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Q6ZQB6

- VIP2_MOUSE

UniProt

Q6ZQB6 - VIP2_MOUSE

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
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    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

    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

    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

    ArrayExpressiQ6ZQB6.
    BgeeiQ6ZQB6.
    CleanExiMM_HISPPD1.
    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.
    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

    MSNSRKMSEP PRFFVGPEDA EINPGNYRRF FHHAEEEEEE EDESPPERQI     50
    VVGICSMAKK SKSKPMKEIL ERISLFKYIT VVVFEEEIIL NEPVENWPLC 100
    DCLISFHSKG FPLDKAVAYA KLRNPFVIND LNMQYLIQDR RDVYSILQAE 150
    GILLPRYAIL NRDPNNPKEC NLIEGEDHVE VNGEVFQKPF VEKPVSAEDH 200
    NVYIYYPTSA GGGSQRLFRK IGSRSSVYSP ESNVRKTGSY IYEEFMPTDG 250
    TDVKVYTVGP DYAHAEARKS PALDGKVERD SEGKEVRYPV ILNAREKLIA 300
    WKVCLAFKQT VCGFDLLRAN GQSYVCDVNG FSFVKNSMKY YDDCAKILGN 350
    IVMRELAPQF HIPWSIPLEA EDIPIVPTTS GTMMELRCVI AVIRHGDRTP 400
    KQKMKMEVRH QKFFDLFEKC DGYKSGKLKL KKPKQLQEVL DIARQLLMEL 450
    GQNNDSEIEE NKSKLEQLKT VLEMYGHFSG INRKVQLTYL PHGCPKTSSE 500
    EEDNRREEPS LLLVLKWGGE LTPAGRVQAE ELGRAFRCMY PGGQGDYAGF 550
    PGCGLLRLHS TYRHDLKIYA SDEGRVQMTA AAFAKGLLAL EGELTPILVQ 600
    MVKSANMNGL LDSDSDSLSS CQQRVKARLH EILQKDRDFT AEDYEKLTPS 650
    GSISVIKSMH LIKNPVKTCD KVYSLIQSLT SQIRYRMEDP KSADIQLYHS 700
    ETLELMLRRW SKLEKDFKTK NGRYDISKIP DIYDCIKYDV QHNGSLKLEN 750
    TMELYRLSKA LADIVIPQEY GITKAEKLEI AKGYCTPLVR KIRSDLQRTQ 800
    DDDTVNKLHP VYSRGVLSPE RHVRTRLYFT SESHVHSLLS ILRYGALCDD 850
    SKDEQWKRAM DYLNVVNELN YMTQIVIMLY EDPNKDLSSE ERFHVELHFS 900
    PGAKGCEEDK NLPSGYGYRP ASRENEGRRS LKTDDDEPHT SKRDEVDRAV 950
    MLFKPLVSEP IHIHRKSPLP RSRKITANEV VSENANYLRT PRNLVEQKQN 1000
    PTVGFELYSM VPSICPLETL HNALFLKQVD DFLASIASPS TEVLRKVPEM 1050
    SSMATRSSPG MRRKISLNTY TPTKILPTPP AALKSSKASS KAAAGGPSQA 1100
    MAPHTSSRKK SINSKTEGHE PKKSTGKKR 1129
    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.
    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

    ArrayExpressi Q6ZQB6.
    Bgeei Q6ZQB6.
    CleanExi MM_HISPPD1.
    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

    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 1, 2014
    This is version 76 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