1-phosphatidylinositol 3-phosphate 5-kinase FAB1 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P34756 (FAB1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 128. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
1-phosphatidylinositol 3-phosphate 5-kinase FAB1
Short name=Phosphatidylinositol 3-phosphate 5-kinase
EC=2.7.1.150

Alternative name(s):
Type III PIP kinase
Short name=PIPkin-III

Gene names

Name:	FAB1
Ordered Locus Names:	YFR019W

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	2278 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Catalyzes the phosphorylation of phosphatidylinositol 3-phosphate on the fifth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 3,5-bisphosphate. Required for endocytic-vacuolar pathway and nuclear migration. The product of the reaction it catalyzes functions as an important regulator of vacuole homeostasis perhaps by controlling membrane flux to and/or from the vacuole. Hyperosmotic shock-induced increase in the levels of PtdIns(3,5)P2 requires the presence of VAC7, VAC14, and/or FIG4. Ref.4 Ref.10
Catalytic activity	ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate. Ref.4
Cofactor	Magnesium or manganese.
Enzyme regulation	Activated by VAC14 and VAC7. VAC14 acts as a specific osmotic response regulator. Ref.5 Ref.6
Subunit structure	Component of the PI(3,5)P2 regulatory complex, composed of ATG18, FIG4, FAB1, VAC14 and VAC7. VAC14 nucleates the assembly of the complex and serves as a scaffold. Ref.12 Ref.13
Subcellular location	Vacuole membrane; Peripheral membrane protein. Endosome membrane; Peripheral membrane protein. Note: Localization to the vacuole membrane requires VAC14 and FIG4. Ref.5 Ref.7 Ref.12 Ref.13
Miscellaneous	Present with 149 molecules/cell in log phase SD medium.
Sequence similarities	Contains 1 FYVE-type zinc finger. Contains 1 PIPK domain.

Ontologies

Keywords
Cellular component	Endosome Membrane Vacuole
Domain	Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular protein metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	PAS complex Inferred from direct assay Ref.12. Source: SGD endosome membrane Inferred from direct assay Ref.5 PubMed 9763421. Source: SGD fungal-type vacuole membrane Inferred from direct assay Ref.5 PubMed 9763421. Source: SGD mitochondrion Inferred from direct assay PubMed 14576278 PubMed 16823961. Source: SGD
Molecular_function	1-phosphatidylinositol-3-phosphate 5-kinase activity Inferred from mutant phenotype PubMed 9763421 Ref.4. Source: SGD ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphatidylinositol-3-phosphate binding Inferred from direct assay PubMed 9702203. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2278

2278

1-phosphatidylinositol 3-phosphate 5-kinase FAB1

PRO_0000185451

Regions

Domain

1932 – 2266

335

PIPK

Zinc finger

240 – 299

FYVE-type

Region

1 – 676

676

Required for localization to the vacuole membrane

Region

800 – 1500

701

Mediates interaction with VAC14 and FIG4

Compositional bias

393 – 397

Poly-Pro

Compositional bias

571 – 590

Poly-Asn

Compositional bias

1808 – 1811

Poly-Thr

Compositional bias

1891 – 1897

Poly-Gln

Amino acid modifications

Modified residue

Phosphoserine Ref.9

Modified residue

Phosphoserine Ref.14

Modified residue

186

Phosphoserine Ref.11 Ref.14

Modified residue

202

Phosphoserine Ref.14

Modified residue

206

Phosphothreonine Ref.14

Modified residue

392

Phosphothreonine Ref.9 Ref.14

Modified residue

720

Phosphoserine Ref.14

Modified residue

1691

Phosphothreonine Ref.14

Modified residue

1713

Phosphoserine Ref.14

Modified residue

1953

Phosphothreonine Ref.9 Ref.14

Experimental info

Mutagenesis

262

C → S: Cells show growth at 38 degrees Celsius. Failure to localize to the vacuole membrane. Ref.13

Mutagenesis

864

G → E: Loss of interaction with VAC14. Failure to localize to the vacuole membrane. Ref.12

Mutagenesis

1017

T → I: Cells are defective for growth at 38 degrees Celsius. Ref.13

Mutagenesis

1243

C → A: Cells are defective for growth at 38 degrees Celsius and show single-lobed, enlarged vacuoles. Ref.13

Mutagenesis

2134

D → R: Cells are defective for growth at 38 degrees Celsius. PtdIns(3,5)P2 levels are severely reduced. Ref.13

Sequence conflict

2275

R → W in BAA09258. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P34756 [UniParc].

Last modified September 21, 2011. Version 3.
Checksum: 1A0A30E13165DE41
Show »

FASTA

2,278

257,420

        10         20         30         40         50         60 
MSSEEPHASI SFPDGSHVRS SSTGTSSVNT IDATLSRPNY IKKPSLHIMS TSTTSTTTDL 

        70         80         90        100        110        120 
VTNPILSNIS VPKISPPTSS SIATATSTSH VTGTASHSNI KANANTSTSV NKKNLPPTTS 

       130        140        150        160        170        180 
GRIPSSTIKR YPSRYKPSHS LQLPIKNDSN FKRSSIYASK STVTAIPIRN NRPISMQNSY 

       190        200        210        220        230        240 
ARTPDSDHDD VGDEVSSIKS ASSSLTASLS KSFLFAFYNN RKKDKTSNNG VLSKEYWMKD 

       250        260        270        280        290        300 
ESSKECFSCG KTFNTFRRKH HCRICGQIFC SSCTLLIDGD RFGCHAKMRV CYNCYEHADT 

       310        320        330        340        350        360 
YEDSSDEEND STMQLNEPRS RSRSRSSNTN PYSHSHSHLH LISQDNHNGT DLHDPVAATD 

       370        380        390        400        410        420 
NPQQQNEVYL LNDDDVQSIM TSGEDSKLFI STPPPPPKMA IPATKQGGSL EISFDSENDR 

       430        440        450        460        470        480 
ALHYQDDNPG RHHHLDSVPT RYTIRDMDNI SHYDTNSNST LRPHYNTNNS TITINNLNNT 

       490        500        510        520        530        540 
TSNNSNYNNT NSNSNINNPA HSLRRSIFHY VSSNSVNKDS NNSSATPASS AQSSSILDPA 

       550        560        570        580        590        600 
NRIIGNYAHR NYKFKFNYNS KGPSQQNDTA NGNNDNNNNN NNNNNNNNNN SASGIADNNN 

       610        620        630        640        650        660 
IPSNDNGTTF TLDKKKRNPL TKSKSTSAYL EYPLNEEDSS EDEGSMSIYS VLNDDHKTDN 

       670        680        690        700        710        720 
PIRSMRNSTK SFQRAQASLQ RMRFRRKSKS KHFPNNSKSS IYRDLNFLTN STPNLLSVVS 

       730        740        750        760        770        780 
DDNLYDDSSP LQDKASSSAA SRLTDRKFSN SSGSNNNSNS NSNINTDPWK RIASISGFKL 

       790        800        810        820        830        840 
KKEKKRELNE VSLLHMHALL KQLLNDQEIS NLQEWITLLD GALRKVLRTI LNARDLNTLD 

       850        860        870        880        890        900 
FRQTYVKIKR ISGGSPQNSE YIDGVVFSKA LPSKTMPRHL KNPRILLIMF PLEYQKNNNH 

       910        920        930        940        950        960 
FLSIESVFRQ EREYLDKLVS RLKSLHPDII YVGANVSGYA LELLNDSGIV VQFNMKPQVI 

       970        980        990       1000       1010       1020 
ERIAKLTEAD IAISVDKLAT NIKMGECETF EVKSYIYGNI SKTYTFLRGC NPELGGTILL 

      1030       1040       1050       1060       1070       1080 
RGDSLENLRK IKQVSEFMVY AIFSLKLESS FFNDNFIQLS TDVYLKRAES KKLQVFEGYF 

      1090       1100       1110       1120       1130       1140 
ADFLIKFNNR ILTVSPTVDF PIPFLLEKAR GLEKKLIERI NQYESESDLD RQTQLNMLQG 

      1150       1160       1170       1180       1190       1200 
LESTITKKHL GNLIKFLHEM EIENLELEFQ KRSRQWEVSY SSSQNLLGTG SHQSITVLYS 

      1210       1220       1230       1240       1250       1260 
MVSTKTATPC VGPQIVTIDY FWDSDISIGQ FIENVVGTAR YPCQQGCNGL YLDHYRSYVH 

      1270       1280       1290       1300       1310       1320 
GSGKVDVLIE KFQTRLPKLK DIILTWSYCK KCGTSTPILQ ISEKTWNHSF GKYLEVMFWS 

      1330       1340       1350       1360       1370       1380 
YKDSVTGIGK CPHDFTKDHV KYFGYNDLVV RLEYSDLEVH ELITPPRKIK WKPHIDIKLK 

      1390       1400       1410       1420       1430       1440 
VELYYKILEK INNFYGSVLS RLERIKLDSM TKDKVLSGQA KIIELKSNAT EEQKLMLQDL 

      1450       1460       1470       1480       1490       1500 
DTFYADSPCD QHLPLNLVIK SLYDKAVNWN STFAIFAKSY LPSETDISRI TAKQLKKLFY 

      1510       1520       1530       1540       1550       1560 
DSSRKDSEDK KSLHDEKAKT RKPEKNELPL EGLKDVEKPK IDSKNTTENR DRTNEPQNAV 

      1570       1580       1590       1600       1610       1620 
TITTFKDDTP IIPTSGTSHL TVTPSASSVS SSLTPQTEER PPISRSGTGI SMTHDKSTRP 

      1630       1640       1650       1660       1670       1680 
NIRKMSSDSS LCGLASLANE YSKNNKVSKL ATFFDQMHFD ALSKEFELER ERERLQLNKD 

      1690       1700       1710       1720       1730       1740 
KYQAIRLQTS TPIVEIYKNV KDAVDEPLHS RSSGNNLSSA NVKTLEAPVG EHSRANNCNP 

      1750       1760       1770       1780       1790       1800 
PNLDQNLETE LENSISQWGE NILNPSGKTT ASTHLNSKPV VKETSENPKS IVRESDNSKS 

      1810       1820       1830       1840       1850       1860 
EPLPPVITTT TVNKVESTPQ PEKSLLMKTL SNFWADRSAY LWKPLVYPTC PSEHIFTDSD 

      1870       1880       1890       1900       1910       1920 
VIIREDEPSS LIAFCLSTSD YRNKMMNLNV QQQQQQQTAE AAPAKTGGNS GGTTQTGDPS 

      1930       1940       1950       1960       1970       1980 
VNISPSVSTT SHNKGRDSEI SSLVTTKEGL LNTPPIEGAR DRTPQESQTH SQANLDTLQE 

      1990       2000       2010       2020       2030       2040 
LEKIMTKKTA THLRYQFEEG LTVMSCKIFF TEHFDVFRKI CDCQENFIQS LSRCVKWDSN 

      2050       2060       2070       2080       2090       2100 
GGKSGSGFLK TLDDRFIIKE LSHAELEAFI KFAPSYFEYM AQAMFHDLPT TLAKVFGFYQ 

      2110       2120       2130       2140       2150       2160 
IQVKSSISSS KSYKMDVIIM ENLFYEKKTT RIFDLKGSMR NRHVEQTGKA NEVLLDENMV 

      2170       2180       2190       2200       2210       2220 
EYIYESPIHV REYDKKLLRA SVWNDTLFLA KMNVMDYSLV IGIDNEGYTL TVGIIDFIRT 

      2230       2240       2250       2260       2270 
FTWDKKLESW VKEKGLVGGA SVIKQPTVVT PRQYKKRFRE AMERYILMVP DPWYREGN

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Novel PI(4)P 5-kinase homologue, Fab1p, essential for normal vacuole function and morphology in yeast." Yamamoto A., Dewald D.B., Boronenkov I.V., Anderson R.A., Emr S.D., Koshland D. Mol. Biol. Cell 6:525-539(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Analysis of the nucleotide sequence of chromosome VI from Saccharomyces cerevisiae." Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., Eki T. Nat. Genet. 10:261-268(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 2275. Strain: ATCC 204508 / S288c.
[4]	"The stress-activated phosphatidylinositol 3-phosphate 5-kinase Fab1p is essential for vacuole function in S. cerevisiae." Cooke F.T., Dove S.K., McEwen R.K., Painter G., Holmes A.B., Hall M.N., Michell R.H., Parker P.J. Curr. Biol. 8:1219-1222(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY.
[5]	"Osmotic stress-induced increase of phosphatidylinositol 3,5-bisphosphate requires Vac14p, an activator of the lipid kinase Fab1p." Bonangelino C.J., Nau J.J., Duex J.E., Brinkman M., Wurmser A.E., Gary J.D., Emr S.D., Weisman L.S. J. Cell Biol. 156:1015-1028(2002) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION, SUBCELLULAR LOCATION.
[6]	"Regulation of Fab1 phosphatidylinositol 3-phosphate 5-kinase pathway by Vac7 protein and Fig4, a polyphosphoinositide phosphatase family member." Gary J.D., Sato T.K., Stefan C.J., Bonangelino C.J., Weisman L.S., Emr S.D. Mol. Biol. Cell 13:1238-1251(2002) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[7]	"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].
[8]	"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].
[9]	"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-20; THR-392 AND THR-1953, MASS SPECTROMETRY. Strain: YAL6B.
[10]	"The Vac14p-Fig4p complex acts independently of Vac7p and couples PI3,5P2 synthesis and turnover." Duex J.E., Tang F., Weisman L.S. J. Cell Biol. 172:693-704(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"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-186, MASS SPECTROMETRY.
[12]	"VAC14 nucleates a protein complex essential for the acute interconversion of PI3P and PI(3,5)P(2) in yeast and mouse." Jin N., Chow C.Y., Liu L., Zolov S.N., Bronson R., Davisson M., Petersen J.L., Zhang Y., Park S., Duex J.E., Goldowitz D., Meisler M.H., Weisman L.S. EMBO J. 27:3221-3234(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE PI(3,5)P2 REGULATORY COMPLEX, SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-864.
[13]	"Assembly of a Fab1 phosphoinositide kinase signaling complex requires the Fig4 phosphoinositide phosphatase." Botelho R.J., Efe J.A., Teis D., Emr S.D. Mol. Biol. Cell 19:4273-4286(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE PI(3,5)P2 REGULATORY COMPLEX, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-262; THR-1017; CYS-1243 AND ASP-2134.
[14]	"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-22; SER-186; SER-202; THR-206; THR-392; SER-720; THR-1691; SER-1713 AND THR-1953, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U01017 Genomic DNA. Translation: AAA81360.1. D50617 Genomic DNA. Translation: BAA09258.1. BK006940 Genomic DNA. Translation: DAA12460.2.
PIR	S56274.
RefSeq	NP_116674.2. NM_001179984.2.
3D structure databases
ProteinModelPortal	P34756.
SMR	P34756. Positions 229-299, 813-1046, 2003-2266.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6784N.
IntAct	P34756. 7 interactions.
MINT	MINT-633047.
STRING	4932.YFR019W.
Proteomic databases
PaxDb	P34756.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YFR019W; YFR019W; YFR019W.
GeneID	850574.
KEGG	sce:YFR019W.
Organism-specific databases
SGD	S000001915. FAB1.
Phylogenomic databases
eggNOG	COG0459.
GeneTree	ENSGT00670000097904.
HOGENOM	HOG000141935.
KO	K00921.
OMA	SEEAWEM.
OrthoDB	EOG4TB7KC.
Enzyme and pathway databases
BioCyc	MetaCyc:YFR019W-MONOMER. YEAST:YFR019W-MONOMER.
BRENDA	2.7.1.150. 984.
Gene expression databases
Genevestigator	P34756.
GermOnline	YFR019W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.30.40.10. 1 hit. 3.30.800.10. 1 hit. 3.30.810.10. 2 hits. 3.50.7.10. 1 hit.
InterPro	IPR002423. Cpn60/TCP-1. IPR027409. GroEL-like_apical_dom. 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. IPR000306. Znf_FYVE. IPR017455. Znf_FYVE-rel. IPR011011. Znf_FYVE_PHD. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
PANTHER	PTHR11353. PTHR11353. 1 hit.
Pfam	PF00118. Cpn60_TCP1. 1 hit. PF01363. FYVE. 1 hit. PF01504. PIP5K. 1 hit. [Graphical view]
SMART	SM00064. FYVE. 1 hit. SM00330. PIPKc. 1 hit. [Graphical view]
SUPFAM	SSF57903. FYVE_PHD_ZnF. 1 hit. SSF52029. SSF52029. 1 hit.
PROSITE	PS51455. PIPK. 1 hit. PS50178. ZF_FYVE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	966395.

Entry information

Entry name

FAB1_YEAST

Accession

Primary (citable) accession number: P34756
Secondary accession number(s): D6VTQ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	September 21, 2011
Last modified:	May 29, 2013
This is version 128 of the entry and version 3 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 VI

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

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

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents