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Entry version 197 (03 Jul 2019)
Sequence version 2 (01 Feb 1994)
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Protein

Fatty acid synthase subunit beta

Gene

FAS1

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 beta subunit contains domains for: [acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase.

Miscellaneous

Present with 91800 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

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 sitei274For acetyltransferase activityBy similarity1
Active sitei1808For malonyltransferase activityBy similarity1

<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 functionHydrolase, Lyase, Multifunctional enzyme, Oxidoreductase, Transferase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandNAD, NADP

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:YKL182W-MONOMER
YEAST:YKL182W-MONOMER

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P07149

<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 beta (EC:2.3.1.86)
Including the following 5 domains:
3-hydroxyacyl-[acyl-carrier-protein] dehydratase (EC:4.2.1.59)
Enoyl-[acyl-carrier-protein] reductase [NADH] (EC:1.3.1.9)
[Acyl-carrier-protein] acetyltransferase (EC:2.3.1.38)
[Acyl-carrier-protein] malonyltransferase (EC:2.3.1.39)
S-acyl fatty acid synthase thioesterase (EC:3.1.2.14)
<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:FAS1
Ordered Locus Names:YKL182W
<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 XI

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YKL182W

Saccharomyces Genome Database

More...
SGDi
S000001665 FAS1

<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 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_00001802821 – 2051Fatty acid synthase subunit betaAdd BLAST2051

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei1N-acetylmethionineCombined sources1
Modified residuei733PhosphothreonineCombined sources1
Modified residuei1121PhosphoserineCombined sources1
<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-linki1364Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P07149

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

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PaxDbi
P07149

PRoteomics IDEntifications database

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PRIDEi
P07149

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
P07149

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P07149

<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).

<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
FAS2P190978EBI-6795,EBI-6806

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
33940, 95 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-1162 Fatty-acyl-CoA synthase

Database of interacting proteins

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DIPi
DIP-742N

Protein interaction database and analysis system

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IntActi
P07149, 101 interactors

Molecular INTeraction database

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MINTi
P07149

STRING: functional protein association networks

More...
STRINGi
4932.YKL182W

<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

12051
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

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SMRi
P07149

Database of comparative protein structure models

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ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P07149

<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>Domaini1523 – 1648MaoC-likeAdd BLAST126

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>Regioni1 – 468AcetyltransferaseAdd BLAST468
Regioni480 – 868Enoyl reductaseAdd BLAST389
Regioni1144 – 1626DehydrataseAdd BLAST483
Regioni1627 – 1845Malonyl/palmitoyl transferaseAdd BLAST219

<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

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GeneTreei
ENSGT00940000176444

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000177963

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P07149

KEGG Orthology (KO)

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KOi
K00668

Identification of Orthologs from Complete Genome Data

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OMAi
GVLTHRN

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.20.20.70, 2 hits
3.40.366.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR001227 Ac_transferase_dom_sf
IPR014043 Acyl_transferase
IPR016035 Acyl_Trfase/lysoPLipase
IPR013785 Aldolase_TIM
IPR013565 DUF1729
IPR041099 FAS1_N
IPR040883 FAS_meander
IPR003965 Fatty_acid_synthase
IPR016452 Fatty_acid_Synthase_bsu_fun
IPR029069 HotDog_dom_sf
IPR039569 MaoC-like_dehydrat_N
IPR002539 MaoC-like_dom
IPR020801 PKS_acyl_transferase
IPR032088 SAT

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00698 Acyl_transf_1, 1 hit
PF08354 DUF1729, 1 hit
PF17951 FAS_meander, 1 hit
PF17828 FAS_N, 1 hit
PF13452 MaoC_dehydrat_N, 1 hit
PF01575 MaoC_dehydratas, 1 hit
PF16073 SAT, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF005562 FAS_yeast_beta, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01483 FASYNTHASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00827 PKS_AT, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52151 SSF52151, 2 hits
SSF54637 SSF54637, 2 hits

<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.

P07149-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDAYSTRPLT LSHGSLEHVL LVPTASFFIA SQLQEQFNKI LPEPTEGFAA
60 70 80 90 100
DDEPTTPAEL VGKFLGYVSS LVEPSKVGQF DQVLNLCLTE FENCYLEGND
110 120 130 140 150
IHALAAKLLQ ENDTTLVKTK ELIKNYITAR IMAKRPFDKK SNSALFRAVG
160 170 180 190 200
EGNAQLVAIF GGQGNTDDYF EELRDLYQTY HVLVGDLIKF SAETLSELIR
210 220 230 240 250
TTLDAEKVFT QGLNILEWLE NPSNTPDKDY LLSIPISCPL IGVIQLAHYV
260 270 280 290 300
VTAKLLGFTP GELRSYLKGA TGHSQGLVTA VAIAETDSWE SFFVSVRKAI
310 320 330 340 350
TVLFFIGVRC YEAYPNTSLP PSILEDSLEN NEGVPSPMLS ISNLTQEQVQ
360 370 380 390 400
DYVNKTNSHL PAGKQVEISL VNGAKNLVVS GPPQSLYGLN LTLRKAKAPS
410 420 430 440 450
GLDQSRIPFS ERKLKFSNRF LPVASPFHSH LLVPASDLIN KDLVKNNVSF
460 470 480 490 500
NAKDIQIPVY DTFDGSDLRV LSGSISERIV DCIIRLPVKW ETTTQFKATH
510 520 530 540 550
ILDFGPGGAS GLGVLTHRNK DGTGVRVIVA GTLDINPDDD YGFKQEIFDV
560 570 580 590 600
TSNGLKKNPN WLEEYHPKLI KNKSGKIFVE TKFSKLIGRP PLLVPGMTPC
610 620 630 640 650
TVSPDFVAAT TNAGYTIELA GGGYFSAAGM TAAIDSVVSQ IEKGSTFGIN
660 670 680 690 700
LIYVNPFMLQ WGIPLIKELR SKGYPIQFLT IGAGVPSLEV ASEYIETLGL
710 720 730 740 750
KYLGLKPGSI DAISQVINIA KAHPNFPIAL QWTGGRGGGH HSFEDAHTPM
760 770 780 790 800
LQMYSKIRRH PNIMLIFGSG FGSADDTYPY LTGEWSTKFD YPPMPFDGFL
810 820 830 840 850
FGSRVMIAKE VKTSPDAKKC IAACTGVPDD KWEQTYKKPT GGIVTVRSEM
860 870 880 890 900
GEPIHKIATR GVMLWKEFDE TIFNLPKNKL VPTLEAKRDY IISRLNADFQ
910 920 930 940 950
KPWFATVNGQ ARDLATMTYE EVAKRLVELM FIRSTNSWFD VTWRTFTGDF
960 970 980 990 1000
LRRVEERFTK SKTLSLIQSY SLLDKPDEAI EKVFNAYPAA REQFLNAQDI
1010 1020 1030 1040 1050
DHFLSMCQNP MQKPVPFVPV LDRRFEIFFK KDSLWQSEHL EAVVDQDVQR
1060 1070 1080 1090 1100
TCILHGPVAA QFTKVIDEPI KSIMDGIHDG HIKKLLHQYY GDDESKIPAV
1110 1120 1130 1140 1150
EYFGGESPVD VQSQVDSSSV SEDSAVFKAT SSTDEESWFK ALAGSEINWR
1160 1170 1180 1190 1200
HASFLCSFIT QDKMFVSNPI RKVFKPSQGM VVEISNGNTS SKTVVTLSEP
1210 1220 1230 1240 1250
VQGELKPTVI LKLLKENIIQ MEMIENRTMD GKPVSLPLLY NFNPDNGFAP
1260 1270 1280 1290 1300
ISEVMEDRNQ RIKEMYWKLW IDEPFNLDFD PRDVIKGKDF EITAKEVYDF
1310 1320 1330 1340 1350
THAVGNNCED FVSRPDRTML APMDFAIVVG WRAIIKAIFP NTVDGDLLKL
1360 1370 1380 1390 1400
VHLSNGYKMI PGAKPLQVGD VVSTTAVIES VVNQPTGKIV DVVGTLSRNG
1410 1420 1430 1440 1450
KPVMEVTSSF FYRGNYTDFE NTFQKTVEPV YQMHIKTSKD IAVLRSKEWF
1460 1470 1480 1490 1500
QLDDEDFDLL NKTLTFETET EVTFKNANIF SSVKCFGPIK VELPTKETVE
1510 1520 1530 1540 1550
IGIVDYEAGA SHGNPVVDFL KRNGSTLEQK VNLENPIPIA VLDSYTPSTN
1560 1570 1580 1590 1600
EPYARVSGDL NPIHVSRHFA SYANLPGTIT HGMFSSASVR ALIENWAADS
1610 1620 1630 1640 1650
VSSRVRGYTC QFVDMVLPNT ALKTSIQHVG MINGRKLIKF ETRNEDDVVV
1660 1670 1680 1690 1700
LTGEAEIEQP VTTFVFTGQG SQEQGMGMDL YKTSKAAQDV WNRADNHFKD
1710 1720 1730 1740 1750
TYGFSILDIV INNPVNLTIH FGGEKGKRIR ENYSAMIFET IVDGKLKTEK
1760 1770 1780 1790 1800
IFKEINEHST SYTFRSEKGL LSATQFTQPA LTLMEKAAFE DLKSKGLIPA
1810 1820 1830 1840 1850
DATFAGHSLG EYAALASLAD VMSIESLVEV VFYRGMTMQV AVPRDELGRS
1860 1870 1880 1890 1900
NYGMIAINPG RVAASFSQEA LQYVVERVGK RTGWLVEIVN YNVENQQYVA
1910 1920 1930 1940 1950
AGDLRALDTV TNVLNFIKLQ KIDIIELQKS LSLEEVEGHL FEIIDEASKK
1960 1970 1980 1990 2000
SAVKPRPLKL ERGFACIPLV GISVPFHSTY LMNGVKPFKS FLKKNIIKEN
2010 2020 2030 2040 2050
VKVARLAGKY IPNLTAKPFQ VTKEYFQDVY DLTGSEPIKE IIDNWEKYEQ

S
Length:2,051
Mass (Da):228,691
Last modified:February 1, 1994 - 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:i43AA85A6071D8EAA
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence CAA27616 differs from that shown. Reason: Frameshift at positions 1845, 1948 and 2017.Curated

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 conflicti191S → F in AAB59310 (PubMed:2034224).Curated1
Sequence conflicti191S → F in CAA27616 (PubMed:3528750).Curated1
Sequence conflicti212G → D in AAA34602 (PubMed:3031066).Curated1
Sequence conflicti403D → G in AAA34602 (PubMed:3031066).Curated1
Sequence conflicti1039H → Q in AAB59310 (PubMed:2034224).Curated1
Sequence conflicti1039H → Q in CAA27616 (PubMed:3528750).Curated1
Sequence conflicti1149W → R in AAA34602 (PubMed:3031066).Curated1
Sequence conflicti1184I → F in AAB59310 (PubMed:2034224).Curated1
Sequence conflicti1184I → F in CAA27616 (PubMed:3528750).Curated1
Sequence conflicti1290 – 1292FEI → SET in AAA34602 (PubMed:3031066).Curated3
Sequence conflicti1331 – 1333WRA → LRG in AAB59310 (PubMed:2034224).Curated3
Sequence conflicti1331 – 1333WRA → LRG in CAA27616 (PubMed:3528750).Curated3
Sequence conflicti1407 – 1411TSSFF → IFLFL in AAA34602 (PubMed:3031066).Curated5
Sequence conflicti1559D → H in AAB59310 (PubMed:2034224).Curated1
Sequence conflicti1559D → H in CAA27616 (PubMed:3528750).Curated1
Sequence conflicti1576P → L in AAA34602 (PubMed:3031066).Curated1
Sequence conflicti1587A → T in AAA34602 (PubMed:3031066).Curated1
Sequence conflicti1631M → T in AAA34602 (PubMed:3031066).Curated1
Sequence conflicti1647D → H in CAA27616 (PubMed:3528750).Curated1
Sequence conflicti1661V → G in AAB59310 (PubMed:2034224).Curated1
Sequence conflicti1661V → G in CAA27616 (PubMed:3528750).Curated1
Sequence conflicti1876E → K in AAA34602 (PubMed:3031066).Curated1
Sequence conflicti1980Y → T in AAA34602 (PubMed:3031066).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
M30162 Genomic DNA Translation: AAB59310.1
X74151 Genomic DNA Translation: CAA52256.1
Z28182 Genomic DNA Translation: CAA82025.1
X03977 Genomic DNA Translation: CAA27616.1 Frameshift.
M31034 Genomic DNA Translation: AAA34602.1
X70069 Genomic DNA Translation: CAA49673.1
BK006944 Genomic DNA Translation: DAA08985.1

Protein sequence database of the Protein Information Resource

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PIRi
S34688

NCBI Reference Sequences

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RefSeqi
NP_012739.1, NM_001179748.1

Genome annotation databases

Ensembl fungal genome annotation project

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EnsemblFungii
YKL182W_mRNA; YKL182W_mRNA; YKL182W

Database of genes from NCBI RefSeq genomes

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GeneIDi
853653

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YKL182W

<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
M30162 Genomic DNA Translation: AAB59310.1
X74151 Genomic DNA Translation: CAA52256.1
Z28182 Genomic DNA Translation: CAA82025.1
X03977 Genomic DNA Translation: CAA27616.1 Frameshift.
M31034 Genomic DNA Translation: AAA34602.1
X70069 Genomic DNA Translation: CAA49673.1
BK006944 Genomic DNA Translation: DAA08985.1
PIRiS34688
RefSeqiNP_012739.1, NM_001179748.1

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
2PFFX-ray4.00B/E/H1-545[»]
B/E/H1669-1940[»]
2UV8X-ray3.10G/H/I1-2051[»]
2VKZX-ray4.00G/H/I1-2051[»]
3HMJX-ray4.00G/H/I1-2051[»]
SMRiP07149
ModBaseiSearch...

Protein-protein interaction databases

BioGridi33940, 95 interactors
ComplexPortaliCPX-1162 Fatty-acyl-CoA synthase
DIPiDIP-742N
IntActiP07149, 101 interactors
MINTiP07149
STRINGi4932.YKL182W

PTM databases

CarbonylDBiP07149
iPTMnetiP07149

Proteomic databases

MaxQBiP07149
PaxDbiP07149
PRIDEiP07149

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKL182W_mRNA; YKL182W_mRNA; YKL182W
GeneIDi853653
KEGGisce:YKL182W

Organism-specific databases

EuPathDBiFungiDB:YKL182W
SGDiS000001665 FAS1

Phylogenomic databases

GeneTreeiENSGT00940000176444
HOGENOMiHOG000177963
InParanoidiP07149
KOiK00668
OMAiGVLTHRN

Enzyme and pathway databases

BioCyciMetaCyc:YKL182W-MONOMER
YEAST:YKL182W-MONOMER
SABIO-RKiP07149

Miscellaneous databases

EvolutionaryTraceiP07149

Protein Ontology

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PROi
PR:P07149

Family and domain databases

Gene3Di3.20.20.70, 2 hits
3.40.366.10, 1 hit
InterProiView protein in InterPro
IPR001227 Ac_transferase_dom_sf
IPR014043 Acyl_transferase
IPR016035 Acyl_Trfase/lysoPLipase
IPR013785 Aldolase_TIM
IPR013565 DUF1729
IPR041099 FAS1_N
IPR040883 FAS_meander
IPR003965 Fatty_acid_synthase
IPR016452 Fatty_acid_Synthase_bsu_fun
IPR029069 HotDog_dom_sf
IPR039569 MaoC-like_dehydrat_N
IPR002539 MaoC-like_dom
IPR020801 PKS_acyl_transferase
IPR032088 SAT
PfamiView protein in Pfam
PF00698 Acyl_transf_1, 1 hit
PF08354 DUF1729, 1 hit
PF17951 FAS_meander, 1 hit
PF17828 FAS_N, 1 hit
PF13452 MaoC_dehydrat_N, 1 hit
PF01575 MaoC_dehydratas, 1 hit
PF16073 SAT, 1 hit
PIRSFiPIRSF005562 FAS_yeast_beta, 1 hit
PRINTSiPR01483 FASYNTHASE
SMARTiView protein in SMART
SM00827 PKS_AT, 1 hit
SUPFAMiSSF52151 SSF52151, 2 hits
SSF54637 SSF54637, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiFAS1_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: P07149
Secondary accession number(s): D6VX19, Q05747
<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: April 1, 1988
Last sequence update: February 1, 1994
Last modified: July 3, 2019
This is version 197 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 XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
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