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Protein

1-phosphatidylinositol 3-phosphate 5-kinase FAB1

Gene

FAB1

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

Functioni

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 FIG4.2 Publications

Catalytic activityi

ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate.1 Publication

Cofactori

Enzyme regulationi

Activated by VAC14 and VAC7. VAC14 acts as a specific osmotic response regulator.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri240 – 29960FYVE-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • 1-phosphatidylinositol-3-phosphate 5-kinase activity Source: SGD
  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • phosphatidylinositol-3-phosphate binding Source: SGD

GO - Biological processi

  • phosphatidylinositol phosphorylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:YFR019W-MONOMER.
YEAST:YFR019W-MONOMER.
BRENDAi2.7.1.150. 984.
ReactomeiR-SCE-1660514. Synthesis of PIPs at the Golgi membrane.
R-SCE-1660516. Synthesis of PIPs at the early endosome membrane.
R-SCE-1660517. Synthesis of PIPs at the late endosome membrane.

Chemistry

SwissLipidsiSLP:000000854.

Names & Taxonomyi

Protein namesi
Recommended name:
1-phosphatidylinositol 3-phosphate 5-kinase FAB1 (EC:2.7.1.150)
Short name:
Phosphatidylinositol 3-phosphate 5-kinase
Alternative name(s):
Type III PIP kinase
Short name:
PIPkin-III
Gene namesi
Name:FAB1
Ordered Locus Names:YFR019W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VI

Organism-specific databases

EuPathDBiFungiDB:YFR019W.
SGDiS000001915. FAB1.

Subcellular locationi

GO - Cellular componenti

  • endosome membrane Source: SGD
  • fungal-type vacuole membrane Source: SGD
  • PAS complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Membrane, Vacuole

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi262 – 2621C → S: Cells show growth at 38 degrees Celsius. Failure to localize to the vacuole membrane. 1 Publication
Mutagenesisi864 – 8641G → E: Loss of interaction with VAC14. Failure to localize to the vacuole membrane. 1 Publication
Mutagenesisi1017 – 10171T → I: Cells are defective for growth at 38 degrees Celsius. 1 Publication
Mutagenesisi1243 – 12431C → A: Cells are defective for growth at 38 degrees Celsius and show single-lobed, enlarged vacuoles. 1 Publication
Mutagenesisi2134 – 21341D → R: Cells are defective for growth at 38 degrees Celsius. PtdIns(3,5)P2 levels are severely reduced. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 227822771-phosphatidylinositol 3-phosphate 5-kinase FAB1PRO_0000185451Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei186 – 1861PhosphoserineCombined sources
Modified residuei1627 – 16271PhosphoserineCombined sources
Modified residuei1630 – 16301PhosphoserineCombined sources
Modified residuei1938 – 19381PhosphoserineCombined sources
Modified residuei1953 – 19531PhosphothreonineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP34756.

PTM databases

iPTMnetiP34756.

Interactioni

Subunit structurei

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FIG4P428374EBI-6754,EBI-28407
VAC14Q067089EBI-6754,EBI-27189

Protein-protein interaction databases

BioGridi31172. 221 interactions.
DIPiDIP-6784N.
IntActiP34756. 9 interactions.
MINTiMINT-633047.

Structurei

3D structure databases

ProteinModelPortaliP34756.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1932 – 2266335PIPKPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 676675Required for localization to the vacuole membraneAdd
BLAST
Regioni800 – 1500701Mediates interaction with VAC14 and FIG4Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi393 – 3975Poly-Pro
Compositional biasi571 – 59020Poly-AsnAdd
BLAST
Compositional biasi1808 – 18114Poly-Thr
Compositional biasi1891 – 18977Poly-Gln

Sequence similaritiesi

Contains 1 FYVE-type zinc finger.PROSITE-ProRule annotation
Contains 1 PIPK domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri240 – 29960FYVE-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00840000129741.
HOGENOMiHOG000141935.
InParanoidiP34756.
KOiK00921.
OMAiIPYAQSY.
OrthoDBiEOG776SZ7.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.30.800.10. 1 hit.
3.30.810.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR002423. 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.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
PF01363. FYVE. 1 hit.
PF01504. PIP5K. 1 hit.
[Graphical view]
SMARTiSM00064. FYVE. 1 hit.
SM00330. PIPKc. 1 hit.
[Graphical view]
SUPFAMiSSF52029. SSF52029. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEiPS51455. PIPK. 1 hit.
PS50178. ZF_FYVE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P34756-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSEEPHASI SFPDGSHVRS SSTGTSSVNT IDATLSRPNY IKKPSLHIMS
60 70 80 90 100
TSTTSTTTDL VTNPILSNIS VPKISPPTSS SIATATSTSH VTGTASHSNI
110 120 130 140 150
KANANTSTSV NKKNLPPTTS GRIPSSTIKR YPSRYKPSHS LQLPIKNDSN
160 170 180 190 200
FKRSSIYASK STVTAIPIRN NRPISMQNSY ARTPDSDHDD VGDEVSSIKS
210 220 230 240 250
ASSSLTASLS KSFLFAFYNN RKKDKTSNNG VLSKEYWMKD ESSKECFSCG
260 270 280 290 300
KTFNTFRRKH HCRICGQIFC SSCTLLIDGD RFGCHAKMRV CYNCYEHADT
310 320 330 340 350
YEDSSDEEND STMQLNEPRS RSRSRSSNTN PYSHSHSHLH LISQDNHNGT
360 370 380 390 400
DLHDPVAATD NPQQQNEVYL LNDDDVQSIM TSGEDSKLFI STPPPPPKMA
410 420 430 440 450
IPATKQGGSL EISFDSENDR ALHYQDDNPG RHHHLDSVPT RYTIRDMDNI
460 470 480 490 500
SHYDTNSNST LRPHYNTNNS TITINNLNNT TSNNSNYNNT NSNSNINNPA
510 520 530 540 550
HSLRRSIFHY VSSNSVNKDS NNSSATPASS AQSSSILDPA NRIIGNYAHR
560 570 580 590 600
NYKFKFNYNS KGPSQQNDTA NGNNDNNNNN NNNNNNNNNN SASGIADNNN
610 620 630 640 650
IPSNDNGTTF TLDKKKRNPL TKSKSTSAYL EYPLNEEDSS EDEGSMSIYS
660 670 680 690 700
VLNDDHKTDN PIRSMRNSTK SFQRAQASLQ RMRFRRKSKS KHFPNNSKSS
710 720 730 740 750
IYRDLNFLTN STPNLLSVVS DDNLYDDSSP LQDKASSSAA SRLTDRKFSN
760 770 780 790 800
SSGSNNNSNS NSNINTDPWK RIASISGFKL KKEKKRELNE VSLLHMHALL
810 820 830 840 850
KQLLNDQEIS NLQEWITLLD GALRKVLRTI LNARDLNTLD FRQTYVKIKR
860 870 880 890 900
ISGGSPQNSE YIDGVVFSKA LPSKTMPRHL KNPRILLIMF PLEYQKNNNH
910 920 930 940 950
FLSIESVFRQ EREYLDKLVS RLKSLHPDII YVGANVSGYA LELLNDSGIV
960 970 980 990 1000
VQFNMKPQVI ERIAKLTEAD IAISVDKLAT NIKMGECETF EVKSYIYGNI
1010 1020 1030 1040 1050
SKTYTFLRGC NPELGGTILL RGDSLENLRK IKQVSEFMVY AIFSLKLESS
1060 1070 1080 1090 1100
FFNDNFIQLS TDVYLKRAES KKLQVFEGYF ADFLIKFNNR ILTVSPTVDF
1110 1120 1130 1140 1150
PIPFLLEKAR GLEKKLIERI NQYESESDLD RQTQLNMLQG LESTITKKHL
1160 1170 1180 1190 1200
GNLIKFLHEM EIENLELEFQ KRSRQWEVSY SSSQNLLGTG SHQSITVLYS
1210 1220 1230 1240 1250
MVSTKTATPC VGPQIVTIDY FWDSDISIGQ FIENVVGTAR YPCQQGCNGL
1260 1270 1280 1290 1300
YLDHYRSYVH GSGKVDVLIE KFQTRLPKLK DIILTWSYCK KCGTSTPILQ
1310 1320 1330 1340 1350
ISEKTWNHSF GKYLEVMFWS YKDSVTGIGK CPHDFTKDHV KYFGYNDLVV
1360 1370 1380 1390 1400
RLEYSDLEVH ELITPPRKIK WKPHIDIKLK VELYYKILEK INNFYGSVLS
1410 1420 1430 1440 1450
RLERIKLDSM TKDKVLSGQA KIIELKSNAT EEQKLMLQDL DTFYADSPCD
1460 1470 1480 1490 1500
QHLPLNLVIK SLYDKAVNWN STFAIFAKSY LPSETDISRI TAKQLKKLFY
1510 1520 1530 1540 1550
DSSRKDSEDK KSLHDEKAKT RKPEKNELPL EGLKDVEKPK IDSKNTTENR
1560 1570 1580 1590 1600
DRTNEPQNAV TITTFKDDTP IIPTSGTSHL TVTPSASSVS SSLTPQTEER
1610 1620 1630 1640 1650
PPISRSGTGI SMTHDKSTRP NIRKMSSDSS LCGLASLANE YSKNNKVSKL
1660 1670 1680 1690 1700
ATFFDQMHFD ALSKEFELER ERERLQLNKD KYQAIRLQTS TPIVEIYKNV
1710 1720 1730 1740 1750
KDAVDEPLHS RSSGNNLSSA NVKTLEAPVG EHSRANNCNP PNLDQNLETE
1760 1770 1780 1790 1800
LENSISQWGE NILNPSGKTT ASTHLNSKPV VKETSENPKS IVRESDNSKS
1810 1820 1830 1840 1850
EPLPPVITTT TVNKVESTPQ PEKSLLMKTL SNFWADRSAY LWKPLVYPTC
1860 1870 1880 1890 1900
PSEHIFTDSD VIIREDEPSS LIAFCLSTSD YRNKMMNLNV QQQQQQQTAE
1910 1920 1930 1940 1950
AAPAKTGGNS GGTTQTGDPS VNISPSVSTT SHNKGRDSEI SSLVTTKEGL
1960 1970 1980 1990 2000
LNTPPIEGAR DRTPQESQTH SQANLDTLQE LEKIMTKKTA THLRYQFEEG
2010 2020 2030 2040 2050
LTVMSCKIFF TEHFDVFRKI CDCQENFIQS LSRCVKWDSN GGKSGSGFLK
2060 2070 2080 2090 2100
TLDDRFIIKE LSHAELEAFI KFAPSYFEYM AQAMFHDLPT TLAKVFGFYQ
2110 2120 2130 2140 2150
IQVKSSISSS KSYKMDVIIM ENLFYEKKTT RIFDLKGSMR NRHVEQTGKA
2160 2170 2180 2190 2200
NEVLLDENMV EYIYESPIHV REYDKKLLRA SVWNDTLFLA KMNVMDYSLV
2210 2220 2230 2240 2250
IGIDNEGYTL TVGIIDFIRT FTWDKKLESW VKEKGLVGGA SVIKQPTVVT
2260 2270
PRQYKKRFRE AMERYILMVP DPWYREGN
Length:2,278
Mass (Da):257,420
Last modified:September 21, 2011 - v3
Checksum:i1A0A30E13165DE41
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2275 – 22751R → W in BAA09258 (PubMed:7670463).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01017 Genomic DNA. Translation: AAA81360.1.
D50617 Genomic DNA. Translation: BAA09258.1.
BK006940 Genomic DNA. Translation: DAA12460.2.
PIRiS56274.
RefSeqiNP_116674.2. NM_001179984.2.

Genome annotation databases

EnsemblFungiiBAA09258; BAA09258; BAA09258.
YFR019W; YFR019W; YFR019W.
GeneIDi850574.
KEGGisce:YFR019W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01017 Genomic DNA. Translation: AAA81360.1.
D50617 Genomic DNA. Translation: BAA09258.1.
BK006940 Genomic DNA. Translation: DAA12460.2.
PIRiS56274.
RefSeqiNP_116674.2. NM_001179984.2.

3D structure databases

ProteinModelPortaliP34756.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31172. 221 interactions.
DIPiDIP-6784N.
IntActiP34756. 9 interactions.
MINTiMINT-633047.

Chemistry

SwissLipidsiSLP:000000854.

PTM databases

iPTMnetiP34756.

Proteomic databases

MaxQBiP34756.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiBAA09258; BAA09258; BAA09258.
YFR019W; YFR019W; YFR019W.
GeneIDi850574.
KEGGisce:YFR019W.

Organism-specific databases

EuPathDBiFungiDB:YFR019W.
SGDiS000001915. FAB1.

Phylogenomic databases

GeneTreeiENSGT00840000129741.
HOGENOMiHOG000141935.
InParanoidiP34756.
KOiK00921.
OMAiIPYAQSY.
OrthoDBiEOG776SZ7.

Enzyme and pathway databases

BioCyciMetaCyc:YFR019W-MONOMER.
YEAST:YFR019W-MONOMER.
BRENDAi2.7.1.150. 984.
ReactomeiR-SCE-1660514. Synthesis of PIPs at the Golgi membrane.
R-SCE-1660516. Synthesis of PIPs at the early endosome membrane.
R-SCE-1660517. Synthesis of PIPs at the late endosome membrane.

Miscellaneous databases

PROiP34756.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
3.30.800.10. 1 hit.
3.30.810.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR002423. 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.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF00118. Cpn60_TCP1. 1 hit.
PF01363. FYVE. 1 hit.
PF01504. PIP5K. 1 hit.
[Graphical view]
SMARTiSM00064. FYVE. 1 hit.
SM00330. PIPKc. 1 hit.
[Graphical view]
SUPFAMiSSF52029. SSF52029. 1 hit.
SSF57903. SSF57903. 1 hit.
PROSITEiPS51455. PIPK. 1 hit.
PS50178. ZF_FYVE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "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.
  10. "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.
  11. "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.
  12. "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-1953, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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-186; SER-1627; SER-1630 AND SER-1938, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFAB1_YEAST
AccessioniPrimary (citable) accession number: P34756
Secondary accession number(s): D6VTQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: September 21, 2011
Last modified: June 8, 2016
This is version 159 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 149 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 VI
    Yeast (Saccharomyces cerevisiae) chromosome VI: entries and gene names

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 one 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.