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Entry version 207 (03 Jul 2019)
Sequence version 2 (15 May 2002)
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Protein

Fatty acid synthase subunit alpha

Gene

FAS2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. This subunit coordinates the binding of the six beta subunits to the enzyme complex.

Miscellaneous

Present with 17000 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by cerulenin by covalent binding to active site of the ketoacyl synthase (KS) region.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1305For beta-ketoacyl synthase activity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi1772Magnesium1
Metal bindingi1773Magnesium; via carbonyl oxygen1
Metal bindingi1774Magnesium1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei1798Acetyl-CoA1 Publication1
Binding sitei1808Acetyl-CoA1 Publication1
Metal bindingi1872Magnesium1
Metal bindingi1873Magnesium; via carbonyl oxygen1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionMultifunctional enzyme, Oxidoreductase, Transferase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandMagnesium, Metal-binding, NAD, NADP

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:YPL231W-MONOMER
YEAST:YPL231W-MONOMER

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P19097

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Fatty acid synthase subunit alpha (EC:2.3.1.86)
Including the following 3 domains:
Acyl carrier
3-oxoacyl-[acyl-carrier-protein] reductase (EC:1.1.1.100)
Alternative name(s):
Beta-ketoacyl reductase
3-oxoacyl-[acyl-carrier-protein] synthase (EC:2.3.1.41)
Alternative name(s):
Beta-ketoacyl synthase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:FAS2
Ordered Locus Names:YPL231W
ORF Names:P1409
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome XVI

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YPL231W

Saccharomyces Genome Database

More...
SGDi
S000006152 FAS2

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi1250G → S: Cerulenin-resistance. 1 Publication1
Mutagenesisi1769V → D: Does not affect oligomerization; when associated with S-1771 and L-1773 or S-1771; L-1773; S-1879 and E-1881. 1 Publication1
Mutagenesisi1770G → D: Loss of transferase activity. 1 Publication1
Mutagenesisi1771V → S: Does not affect oligomerization but lacks transferase activity; when associated with D-1769 and L-1773 or D-1769; L-1773; S-1879 and E-1881. 1 Publication1
Mutagenesisi1772D → S: Loss of transferase activity; when associated with S-1774. 1 Publication1
Mutagenesisi1773V → L: Does not affect oligomerization but lacks transferase activity; when associated with D-1769 and S-1771 or D-1769; S-1771; S-1879 and E-1881. 1 Publication1
Mutagenesisi1774E → S: Loss of transferase activity; when associated with S-1772. 1 Publication1
Mutagenesisi1841R → A: Loss off transferase activity. 1 Publication1
Mutagenesisi1879V → S: Does not affect oligomerization but lacks transferase activity; when associated with D-1769; S-1771; L-1773 and E-1881. 1 Publication1
Mutagenesisi1881V → E: Does not affect oligomerization but lacks transferase activity; when associated with D-1769; S-1771; L-1773 and S-1879. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001802871 – 1887Fatty acid synthase subunit alphaAdd BLAST1887

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki37Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei50PhosphoserineCombined sources1
Modified residuei180O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1 Publication1
Modified residuei523PhosphoserineCombined sources1
Modified residuei958PhosphoserineCombined sources1
Modified residuei1440PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

4'-phosphopantetheine is transferred from CoA to a specific serine of the Acyl carrier domain by the C-terminal PPT domain. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.

Keywords - PTMi

Isopeptide bond, Phosphopantetheine, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P19097

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P19097

PRoteomics IDEntifications database

More...
PRIDEi
P19097

Consortium for Top Down Proteomics

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TopDownProteomicsi
P19097

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P19097

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

[Alpha6beta6] hexamers of two multifunctional subunits (alpha and beta).

4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
FAS1P071498EBI-6806,EBI-6795

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
35931, 384 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-1162 Fatty-acyl-CoA synthase

Database of interacting proteins

More...
DIPi
DIP-960N

Protein interaction database and analysis system

More...
IntActi
P19097, 20 interactors

Molecular INTeraction database

More...
MINTi
P19097

STRING: functional protein association networks

More...
STRINGi
4932.YPL231W

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11887
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P19097

Database of comparative protein structure models

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ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P19097

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini145 – 220CarrierPROSITE-ProRule annotationAdd BLAST76

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni675 – 874Beta-ketoacyl reductaseAdd BLAST200
Regioni1149 – 1363Beta-ketoacyl synthaseAdd BLAST215
Regioni1772 – 1774Acetyl-CoA binding3
Regioni1817 – 1833Acetyl-CoA bindingAdd BLAST17
Regioni1841 – 1844Acetyl-CoA binding4
Regioni1871 – 1873Acetyl-CoA binding3

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000176444

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000177974

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P19097

KEGG Orthology (KO)

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KOi
K00667

Identification of Orthologs from Complete Genome Data

More...
OMAi
NRWHSES

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.40.47.10, 3 hits
3.90.470.20, 1 hit

HAMAP database of protein families

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HAMAPi
MF_00101 AcpS, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR008278 4-PPantetheinyl_Trfase_dom
IPR037143 4-PPantetheinyl_Trfase_dom_sf
IPR002582 ACPS
IPR016035 Acyl_Trfase/lysoPLipase
IPR040899 Fas_alpha_ACP
IPR026025 FAS_alpha_yeast
IPR041550 FASI_helical
IPR018201 Ketoacyl_synth_AS
IPR014031 Ketoacyl_synth_C
IPR014030 Ketoacyl_synth_N
IPR036291 NAD(P)-bd_dom_sf
IPR009081 PP-bd_ACP
IPR004568 Ppantetheine-prot_Trfase_dom
IPR016039 Thiolase-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01648 ACPS, 1 hit
PF18325 Fas_alpha_ACP, 1 hit
PF18314 FAS_I_H, 1 hit
PF00109 ketoacyl-synt, 1 hit
PF02801 Ketoacyl-synt_C, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000454 FAS_yeast_alpha, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51735 SSF51735, 1 hit
SSF52151 SSF52151, 1 hit
SSF53901 SSF53901, 2 hits
SSF56214 SSF56214, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00556 pantethn_trn, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00606 B_KETOACYL_SYNTHASE, 1 hit
PS50075 CARRIER, 1 hit
PS00012 PHOSPHOPANTETHEINE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P19097-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKPEVEQELA HILLTELLAY QFASPVRWIE TQDVFLKDFN TERVVEIGPS
60 70 80 90 100
PTLAGMAQRT LKNKYESYDA ALSLHREILC YSKDAKEIYY TPDPSELAAK
110 120 130 140 150
EEPAKEEAPA PTPAASAPAP AAAAPAPVAA AAPAAAAAEI ADEPVKASLL
160 170 180 190 200
LHVLVAHKLK KSLDSIPMSK TIKDLVGGKS TVQNEILGDL GKEFGTTPEK
210 220 230 240 250
PEETPLEELA ETFQDTFSGA LGKQSSSLLS RLISSKMPGG FTITVARKYL
260 270 280 290 300
QTRWGLPSGR QDGVLLVALS NEPAARLGSE ADAKAFLDSM AQKYASIVGV
310 320 330 340 350
DLSSAASASG AAGAGAAAGA AMIDAGALEE ITKDHKVLAR QQLQVLARYL
360 370 380 390 400
KMDLDNGERK FLKEKDTVAE LQAQLDYLNA ELGEFFVNGV ATSFSRKKAR
410 420 430 440 450
TFDSSWNWAK QSLLSLYFEI IHGVLKNVDR EVVSEAINIM NRSNDALIKF
460 470 480 490 500
MEYHISNTDE TKGENYQLVK TLGEQLIENC KQVLDVDPVY KDVAKPTGPK
510 520 530 540 550
TAIDKNGNIT YSEEPREKVR KLSQYVQEMA LGGPITKESQ PTIEEDLTRV
560 570 580 590 600
YKAISAQADK QDISSSTRVE FEKLYSDLMK FLESSKEIDP SQTTQLAGMD
610 620 630 640 650
VEDALDKDST KEVASLPNKS TISKTVSSTI PRETIPFLHL RKKTPAGDWK
660 670 680 690 700
YDRQLSSLFL DGLEKAAFNG VTFKDKYVLI TGAGKGSIGA EVLQGLLQGG
710 720 730 740 750
AKVVVTTSRF SKQVTDYYQS IYAKYGAKGS TLIVVPFNQG SKQDVEALIE
760 770 780 790 800
FIYDTEKNGG LGWDLDAIIP FAAIPEQGIE LEHIDSKSEF AHRIMLTNIL
810 820 830 840 850
RMMGCVKKQK SARGIETRPA QVILPMSPNH GTFGGDGMYS ESKLSLETLF
860 870 880 890 900
NRWHSESWAN QLTVCGAIIG WTRGTGLMSA NNIIAEGIEK MGVRTFSQKE
910 920 930 940 950
MAFNLLGLLT PEVVELCQKS PVMADLNGGL QFVPELKEFT AKLRKELVET
960 970 980 990 1000
SEVRKAVSIE TALEHKVVNG NSADAAYAQV EIQPRANIQL DFPELKPYKQ
1010 1020 1030 1040 1050
VKQIAPAELE GLLDLERVIV VTGFAEVGPW GSARTRWEME AFGEFSLEGC
1060 1070 1080 1090 1100
VEMAWIMGFI SYHNGNLKGR PYTGWVDSKT KEPVDDKDVK AKYETSILEH
1110 1120 1130 1140 1150
SGIRLIEPEL FNGYNPEKKE MIQEVIVEED LEPFEASKET AEQFKHQHGD
1160 1170 1180 1190 1200
KVDIFEIPET GEYSVKLLKG ATLYIPKALR FDRLVAGQIP TGWNAKTYGI
1210 1220 1230 1240 1250
SDDIISQVDP ITLFVLVSVV EAFIASGITD PYEMYKYVHV SEVGNCSGSG
1260 1270 1280 1290 1300
MGGVSALRGM FKDRFKDEPV QNDILQESFI NTMSAWVNML LISSSGPIKT
1310 1320 1330 1340 1350
PVGACATSVE SVDIGVETIL SGKARICIVG GYDDFQEEGS FEFGNMKATS
1360 1370 1380 1390 1400
NTLEEFEHGR TPAEMSRPAT TTRNGFMEAQ GAGIQIIMQA DLALKMGVPI
1410 1420 1430 1440 1450
YGIVAMAATA TDKIGRSVPA PGKGILTTAR EHHSSVKYAS PNLNMKYRKR
1460 1470 1480 1490 1500
QLVTREAQIK DWVENELEAL KLEAEEIPSE DQNEFLLERT REIHNEAESQ
1510 1520 1530 1540 1550
LRAAQQQWGN DFYKRDPRIA PLRGALATYG LTIDDLGVAS FHGTSTKAND
1560 1570 1580 1590 1600
KNESATINEM MKHLGRSEGN PVIGVFQKFL TGHPKGAAGA WMMNGALQIL
1610 1620 1630 1640 1650
NSGIIPGNRN ADNVDKILEQ FEYVLYPSKT LKTDGVRAVS ITSFGFGQKG
1660 1670 1680 1690 1700
GQAIVVHPDY LYGAITEDRY NEYVAKVSAR EKSAYKFFHN GMIYNKLFVS
1710 1720 1730 1740 1750
KEHAPYTDEL EEDVYLDPLA RVSKDKKSGS LTFNSKNIQS KDSYINANTI
1760 1770 1780 1790 1800
ETAKMIENMT KEKVSNGGVG VDVELITSIN VENDTFIERN FTPQEIEYCS
1810 1820 1830 1840 1850
AQPSVQSSFA GTWSAKEAVF KSLGVKSLGG GAALKDIEIV RVNKNAPAVE
1860 1870 1880
LHGNAKKAAE EAGVTDVKVS ISHDDLQAVA VAVSTKK
Length:1,887
Mass (Da):206,947
Last modified:May 15, 2002 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i08B872734CF3AEEA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti310G → GTTGTGG in AAA34601 (PubMed:2900835).Curated1
Sequence conflicti594T → I in AAA34601 (PubMed:2900835).Curated1
Sequence conflicti941 – 1019AKLRK…LERVI → CLNCVKSWLKLLKLERQFPS KLLWSIRLSMAIALMLHMLK SKFNQELTFNWTSQNRNHTN RLNKLLPLSLRVCWIWKELF in AAA34601 (PubMed:2900835).CuratedAdd BLAST79
Sequence conflicti1036 – 1041RWEMEA → KMGNGS in AAA34601 (PubMed:2900835).Curated6
Sequence conflicti1408A → S in AAA34601 (PubMed:2900835).Curated1
Sequence conflicti1671N → T in AAA34601 (PubMed:2900835).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
J03936 Genomic DNA Translation: AAA34601.1
X76890 Genomic DNA Translation: CAA54218.1
X94561 Genomic DNA Translation: CAA64256.1
Z73586 Genomic DNA Translation: CAA97947.1
Z73587 Genomic DNA Translation: CAA97948.1
BK006949 Genomic DNA Translation: DAA11205.1

Protein sequence database of the Protein Information Resource

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PIRi
S61703

NCBI Reference Sequences

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RefSeqi
NP_015093.1, NM_001184045.1

Genome annotation databases

Ensembl fungal genome annotation project

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EnsemblFungii
YPL231W_mRNA; YPL231W_mRNA; YPL231W

Database of genes from NCBI RefSeq genomes

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GeneIDi
855845

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YPL231W

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03936 Genomic DNA Translation: AAA34601.1
X76890 Genomic DNA Translation: CAA54218.1
X94561 Genomic DNA Translation: CAA64256.1
Z73586 Genomic DNA Translation: CAA97947.1
Z73587 Genomic DNA Translation: CAA97948.1
BK006949 Genomic DNA Translation: DAA11205.1
PIRiS61703
RefSeqiNP_015093.1, NM_001184045.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ML8NMR-A138-302[»]
2PFFX-ray4.00A/D/G671-1744[»]
2UV8X-ray3.10A/B/C1-1887[»]
2VKZX-ray4.00A/B/C1-1887[»]
2WASX-ray1.90A/B/C/D/E/F1766-1887[»]
2WATX-ray2.20A/B/C/D/E/F1766-1887[»]
3HMJX-ray4.00A/B/C1-1887[»]
SMRiP19097
ModBaseiSearch...

Protein-protein interaction databases

BioGridi35931, 384 interactors
ComplexPortaliCPX-1162 Fatty-acyl-CoA synthase
DIPiDIP-960N
IntActiP19097, 20 interactors
MINTiP19097
STRINGi4932.YPL231W

PTM databases

iPTMnetiP19097

Proteomic databases

MaxQBiP19097
PaxDbiP19097
PRIDEiP19097
TopDownProteomicsiP19097

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL231W_mRNA; YPL231W_mRNA; YPL231W
GeneIDi855845
KEGGisce:YPL231W

Organism-specific databases

EuPathDBiFungiDB:YPL231W
SGDiS000006152 FAS2

Phylogenomic databases

GeneTreeiENSGT00940000176444
HOGENOMiHOG000177974
InParanoidiP19097
KOiK00667
OMAiNRWHSES

Enzyme and pathway databases

BioCyciMetaCyc:YPL231W-MONOMER
YEAST:YPL231W-MONOMER
SABIO-RKiP19097

Miscellaneous databases

EvolutionaryTraceiP19097

Protein Ontology

More...
PROi
PR:P19097

Family and domain databases

Gene3Di3.40.47.10, 3 hits
3.90.470.20, 1 hit
HAMAPiMF_00101 AcpS, 1 hit
InterProiView protein in InterPro
IPR008278 4-PPantetheinyl_Trfase_dom
IPR037143 4-PPantetheinyl_Trfase_dom_sf
IPR002582 ACPS
IPR016035 Acyl_Trfase/lysoPLipase
IPR040899 Fas_alpha_ACP
IPR026025 FAS_alpha_yeast
IPR041550 FASI_helical
IPR018201 Ketoacyl_synth_AS
IPR014031 Ketoacyl_synth_C
IPR014030 Ketoacyl_synth_N
IPR036291 NAD(P)-bd_dom_sf
IPR009081 PP-bd_ACP
IPR004568 Ppantetheine-prot_Trfase_dom
IPR016039 Thiolase-like
PfamiView protein in Pfam
PF01648 ACPS, 1 hit
PF18325 Fas_alpha_ACP, 1 hit
PF18314 FAS_I_H, 1 hit
PF00109 ketoacyl-synt, 1 hit
PF02801 Ketoacyl-synt_C, 1 hit
PIRSFiPIRSF000454 FAS_yeast_alpha, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
SSF52151 SSF52151, 1 hit
SSF53901 SSF53901, 2 hits
SSF56214 SSF56214, 1 hit
TIGRFAMsiTIGR00556 pantethn_trn, 1 hit
PROSITEiView protein in PROSITE
PS00606 B_KETOACYL_SYNTHASE, 1 hit
PS50075 CARRIER, 1 hit
PS00012 PHOSPHOPANTETHEINE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFAS2_YEAST
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P19097
Secondary accession number(s): D6W3D9, Q12533
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: May 15, 2002
Last modified: July 3, 2019
This is version 207 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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