Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q12494

- KCS1_YEAST

UniProt

Q12494 - KCS1_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Inositol hexakisphosphate kinase 1

Gene

KCS1

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

Functioni

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.7 Publications

Catalytic activityi

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.

Kineticsi

  1. KM=3.3 µM for InsP61 Publication
  2. KM=1.2 µM for InsP51 Publication

Vmax=2 µmol/min/mg enzyme1 Publication

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. inositol-1,3,4,5,6-pentakisphosphate kinase activity Source: SGD
  3. inositol-1,4,5-trisphosphate 3-kinase activity Source: InterPro
  4. inositol heptakisphosphate 5-kinase activity Source: SGD
  5. inositol heptakisphosphate kinase activity Source: SGD
  6. inositol hexakisphosphate 1-kinase activity Source: UniProtKB-EC
  7. inositol hexakisphosphate 3-kinase activity Source: UniProtKB-EC
  8. inositol hexakisphosphate 5-kinase activity Source: UniProtKB-EC
  9. inositol hexakisphosphate kinase activity Source: SGD

GO - Biological processi

  1. inositol phosphate biosynthetic process Source: SGD
  2. regulation of inositol phosphate biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29635-MONOMER.
YEAST:MONOMER3O-205.
ReactomeiREACT_188940. Synthesis of IPs in the nucleus.
REACT_188944. Synthesis of pyrophosphates in the cytosol.

Names & Taxonomyi

Protein namesi
Recommended name:
Inositol hexakisphosphate kinase 1 (EC:2.7.4.21)
Short name:
InsP6 kinase 1
Alternative name(s):
InsP6 kinase KCS1
PKC1 suppressor protein 1
Gene namesi
Name:KCS1
Ordered Locus Names:YDR017C
ORF Names:PZF1050
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDR017c.
SGDiS000002424. KCS1.

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10501050Inositol hexakisphosphate kinase 1PRO_0000255955Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei150 – 1501Phosphoserine2 Publications
Modified residuei396 – 3961Phosphoserine2 Publications
Modified residuei469 – 4691Phosphoserine1 Publication
Modified residuei537 – 5371Phosphoserine3 Publications
Modified residuei539 – 5391Phosphoserine1 Publication
Modified residuei566 – 5661Phosphoserine1 Publication
Modified residuei583 – 5831Phosphoserine1 Publication
Modified residuei589 – 5891Phosphoserine1 Publication
Modified residuei646 – 6461Phosphoserine1 Publication
Modified residuei664 – 6641Phosphoserine1 Publication
Modified residuei670 – 6701Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ12494.
PaxDbiQ12494.
PeptideAtlasiQ12494.

Expressioni

Gene expression databases

GenevestigatoriQ12494.

Interactioni

Protein-protein interaction databases

BioGridi32067. 277 interactions.
DIPiDIP-1402N.
IntActiQ12494. 5 interactions.
MINTiMINT-397897.

Structurei

3D structure databases

ProteinModelPortaliQ12494.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni772 – 7809Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG274869.
GeneTreeiENSGT00390000014381.
HOGENOMiHOG000001029.
InParanoidiQ12494.
OMAiCATDTEE.
OrthoDBiEOG7T1RKK.

Family and domain databases

InterProiIPR005522. IPK.
[Graphical view]
PANTHERiPTHR12400. PTHR12400. 1 hit.
PfamiPF03770. IPK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12494-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDTSHEIHDK IPDTLREQQQ HLRQKESEGC ITTLKDLNVP ETKKLSSVLH
60 70 80 90 100
GRKASTYLRI FRDDECLADN NNGVDSNNGG SVTCADKITR SEATPKSVPE
110 120 130 140 150
GLQVSEKKNN PDTLSSSLSS FILSNHEEPA IKPNKHVAHR NNITETGQGS
160 170 180 190 200
GEDIAKQQSH QPQVLHHQTS LKPIQNVDEG CISPKSTYQE SLHGISEDLT
210 220 230 240 250
LKPVSSATYY PHKSKADSGY EEKDKMENDI DTIQPATINC ASGIATLPSS
260 270 280 290 300
YNRHTFKVKT YSTLSQSLRQ ENVNNRSNEK KPQQFVPHSE SIKEKPNTFE
310 320 330 340 350
QDKEGEQADE EEDEGDNEHR EYPLAVELKP FTNRVGGHTA IFRFSKRAVC
360 370 380 390 400
KALVNRENRW YENIELCHKE LLQFMPRYIG VLNVRQHFQS KDDFLSDLDQ
410 420 430 440 450
ENNGKNDTSN ENKDIEVNHN NNDDIALNTE PTGTPLTHIH SFPLEHSSRQ
460 470 480 490 500
VLEKEHPEIE SVHPHVKRSL SSSNQPSLLP EVVLNDNRHI IPESLWYKYS
510 520 530 540 550
DSPNSAPNDS YFSSSSSHNS CSFGERGNTN KLKRRDSGST MINTELKNLV
560 570 580 590 600
IREVFAPKCF RRKRNSNTTT MGNHNARLGS SPSFLTQKSR ASSHDASNTS
610 620 630 640 650
MKTLGDSSSQ ASLQMDDSKV NPNLQDPFLK KSLHEKISNA LDGSHSVMDL
660 670 680 690 700
KQFHKNEQIK HKNSFCNSLS PILTATNSRD DGEFATSPNY ISNAQDGVFD
710 720 730 740 750
MDEDTGNETI NMDNHGCHLD SGKNMIIKSL AYNVSNDYSH HDIESITFEE
760 770 780 790 800
TSHTIVSKFI LLEDLTRNMN KPCALDLKMG TRQYGVDAKR AKQLSQRAKC
810 820 830 840 850
LKTTSRRLGV RICGLKVWNK DYYITRDKYF GRRVKVGWQF ARVLARFLYD
860 870 880 890 900
GKTIESLIRQ IPRLIKQLDT LYSEIFNLKG YRLYGASLLL MYDGDANKSN
910 920 930 940 950
SKRKKAANVK VNLIDFARCV TKEDAMECMD KFRIPPKSPN IEDKGFLRGV
960 970 980 990 1000
KSLRFYLLLI WNYLTSDMPL IFDEVEMNDM ISEEADSNSF TSATGSKINF
1010 1020 1030 1040 1050
NSKWDWLDEF DKEDEEMYND PNSKLRQKWR KYELIFDAEP RYNDDAQVSD
Length:1,050
Mass (Da):119,550
Last modified:November 1, 1996 - v1
Checksum:i9C7507CA5F4B0FC7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiS54640.
RefSeqiNP_010300.3. NM_001180325.3.

Genome annotation databases

EnsemblFungiiYDR017C; YDR017C; YDR017C.
GeneIDi851580.
KEGGisce:YDR017C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi S54640.
RefSeqi NP_010300.3. NM_001180325.3.

3D structure databases

ProteinModelPortali Q12494.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32067. 277 interactions.
DIPi DIP-1402N.
IntActi Q12494. 5 interactions.
MINTi MINT-397897.

Proteomic databases

MaxQBi Q12494.
PaxDbi Q12494.
PeptideAtlasi Q12494.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDR017C ; YDR017C ; YDR017C .
GeneIDi 851580.
KEGGi sce:YDR017C.

Organism-specific databases

CYGDi YDR017c.
SGDi S000002424. KCS1.

Phylogenomic databases

eggNOGi NOG274869.
GeneTreei ENSGT00390000014381.
HOGENOMi HOG000001029.
InParanoidi Q12494.
OMAi CATDTEE.
OrthoDBi EOG7T1RKK.

Enzyme and pathway databases

BioCyci YEAST:G3O-29635-MONOMER.
YEAST:MONOMER3O-205.
Reactomei REACT_188940. Synthesis of IPs in the nucleus.
REACT_188944. Synthesis of pyrophosphates in the cytosol.

Miscellaneous databases

NextBioi 969043.

Gene expression databases

Genevestigatori Q12494.

Family and domain databases

InterProi IPR005522. IPK.
[Graphical view ]
PANTHERi PTHR12400. PTHR12400. 1 hit.
Pfami PF03770. IPK. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  9. 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].

Entry informationi

Entry nameiKCS1_YEAST
AccessioniPrimary (citable) accession number: Q12494
Secondary accession number(s): D6VS03, P89899, Q7LGR2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 111 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 1940 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3