Phosphatidylinositol 4-kinase PIK1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P39104 (PIK1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 100. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Phosphatidylinositol 4-kinase PIK1
Short name=PI4-kinase
Short name=PtdIns-4-kinase
EC=2.7.1.67

Gene names

Name:	PIK1
Ordered Locus Names:	YNL267W
ORF Names:	N0795

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	1066 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 4-phosphate.
Subunit structure	Interacts with FRQ1. Ref.6
Subcellular location	Nucleus.
Miscellaneous	Present with 1600 molecules/cell in log phase SD medium. Ref.7
Sequence similarities	Belongs to the PI3/PI4-kinase family. Type III PI4K subfamily. Contains 1 PI3K/PI4K domain. Contains 1 PIK helical domain.

Ontologies

Keywords
Cellular component	Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	phosphatidylinositol-mediated signaling Inferred from electronic annotation. Source: InterPro
Cellular component	nucleus Inferred from direct assay Ref.1. Source: SGD trans-Golgi network Inferred from direct assay. Source: SGD
Molecular function	1-phosphatidylinositol 4-kinase activity Inferred from direct assay Ref.1 Ref.2. Source: SGD ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FRQ1	Q06389	3	EBI-13423,EBI-11946

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1066

1066

Phosphatidylinositol 4-kinase PIK1

PRO_0000088834

Regions

Domain

1 – 133

133

PIK helical

Domain

793 – 1041

249

PI3K/PI4K

Amino acid modifications

Modified residue

Phosphoserine Ref.10 Ref.11 Ref.12

Modified residue

231

Phosphoserine Ref.12

Modified residue

232

Phosphoserine Ref.12

Modified residue

233

Phosphothreonine Ref.8 Ref.12

Modified residue

236

Phosphoserine Ref.8 Ref.9 Ref.12

Modified residue

282

Phosphoserine Ref.12

Modified residue

378

Phosphoserine Ref.12

Modified residue

379

Phosphoserine Ref.12

Modified residue

382

Phosphoserine Ref.12

Modified residue

384

Phosphoserine Ref.12

Modified residue

394

Phosphothreonine Ref.10

Modified residue

396

Phosphoserine Ref.10 Ref.12

Modified residue

586

Phosphoserine Ref.12

Modified residue

592

Phosphoserine Ref.12

Modified residue

605

Phosphoserine Ref.11 Ref.12

Modified residue

608

Phosphothreonine Ref.11

Secondary structure

1066

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P39104 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 7666979CA14B1CB5
Show »

FASTA

1,066

119,923

        10         20         30         40         50         60 
MHKASSSKKS FDDTIELKKN EQLLKLINSS EFTLHNCVEL LCKHSENIGI HYYLCQKLAT 

        70         80         90        100        110        120 
FPHSELQFYI PQLVQVLVTM ETESMALEDL LLRLRAENPH FALLTFWQLQ ALLTDLSTDP 

       130        140        150        160        170        180 
ASYGFQVARR VLNNLQTNLF NTSSGSDKNV KIHENVAPAL VLSSMIMSAI AFPQLSEVTK 

       190        200        210        220        230        240 
PLVESQGRRQ KAFVFKLARS AMKDFTKNMT LKNTLLNKKT SRSKRVSSNR SSTPTSPIDL 

       250        260        270        280        290        300 
IDPIKTKEDA SFRKSRHSEV KLDFDIVDDI GNQVFEERIS SSIKLPKRKP KYLDNSYVHR 

       310        320        330        340        350        360 
TYDGKNINRD GSISNTAKAL DGNKGDYISP KGRNDENNEI GNNEDETGGE TEEDADALNS 

       370        380        390        400        410        420 
DHFTSSMPDL HNIQPRTSSA SSASLEGTPK LNRTNSQPLS RQAFKNSKKA NSSLSQEIDL 

       430        440        450        460        470        480 
SQLSTTSKIK MLKANYFRCE TQFAIALETI SQRLARVPTE ARLSALRAEL FLLNRDLPAE 

       490        500        510        520        530        540 
VDIPTLLPPN KKGKLHKLVT ITANEAQVLN SAEKVPYLLL IEYLRDEFDF DPTSETNERL 

       550        560        570        580        590        600 
LKKISGNQGG LIFDLNYMNR KENNENRNES TLTSNNTRSS VYDSNSFNNG ASRNEGLSST 

       610        620        630        640        650        660 
SRSDSASTAH VRTEVNKEED LGDMSMVKVR NRTDDEAYRN ALVIQSAANV PILPDDSQDR 

       670        680        690        700        710        720 
SPELNFGSNL DEVLIENGIN SKNIHSQTDA LADQMRVSAV MLAQLDKSPQ QLSESTKQIR 

       730        740        750        760        770        780 
AQIISSMKEV QDKFGYHDLE ALHGMAGERK LENDLMTGGI DTSYLGEDWA TKKERIRKTS 

       790        800        810        820        830        840 
EYGHFENWDL CSVIAKTGDD LRQEAFAYQM IQAMANIWVK EKVDVWVKRM KILITSANTG 

       850        860        870        880        890        900 
LVETITNAMS VHSIKKALTK KMIEDAELDD KGGIASLNDH FLRAFGNPNG FKYRRAQDNF 

       910        920        930        940        950        960 
ASSLAAYSVI CYLLQVKDRH NGNIMIDNEG HVSHIDFGFM LSNSPGSVGF EAAPFKLTYE 

       970        980        990       1000       1010       1020 
YIELLGGVEG EAFKKFVELT KSSFKALRKY ADQIVSMCEI MQKDNMQPCF DAGEQTSVQL 

      1030       1040       1050       1060 
RQRFQLDLSE KEVDDFVENF LIGKSLGSIY TRIYDQFQLI TQGIYS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8194527] [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: 8248783] [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: 8740425] [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. Hani J. Nature 387:93-98(1997) [PubMed: 9169873] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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: 10559922] [Abstract] Cited for: INTERACTION WITH FRQ1.
[7]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-233 AND SER-236, MASS SPECTROMETRY. Strain: YAL6B.
[9]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236, MASS SPECTROMETRY. Strain: ADR376.
[10]	"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: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; THR-394 AND SER-396, MASS SPECTROMETRY.
[11]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-605 AND THR-608, MASS SPECTROMETRY.
[12]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-231; SER-232; THR-233; SER-236; SER-282; SER-378; SER-379; SER-382; SER-384; SER-396; SER-586; SER-592 AND SER-605, MASS SPECTROMETRY.
[13]	"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: 17720810] [Abstract] Cited for: STRUCTURE BY NMR OF 121-172.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

A49335.

RefSeq

NP_014132.1. NM_001183105.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JU0	NMR	-	B	121-172	[»]

ProteinModelPortal

P39104.

SMR

P39104. Positions 121-172, 792-1050.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6770N.

IntAct

P39104. 2 interactions.

MINT

MINT-622692.

STRING

P39104.

Proteomic databases

PeptideAtlas

P39104.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YNL267W; YNL267W; YNL267W.

GeneID

855454.

KEGG

sce:YNL267W.

NMPDR

fig|4932.3.peg.5197.

Organism-specific databases

CYGD

YNL267w.

SGD

S000005211. PIK1.

Phylogenomic databases

eggNOG

fuNOG04850.

GeneTree

EFGT00050000002040.

HOGENOM

HBG397287.

OMA

WDLCSVI.

OrthoDB

EOG45XC4T.

Gene expression databases

ArrayExpress

P39104.

Genevestigator

P39104.

GermOnline

YNL267W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR016024. ARM-type_fold.
IPR011009. Kinase-like_dom.
IPR021601. Phosphatidylinositol_kinase.
IPR000403. PI3/4_kinase_cat.
IPR018936. PI3/4_kinase_CS.
IPR015433. PI_Kinase.
IPR001263. PInositide-3_kin_accessory_dom.
[Graphical view]

Gene3D

G3DSA:1.10.1070.11. PI3/4_kinase_cat. 1 hit.
G3DSA:1.25.40.70. PI3Ka. 1 hit.

K00888.

PANTHER

PTHR10048. PI_Kinase. 1 hit.

Pfam

PF00454. PI3_PI4_kinase. 1 hit.
PF00613. PI3Ka. 1 hit.
PF11522. Pik1. 1 hit.
[Graphical view]

SMART

SM00146. PI3Kc. 1 hit.
[Graphical view]

SUPFAM

SSF48371. ARM-type_fold. 1 hit.
SSF56112. Kinase_like. 1 hit.

PROSITE

PS00915. 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]

ProtoNet

Search...

Other

NextBio

979370.

Entry information

Entry name

PIK1_YEAST

Accession

Primary (citable) accession number: P39104
Secondary accession number(s): D6W0S7

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	December 14, 2011
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XIV

Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents