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Protein

Phosphatidylinositol 4-kinase PIK1

Gene

PIK1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts on phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol 1,4,5,-trisphosphate. PIK1 is part of a nuclear phosphoinositide cycle and could control cytokinesis through the actin cytoskeleton.

Catalytic activityi

ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 4-phosphate.

GO - Molecular functioni

  • 1-phosphatidylinositol 4-kinase activity Source: SGD
  • ATP binding Source: UniProtKB-KW

GO - Biological processi

  • endocytosis Source: CACAO
  • phosphatidylinositol-mediated signaling Source: InterPro
  • phosphatidylinositol phosphorylation Source: SGD
  • positive regulation of Golgi to plasma membrane protein transport Source: CACAO
  • positive regulation of protein secretion Source: CACAO
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:YNL267W-MONOMER.
ReactomeiR-SCE-1660514. Synthesis of PIPs at the Golgi membrane.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylinositol 4-kinase PIK1 (EC:2.7.1.67)
Short name:
PI4-kinase
Short name:
PtdIns-4-kinase
Gene namesi
Name:PIK1
Ordered Locus Names:YNL267W
ORF Names:N0795
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL267W.
SGDiS000005211. PIK1.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: SGD
  • trans-Golgi network Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10661066Phosphatidylinositol 4-kinase PIK1PRO_0000088834Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei10 – 101PhosphoserineCombined sources
Modified residuei236 – 2361PhosphoserineCombined sources
Modified residuei384 – 3841PhosphoserineCombined sources
Modified residuei394 – 3941PhosphothreonineCombined sources
Modified residuei396 – 3961PhosphoserineCombined sources
Modified residuei592 – 5921PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP39104.
PeptideAtlasiP39104.

PTM databases

iPTMnetiP39104.

Interactioni

Subunit structurei

Interacts with FRQ1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
FRQ1Q063893EBI-13423,EBI-11946

Protein-protein interaction databases

BioGridi35573. 148 interactions.
DIPiDIP-6770N.
IntActiP39104. 4 interactions.
MINTiMINT-622692.

Structurei

Secondary structure

1
1066
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi126 – 13510Combined sources
Helixi156 – 16813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JU0NMR-B121-172[»]
ProteinModelPortaliP39104.
SMRiP39104. Positions 121-172, 411-534, 765-1043.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39104.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 133133PIK helicalPROSITE-ProRule annotationAdd
BLAST
Domaini793 – 1041249PI3K/PI4KPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PI3K/PI4K domain.PROSITE-ProRule annotation
Contains 1 PIK helical domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00550000074892.
HOGENOMiHOG000248748.
InParanoidiP39104.
KOiK19801.
OMAiYTRLYDQ.
OrthoDBiEOG7T4MTW.

Family and domain databases

Gene3Di1.10.1070.11. 1 hit.
1.25.40.70. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR011009. Kinase-like_dom.
IPR021601. Phosphatidylino_kinase_fungi.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR015433. PI_Kinase.
IPR001263. PInositide-3_kin_accessory_dom.
[Graphical view]
PANTHERiPTHR10048. PTHR10048. 3 hits.
PfamiPF00454. PI3_PI4_kinase. 1 hit.
PF11522. Pik1. 1 hit.
[Graphical view]
SMARTiSM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF56112. SSF56112. 2 hits.
PROSITEiPS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
PS51545. PIK_HELICAL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P39104-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHKASSSKKS FDDTIELKKN EQLLKLINSS EFTLHNCVEL LCKHSENIGI
60 70 80 90 100
HYYLCQKLAT FPHSELQFYI PQLVQVLVTM ETESMALEDL LLRLRAENPH
110 120 130 140 150
FALLTFWQLQ ALLTDLSTDP ASYGFQVARR VLNNLQTNLF NTSSGSDKNV
160 170 180 190 200
KIHENVAPAL VLSSMIMSAI AFPQLSEVTK PLVESQGRRQ KAFVFKLARS
210 220 230 240 250
AMKDFTKNMT LKNTLLNKKT SRSKRVSSNR SSTPTSPIDL IDPIKTKEDA
260 270 280 290 300
SFRKSRHSEV KLDFDIVDDI GNQVFEERIS SSIKLPKRKP KYLDNSYVHR
310 320 330 340 350
TYDGKNINRD GSISNTAKAL DGNKGDYISP KGRNDENNEI GNNEDETGGE
360 370 380 390 400
TEEDADALNS DHFTSSMPDL HNIQPRTSSA SSASLEGTPK LNRTNSQPLS
410 420 430 440 450
RQAFKNSKKA NSSLSQEIDL SQLSTTSKIK MLKANYFRCE TQFAIALETI
460 470 480 490 500
SQRLARVPTE ARLSALRAEL FLLNRDLPAE VDIPTLLPPN KKGKLHKLVT
510 520 530 540 550
ITANEAQVLN SAEKVPYLLL IEYLRDEFDF DPTSETNERL LKKISGNQGG
560 570 580 590 600
LIFDLNYMNR KENNENRNES TLTSNNTRSS VYDSNSFNNG ASRNEGLSST
610 620 630 640 650
SRSDSASTAH VRTEVNKEED LGDMSMVKVR NRTDDEAYRN ALVIQSAANV
660 670 680 690 700
PILPDDSQDR SPELNFGSNL DEVLIENGIN SKNIHSQTDA LADQMRVSAV
710 720 730 740 750
MLAQLDKSPQ QLSESTKQIR AQIISSMKEV QDKFGYHDLE ALHGMAGERK
760 770 780 790 800
LENDLMTGGI DTSYLGEDWA TKKERIRKTS EYGHFENWDL CSVIAKTGDD
810 820 830 840 850
LRQEAFAYQM IQAMANIWVK EKVDVWVKRM KILITSANTG LVETITNAMS
860 870 880 890 900
VHSIKKALTK KMIEDAELDD KGGIASLNDH FLRAFGNPNG FKYRRAQDNF
910 920 930 940 950
ASSLAAYSVI CYLLQVKDRH NGNIMIDNEG HVSHIDFGFM LSNSPGSVGF
960 970 980 990 1000
EAAPFKLTYE YIELLGGVEG EAFKKFVELT KSSFKALRKY ADQIVSMCEI
1010 1020 1030 1040 1050
MQKDNMQPCF DAGEQTSVQL RQRFQLDLSE KEVDDFVENF LIGKSLGSIY
1060
TRIYDQFQLI TQGIYS
Length:1,066
Mass (Da):119,923
Last modified:February 1, 1995 - v1
Checksum:i7666979CA14B1CB5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76058 Genomic DNA. Translation: CAA53658.1.
L20220 Genomic DNA. Translation: AAA34873.1.
X92494 Genomic DNA. Translation: CAA63231.1.
Z71543 Genomic DNA. Translation: CAA96174.1.
BK006947 Genomic DNA. Translation: DAA10293.1.
PIRiA49335.
RefSeqiNP_014132.1. NM_001183105.1.

Genome annotation databases

EnsemblFungiiYNL267W; YNL267W; YNL267W.
GeneIDi855454.
KEGGisce:YNL267W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76058 Genomic DNA. Translation: CAA53658.1.
L20220 Genomic DNA. Translation: AAA34873.1.
X92494 Genomic DNA. Translation: CAA63231.1.
Z71543 Genomic DNA. Translation: CAA96174.1.
BK006947 Genomic DNA. Translation: DAA10293.1.
PIRiA49335.
RefSeqiNP_014132.1. NM_001183105.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JU0NMR-B121-172[»]
ProteinModelPortaliP39104.
SMRiP39104. Positions 121-172, 411-534, 765-1043.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35573. 148 interactions.
DIPiDIP-6770N.
IntActiP39104. 4 interactions.
MINTiMINT-622692.

PTM databases

iPTMnetiP39104.

Proteomic databases

MaxQBiP39104.
PeptideAtlasiP39104.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL267W; YNL267W; YNL267W.
GeneIDi855454.
KEGGisce:YNL267W.

Organism-specific databases

EuPathDBiFungiDB:YNL267W.
SGDiS000005211. PIK1.

Phylogenomic databases

GeneTreeiENSGT00550000074892.
HOGENOMiHOG000248748.
InParanoidiP39104.
KOiK19801.
OMAiYTRLYDQ.
OrthoDBiEOG7T4MTW.

Enzyme and pathway databases

BioCyciYEAST:YNL267W-MONOMER.
ReactomeiR-SCE-1660514. Synthesis of PIPs at the Golgi membrane.

Miscellaneous databases

EvolutionaryTraceiP39104.
NextBioi979370.
PROiP39104.

Family and domain databases

Gene3Di1.10.1070.11. 1 hit.
1.25.40.70. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR011009. Kinase-like_dom.
IPR021601. Phosphatidylino_kinase_fungi.
IPR000403. PI3/4_kinase_cat_dom.
IPR018936. PI3/4_kinase_CS.
IPR015433. PI_Kinase.
IPR001263. PInositide-3_kin_accessory_dom.
[Graphical view]
PANTHERiPTHR10048. PTHR10048. 3 hits.
PfamiPF00454. PI3_PI4_kinase. 1 hit.
PF11522. Pik1. 1 hit.
[Graphical view]
SMARTiSM00146. PI3Kc. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF56112. SSF56112. 2 hits.
PROSITEiPS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
PS51545. PIK_HELICAL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "PIK1, an essential phosphatidylinositol 4-kinase associated with the yeast nucleus."
    Garcia-Bustos J.F., Marini F., Stevenson I., Frei C., Hall M.N.
    EMBO J. 13:2352-2361(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: JK9-3D.
  2. "Phosphatidylinositol 4-kinase: gene structure and requirement for yeast cell viability."
    Flanagan C.A., Schnieders E.A., Emerick A.W., Kunisawa R., Admon A., Thorner J.
    Science 262:1444-1448(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The sequence of a 24,152 bp segment from the left arm of chromosome XIV from Saccharomyces cerevisiae between the BNI1 and the POL2 genes."
    Sen-Gupta M., Lyck R., Fleig U., Niedenthal R.K., Hegemann J.H.
    Yeast 12:505-514(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "Yeast homologue of neuronal frequenin is a regulator of phosphatidylinositol-4-OH kinase."
    Hendricks K.B., Wang B.Q., Schnieders E.A., Thorner J.
    Nat. Cell Biol. 1:234-241(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FRQ1.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  9. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; THR-394 AND SER-396, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-384 AND SER-592, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Structural insights into activation of phosphatidylinositol 4-kinase (Pik1) by yeast frequenin (Frq1)."
    Strahl T., Huttner I.G., Lusin J.D., Osawa M., King D., Thorner J., Ames J.B.
    J. Biol. Chem. 282:30949-30959(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 121-172.

Entry informationi

Entry nameiPIK1_YEAST
AccessioniPrimary (citable) accession number: P39104
Secondary accession number(s): D6W0S7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 11, 2016
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 1600 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

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 one 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.