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Protein

Probable phosphatidylinositol 4-phosphate 5-kinase MSS4

Gene

MSS4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate on the fifth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 4,5-bisphosphate. Acts downstream of STT4, but in a pathway that does not involve PKC1. May be involved in the organization of the actin cytoskeleton.

Catalytic activityi

ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.

GO - Molecular functioni

  • 1-phosphatidylinositol-4-phosphate 5-kinase activity Source: SGD
  • ATP binding Source: UniProtKB-KW

GO - Biological processi

  • ascospore-type prospore assembly Source: SGD
  • cortical actin cytoskeleton organization Source: CACAO
  • phosphatidylinositol phosphorylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:YDR208W-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable phosphatidylinositol 4-phosphate 5-kinase MSS4 (EC:2.7.1.68)
Alternative name(s):
1-phosphatidylinositol 4-phosphate kinase
Diphosphoinositide kinase
PIP5K
Gene namesi
Name:MSS4
Ordered Locus Names:YDR208W
ORF Names:YD8142A.05
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome IV

Organism-specific databases

CYGDiYDR208w.
EuPathDBiFungiDB:YDR208W.
SGDiS000002616. MSS4.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: SGD
  • plasma membrane Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 779779Probable phosphatidylinositol 4-phosphate 5-kinase MSS4PRO_0000185455Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei207 – 2071Phosphoserine1 Publication
Modified residuei222 – 2221Phosphothreonine2 Publications
Modified residuei225 – 2251Phosphoserine1 Publication
Modified residuei659 – 6591Phosphothreonine2 Publications
Modified residuei661 – 6611Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38994.
PaxDbiP38994.
PeptideAtlasiP38994.

Interactioni

Protein-protein interaction databases

BioGridi32258. 84 interactions.
IntActiP38994. 3 interactions.
MINTiMINT-2731747.
STRINGi4932.YDR208W.

Structurei

3D structure databases

ProteinModelPortaliP38994.
SMRiP38994. Positions 392-752.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini376 – 756381PIPKPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PIPK domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5253.
GeneTreeiENSGT00760000119184.
HOGENOMiHOG000193875.
InParanoidiP38994.
KOiK00889.
OMAiHSEHIHL.
OrthoDBiEOG7XSTPB.

Family and domain databases

Gene3Di3.30.800.10. 1 hit.
3.30.810.10. 1 hit.
InterProiIPR023610. PInositol-4-P-5-kinase.
IPR027483. PInositol-4-P-5-kinase_C.
IPR002498. PInositol-4-P-5-kinase_core.
IPR027484. PInositol-4-P-5-kinase_N.
IPR016034. PInositol-4P-5-kinase_core_sub.
[Graphical view]
PANTHERiPTHR23086. PTHR23086. 1 hit.
PfamiPF01504. PIP5K. 1 hit.
[Graphical view]
SMARTiSM00330. PIPKc. 1 hit.
[Graphical view]
PROSITEiPS51455. PIPK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38994-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVLRSQPPS VVPLHLTTST SRKTEQEPSL LHSAIIERHQ DRSVPNSNSN
60 70 80 90 100
PDSNHRIKKD RNNHTSYHSS SNSESNMESP RLSDGESSTP TSIEELNPTI
110 120 130 140 150
NNSRLVKRNY SISIDPLHDN SNNNTDDDHP NTITSPRPNS TSNKEMQKYS
160 170 180 190 200
FPEGKESKKI TTPSLNSNNC LDLDNSSLVH TDSYIQDLND DHILLNKRVS
210 220 230 240 250
RRSSRISAVT ATSTTIKQRR NTQDSNLPNI PFHASKHSQI LPMDDSDVIK
260 270 280 290 300
LANGDTSMKP NSATKISHSM TSLPLHPLPQ PSQKSKQYHM ISKSTTSLPP
310 320 330 340 350
ENDHYYQHSR GTNHNHAANA AAVNNNTTTT TAATGLKRSE SATAEIKKMR
360 370 380 390 400
QSLLHKREMK RKRKTFLVDD DRVLIGNKVS EGHVNFIIAY NMLTGIRVAV
410 420 430 440 450
SRCSGIMKPL TPADFRFTKK LAFDYHGNEL TPSSQYAFKF KDYCPEVFRE
460 470 480 490 500
LRALFGLDPA DYLVSLTSKY ILSELNSPGK SGSFFYYSRD YKYIIKTIHH
510 520 530 540 550
SEHIHLRKHI QEYYNHVRDN PNTLICQFYG LHRVKMPISF QNKIKHRKIY
560 570 580 590 600
FLVMNNLFPP HLDIHITYDL KGSTWGRFTN LDKERLAKDR SYRPVMKDLN
610 620 630 640 650
WLEEGQKIKF GPLKKKTFLT QLKKDVELLA KLNTMDYSLL IGIHDINKAK
660 670 680 690 700
EDDLQLADTA SIEEQPQTQG PIRTGTGTVV RHFFREFEGG IRASDQFNND
710 720 730 740 750
VDLIYYVGII DFLTNYSVMK KLETFWRSLR HDTKLVSAIP PRDYANRFYE
760 770
FIEDSVDPLP QKKTQSSYRD DPNQKNYKD
Length:779
Mass (Da):89,320
Last modified:October 1, 1996 - v2
Checksum:iF66B796229CFB8F6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti610 – 6101F → L in BAA02869 (PubMed:8152413).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13716 Genomic DNA. Translation: BAA02869.1.
Z68194 Genomic DNA. Translation: CAA92347.1.
BK006938 Genomic DNA. Translation: DAA12049.1.
PIRiS61571.
RefSeqiNP_010494.1. NM_001180516.1.

Genome annotation databases

EnsemblFungiiYDR208W; YDR208W; YDR208W.
GeneIDi851789.
KEGGisce:YDR208W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13716 Genomic DNA. Translation: BAA02869.1.
Z68194 Genomic DNA. Translation: CAA92347.1.
BK006938 Genomic DNA. Translation: DAA12049.1.
PIRiS61571.
RefSeqiNP_010494.1. NM_001180516.1.

3D structure databases

ProteinModelPortaliP38994.
SMRiP38994. Positions 392-752.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32258. 84 interactions.
IntActiP38994. 3 interactions.
MINTiMINT-2731747.
STRINGi4932.YDR208W.

Proteomic databases

MaxQBiP38994.
PaxDbiP38994.
PeptideAtlasiP38994.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR208W; YDR208W; YDR208W.
GeneIDi851789.
KEGGisce:YDR208W.

Organism-specific databases

CYGDiYDR208w.
EuPathDBiFungiDB:YDR208W.
SGDiS000002616. MSS4.

Phylogenomic databases

eggNOGiCOG5253.
GeneTreeiENSGT00760000119184.
HOGENOMiHOG000193875.
InParanoidiP38994.
KOiK00889.
OMAiHSEHIHL.
OrthoDBiEOG7XSTPB.

Enzyme and pathway databases

BioCyciYEAST:YDR208W-MONOMER.

Miscellaneous databases

NextBioi969609.
PROiP38994.

Family and domain databases

Gene3Di3.30.800.10. 1 hit.
3.30.810.10. 1 hit.
InterProiIPR023610. PInositol-4-P-5-kinase.
IPR027483. PInositol-4-P-5-kinase_C.
IPR002498. PInositol-4-P-5-kinase_core.
IPR027484. PInositol-4-P-5-kinase_N.
IPR016034. PInositol-4P-5-kinase_core_sub.
[Graphical view]
PANTHERiPTHR23086. PTHR23086. 1 hit.
PfamiPF01504. PIP5K. 1 hit.
[Graphical view]
SMARTiSM00330. PIPKc. 1 hit.
[Graphical view]
PROSITEiPS51455. PIPK. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genetic interactions among genes involved in the STT4-PKC1 pathway of Saccharomyces cerevisiae."
    Yoshida S., Ohya Y., Nakano A., Anraku Y.
    Mol. Gen. Genet. 242:631-640(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "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.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "MSS4, a phosphatidylinositol-4-phosphate 5-kinase required for organization of the actin cytoskeleton in Saccharomyces cerevisiae."
    Desrivieres S., Cooke F.T., Parker P.J., Hall M.N.
    J. Biol. Chem. 273:15787-15793(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  5. "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 THR-222, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  6. "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 THR-659 AND SER-661, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "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-207; THR-222; SER-225; THR-659 AND SER-661, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMSS4_YEAST
AccessioniPrimary (citable) accession number: P38994
Secondary accession number(s): D6VSI9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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

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 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.