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UniProtKB - P07149 (FAS1_YEAST)

Entry version 213 (25 May 2022)
Sequence version 2 (01 Feb 1994)
Previous versions | rss
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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%5Fsection">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%5Fsection">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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.3.1.86, 984

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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

Saccharomyces Genome Database

More...SGDi		S000001665, FAS1

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:YKL182W

<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

<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 or proteolytic cleavage.<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%5Fprocessing%5Fsection">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

More...PaxDbi		P07149

PRoteomics IDEntifications database

More...PRIDEi		P07149

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		P07149

iPTMnet integrated resource for PTMs in systems biology context

More...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%5Fsection">'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%5Fsection">'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%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		33940, 126 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-1162, Fatty-acyl-CoA synthase

Database of interacting proteins

More...DIPi		DIP-742N

Protein interaction database and analysis system

More...IntActi		P07149, 101 interactors

Molecular INTeraction database

More...MINTi		P07149

STRING: functional protein association networks

More...STRINGi		4932.YKL182W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P07149, protein

<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

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P07149

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

More...SMRi		P07149

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...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%5Fand%5Fdomains%5Fsection">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

Belongs to the fungal fatty acid synthetase subunit beta family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG502QQJX, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000176444

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000114_5_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P07149

Identification of Orthologs from Complete Genome Data

More...OMAi		LTHRNKD

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.20.20.70, 2 hits
3.40.366.10, 3 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001227, Ac_transferase_dom_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR013785, Aldolase_TIM
IPR016452, Fas1/AflB-like
IPR013565, Fas1/AflB-like_central
IPR041099, FAS1_N
IPR040883, FAS_meander
IPR003965, Fatty_acid_synthase
IPR029069, HotDog_dom_sf
IPR039569, MaoC-like_dehydrat_N
IPR002539, MaoC-like_dom
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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.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

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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

More...PIRi		S34688

NCBI Reference Sequences

More...RefSeqi		NP_012739.1, NM_001179748.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YKL182W_mRNA; YKL182W; YKL182W

Database of genes from NCBI RefSeq genomes

More...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

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...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[»]
6JSHelectron microscopy5.10B/F/G1-2051[»]
6JSIelectron microscopy4.70B/F/G1-2051[»]
6QL5electron microscopy2.80G/H/I/J/K/L5-2050[»]
6QL6electron microscopy2.90G/H/I/J/K/L5-2050[»]
6QL7X-ray4.60G/H/I/J/K/L/g/h/i/j/k/l1-2051[»]
6QL9X-ray2.82G/H/I/J/K/L1-2051[»]
6TA1electron microscopy3.10C/E/G/H/J/L1-2051[»]
6U5Telectron microscopy2.90G1-2051[»]
6U5Uelectron microscopy2.80G1-2051[»]
6WC7electron microscopy5.80G1-2051[»]
AlphaFoldDBiP07149
SMRiP07149
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi33940, 126 interactors
ComplexPortaliCPX-1162, Fatty-acyl-CoA synthase
DIPiDIP-742N
IntActiP07149, 101 interactors
MINTiP07149
STRINGi4932.YKL182W

PTM databases

CarbonylDBiP07149
iPTMnetiP07149

Proteomic databases

MaxQBiP07149
PaxDbiP07149
PRIDEiP07149

Genome annotation databases

EnsemblFungiiYKL182W_mRNA; YKL182W; YKL182W
GeneIDi853653
KEGGisce:YKL182W

Organism-specific databases

SGDiS000001665, FAS1
VEuPathDBiFungiDB:YKL182W

Phylogenomic databases

eggNOGiENOG502QQJX, Eukaryota
GeneTreeiENSGT00940000176444
HOGENOMiCLU_000114_5_0_1
InParanoidiP07149
OMAiLTHRNKD

Enzyme and pathway databases

BRENDAi2.3.1.86, 984
SABIO-RKiP07149

Miscellaneous databases

EvolutionaryTraceiP07149

Protein Ontology

More...PROi		PR:P07149
RNActiP07149, protein

Family and domain databases

Gene3Di3.20.20.70, 2 hits
3.40.366.10, 3 hits
InterProiView protein in InterPro
IPR001227, Ac_transferase_dom_sf
IPR014043, Acyl_transferase
IPR016035, Acyl_Trfase/lysoPLipase
IPR013785, Aldolase_TIM
IPR016452, Fas1/AflB-like
IPR013565, Fas1/AflB-like_central
IPR041099, FAS1_N
IPR040883, FAS_meander
IPR003965, Fatty_acid_synthase
IPR029069, HotDog_dom_sf
IPR039569, MaoC-like_dehydrat_N
IPR002539, MaoC-like_dom
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

MobiDB: a database of protein disorder and mobility annotations

More...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 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%5Fand%5Fisoforms">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: May 25, 2022
This is version 213 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, Reference proteome

Documents

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