binding sitei193 – 1931ATPBy similarity
Binding sitei200 – 2001ATPBy similarity
Binding sitei219 – 2191ATPBy similarity
Binding sitei254 – 2541SubstrateBy similarity
Binding sitei268 – 2681SubstrateBy similarity
Binding sitei270 – 2701ATPBy similarity
Binding sitei315 – 3151ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi243 – 2464ATPBy similarity
Nucleotide bindingi252 – 2543ATPBy similarity
Nucleotide bindingi327 – 3293ATPBy 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

Enzyme and pathway databases

ReactomeiREACT_196482. Synthesis of pyrophosphates in the cytosol.

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
Short name:
mmVIP2
Gene namesi
Name:Ppip5k2
Synonyms:Hisppd1, Kiaa0433, Vip2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 1

Organism-specific databases

MGIiMGI:2142810. 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 – 11291129Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2PRO_0000315693Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441PhosphoserineBy similarity
Modified residuei1058 – 10581PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ6ZQB6.
PaxDbiQ6ZQB6.
PRIDEiQ6ZQB6.

PTM databases

PhosphoSiteiQ6ZQB6.

Expressioni

Gene expression databases

BgeeiQ6ZQB6.
CleanExiMM_HISPPD1.
ExpressionAtlasiQ6ZQB6. baseline and differential.
GenevestigatoriQ6ZQB6.

Structurei

3D structure databases

ProteinModelPortaliQ6ZQB6.
SMRiQ6ZQB6. Positions 48-366.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni59 – 602Substrate bindingBy similarity
Regioni219 – 2202Substrate bindingBy similarity
Regioni332 – 3354Substrate bindingBy similarity
Regioni377 – 44872Polyphosphoinositide-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

eggNOGiNOG245915.
GeneTreeiENSGT00390000009048.
HOGENOMiHOG000177917.
HOVERGENiHBG108657.
InParanoidiQ6ZQB6.
KOiK13024.
OrthoDBiEOG77M8MT.

Family and domain databases

Gene3Di3.40.50.1240. 4 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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q6ZQB6-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSNSRKMSEP PRFFVGPEDA EINPGNYRRF FHHAEEEEEE EDESPPERQI
60 70 80 90 100
VVGICSMAKK SKSKPMKEIL ERISLFKYIT VVVFEEEIIL NEPVENWPLC
110 120 130 140 150
DCLISFHSKG FPLDKAVAYA KLRNPFVIND LNMQYLIQDR RDVYSILQAE
160 170 180 190 200
GILLPRYAIL NRDPNNPKEC NLIEGEDHVE VNGEVFQKPF VEKPVSAEDH
210 220 230 240 250
NVYIYYPTSA GGGSQRLFRK IGSRSSVYSP ESNVRKTGSY IYEEFMPTDG
260 270 280 290 300
TDVKVYTVGP DYAHAEARKS PALDGKVERD SEGKEVRYPV ILNAREKLIA
310 320 330 340 350
WKVCLAFKQT VCGFDLLRAN GQSYVCDVNG FSFVKNSMKY YDDCAKILGN
360 370 380 390 400
IVMRELAPQF HIPWSIPLEA EDIPIVPTTS GTMMELRCVI AVIRHGDRTP
410 420 430 440 450
KQKMKMEVRH QKFFDLFEKC DGYKSGKLKL KKPKQLQEVL DIARQLLMEL
460 470 480 490 500
GQNNDSEIEE NKSKLEQLKT VLEMYGHFSG INRKVQLTYL PHGCPKTSSE
510 520 530 540 550
EEDNRREEPS LLLVLKWGGE LTPAGRVQAE ELGRAFRCMY PGGQGDYAGF
560 570 580 590 600
PGCGLLRLHS TYRHDLKIYA SDEGRVQMTA AAFAKGLLAL EGELTPILVQ
610 620 630 640 650
MVKSANMNGL LDSDSDSLSS CQQRVKARLH EILQKDRDFT AEDYEKLTPS
660 670 680 690 700
GSISVIKSMH LIKNPVKTCD KVYSLIQSLT SQIRYRMEDP KSADIQLYHS
710 720 730 740 750
ETLELMLRRW SKLEKDFKTK NGRYDISKIP DIYDCIKYDV QHNGSLKLEN
760 770 780 790 800
TMELYRLSKA LADIVIPQEY GITKAEKLEI AKGYCTPLVR KIRSDLQRTQ
810 820 830 840 850
DDDTVNKLHP VYSRGVLSPE RHVRTRLYFT SESHVHSLLS ILRYGALCDD
860 870 880 890 900
SKDEQWKRAM DYLNVVNELN YMTQIVIMLY EDPNKDLSSE ERFHVELHFS
910 920 930 940 950
PGAKGCEEDK NLPSGYGYRP ASRENEGRRS LKTDDDEPHT SKRDEVDRAV
960 970 980 990 1000
MLFKPLVSEP IHIHRKSPLP RSRKITANEV VSENANYLRT PRNLVEQKQN
1010 1020 1030 1040 1050
PTVGFELYSM VPSICPLETL HNALFLKQVD DFLASIASPS TEVLRKVPEM
1060 1070 1080 1090 1100
SSMATRSSPG MRRKISLNTY TPTKILPTPP AALKSSKASS KAAAGGPSQA
1110 1120
MAPHTSSRKK SINSKTEGHE PKKSTGKKR
Length:1,129
Mass (Da):128,427
Last modified:July 27, 2011 - v3
Checksum:iA563826CC0085E3C
GO
Isoform 2 (identifier: Q6ZQB6-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:1,058
Mass (Da):121,181
Checksum:iEAD1A1398DB250E7
GO
Isoform 3 (identifier: Q6ZQB6-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,123
Mass (Da):127,723
Checksum:i7B7941A5E5AB948F
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti197 – 1971A → V in BAE38567. (PubMed:14621295)Curated
Sequence conflicti582 – 5821A → T in AAH53396. (PubMed:15489334)Curated
Sequence conflicti729 – 7291I → V in AAH53396. (PubMed:15489334)Curated
Sequence conflicti1035 – 10351S → P in AAH53396. (PubMed:15489334)Curated
Sequence conflicti1109 – 11091K → M in BAC97950. (PubMed:14621295)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 66Missing in isoform 3. 1 PublicationVSP_041618
Alternative sequencei545 – 5451Missing in isoform 2. 1 PublicationVSP_030637
Alternative sequencei1051 – 112979SSMAT…TGKKR → CMEFTFIVT in isoform 2. 1 PublicationVSP_030638Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS35678.1. [Q6ZQB6-1]
RefSeqiNP_776121.4. NM_173760.5. [Q6ZQB6-1]
UniGeneiMm.220817.
Mm.417682.

Genome annotation databases

EnsembliENSMUST00000042509; ENSMUSP00000043401; ENSMUSG00000040648. [Q6ZQB6-3]
ENSMUST00000171129; ENSMUSP00000132889; ENSMUSG00000040648. [Q6ZQB6-3]
GeneIDi227399.
KEGGimmu:227399.
UCSCiuc007cfk.2. mouse. [Q6ZQB6-1]
uc007cfl.1. mouse. [Q6ZQB6-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS35678.1. [Q6ZQB6-1 ]
RefSeqi NP_776121.4. NM_173760.5. [Q6ZQB6-1 ]
UniGenei Mm.220817.
Mm.417682.

3D structure databases

ProteinModelPortali Q6ZQB6.
SMRi Q6ZQB6. Positions 48-366.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q6ZQB6.

Proteomic databases

MaxQBi Q6ZQB6.
PaxDbi Q6ZQB6.
PRIDEi Q6ZQB6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000042509 ; ENSMUSP00000043401 ; ENSMUSG00000040648 . [Q6ZQB6-3 ]
ENSMUST00000171129 ; ENSMUSP00000132889 ; ENSMUSG00000040648 . [Q6ZQB6-3 ]
GeneIDi 227399.
KEGGi mmu:227399.
UCSCi uc007cfk.2. mouse. [Q6ZQB6-1 ]
uc007cfl.1. mouse. [Q6ZQB6-2 ]

Organism-specific databases

CTDi 23262.
MGIi MGI:2142810. Ppip5k2.
Rougei Search...

Phylogenomic databases

eggNOGi NOG245915.
GeneTreei ENSGT00390000009048.
HOGENOMi HOG000177917.
HOVERGENi HBG108657.
InParanoidi Q6ZQB6.
KOi K13024.
OrthoDBi EOG77M8MT.

Enzyme and pathway databases

Reactomei REACT_196482. Synthesis of pyrophosphates in the cytosol.

Miscellaneous databases

NextBioi 378596.
PROi Q6ZQB6.
SOURCEi Search...

Gene expression databases

Bgeei Q6ZQB6.
CleanExi MM_HISPPD1.
ExpressionAtlasi Q6ZQB6. baseline and differential.
Genevestigatori Q6ZQB6.

Family and domain databases

Gene3Di 3.40.50.1240. 4 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

« Hide 'large scale' publications
  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.
    , 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. 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].

Entry informationi

Entry nameiVIP2_MOUSE
AccessioniPrimary (citable) accession number: Q6ZQB6
Secondary accession number(s): E9PVE9
, Q3TM75, Q3UUA3, Q7TPU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 77 of the entry and version 3 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3