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Entry version 88 (02 Jun 2021)
Sequence version 1 (05 Jul 2004)
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Protein

Fatty acid synthase subunit alpha

Gene

FAS2

Organism
Lachancea kluyveri (Yeast) (Saccharomyces kluyveri)
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>
-Protein inferred from homologyi <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. In this species, higher amounts of C18 than C16 fatty acids are produced.

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 sitei1305For beta-ketoacyl synthase activityBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi1774MagnesiumBy similarity1
Metal bindingi1775Magnesium; via carbonyl oxygenBy similarity1
Metal bindingi1776MagnesiumBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei1800Acetyl-CoABy similarity1
Binding sitei1810Acetyl-CoABy similarity1
Metal bindingi1874MagnesiumBy similarity1
Metal bindingi1875Magnesium; via carbonyl oxygenBy 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 functionMultifunctional enzyme, Oxidoreductase, Transferase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandMagnesium, Metal-binding, NAD, NADP

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.3.1.86, 6897

<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 alpha (EC:2.3.1.86)
Alternative name(s):
p190/210
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%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:FAS2
Synonyms:Sk-FAS2
<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>OrganismiLachancea kluyveri (Yeast) (Saccharomyces kluyveri)
<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 identifieri4934 [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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeLachancea

<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_00004192521 – 1888Fatty acid synthase subunit alphaAdd BLAST1888

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 residuei181O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q765N2

<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

Fatty acid synthase is composed of alpha and beta subunits.

By similarity

<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

3D structure databases

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

More...
SMRi
Q765N2

Database of comparative protein structure models

More...
ModBasei
Search...

<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>Domaini146 – 221CarrierPROSITE-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>Regioni98 – 118DisorderedSequence analysisAdd BLAST21
Regioni675 – 874Beta-ketoacyl reductaseBy similarityAdd BLAST200
Regioni1149 – 1363Beta-ketoacyl synthaseBy similarityAdd BLAST215
Regioni1774 – 1776Acetyl-CoA bindingBy similarity3
Regioni1819 – 1835Acetyl-CoA bindingBy similarityAdd BLAST17
Regioni1843 – 1846Acetyl-CoA bindingBy similarity4
Regioni1873 – 1875Acetyl-CoA bindingBy similarity3

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The N-terminal ACP and almost all of the KR domains play an important role in determining the carbon chain length of fatty acids produced.1 Publication

<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

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.47.10, 3 hits
3.90.470.20, 1 hit

HAMAP database of protein families

More...
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%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.

Q765N2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAMKPEVEQE LAHVLLTELL AYQFASPVRW IETQDVFLKD FNTERVVEIG
60 70 80 90 100
PSPTLAGMAQ RTIKNKYESY DAALSLQRQV LCYSKDAKEI YYTPDPADLA
110 120 130 140 150
PVEEPNAEEQ TGAAATPAAA AAPAAAAAAP AAPAARPVAE LPDEAVKASL
160 170 180 190 200
LLHVLVAQKL KKSLEQVPMS KTIKDLVGGK STVQNEILGD LGKEFGSTPE
210 220 230 240 250
KPEETPLEEL AETFQDTFAG SLGKQSSSLI SRLMSSKMPG GFTITVARKY
260 270 280 290 300
LQTRWGLGSG RQDSVLLIAL TNEPASRLGG EADAKSFLDS MAQKYASISG
310 320 330 340 350
VDLSSASAGA SAGAGAGGAG GATIDAAAFE ELTKDQKVMA RQQLEVLARY
360 370 380 390 400
LKMDLNGGEK KFLQEKNTVA ELQSQLDYLN NELGEYFIQG ISTSFSRKKA
410 420 430 440 450
RVFDSSWNWA KQALLTLYFQ IIHGVLKNVD REVVTEAINI MNRSNETLIK
460 470 480 490 500
FMEYHISHCD ENNGENYKLA KTLGHQLIEN CKQVLDMDPV YKDISKPTGP
510 520 530 540 550
KTNIDKNGNI KYSEEPRAAV RKLSQYVQEM ALGGPLTKES QPTIQEDLTR
560 570 580 590 600
VYKAINAQAA EHNISDSTKL EFEKLYGELL KFLETSNEID ASATTRLAGV
610 620 630 640 650
VDDDLDKDST KEVASLPNKS EISKNVSSII PRETVPFLHL KKKLPSCEWA
660 670 680 690 700
YDRQLSTLFL DGLEKAAING VTFKDKYVLI TGAGAGSIGA EVLQGLVQGG
710 720 730 740 750
AKVIVTTSRF SKKVTDYYQS IYAQYGAKGS TLVVVPFNQG SKQDVEALID
760 770 780 790 800
FIYDDEKNGG LGWDLDAVIP FAAIPENGIE LDKIDSKSEF AHRIMLTNIL
810 820 830 840 850
RMLGSVKKQK SARGIETRPA QVILPLSPNH GTFGGDGMYS ESKLSLETLF
860 870 880 890 900
NRWHSESWSN QLTICGAIIG WTRGTGLMNA NNIIAEGIEK MGVRTFSQKE
910 920 930 940 950
MAFNLLGLLI PEVVNLCQRS PVMADLNGGL QFLTDLKEFT GKLRGELTET
960 970 980 990 1000
SEIRKAVSIE TALEHKTVAG ANADAAFAQV EVQPRANIQL EFPTLKPYET
1010 1020 1030 1040 1050
VKKIGSPDLE GLLDLEKVIV VTGFSEVGPW GSSRTRGEME AFGEFSLEGC
1060 1070 1080 1090 1100
VEMSWIMGLI KYHNGNLKGR PYTGWVDSKT NEPVDDKDIK AKDESHVLEH
1110 1120 1130 1140 1150
SGIRLIEPEL FNSYNPEKKQ MIQEVVIEED LEPFEASKET AEQFKHEHGD
1160 1170 1180 1190 1200
KVDIFEIPET GEFSVRLLKG ATLYIPKALR FDRLVAGQIP TGWNAKTYGI
1210 1220 1230 1240 1250
SDDTISQVDP ITLFVLVSVI EAFIASGITD PYEMYKYVHV SEVGNCSGSG
1260 1270 1280 1290 1300
MGGVSALRGM FKDRYKDQPV QNDILQESFI NTMSAWVNML LISSSGPIKT
1310 1320 1330 1340 1350
PVGACATAVE SLDIGVETIL SGKAKICIVG GYDDFQEEGS YEFGNMNATS
1360 1370 1380 1390 1400
NSLDEFDHGR TPAEMSRPAT TTRNGFMEAQ GAGIQVIMNA DLALKMGVPI
1410 1420 1430 1440 1450
YGILALTATA TDKIGRSVPA PGKGILTTAR EHHGNLKFPT PLLDIKYRKR
1460 1470 1480 1490 1500
QLKNREAQIK QWVETELEML KYEAEGIPAE DQETFYAERT EEIKREATRQ
1510 1520 1530 1540 1550
LKSAQAQWGS EFYKNDPRIA PLRGALATYG LTIDDLGVAS FHGTSTKAND
1560 1570 1580 1590 1600
KNESATINEM MKHLGRSEGN PVLGVFQKYL TGHPKGAAGA WMMNGALQIL
1610 1620 1630 1640 1650
NSGIVPGNRN ADNVDKLLQQ FEYILYPSRS LKTDGIKAVS VTSFGFGQKG
1660 1670 1680 1690 1700
AQAVAVHPDF LYAAVDEATY NAYVAKVTAR EKAAYKYFHN GMIHNTLFVS
1710 1720 1730 1740 1750
KEHAPYSDEL EQPVYLDPLA RVSSDKKTGA LVFNGKGIQS SSQFVSEENR
1760 1770 1780 1790 1800
KTATIVSELA KKTAGTDASG VGVDVELIKS INVENDTFIE RNFTEAEIAY
1810 1820 1830 1840 1850
CKKQPSVQSS FAGTWSAKEA VFKSLGVKSQ GGGASLKDIE ITREAGKGPE
1860 1870 1880
VVLHGAAKEA ATKANVKNVK VSISHDDFQS VAVAVSEK
Length:1,888
Mass (Da):206,206
Last modified:July 5, 2004 - v1
<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:i6301BD0A025B7919
GO

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
AB115969 Genomic DNA Translation: BAD08376.1

<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
AB115969 Genomic DNA Translation: BAD08376.1

3D structure databases

SMRiQ765N2
ModBaseiSearch...

Proteomic databases

PRIDEiQ765N2

Enzyme and pathway databases

BRENDAi2.3.1.86, 6897

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

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 nameiFAS2_LACKL
<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: Q765N2
<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: October 3, 2012
Last sequence update: July 5, 2004
Last modified: June 2, 2021
This is version 88 of the entry and version 1 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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