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Q12494 (KCS1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1050 AA.
Sequence statusComplete.
Protein existenceEvidence 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-diphosphate 2,3,4,5,6-pentakisphosphate = ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate.

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:

KM=3.3 µM for InsP6 Ref.6

KM=1.2 µM for InsP5

Vmax=2 µmol/min/mg enzyme

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10501050Inositol hexakisphosphate kinase 1
PRO_0000255955

Regions

Region772 – 7809Substrate binding By similarity

Amino acid modifications

Modified residue1501Phosphoserine Ref.16 Ref.17
Modified residue3961Phosphoserine Ref.16 Ref.17
Modified residue4691Phosphoserine Ref.17
Modified residue5371Phosphoserine Ref.14 Ref.15 Ref.17
Modified residue5391Phosphoserine Ref.17
Modified residue5661Phosphoserine Ref.15
Modified residue5831Phosphoserine Ref.16
Modified residue5891Phosphoserine Ref.15
Modified residue6461Phosphoserine Ref.17
Modified residue6641Phosphoserine Ref.17
Modified residue6701Phosphoserine Ref.16 Ref.17

Sequences

Sequence LengthMass (Da)Tools
Q12494 [UniParc].

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

FASTA1,050119,550
        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 

« Hide

References

« Hide '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. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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-566 AND SER-589, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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-396; SER-583 AND SER-670, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"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-150; SER-396; SER-469; SER-537; SER-539; SER-646; SER-664 AND SER-670, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
PIRS54640.
RefSeqNP_010300.3. NM_001180325.3.

3D structure databases

ProteinModelPortalQ12494.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32067. 277 interactions.
DIPDIP-1402N.
IntActQ12494. 5 interactions.
MINTMINT-397897.

Proteomic databases

PaxDbQ12494.
PeptideAtlasQ12494.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR017C; YDR017C; YDR017C.
GeneID851580.
KEGGsce:YDR017C.

Organism-specific databases

CYGDYDR017c.
SGDS000002424. KCS1.

Phylogenomic databases

eggNOGNOG274869.
GeneTreeENSGT00390000014381.
HOGENOMHOG000001029.
OMACATDTEE.
OrthoDBEOG7T1RKK.

Enzyme and pathway databases

BioCycYEAST:G3O-29635-MONOMER.
YEAST:MONOMER3O-205.

Gene expression databases

GenevestigatorQ12494.

Family and domain databases

InterProIPR005522. IPK.
[Graphical view]
PANTHERPTHR12400. PTHR12400. 1 hit.
PfamPF03770. IPK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio969043.

Entry information

Entry nameKCS1_YEAST
AccessionPrimary (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 16, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

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

Yeast

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

SIMILARITY comments

Index of protein domains and families