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P0C644

- VIP1_RAT

UniProt

P0C644 - VIP1_RAT

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Protein

Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1

Gene
Ppip5k1, Hisppd2a, Vip1
Organism
Rattus norvegicus (Rat)
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 By similarity.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.

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi250 – 2534ATP By similarity
Nucleotide bindingi259 – 2613ATP By similarity
Nucleotide bindingi334 – 3363ATP 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
Complete GO annotation...

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
Complete GO annotation...

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 – 11491Phosphoserine By 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.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni66 – 672Substrate binding By similarity
Regioni226 – 2272Substrate binding By similarity
Regioni339 – 3424Substrate binding By similarity
Regioni384 – 45572Polyphosphoinositide-binding domain By 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.

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 51 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

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