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Q6PFW1

- VIP1_HUMAN

UniProt

Q6PFW1 - VIP1_HUMAN

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Protein

Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1

Gene
PPIP5K1, HISPPD2A, IP6K, IPS1, KIAA0377, VIP1
Organism
Homo sapiens (Human)
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. 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.5 Publications
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.5 Publications
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.5 Publications
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 InsP7

Vmax=0.03 nmol/min/mg enzyme with InsP6 as substrate

Vmax=0.13 nmol/min/mg enzyme with InsP7 as substrate

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi248 – 2514ATP By similarity
Nucleotide bindingi257 – 2593ATP By similarity
Nucleotide bindingi332 – 3343ATP By 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
Complete GO annotation...

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.3 Publications

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

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.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni64 – 652Substrate binding By similarity
Regioni224 – 2252Substrate binding By similarity
Regioni337 – 3404Substrate binding By 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 (1 Publication).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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei653 – 6531Missing in isoform 4. VSP_030615
Alternative sequencei810 – 82112Missing in isoform 5. VSP_030616Add
BLAST
Alternative sequencei818 – 1433616Missing in isoform 6. VSP_030617Add
BLAST
Alternative sequencei818 – 8214Missing in isoform 2, isoform 3, isoform 4 and isoform 7. VSP_030618
Alternative sequencei865 – 95793Missing in isoform 5. VSP_030619Add
BLAST
Alternative sequencei1020 – 108263Missing in isoform 7. VSP_030620Add
BLAST
Alternative sequencei1062 – 108221Missing in isoform 3 and isoform 4. VSP_030621Add
BLAST
Alternative sequencei1082 – 10821N → NG in isoform 2. VSP_030622
Alternative sequencei1107 – 1240134Missing in isoform 5. VSP_030623Add
BLAST
Alternative sequencei1167 – 11671Y → LETRFCHVGQAGLELLTSSD LPASASQSAGITGVSHRTQP D in isoform 7. VSP_030624

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti44 – 441D → G in CAD97968. 1 Publication
Sequence conflicti304 – 3041V → M in CAD97968. 1 Publication
Sequence conflicti374 – 3741E → V in CAD97968. 1 Publication
Sequence conflicti423 – 4231E → Q in AAP30843. 1 Publication
Sequence conflicti423 – 4231E → Q in AAP30845. 1 Publication
Sequence conflicti423 – 4231E → Q in AAN40768. 1 Publication
Sequence conflicti473 – 4731L → P in CAD97968. 1 Publication
Sequence conflicti483 – 4831F → S in AAP30845. 1 Publication
Sequence conflicti483 – 4831F → S in AAN40768. 1 Publication
Sequence conflicti490 – 4901V → E in CAD97968. 1 Publication
Sequence conflicti548 – 5481G → V in CAD97968. 1 Publication
Sequence conflicti738 – 7381I → L in AAP30845. 1 Publication
Sequence conflicti738 – 7381I → L in AAN40768. 1 Publication
Sequence conflicti788 – 7881V → A in AAP30845. 1 Publication
Sequence conflicti788 – 7881V → A in AAN40768. 1 Publication
Sequence conflicti936 – 9361E → G in CAI46011. 1 Publication
Sequence conflicti985 – 9851A → V in AAP30845. 1 Publication
Sequence conflicti985 – 9851A → V in AAN40768. 1 Publication
Sequence conflicti1020 – 10201G → A in AAP30843. 1 Publication
Sequence conflicti1041 – 10411L → P in AAP30845. 1 Publication
Sequence conflicti1041 – 10411L → P in AAN40768. 1 Publication
Sequence conflicti1066 – 10661V → L in AAP30842. 1 Publication
Sequence conflicti1126 – 11261A → T in CAI46011. 1 Publication
Sequence conflicti1134 – 11341M → V in CAI46011. 1 Publication
Sequence conflicti1198 – 11981P → R in CAI46011. 1 Publication
Sequence conflicti1293 – 12931H → M in AAP30845. 1 Publication
Sequence conflicti1293 – 12931H → M in AAN40768. 1 Publication
Sequence conflicti1294 – 12941D → T in AAP30845. 1 Publication
Sequence conflicti1294 – 12941D → T in AAN40768. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 97 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

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