Inositol hexakisphosphate kinase 1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Inositol hexakisphosphate kinase 1
Short name=InsP6 kinase 1
EC=2.7.4.21

Alternative name(s):
InsP6 kinase KCS1
PKC1 suppressor protein 1

Gene names

Name:	KCS1
Ordered Locus Names:	YDR017C
ORF Names:	PZF1050

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1050 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Converts inositol hexakisphosphate (InsP6) to diphosphoinositol pentakisphosphate (InsP7/PP-InsP5). Involved in phosphate regulation and polyphosphate accumulation. Required for resistance to salt stress, cell wall integrity, vacuole morphogenesis, and telomere maintenance. Ref.1 Ref.5 Ref.6 Ref.7 Ref.10 Ref.11 Ref.12
Catalytic activity	ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate. ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate = ADP + 1D-myo-inositol diphosphate tetrakisphosphate (isomeric configuration unknown).
Subcellular location	Cytoplasm Ref.8.
Miscellaneous	Present with 1940 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the inositol phosphokinase (IPK) family.
Biophysicochemical properties	Kinetic parameters: K_M=3.3 µM for InsP6 Ref.6 K_M=1.2 µM for InsP5 V_max=2 µmol/min/mg enzyme

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	inositol phosphate biosynthetic process Inferred from direct assay Ref.5 PubMed 17412958. Source: SGD
Cellular_component	cytoplasm Inferred from direct assay Ref.8. Source: SGD
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW inositol heptakisphosphate 5-kinase activity Inferred from sequence or structural similarity Ref.5. Source: SGD inositol hexakisphosphate 1-kinase activity Inferred from electronic annotation. Source: EC inositol hexakisphosphate 3-kinase activity Inferred from electronic annotation. Source: EC inositol hexakisphosphate 5-kinase activity Inferred from electronic annotation. Source: EC inositol hexakisphosphate kinase activity Inferred from direct assay Ref.5 Ref.7. Source: SGD inositol-1,3,4,5,6-pentakisphosphate kinase activity Inferred from direct assay Ref.6. Source: SGD inositol-1,4,5-trisphosphate 3-kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1050

1050

Inositol hexakisphosphate kinase 1

PRO_0000255955

Regions

Region

772 – 780

9

Substrate binding By similarity

Amino acid modifications

Modified residue

150

1

Phosphoserine Ref.17

Modified residue

206

1

Phosphoserine Ref.17

Modified residue

210

1

Phosphotyrosine Ref.17

Modified residue

396

1

Phosphoserine Ref.17

Modified residue

441

1

Phosphoserine Ref.17

Modified residue

469

1

Phosphoserine Ref.16

Modified residue

471

1

Phosphoserine Ref.13 Ref.16 Ref.17

Modified residue

472

1

Phosphoserine Ref.16 Ref.17

Modified residue

477

1

Phosphoserine Ref.17

Modified residue

537

1

Phosphoserine Ref.14 Ref.15 Ref.17

Modified residue

539

1

Phosphoserine Ref.15

Modified residue

566

1

Phosphoserine Ref.15 Ref.16

Modified residue

581

1

Phosphoserine Ref.13 Ref.17

Modified residue

583

1

Phosphoserine Ref.17

Modified residue

589

1

Phosphoserine Ref.13 Ref.15

Modified residue

592

1

Phosphoserine Ref.15

Modified residue

593

1

Phosphoserine Ref.15 Ref.17

Modified residue

597

1

Phosphoserine Ref.16

Modified residue

609

1

Phosphoserine Ref.17

Modified residue

644

1

Phosphoserine Ref.13 Ref.17

Modified residue

646

1

Phosphoserine Ref.16 Ref.17

Modified residue

664

1

Phosphoserine Ref.17

Modified residue

670

1

Phosphoserine Ref.17

Sequences

Sequence

Length

Mass (Da)

Tools

Q12494 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 9C7507CA5F4B0FC7
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FASTA

1,050

119,550

        10         20         30         40         50         60 
MDTSHEIHDK IPDTLREQQQ HLRQKESEGC ITTLKDLNVP ETKKLSSVLH GRKASTYLRI 

        70         80         90        100        110        120 
FRDDECLADN NNGVDSNNGG SVTCADKITR SEATPKSVPE GLQVSEKKNN PDTLSSSLSS 

       130        140        150        160        170        180 
FILSNHEEPA IKPNKHVAHR NNITETGQGS GEDIAKQQSH QPQVLHHQTS LKPIQNVDEG 

       190        200        210        220        230        240 
CISPKSTYQE SLHGISEDLT LKPVSSATYY PHKSKADSGY EEKDKMENDI DTIQPATINC 

       250        260        270        280        290        300 
ASGIATLPSS YNRHTFKVKT YSTLSQSLRQ ENVNNRSNEK KPQQFVPHSE SIKEKPNTFE 

       310        320        330        340        350        360 
QDKEGEQADE EEDEGDNEHR EYPLAVELKP FTNRVGGHTA IFRFSKRAVC KALVNRENRW 

       370        380        390        400        410        420 
YENIELCHKE LLQFMPRYIG VLNVRQHFQS KDDFLSDLDQ ENNGKNDTSN ENKDIEVNHN 

       430        440        450        460        470        480 
NNDDIALNTE PTGTPLTHIH SFPLEHSSRQ VLEKEHPEIE SVHPHVKRSL SSSNQPSLLP 

       490        500        510        520        530        540 
EVVLNDNRHI IPESLWYKYS DSPNSAPNDS YFSSSSSHNS CSFGERGNTN KLKRRDSGST 

       550        560        570        580        590        600 
MINTELKNLV IREVFAPKCF RRKRNSNTTT MGNHNARLGS SPSFLTQKSR ASSHDASNTS 

       610        620        630        640        650        660 
MKTLGDSSSQ ASLQMDDSKV NPNLQDPFLK KSLHEKISNA LDGSHSVMDL KQFHKNEQIK 

       670        680        690        700        710        720 
HKNSFCNSLS PILTATNSRD DGEFATSPNY ISNAQDGVFD MDEDTGNETI NMDNHGCHLD 

       730        740        750        760        770        780 
SGKNMIIKSL AYNVSNDYSH HDIESITFEE TSHTIVSKFI LLEDLTRNMN KPCALDLKMG 

       790        800        810        820        830        840 
TRQYGVDAKR AKQLSQRAKC LKTTSRRLGV RICGLKVWNK DYYITRDKYF GRRVKVGWQF 

       850        860        870        880        890        900 
ARVLARFLYD GKTIESLIRQ IPRLIKQLDT LYSEIFNLKG YRLYGASLLL MYDGDANKSN 

       910        920        930        940        950        960 
SKRKKAANVK VNLIDFARCV TKEDAMECMD KFRIPPKSPN IEDKGFLRGV KSLRFYLLLI 

       970        980        990       1000       1010       1020 
WNYLTSDMPL IFDEVEMNDM ISEEADSNSF TSATGSKINF NSKWDWLDEF DKEDEEMYND 

      1030       1040       1050 
PNSKLRQKWR KYELIFDAEP RYNDDAQVSD

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Suppressors of a Saccharomyces cerevisiae pkc1 mutation identify alleles of the phosphatase gene PTC1 and of a novel gene encoding a putative basic leucine zipper protein." Huang K.N., Symington L.S. Genetics 141:1275-1285(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]	"Sequencing and analysis of a 35.4 kb region on the right arm of chromosome IV from Saccharomyces cerevisiae reveal 23 open reading frames." Eide L.G., Sander C., Prydz H. Yeast 12:1085-1090(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. Zaccaria P. Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Synthesis of diphosphoinositol pentakisphosphate by a newly identified family of higher inositol polyphosphate kinases." Saiardi A., Erdjument-Bromage H., Snowman A.M., Tempst P., Snyder S.H. Curr. Biol. 9:1323-1326(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"The inositol hexakisphosphate kinase family. Catalytic flexibility and function in yeast vacuole biogenesis." Saiardi A., Caffrey J.J., Snyder S.H., Shears S.B. J. Biol. Chem. 275:24686-24692(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[7]	"In Saccharomyces cerevisiae, the inositol polyphosphate kinase activity of Kcs1p is required for resistance to salt stress, cell wall integrity, and vacuolar morphogenesis." Dubois E., Scherens B., Vierendeels F., Ho M.M.W., Messenguy F., Shears S.B. J. Biol. Chem. 277:23755-23763(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]	"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] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]	"Inositol diphosphate signaling regulates telomere length." York S.J., Armbruster B.N., Greenwell P., Petes T.D., York J.D. J. Biol. Chem. 280:4264-4269(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"Plc1p, Arg82p, and Kcs1p, enzymes involved in inositol pyrophosphate synthesis, are essential for phosphate regulation and polyphosphate accumulation in Saccharomyces cerevisiae." Auesukaree C., Tochio H., Shirakawa M., Kaneko Y., Harashima S. J. Biol. Chem. 280:25127-25133(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"Molecular definition of a novel inositol polyphosphate metabolic pathway initiated by inositol 1,4,5-trisphosphate 3-kinase activity in Saccharomyces cerevisiae." Seeds A.M., Bastidas R.J., York J.D. J. Biol. Chem. 280:27654-27661(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-471; SER-581; SER-589 AND SER-644, MASS SPECTROMETRY. Strain: YAL6B.
[14]	"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-537, MASS SPECTROMETRY. Strain: ADR376.
[15]	"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-537; SER-539; SER-566; SER-589; SER-592 AND SER-593, MASS SPECTROMETRY.
[16]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-469; SER-471; SER-472; SER-566; SER-597 AND SER-646, MASS SPECTROMETRY.
[17]	"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-150; SER-206; TYR-210; SER-396; SER-441; SER-471; SER-472; SER-477; SER-537; SER-581; SER-583; SER-593; SER-609; SER-644; SER-646; SER-664 AND SER-670, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	S81651 Genomic DNA. Translation: AAB36234.1. X95966 Genomic DNA. Translation: CAA65208.1. Z49770 Genomic DNA. Translation: CAA89842.1. Z74313 Genomic DNA. Translation: CAA98837.1. Z74314 Genomic DNA. Translation: CAA98839.1. BK006938 Genomic DNA. Translation: DAA11863.1.
PIR	S54640.
RefSeq	NP_010300.3. NM_001180325.3.
3D structure databases
ProteinModelPortal	Q12494.
SMR	Q12494. Positions 348-398, 759-961.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-1402N.
IntAct	Q12494. 5 interactions.
MINT	MINT-397897.
Proteomic databases
PaxDb	Q12494.
PeptideAtlas	Q12494.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YDR017C; YDR017C; YDR017C.
GeneID	851580.
KEGG	sce:YDR017C. sce:YDR021W.
Organism-specific databases
CYGD	YDR017c.
SGD	S000002424. KCS1.
Phylogenomic databases
eggNOG	NOG274869.
GeneTree	ENSGT00390000014381.
HOGENOM	HOG000001029.
KO	K13025.
OMA	RKASTYL.
OrthoDB	EOG4JWZPQ.
Gene expression databases
Genevestigator	Q12494.
GermOnline	YDR017C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR005522. IPK. [Graphical view]
PANTHER	PTHR12400. PTHR12400. 1 hit.
Pfam	PF03770. IPK. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	969043.

Entry information

Entry name

KCS1_YEAST

Accession

Primary (citable) accession number: Q12494
Secondary accession number(s): D6VS03, P89899, Q7LGR2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 99 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 IV

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

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

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