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P0C644

- VIP1_RAT

UniProt

P0C644 - VIP1_RAT

Protein

Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1

Gene

Ppip5k1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 52 (01 Oct 2014)
      Sequence version 1 (15 Jan 2008)
      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. Activated when cells are exposed to hyperosmotic stress By similarity.By similarity

    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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei147 – 1471ATPBy similarity
    Binding sitei200 – 2001ATPBy similarity
    Binding sitei207 – 2071ATPBy similarity
    Binding sitei226 – 2261ATPBy similarity
    Binding sitei261 – 2611SubstrateBy similarity
    Binding sitei275 – 2751SubstrateBy similarity
    Binding sitei277 – 2771ATPBy similarity
    Binding sitei322 – 3221ATPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi250 – 2534ATPBy similarity
    Nucleotide bindingi259 – 2613ATPBy similarity
    Nucleotide bindingi334 – 3363ATPBy 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_198653. Synthesis of pyrophosphates in the cytosol.

    Names & Taxonomyi

    Protein namesi
    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
    VIP1 homolog
    Gene namesi
    Name:Ppip5k1
    Synonyms:Hisppd2a, Vip1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi1311552. Ppip5k1.

    Subcellular locationi

    Cytoplasmcytosol By similarity. Cell membrane By similarity
    Note: Relocalizes to the plasma membrane upon activation of the PtdIns 3-kinase pathway.By similarity

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. nucleus Source: Ensembl
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14341434Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1PRO_0000315691Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1149 – 11491PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP0C644.
    PRIDEiP0C644.

    Expressioni

    Gene expression databases

    GenevestigatoriP0C644.

    Interactioni

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000059430.

    Structurei

    3D structure databases

    ProteinModelPortaliP0C644.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni66 – 672Substrate bindingBy similarity
    Regioni226 – 2272Substrate bindingBy similarity
    Regioni339 – 3424Substrate bindingBy similarity
    Regioni384 – 45572Polyphosphoinositide-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.
    HOGENOMiHOG000177917.
    HOVERGENiHBG108657.
    InParanoidiP0C644.
    PhylomeDBiP0C644.

    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.

    P0C644-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWSLTANEDE DESATAHFFL GAGDEGLGTC GIGMRTGESD SELLEDEEDE     50
    VPPEPQIIVG ICAMTKKSKS KPMTQILERL CRFDYLTVVI LGEDVILNEP 100
    VENWPPCHCL ISFHSKGFPL DKAVAYSKLR NPFLINDLTM QYYIQDRREV 150
    YRILQEEGID LPRYAVLNRD PACPEECNLI EGEDQVEVNG AVFPKPFVEK 200
    PVSAEDHNVY IYYPSSAGGG SQRLFRKIGS RSSVYSPESS VRKTGSYIYE 250
    EFMPTDGTDV KVYTVGPDYA HAEARKSPAL DGKVERDSEG KEVRYPVMLT 300
    AMEKLVARKV CVAFKQTVCG FDLLRANGHS FVCDVNGFSF VKNSMKYYDD 350
    CAKILGNTIM RELAPQFQIP WSIPTEAEDI PIVPTTSGTM MELRCVIAII 400
    RHGDRTPKQK MKMEVTHPRF FALFEKHGGY KTGKLKLKRP EQLQEVLDIT 450
    RLLLAELEKE PGAEIEEKTG KLEQLKSVLE MYGHFSGINR KVQLTYYPHG 500
    VKASSEGQDL QREPPAPSLL LVLKWGGELT PDGRVQAEEL GRAFRCMYPG 550
    GQGDYAGFPG CGLLRLHSTF RHDLKIYASD EGRVQMTAAA FAKGLLALEG 600
    ELTPILVQMV KSANMNGLLD SDSDSLSSCQ HRVKARLHHI LQQDAPFGPE 650
    DYDQLAPTGS TSLLNSMSVI QNPVKVCDQV FALIENLTHQ IRERMQDPSS 700
    VDLQLYHSET LELMLQRWSK LERDFRQKSG RYDISKIPDI YDCVKYDVQH 750
    NGSLGLQGTA ELLRLSKALA DVVIPQEYGI SREEKVEIAV GFCLPLLRKI 800
    LLDLQRTHED ESVNKLHPLY SRGVLSPGRH VRTRLYFTSE SHVHSLLSVF 850
    RYGGLLDETK DAQWQRALAY LSAISELNYM TQIVIMLYED NTRDPLSEER 900
    FHVELHFSPG VKGVEEGSAP AGCGFRPASS ENEEMKTDPG SIENLCPAKP 950
    SDEPDRALQT SPQPVEGTGL PRRSPLIRNR KAGSMEVLSE TSSSRPGGYR 1000
    LFSSSRPPTE MKQSGLGSQC TGLFSTTVLG GSSSAPNLQD YARTHGKKLP 1050
    PAGLKHRDEL LFVPAVKRFS VSFAKHPTNG FEGCSMVPTI YPLETLHNAL 1100
    SLRQVSEFLT KVCQRHTDAH AQASAALFDS MHNHQASDNP FSPPRTLHSP 1150
    PLQLRHRSEK PPWYSSGPSS TVSSAGPSSP TTVDGNSHFG FSDQSSVNTQ 1200
    MIEEKQGLGL LQETPGDGTP EFHIELAEST QSPQEPPVEI SPPGSQDDTE 1250
    VNQTCQEVPD TIQPCHDILE EIGQPNQEVP DISQLLLKNH DTATNTCQPC 1300
    QASQLSKKVY EEICQLCQDN PEESNQLCQE VSVELGRMVH RFPVSIGSTT 1350
    QETLMEIGRP TQEIPEEPCQ EFSEKVGMLT QKASAISELS QDILETDNPS 1400
    QELSEETDLQ AQEVSEEIDQ EPEVVDELSN EDIS 1434
    Length:1,434
    Mass (Da):159,619
    Last modified:January 15, 2008 - v1
    Checksum:iA3C2C9C28B4EAB47
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC116071 Genomic DNA. No translation available.
    UniGeneiRn.46305.

    Genome annotation databases

    UCSCiRGD:1311552. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC116071 Genomic DNA. No translation available.
    UniGenei Rn.46305.

    3D structure databases

    ProteinModelPortali P0C644.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000059430.

    Proteomic databases

    PaxDbi P0C644.
    PRIDEi P0C644.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    UCSCi RGD:1311552. rat.

    Organism-specific databases

    RGDi 1311552. Ppip5k1.

    Phylogenomic databases

    eggNOGi NOG245915.
    HOGENOMi HOG000177917.
    HOVERGENi HBG108657.
    InParanoidi P0C644.
    PhylomeDBi P0C644.

    Enzyme and pathway databases

    Reactomei REACT_198653. Synthesis of pyrophosphates in the cytosol.

    Miscellaneous databases

    PROi P0C644.

    Gene expression databases

    Genevestigatori P0C644.

    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. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
      Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
      , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
      Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Brown Norway.
    2. "Purification, sequencing, and molecular identification of a mammalian PP-InsP5 kinase that is activated when cells are exposed to hyperosmotic stress."
      Choi J.H., Williams J., Cho J., Falck J.R., Shears S.B.
      J. Biol. Chem. 282:30763-30775(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY.

    Entry informationi

    Entry nameiVIP1_RAT
    AccessioniPrimary (citable) accession number: P0C644
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    This is version 52 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