P38994 (MSS4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	MSS4
Ordered Locus Names:	YDR208W
ORF Names:	YD8142A.05

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	779 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the phosphorylation of phosphatidylinositol-4-phosphate on the fifth hydroxyl of the myo-inositol ring, to form phosphatidylinositol-4,5-biphosphate. Acts downstream of STT4, but in a pathway that does not involve PKC1. May be involved in the organization of the actin cytoskeleton.
Catalytic activity	ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.
Sequence similarities	Contains 1 PIPK domain.

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ascospore-type prospore assembly Inferred from genetic interaction. Source: SGD
Cellular component	nucleus Inferred from direct assay. Source: SGD plasma membrane Inferred from direct assay. Source: SGD
Molecular function	1-phosphatidylinositol-4-phosphate 5-kinase activity Inferred from direct assay Ref.4. Source: SGD ATP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 779	779	Probable phosphatidylinositol-4-phosphate 5-kinase MSS4		PRO_0000185455
Regions
	Domain	376 – 756	381	PIPK
Amino acid modifications
	Modified residue	222	1	Phosphothreonine Ref.5
	Modified residue	269	1	Phosphoserine Ref.7
	Modified residue	659	1	Phosphothreonine Ref.6 Ref.7
	Modified residue	661	1	Phosphoserine Ref.6 Ref.7
Experimental info
	Sequence conflict	610	1	F → L in BAA02869. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P38994 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: F66B796229CFB8F6	FASTA	779	89,320
	10 20 30 40 50 60 MSVLRSQPPS VVPLHLTTST SRKTEQEPSL LHSAIIERHQ DRSVPNSNSN PDSNHRIKKD 70 80 90 100 110 120 RNNHTSYHSS SNSESNMESP RLSDGESSTP TSIEELNPTI NNSRLVKRNY SISIDPLHDN 130 140 150 160 170 180 SNNNTDDDHP NTITSPRPNS TSNKEMQKYS FPEGKESKKI TTPSLNSNNC LDLDNSSLVH 190 200 210 220 230 240 TDSYIQDLND DHILLNKRVS RRSSRISAVT ATSTTIKQRR NTQDSNLPNI PFHASKHSQI 250 260 270 280 290 300 LPMDDSDVIK LANGDTSMKP NSATKISHSM TSLPLHPLPQ PSQKSKQYHM ISKSTTSLPP 310 320 330 340 350 360 ENDHYYQHSR GTNHNHAANA AAVNNNTTTT TAATGLKRSE SATAEIKKMR QSLLHKREMK 370 380 390 400 410 420 RKRKTFLVDD DRVLIGNKVS EGHVNFIIAY NMLTGIRVAV SRCSGIMKPL TPADFRFTKK 430 440 450 460 470 480 LAFDYHGNEL TPSSQYAFKF KDYCPEVFRE LRALFGLDPA DYLVSLTSKY ILSELNSPGK 490 500 510 520 530 540 SGSFFYYSRD YKYIIKTIHH SEHIHLRKHI QEYYNHVRDN PNTLICQFYG LHRVKMPISF 550 560 570 580 590 600 QNKIKHRKIY FLVMNNLFPP HLDIHITYDL KGSTWGRFTN LDKERLAKDR SYRPVMKDLN 610 620 630 640 650 660 WLEEGQKIKF GPLKKKTFLT QLKKDVELLA KLNTMDYSLL IGIHDINKAK EDDLQLADTA 670 680 690 700 710 720 SIEEQPQTQG PIRTGTGTVV RHFFREFEGG IRASDQFNND VDLIYYVGII DFLTNYSVMK 730 740 750 760 770 KLETFWRSLR HDTKLVSAIP PRDYANRFYE FIEDSVDPLP QKKTQSSYRD DPNQKNYKD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8152413] [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: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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: 9624178] [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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-222, MASS SPECTROMETRY. Strain: ADR376.
[6]	"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 THR-659 AND SER-661, MASS SPECTROMETRY.
[7]	"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-269; THR-659 AND SER-661, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D13716 Genomic DNA. Translation: BAA02869.1. Z68194 Genomic DNA. Translation: CAA92347.1. BK006938 Genomic DNA. Translation: DAA12049.1.
PIR	S61571.
RefSeq	NP_010494.1. NM_001180516.1.
3D structure databases
ProteinModelPortal	P38994.
SMR	P38994. Positions 384-756.
ModBase	Search...
Protein-protein interaction databases
IntAct	P38994. 3 interactions.
MINT	MINT-2731747.
STRING	P38994.
Proteomic databases
PeptideAtlas	P38994.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YDR208W; YDR208W; YDR208W.
GeneID	851789.
KEGG	sce:YDR208W.
NMPDR	fig|4932.3.peg.1247.
Organism-specific databases
CYGD	YDR208w.
SGD	S000002616. MSS4.
Phylogenomic databases
eggNOG	fuNOG07600.
GeneTree	EFGT00050000002191.
HOGENOM	HBG588608.
OMA	SEHIHLR.
OrthoDB	EOG4H49CG.
Gene expression databases
ArrayExpress	P38994.
Genevestigator	P38994.
GermOnline	YDR208W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR023610. PInositol-4-P-5-kinase. IPR002498. PInositol-4-P-5-kinase_core. IPR016034. PInositol-4P-5-kinase_core_sub. [Graphical view]
KO	K00889.
PANTHER	PTHR23086. PIP5K. 1 hit.
Pfam	PF01504. PIP5K. 1 hit. [Graphical view]
SMART	SM00330. PIPKc. 1 hit. [Graphical view]
PROSITE	PS51455. PIPK. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	969609.

Entry information

Entry name

MSS4_YEAST

Accession

Primary (citable) accession number: P38994
Secondary accession number(s): D6VSI9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	October 1, 1996
Last modified:	December 14, 2011
This is version 96 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program