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Q6PFW1

- VIP1_HUMAN

UniProt

Q6PFW1 - VIP1_HUMAN

Protein

Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1

Gene

PPIP5K1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      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.3 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

    The catalytic efficiency is 80 folds higher for 5-PP-InsP5 (InsP7) compared to InsP6.

    1. KM=0.12 µM for InsP63 Publications
    2. KM=0.10 µM for InsP73 Publications

    Vmax=0.03 nmol/min/mg enzyme with InsP6 as substrate3 Publications

    Vmax=0.13 nmol/min/mg enzyme with InsP7 as substrate3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei145 – 1451ATPBy similarity
    Binding sitei198 – 1981ATPBy similarity
    Binding sitei205 – 2051ATPBy similarity
    Binding sitei224 – 2241ATPBy similarity
    Binding sitei259 – 2591SubstrateBy similarity
    Binding sitei273 – 2731SubstrateBy similarity
    Binding sitei275 – 2751ATPBy similarity
    Binding sitei320 – 3201ATPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi248 – 2514ATPBy similarity
    Nucleotide bindingi257 – 2593ATPBy similarity
    Nucleotide bindingi332 – 3343ATPBy 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
    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

    BioCyciMetaCyc:HS09822-MONOMER.
    ReactomeiREACT_150188. 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
    IP6 kinase
    Inositol pyrophosphate synthase 1
    InsP6 and PP-IP5 kinase 1
    VIP1 homolog
    Short name:
    hsVIP1
    Gene namesi
    Name:PPIP5K1
    Synonyms:HISPPD2A, IP6K, IPS1, KIAA0377, VIP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:29023. PPIP5K1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi399 – 3991R → A: Decreases 8-fold the affinity for PtdIns(3,4,5)P3. 1 Publication
    Mutagenesisi417 – 4171R → A: Decreases 16-fold the affinity for PtdIns(3,4,5)P3. 1 Publication

    Organism-specific databases

    PharmGKBiPA165479401.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14331433Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1PRO_0000315688Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1152 – 11521Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ6PFW1.
    PaxDbiQ6PFW1.
    PRIDEiQ6PFW1.

    PTM databases

    PhosphoSiteiQ6PFW1.

    Expressioni

    Tissue specificityi

    Widely expressed, with a higher expression in skeletal muscle, heart and brain.1 Publication

    Gene expression databases

    ArrayExpressiQ6PFW1.
    BgeeiQ6PFW1.
    GenevestigatoriQ6PFW1.

    Organism-specific databases

    HPAiHPA039380.

    Interactioni

    Protein-protein interaction databases

    BioGridi115031. 11 interactions.
    STRINGi9606.ENSP00000380129.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6PFW1.
    SMRiQ6PFW1. Positions 54-371.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni64 – 652Substrate bindingBy similarity
    Regioni224 – 2252Substrate bindingBy similarity
    Regioni337 – 3404Substrate bindingBy similarity
    Regioni382 – 45372Polyphosphoinositide-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 (PubMed:21222653).1 Publication

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG245915.
    HOVERGENiHBG108657.
    InParanoidiQ6PFW1.
    KOiK13024.
    OMAiEEVSQPC.
    PhylomeDBiQ6PFW1.
    TreeFamiTF313594.

    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 (7)i

    Sequence statusi: Complete.

    This entry describes 7 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q6PFW1-1) [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

    MWSLTASEGE STTAHFFLGA GDEGLGTRGI GMRPEESDSE LLEDEEDEVP     50
    PEPQIIVGIC AMTKKSKSKP MTQILERLCR FDYLTVVILG EDVILNEPVE 100
    NWPSCHCLIS FHSKGFPLDK AVAYSKLRNP FLINDLAMQY YIQDRREVYR 150
    ILQEEGIDLP RYAVLNRDPA RPEECNLIEG EDQVEVNGAV FPKPFVEKPV 200
    SAEDHNVYIY YPSSAGGGSQ RLFRKIGSRS SVYSPESSVR KTGSYIYEEF 250
    MPTDGTDVKV YTVGPDYAHA EARKSPALDG KVERDSEGKE IRYPVMLTAM 300
    EKLVARKVCV AFKQTVCGFD LLRANGHSFV CDVNGFSFVK NSMKYYDDCA 350
    KILGNTIMRE LAPQFQIPWS IPTEAEDIPI VPTTSGTMME LRCVIAIIRH 400
    GDRTPKQKMK MEVKHPRFFA LFEKHGGYKT GKLKLKRPEQ LQEVLDITRL 450
    LLAELEKEPG GEIEEKTGKL EQLKSVLEMY GHFSGINRKV QLTYYPHGVK 500
    ASNEGQDPQR ETLAPSLLLV LKWGGELTPA GRVQAEELGR AFRCMYPGGQ 550
    GDYAGFPGCG LLRLHSTFRH DLKIYASDEG RVQMTAAAFA KGLLALEGEL 600
    TPILVQMVKS ANMNGLLDSD GDSLSSCQHR VKARLHHILQ QDAPFGPEDY 650
    DQLAPTRSTS LLNSMTIIQN PVKVCDQVFA LIENLTHQIR ERMQDPRSVD 700
    LQLYHSETLE LMLQRWSKLE RDFRQKSGRY DISKIPDIYD CVKYDVQHNG 750
    SLGLQGTAEL LRLSKALADV VIPQEYGISR EEKLEIAVGF CLPLLRKILL 800
    DLQRTHEDES VNKLHPLCYL RYSRGVLSPG RHVRTRLYFT SESHVHSLLS 850
    VFRYGGLLDE TQDAQWQRAL DYLSAISELN YMTQIVIMLY EDNTQDPLSE 900
    ERFHVELHFS PGVKGVEEEG SAPAGCGFRP ASSENEEMKT NQGSMENLCP 950
    GKASDEPDRA LQTSPQPPEG PGLPRRSPLI RNRKAGSMEV LSETSSSRPG 1000
    GYRLFSSSRP PTEMKQSGLG SQCTGLFSTT VLGGSSSAPN LQDYARSHGK 1050
    KLPPASLKHR DELLFVPAVK RFSVSFAKHP TNGFEGCSMV PTIYPLETLH 1100
    NALSLRQVSE FLSRVCQRHT DAQAQASAAL FDSMHSSQAS DNPFSPPRTL 1150
    HSPPLQLQQR SEKPPWYSSG PSSTVSSAGP SSPTTVDGNS QFGFSDQPSL 1200
    NSHVAEEHQG LGLLQETPGS GAQELSIEGE QELFEPNQSP QVPPMETSQP 1250
    YEEVSQPCQE VPDISQPCQD ISEALSQPCQ KVPDISQQCQ ENHDNGNHTC 1300
    QEVPHISQPC QKSSQLCQKV SEEVCQLCLE NSEEVSQPCQ GVSVEVGKLV 1350
    HKFHVGVGSL VQETLVEVGS PAEEIPEEVI QPYQEFSVEV GRLAQETSAI 1400
    NLLSQGIPEI DKPSQEFPEE IDLQAQEVPE EIN 1433
    Length:1,433
    Mass (Da):159,521
    Last modified:July 5, 2004 - v1
    Checksum:iBA0DEFB2A71B1467
    GO
    Isoform 2 (identifier: Q6PFW1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         818-821: Missing.
         1082-1082: N → NG

    Show »
    Length:1,430
    Mass (Da):159,042
    Checksum:i11E6EC888FB5703C
    GO
    Isoform 3 (identifier: Q6PFW1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         818-821: Missing.
         1062-1082: Missing.

    Show »
    Length:1,408
    Mass (Da):156,616
    Checksum:iE88E96597599F5BA
    GO
    Isoform 4 (identifier: Q6PFW1-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         653-653: Missing.
         818-821: Missing.
         1062-1082: Missing.

    Show »
    Length:1,407
    Mass (Da):156,502
    Checksum:i1DC5FCBF5A726F14
    GO
    Isoform 5 (identifier: Q6PFW1-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         810-821: Missing.
         865-957: Missing.
         1107-1240: Missing.

    Show »
    Length:1,194
    Mass (Da):133,447
    Checksum:iF29D866BFAD98841
    GO
    Isoform 6 (identifier: Q6PFW1-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         818-1433: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:817
    Mass (Da):92,061
    Checksum:i4DBCE9B366905530
    GO
    Isoform 7 (identifier: Q6PFW1-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         818-821: Missing.
         1020-1082: Missing.
         1167-1167: Y → LETRFCHVGQAGLELLTSSDLPASASQSAGITGVSHRTQPD

    Note: No experimental confirmation available.

    Show »
    Length:1,406
    Mass (Da):156,320
    Checksum:i77C01F2E2AC7446D
    GO

    Sequence cautioni

    The sequence BAA20831.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti44 – 441D → G in CAD97968. (PubMed:17974005)Curated
    Sequence conflicti304 – 3041V → M in CAD97968. (PubMed:17974005)Curated
    Sequence conflicti374 – 3741E → V in CAD97968. (PubMed:17974005)Curated
    Sequence conflicti423 – 4231E → Q in AAP30843. (PubMed:12825070)Curated
    Sequence conflicti423 – 4231E → Q in AAP30845. (PubMed:12825070)Curated
    Sequence conflicti423 – 4231E → Q in AAN40768. (PubMed:12825070)Curated
    Sequence conflicti473 – 4731L → P in CAD97968. (PubMed:17974005)Curated
    Sequence conflicti483 – 4831F → S in AAP30845. (PubMed:12825070)Curated
    Sequence conflicti483 – 4831F → S in AAN40768. (PubMed:12825070)Curated
    Sequence conflicti490 – 4901V → E in CAD97968. (PubMed:17974005)Curated
    Sequence conflicti548 – 5481G → V in CAD97968. (PubMed:17974005)Curated
    Sequence conflicti738 – 7381I → L in AAP30845. (PubMed:12825070)Curated
    Sequence conflicti738 – 7381I → L in AAN40768. (PubMed:12825070)Curated
    Sequence conflicti788 – 7881V → A in AAP30845. (PubMed:12825070)Curated
    Sequence conflicti788 – 7881V → A in AAN40768. (PubMed:12825070)Curated
    Sequence conflicti936 – 9361E → G in CAI46011. (PubMed:17974005)Curated
    Sequence conflicti985 – 9851A → V in AAP30845. (PubMed:12825070)Curated
    Sequence conflicti985 – 9851A → V in AAN40768. (PubMed:12825070)Curated
    Sequence conflicti1020 – 10201G → A in AAP30843. (PubMed:12825070)Curated
    Sequence conflicti1041 – 10411L → P in AAP30845. (PubMed:12825070)Curated
    Sequence conflicti1041 – 10411L → P in AAN40768. (PubMed:12825070)Curated
    Sequence conflicti1066 – 10661V → L in AAP30842. (PubMed:12825070)Curated
    Sequence conflicti1126 – 11261A → T in CAI46011. (PubMed:17974005)Curated
    Sequence conflicti1134 – 11341M → V in CAI46011. (PubMed:17974005)Curated
    Sequence conflicti1198 – 11981P → R in CAI46011. (PubMed:17974005)Curated
    Sequence conflicti1293 – 12931H → M in AAP30845. (PubMed:12825070)Curated
    Sequence conflicti1293 – 12931H → M in AAN40768. (PubMed:12825070)Curated
    Sequence conflicti1294 – 12941D → T in AAP30845. (PubMed:12825070)Curated
    Sequence conflicti1294 – 12941D → T in AAN40768. (PubMed:12825070)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei653 – 6531Missing in isoform 4. 1 PublicationVSP_030615
    Alternative sequencei810 – 82112Missing in isoform 5. 1 PublicationVSP_030616Add
    BLAST
    Alternative sequencei818 – 1433616Missing in isoform 6. 1 PublicationVSP_030617Add
    BLAST
    Alternative sequencei818 – 8214Missing in isoform 2, isoform 3, isoform 4 and isoform 7. 3 PublicationsVSP_030618
    Alternative sequencei865 – 95793Missing in isoform 5. 1 PublicationVSP_030619Add
    BLAST
    Alternative sequencei1020 – 108263Missing in isoform 7. 1 PublicationVSP_030620Add
    BLAST
    Alternative sequencei1062 – 108221Missing in isoform 3 and isoform 4. 2 PublicationsVSP_030621Add
    BLAST
    Alternative sequencei1082 – 10821N → NG in isoform 2. 1 PublicationVSP_030622
    Alternative sequencei1107 – 1240134Missing in isoform 5. 1 PublicationVSP_030623Add
    BLAST
    Alternative sequencei1167 – 11671Y → LETRFCHVGQAGLELLTSSD LPASASQSAGITGVSHRTQP D in isoform 7. 1 PublicationVSP_030624

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF502586 mRNA. Translation: AAP30842.1.
    AF502587 mRNA. Translation: AAP30843.1.
    AF502588 mRNA. Translation: AAP30844.1.
    AF502589 mRNA. Translation: AAP30845.1.
    AF543190 mRNA. Translation: AAN40768.1.
    AB002375 mRNA. Translation: BAA20831.2. Different initiation.
    BX538022 mRNA. Translation: CAD97968.1.
    BX647814 mRNA. Translation: CAI46011.1.
    BC050263 mRNA. Translation: AAH50263.1.
    BC057395 mRNA. Translation: AAH57395.1.
    CCDSiCCDS32215.1. [Q6PFW1-3]
    CCDS45252.1. [Q6PFW1-1]
    CCDS53937.1. [Q6PFW1-7]
    RefSeqiNP_001124330.1. NM_001130858.2. [Q6PFW1-1]
    NP_001124331.1. NM_001130859.2. [Q6PFW1-3]
    NP_001177143.1. NM_001190214.1. [Q6PFW1-7]
    NP_055474.3. NM_014659.5. [Q6PFW1-3]
    XP_005254861.1. XM_005254804.1. [Q6PFW1-3]
    UniGeneiHs.156814.
    Hs.679911.

    Genome annotation databases

    EnsembliENST00000334933; ENSP00000334779; ENSG00000168781. [Q6PFW1-3]
    ENST00000348806; ENSP00000308773; ENSG00000168781. [Q6PFW1-7]
    ENST00000360135; ENSP00000353253; ENSG00000168781. [Q6PFW1-7]
    ENST00000360301; ENSP00000353446; ENSG00000168781. [Q6PFW1-3]
    ENST00000396923; ENSP00000380129; ENSG00000168781. [Q6PFW1-1]
    ENST00000420765; ENSP00000400887; ENSG00000168781. [Q6PFW1-1]
    GeneIDi9677.
    KEGGihsa:9677.
    UCSCiuc001zrw.3. human. [Q6PFW1-1]
    uc001zrx.2. human. [Q6PFW1-7]
    uc001zry.4. human. [Q6PFW1-3]
    uc021sjz.1. human. [Q6PFW1-5]

    Polymorphism databases

    DMDMi74758334.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF502586 mRNA. Translation: AAP30842.1 .
    AF502587 mRNA. Translation: AAP30843.1 .
    AF502588 mRNA. Translation: AAP30844.1 .
    AF502589 mRNA. Translation: AAP30845.1 .
    AF543190 mRNA. Translation: AAN40768.1 .
    AB002375 mRNA. Translation: BAA20831.2 . Different initiation.
    BX538022 mRNA. Translation: CAD97968.1 .
    BX647814 mRNA. Translation: CAI46011.1 .
    BC050263 mRNA. Translation: AAH50263.1 .
    BC057395 mRNA. Translation: AAH57395.1 .
    CCDSi CCDS32215.1. [Q6PFW1-3 ]
    CCDS45252.1. [Q6PFW1-1 ]
    CCDS53937.1. [Q6PFW1-7 ]
    RefSeqi NP_001124330.1. NM_001130858.2. [Q6PFW1-1 ]
    NP_001124331.1. NM_001130859.2. [Q6PFW1-3 ]
    NP_001177143.1. NM_001190214.1. [Q6PFW1-7 ]
    NP_055474.3. NM_014659.5. [Q6PFW1-3 ]
    XP_005254861.1. XM_005254804.1. [Q6PFW1-3 ]
    UniGenei Hs.156814.
    Hs.679911.

    3D structure databases

    ProteinModelPortali Q6PFW1.
    SMRi Q6PFW1. Positions 54-371.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115031. 11 interactions.
    STRINGi 9606.ENSP00000380129.

    Chemistry

    ChEMBLi CHEMBL5046.

    PTM databases

    PhosphoSitei Q6PFW1.

    Polymorphism databases

    DMDMi 74758334.

    Proteomic databases

    MaxQBi Q6PFW1.
    PaxDbi Q6PFW1.
    PRIDEi Q6PFW1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000334933 ; ENSP00000334779 ; ENSG00000168781 . [Q6PFW1-3 ]
    ENST00000348806 ; ENSP00000308773 ; ENSG00000168781 . [Q6PFW1-7 ]
    ENST00000360135 ; ENSP00000353253 ; ENSG00000168781 . [Q6PFW1-7 ]
    ENST00000360301 ; ENSP00000353446 ; ENSG00000168781 . [Q6PFW1-3 ]
    ENST00000396923 ; ENSP00000380129 ; ENSG00000168781 . [Q6PFW1-1 ]
    ENST00000420765 ; ENSP00000400887 ; ENSG00000168781 . [Q6PFW1-1 ]
    GeneIDi 9677.
    KEGGi hsa:9677.
    UCSCi uc001zrw.3. human. [Q6PFW1-1 ]
    uc001zrx.2. human. [Q6PFW1-7 ]
    uc001zry.4. human. [Q6PFW1-3 ]
    uc021sjz.1. human. [Q6PFW1-5 ]

    Organism-specific databases

    CTDi 9677.
    GeneCardsi GC15M043826.
    H-InvDB HIX0012186.
    HGNCi HGNC:29023. PPIP5K1.
    HPAi HPA039380.
    MIMi 610979. gene.
    neXtProti NX_Q6PFW1.
    PharmGKBi PA165479401.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG245915.
    HOVERGENi HBG108657.
    InParanoidi Q6PFW1.
    KOi K13024.
    OMAi EEVSQPC.
    PhylomeDBi Q6PFW1.
    TreeFami TF313594.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS09822-MONOMER.
    Reactomei REACT_150188. Synthesis of pyrophosphates in the cytosol.

    Miscellaneous databases

    ChiTaRSi PPIP5K1. human.
    GenomeRNAii 9677.
    NextBioi 36337.
    PROi Q6PFW1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6PFW1.
    Bgeei Q6PFW1.
    Genevestigatori Q6PFW1.

    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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 5).
      Tissue: Bone marrow, Testis and Trachea.
    2. "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
      Tissue: Brain.
    3. Ohara O., Nagase T., Kikuno R., Nomura N.
      Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
      Tissue: Endometrial adenocarcinoma.
    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] (ISOFORMS 1 AND 6).
      Tissue: Eye and Uterus.
    6. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "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, TISSUE SPECIFICITY.
    8. "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, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
    9. "A conserved family of enzymes that phosphorylate inositol hexakisphosphate."
      Mulugu S., Bai W., Fridy P.C., Bastidas R.J., Otto J.C., Dollins D.E., Haystead T.A., Ribeiro A.A., York J.D.
      Science 316:106-109(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME ACTIVITY.
    10. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1152, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Structural analysis and detection of biological inositol pyrophosphates reveal that the family of VIP/diphosphoinositol pentakisphosphate kinases are 1/3-kinases."
      Lin H., Fridy P.C., Ribeiro A.A., Choi J.H., Barma D.K., Vogel G., Falck J.R., Shears S.B., York J.D., Mayr G.W.
      J. Biol. Chem. 284:1863-1872(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY.
    14. "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: BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, POLYPHOSPHOINOSITIDE-BINDING DOMAIN, MUTAGENESIS OF ARG-399 AND ARG-417.

    Entry informationi

    Entry nameiVIP1_HUMAN
    AccessioniPrimary (citable) accession number: Q6PFW1
    Secondary accession number(s): O15082
    , Q5HYF8, Q7Z3A7, Q86TE7, Q86UV3, Q86UV4, Q86XW8, Q8IZN0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 98 of the entry and version 1 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3