Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

O43314

- VIP2_HUMAN

UniProt

O43314 - VIP2_HUMAN

Protein

Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2

Gene

PPIP5K2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 3 (15 Jan 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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-InsP4.2 Publications

    Catalytic activityi

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

    Kineticsi

    1. KM=0.13 µM for InsP61 Publication
    2. KM=0.19 µM for InsP71 Publication

    Vmax=0.39 nmol/min/mg enzyme with InsP6 as substrate1 Publication

    Vmax=1.38 nmol/min/mg enzyme with InsP7 as substrate1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei134 – 1341ATP
    Binding sitei187 – 1871ATP
    Binding sitei194 – 1941ATP
    Binding sitei213 – 2131ATP
    Binding sitei248 – 2481Substrate
    Binding sitei262 – 2621Substrate
    Binding sitei264 – 2641ATP
    Binding sitei309 – 3091ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi237 – 2404ATP
    Nucleotide bindingi246 – 2483ATP
    Nucleotide bindingi321 – 3233ATP

    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
    2. inositol phosphate metabolic process Source: Reactome
    3. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_150188. 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:
    hsVIP2
    Gene namesi
    Name:PPIP5K2
    Synonyms:HISPPD1, KIAA0433, VIP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:29035. PPIP5K2.

    Subcellular locationi

    Cytoplasmcytosol 1 Publication

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi213 – 2131R → A or K: Reduces enzyme activity by about 99%. 1 Publication
    Mutagenesisi248 – 2481K → A: Loss of enzyme activity. 1 Publication
    Mutagenesisi262 – 2621R → A: Reduces enzyme activity by about 99%. 1 Publication

    Organism-specific databases

    PharmGKBiPA165660454.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12431243Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2PRO_0000315692Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei38 – 381Phosphoserine1 Publication
    Modified residuei1006 – 10061Phosphoserine1 Publication
    Modified residuei1016 – 10161Phosphoserine1 Publication
    Modified residuei1172 – 11721Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO43314.
    PaxDbiO43314.
    PRIDEiO43314.

    PTM databases

    PhosphoSiteiO43314.

    Expressioni

    Gene expression databases

    ArrayExpressiO43314.
    BgeeiO43314.
    CleanExiHS_HISPPD1.
    GenevestigatoriO43314.

    Organism-specific databases

    HPAiHPA038442.

    Interactioni

    Protein-protein interaction databases

    BioGridi116864. 8 interactions.
    IntActiO43314. 1 interaction.

    Structurei

    Secondary structure

    1
    1243
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi44 – 507
    Helixi52 – 554
    Helixi58 – 6710
    Beta strandi73 – 775
    Helixi80 – 856
    Helixi88 – 903
    Beta strandi95 – 995
    Helixi107 – 11711
    Beta strandi120 – 1234
    Helixi127 – 1315
    Helixi134 – 14310
    Beta strandi151 – 1544
    Beta strandi158 – 1603
    Helixi161 – 1633
    Beta strandi164 – 1685
    Beta strandi170 – 1756
    Beta strandi178 – 19013
    Beta strandi197 – 1993
    Helixi202 – 2043
    Beta strandi208 – 2158
    Beta strandi218 – 2247
    Beta strandi230 – 2323
    Beta strandi234 – 2385
    Beta strandi243 – 25311
    Beta strandi257 – 2637
    Beta strandi265 – 2673
    Beta strandi275 – 2795
    Helixi288 – 30013
    Beta strandi303 – 31311
    Beta strandi316 – 32510
    Helixi332 – 35423

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3T54X-ray1.90A37-366[»]
    3T7AX-ray1.70A41-366[»]
    3T99X-ray2.10A37-366[»]
    3T9AX-ray1.80A41-366[»]
    3T9BX-ray1.85A41-366[»]
    3T9CX-ray1.90A41-366[»]
    3T9DX-ray1.85A41-366[»]
    3T9EX-ray1.90A41-366[»]
    3T9FX-ray2.00A41-366[»]
    4HN2X-ray1.90A41-366[»]
    4NZMX-ray2.00A41-366[»]
    4NZNX-ray1.75A41-366[»]
    4NZOX-ray1.90A41-366[»]
    ProteinModelPortaliO43314.
    SMRiO43314. Positions 42-360.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni53 – 542Substrate binding
    Regioni213 – 2142Substrate binding
    Regioni326 – 3294Substrate binding
    Regioni371 – 44272Polyphosphoinositide-binding domainAdd
    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.

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG245915.
    HOGENOMiHOG000177917.
    HOVERGENiHBG108657.
    InParanoidiO43314.
    KOiK13024.
    OMAiYPINILA.
    PhylomeDBiO43314.
    TreeFamiTF313594.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O43314-1) [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

    MSEAPRFFVG PEDTEINPGN YRHFFHHADE DDEEEDDSPP ERQIVVGICS     50
    MAKKSKSKPM KEILERISLF KYITVVVFEE EVILNEPVEN WPLCDCLISF 100
    HSKGFPLDKA VAYAKLRNPF VINDLNMQYL IQDRREVYSI LQAEGILLPR 150
    YAILNRDPNN PKECNLIEGE DHVEVNGEVF QKPFVEKPVS AEDHNVYIYY 200
    PTSAGGGSQR LFRKIGSRSS VYSPESNVRK TGSYIYEEFM PTDGTDVKVY 250
    TVGPDYAHAE ARKSPALDGK VERDSEGKEV RYPVILNARE KLIAWKVCLA 300
    FKQTVCGFDL LRANGQSYVC DVNGFSFVKN SMKYYDDCAK ILGNIVMREL 350
    APQFHIPWSI PLEAEDIPIV PTTSGTMMEL RCVIAVIRHG DRTPKQKMKM 400
    EVRHQKFFDL FEKCDGYKSG KLKLKKPKQL QEVLDIARQL LMELGQNNDS 450
    EIEENKPKLE QLKTVLEMYG HFSGINRKVQ LTYLPHGCPK TSSEEEDSRR 500
    EEPSLLLVLK WGGELTPAGR VQAEELGRAF RCMYPGGQGD YAGFPGCGLL 550
    RLHSTYRHDL KIYASDEGRV QMTAAAFAKG LLALEGELTP ILVQMVKSAN 600
    MNGLLDSDSD SLSSCQQRVK ARLHEILQKD RDFTAEDYEK LTPSGSISLI 650
    KSMHLIKNPV KTCDKVYSLI QSLTSQIRHR MEDPKSSDIQ LYHSETLELM 700
    LRRWSKLEKD FKTKNGRYDI SKIPDIYDCI KYDVQHNGSL KLENTMELYR 750
    LSKALADIVI PQEYGITKAE KLEIAKGYCT PLVRKIRSDL QRTQDDDTVN 800
    KLHPVYSRGV LSPERHVRTR LYFTSESHVH SLLSILRYGA LCNESKDEQW 850
    KRAMDYLNVV NELNYMTQIV IMLYEDPNKD LSSEERFHVE LHFSPGAKGC 900
    EEDKNLPSGY GYRPASRENE GRRPFKIDND DEPHTSKRDE VDRAVILFKP 950
    MVSEPIHIHR KSPLPRSRKT ATNDEESPLS VSSPEGTGTW LHYTSGVGTG 1000
    RRRRRSGEQI TSSPVSPKSL AFTSSIFGSW QQVVSENANY LRTPRTLVEQ 1050
    KQNPTVGSHC AGLFSTSVLG GSSSAPNLQD YARTHRKKLT SSGCIDDATR 1100
    GSAVKRFSIS FARHPTNGFE LYSMVPSICP LETLHNALSL KQVDEFLASI 1150
    ASPSSDVPRK TAEISSTALR SSPIMRKKVS LNTYTPAKIL PTPPATLKST 1200
    KASSKPATSG PSSAVVPNTS SRKKNITSKT ETHEHKKNTG KKK 1243
    Length:1,243
    Mass (Da):140,407
    Last modified:January 15, 2008 - v3
    Checksum:iA8831DDDAB9B2E6E
    GO
    Isoform 2 (identifier: O43314-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1097-1117: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,222
    Mass (Da):138,106
    Checksum:iC61F832FE77F87F3
    GO

    Sequence cautioni

    The sequence BAA24863.2 differs from that shown. Reason: Erroneous initiation.
    The sequence EAW49076.1 differs from that shown. Reason: Erroneous gene model prediction.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti944 – 9441A → G.
    Corresponds to variant rs17155115 [ dbSNP | Ensembl ].
    VAR_038276
    Natural varianti985 – 9851E → K.
    Corresponds to variant rs12519525 [ dbSNP | Ensembl ].
    VAR_038277
    Natural varianti1003 – 10031R → K.
    Corresponds to variant rs12520040 [ dbSNP | Ensembl ].
    VAR_038278
    Natural varianti1206 – 12061P → Q.
    Corresponds to variant rs17155138 [ dbSNP | Ensembl ].
    VAR_038279
    Natural varianti1232 – 12321T → M.
    Corresponds to variant rs17155147 [ dbSNP | Ensembl ].
    VAR_038280

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1097 – 111721Missing in isoform 2. 1 PublicationVSP_030636Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB007893 mRNA. Translation: BAA24863.2. Different initiation.
    AC011362 Genomic DNA. No translation available.
    CH471086 Genomic DNA. Translation: EAW49076.1. Sequence problems.
    BC024591 mRNA. Translation: AAH24591.1.
    CCDSiCCDS34207.1. [O43314-2]
    CCDS64212.1. [O43314-1]
    RefSeqiNP_001263206.1. NM_001276277.1. [O43314-1]
    NP_001268400.1. NM_001281471.1.
    NP_056031.2. NM_015216.3. [O43314-2]
    XP_005271992.1. XM_005271935.1. [O43314-2]
    UniGeneiHs.212046.

    Genome annotation databases

    EnsembliENST00000321521; ENSP00000313070; ENSG00000145725. [O43314-2]
    ENST00000358359; ENSP00000351126; ENSG00000145725. [O43314-1]
    ENST00000414217; ENSP00000416016; ENSG00000145725. [O43314-2]
    GeneIDi23262.
    KEGGihsa:23262.
    UCSCiuc003kod.5. human. [O43314-1]
    uc003koe.4. human. [O43314-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB007893 mRNA. Translation: BAA24863.2 . Different initiation.
    AC011362 Genomic DNA. No translation available.
    CH471086 Genomic DNA. Translation: EAW49076.1 . Sequence problems.
    BC024591 mRNA. Translation: AAH24591.1 .
    CCDSi CCDS34207.1. [O43314-2 ]
    CCDS64212.1. [O43314-1 ]
    RefSeqi NP_001263206.1. NM_001276277.1. [O43314-1 ]
    NP_001268400.1. NM_001281471.1.
    NP_056031.2. NM_015216.3. [O43314-2 ]
    XP_005271992.1. XM_005271935.1. [O43314-2 ]
    UniGenei Hs.212046.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3T54 X-ray 1.90 A 37-366 [» ]
    3T7A X-ray 1.70 A 41-366 [» ]
    3T99 X-ray 2.10 A 37-366 [» ]
    3T9A X-ray 1.80 A 41-366 [» ]
    3T9B X-ray 1.85 A 41-366 [» ]
    3T9C X-ray 1.90 A 41-366 [» ]
    3T9D X-ray 1.85 A 41-366 [» ]
    3T9E X-ray 1.90 A 41-366 [» ]
    3T9F X-ray 2.00 A 41-366 [» ]
    4HN2 X-ray 1.90 A 41-366 [» ]
    4NZM X-ray 2.00 A 41-366 [» ]
    4NZN X-ray 1.75 A 41-366 [» ]
    4NZO X-ray 1.90 A 41-366 [» ]
    ProteinModelPortali O43314.
    SMRi O43314. Positions 42-360.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116864. 8 interactions.
    IntActi O43314. 1 interaction.

    PTM databases

    PhosphoSitei O43314.

    Proteomic databases

    MaxQBi O43314.
    PaxDbi O43314.
    PRIDEi O43314.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000321521 ; ENSP00000313070 ; ENSG00000145725 . [O43314-2 ]
    ENST00000358359 ; ENSP00000351126 ; ENSG00000145725 . [O43314-1 ]
    ENST00000414217 ; ENSP00000416016 ; ENSG00000145725 . [O43314-2 ]
    GeneIDi 23262.
    KEGGi hsa:23262.
    UCSCi uc003kod.5. human. [O43314-1 ]
    uc003koe.4. human. [O43314-2 ]

    Organism-specific databases

    CTDi 23262.
    GeneCardsi GC05P102455.
    H-InvDB HIX0005068.
    HIX0029534.
    HGNCi HGNC:29035. PPIP5K2.
    HPAi HPA038442.
    MIMi 611648. gene.
    neXtProti NX_O43314.
    PharmGKBi PA165660454.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG245915.
    HOGENOMi HOG000177917.
    HOVERGENi HBG108657.
    InParanoidi O43314.
    KOi K13024.
    OMAi YPINILA.
    PhylomeDBi O43314.
    TreeFami TF313594.

    Enzyme and pathway databases

    Reactomei REACT_150188. Synthesis of pyrophosphates in the cytosol.

    Miscellaneous databases

    GenomeRNAii 23262.
    NextBioi 45000.
    PROi O43314.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43314.
    Bgeei O43314.
    CleanExi HS_HISPPD1.
    Genevestigatori O43314.

    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. "Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro."
      Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 4:307-313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    3. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 2).
      Tissue: Uterus.
    6. "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, SUBCELLULAR LOCATION.
    7. "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: FUNCTION, ENZYME ACTIVITY.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1006; SER-1016 AND SER-1172, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Receptor-dependent compartmentalization of PPIP5K1, a kinase with a cryptic polyphosphoinositide binding domain."
      Gokhale N.A., Zaremba A., Shears S.B.
      Biochem. J. 434:415-426(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, POLYPHOSPHOINOSITIDE-BINDING DOMAIN.
    12. "Structural basis for an inositol pyrophosphate kinase surmounting phosphate crowding."
      Wang H., Falck J.R., Hall T.M., Shears S.B.
      Nat. Chem. Biol. 8:111-116(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 41-366 IN COMPLEXES WITH ATP; SUBSTRATE AND TRANSITION STATE ANALOG, MUTAGENESIS OF ARG-213; LYS-248 AND ARG-262.

    Entry informationi

    Entry nameiVIP2_HUMAN
    AccessioniPrimary (citable) accession number: O43314
    Secondary accession number(s): A1NI53, A6NGS8, Q8TB50
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    This is version 104 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3