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Protein

Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1

Gene

Ppip5k1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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).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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.4.24. 5301.
ReactomeiREACT_350195. 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 Componenti: 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

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 residuei941 – 9411PhosphoserineBy similarity
Modified residuei1149 – 11491PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP0C644.
PRIDEiP0C644.

Expressioni

Gene expression databases

ExpressionAtlasiP0C644. baseline.

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.
IPR030138. PPIP5K1.
[Graphical view]
PANTHERiPTHR12750:SF11. PTHR12750:SF11. 1 hit.
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

        10         20         30         40         50
MWSLTANEDE DESATAHFFL GAGDEGLGTC GIGMRTGESD SELLEDEEDE
60 70 80 90 100
VPPEPQIIVG ICAMTKKSKS KPMTQILERL CRFDYLTVVI LGEDVILNEP
110 120 130 140 150
VENWPPCHCL ISFHSKGFPL DKAVAYSKLR NPFLINDLTM QYYIQDRREV
160 170 180 190 200
YRILQEEGID LPRYAVLNRD PACPEECNLI EGEDQVEVNG AVFPKPFVEK
210 220 230 240 250
PVSAEDHNVY IYYPSSAGGG SQRLFRKIGS RSSVYSPESS VRKTGSYIYE
260 270 280 290 300
EFMPTDGTDV KVYTVGPDYA HAEARKSPAL DGKVERDSEG KEVRYPVMLT
310 320 330 340 350
AMEKLVARKV CVAFKQTVCG FDLLRANGHS FVCDVNGFSF VKNSMKYYDD
360 370 380 390 400
CAKILGNTIM RELAPQFQIP WSIPTEAEDI PIVPTTSGTM MELRCVIAII
410 420 430 440 450
RHGDRTPKQK MKMEVTHPRF FALFEKHGGY KTGKLKLKRP EQLQEVLDIT
460 470 480 490 500
RLLLAELEKE PGAEIEEKTG KLEQLKSVLE MYGHFSGINR KVQLTYYPHG
510 520 530 540 550
VKASSEGQDL QREPPAPSLL LVLKWGGELT PDGRVQAEEL GRAFRCMYPG
560 570 580 590 600
GQGDYAGFPG CGLLRLHSTF RHDLKIYASD EGRVQMTAAA FAKGLLALEG
610 620 630 640 650
ELTPILVQMV KSANMNGLLD SDSDSLSSCQ HRVKARLHHI LQQDAPFGPE
660 670 680 690 700
DYDQLAPTGS TSLLNSMSVI QNPVKVCDQV FALIENLTHQ IRERMQDPSS
710 720 730 740 750
VDLQLYHSET LELMLQRWSK LERDFRQKSG RYDISKIPDI YDCVKYDVQH
760 770 780 790 800
NGSLGLQGTA ELLRLSKALA DVVIPQEYGI SREEKVEIAV GFCLPLLRKI
810 820 830 840 850
LLDLQRTHED ESVNKLHPLY SRGVLSPGRH VRTRLYFTSE SHVHSLLSVF
860 870 880 890 900
RYGGLLDETK DAQWQRALAY LSAISELNYM TQIVIMLYED NTRDPLSEER
910 920 930 940 950
FHVELHFSPG VKGVEEGSAP AGCGFRPASS ENEEMKTDPG SIENLCPAKP
960 970 980 990 1000
SDEPDRALQT SPQPVEGTGL PRRSPLIRNR KAGSMEVLSE TSSSRPGGYR
1010 1020 1030 1040 1050
LFSSSRPPTE MKQSGLGSQC TGLFSTTVLG GSSSAPNLQD YARTHGKKLP
1060 1070 1080 1090 1100
PAGLKHRDEL LFVPAVKRFS VSFAKHPTNG FEGCSMVPTI YPLETLHNAL
1110 1120 1130 1140 1150
SLRQVSEFLT KVCQRHTDAH AQASAALFDS MHNHQASDNP FSPPRTLHSP
1160 1170 1180 1190 1200
PLQLRHRSEK PPWYSSGPSS TVSSAGPSSP TTVDGNSHFG FSDQSSVNTQ
1210 1220 1230 1240 1250
MIEEKQGLGL LQETPGDGTP EFHIELAEST QSPQEPPVEI SPPGSQDDTE
1260 1270 1280 1290 1300
VNQTCQEVPD TIQPCHDILE EIGQPNQEVP DISQLLLKNH DTATNTCQPC
1310 1320 1330 1340 1350
QASQLSKKVY EEICQLCQDN PEESNQLCQE VSVELGRMVH RFPVSIGSTT
1360 1370 1380 1390 1400
QETLMEIGRP TQEIPEEPCQ EFSEKVGMLT QKASAISELS QDILETDNPS
1410 1420 1430
QELSEETDLQ AQEVSEEIDQ EPEVVDELSN EDIS
Length:1,434
Mass (Da):159,619
Last modified:January 15, 2008 - v1
Checksum:iA3C2C9C28B4EAB47
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC116071 Genomic DNA. No translation available.
UniGeneiRn.46305.

Genome annotation databases

UCSCiRGD:1311552. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC116071 Genomic DNA. No translation available.
UniGeneiRn.46305.

3D structure databases

ProteinModelPortaliP0C644.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000059430.

Proteomic databases

PaxDbiP0C644.
PRIDEiP0C644.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:1311552. rat.

Organism-specific databases

RGDi1311552. Ppip5k1.

Phylogenomic databases

eggNOGiNOG245915.
HOGENOMiHOG000177917.
HOVERGENiHBG108657.
InParanoidiP0C644.
PhylomeDBiP0C644.

Enzyme and pathway databases

BRENDAi2.7.4.24. 5301.
ReactomeiREACT_350195. Synthesis of pyrophosphates in the cytosol.

Miscellaneous databases

PROiP0C644.

Gene expression databases

ExpressionAtlasiP0C644. baseline.

Family and domain databases

Gene3Di3.40.50.1240. 3 hits.
InterProiIPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
IPR030138. PPIP5K1.
[Graphical view]
PANTHERiPTHR12750:SF11. PTHR12750:SF11. 1 hit.
PfamiPF00328. His_Phos_2. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 3 hits.
PROSITEiPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: June 24, 2015
This is version 58 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.