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P07149 (FAS1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fatty acid synthase subunit beta

EC=2.3.1.86

Including the following 5 domains:

  1. 3-hydroxyacyl-[acyl-carrier-protein] dehydratase
    EC=4.2.1.59
  2. Enoyl-[acyl-carrier-protein] reductase [NADH]
    EC=1.3.1.9
  3. [Acyl-carrier-protein] acetyltransferase
    EC=2.3.1.38
  4. [Acyl-carrier-protein] malonyltransferase
    EC=2.3.1.39
  5. S-acyl fatty acid synthase thioesterase
    EC=3.1.2.14
Gene names
Name:FAS1
Ordered Locus Names:YKL182W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length2051 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

Acetyl-CoA + n malonyl-CoA + 2n NADPH = long-chain-acyl-CoA + n CoA + n CO2 + 2n NADP+.

Acetyl-CoA + [acyl-carrier-protein] = CoA + acetyl-[acyl-carrier-protein].

Malonyl-CoA + [acyl-carrier-protein] = CoA + malonyl-[acyl-carrier-protein].

A (3R)-3-hydroxyacyl-[acyl-carrier protein] = a trans-2-enoyl-[acyl-carrier protein] + H2O.

An acyl-[acyl-carrier protein] + NAD+ = a trans-2,3-dehydroacyl-[acyl-carrier protein] + NADH.

Oleoyl-[acyl-carrier-protein] + H2O = [acyl-carrier-protein] + oleate.

Subunit structure

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

Miscellaneous

Present with 91800 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the fungal fatty acid synthetase subunit beta family.

Contains 1 MaoC-like domain.

Sequence caution

The sequence CAA27616.1 differs from that shown. Reason: Frameshift at positions 1845, 1948 and 2017.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
   LigandNAD
NADP
   Molecular functionHydrolase
Lyase
Oxidoreductase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processfatty acid biosynthetic process

Inferred from mutant phenotype PubMed 1735446PubMed 4127627. Source: SGD

   Cellular_componentcytosol

Inferred from direct assay PubMed 6025308. Source: SGD

fatty acid synthase complex

Inferred from direct assay PubMed 65153. Source: SGD

lipid particle

Inferred from direct assay PubMed 17803462. Source: SGD

   Molecular_function3-hydroxyacyl-[acyl-carrier-protein] dehydratase activity

Inferred from direct assay PubMed 374077. Source: SGD

3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity

Inferred from electronic annotation. Source: UniProtKB-EC

[acyl-carrier-protein] S-acetyltransferase activity

Inferred from direct assay PubMed 374077. Source: SGD

[acyl-carrier-protein] S-malonyltransferase activity

Inferred from direct assay PubMed 365179PubMed 374077. Source: SGD

enoyl-[acyl-carrier-protein] reductase (NADH) activity

Inferred from electronic annotation. Source: UniProtKB-EC

enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity

Inferred from direct assay PubMed 374077. Source: SGD

fatty-acyl-CoA synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

myristoyl-[acyl-carrier-protein] hydrolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

oleoyl-[acyl-carrier-protein] hydrolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

palmitoyl-[acyl-carrier-protein] hydrolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

palmitoyltransferase activity

Inferred from direct assay PubMed 365179. Source: SGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FAS2P190973EBI-6795,EBI-6806

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 20512051Fatty acid synthase subunit beta
PRO_0000180282

Regions

Domain1523 – 1648126MaoC-like
Region1 – 468468Acetyltransferase
Region480 – 868389Enoyl reductase
Region1144 – 1626483Dehydratase
Region1627 – 1845219Malonyl/palmitoyl transferase

Sites

Active site2741For acetyltransferase activity By similarity
Active site18081For malonyltransferase activity By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.11
Modified residue7331Phosphothreonine Ref.10
Modified residue11211Phosphoserine Ref.9 Ref.10

Experimental info

Sequence conflict1911S → F in AAB59310. Ref.1
Sequence conflict1911S → F in CAA27616. Ref.5
Sequence conflict2121G → D in AAA34602. Ref.6
Sequence conflict4031D → G in AAA34602. Ref.6
Sequence conflict10391H → Q in AAB59310. Ref.1
Sequence conflict10391H → Q in CAA27616. Ref.5
Sequence conflict11491W → R in AAA34602. Ref.6
Sequence conflict11841I → F in AAB59310. Ref.1
Sequence conflict11841I → F in CAA27616. Ref.5
Sequence conflict1290 – 12923FEI → SET in AAA34602. Ref.6
Sequence conflict1331 – 13333WRA → LRG in AAB59310. Ref.1
Sequence conflict1331 – 13333WRA → LRG in CAA27616. Ref.5
Sequence conflict1407 – 14115TSSFF → IFLFL in AAA34602. Ref.6
Sequence conflict15591D → H in AAB59310. Ref.1
Sequence conflict15591D → H in CAA27616. Ref.5
Sequence conflict15761P → L in AAA34602. Ref.6
Sequence conflict15871A → T in AAA34602. Ref.6
Sequence conflict16311M → T in AAA34602. Ref.6
Sequence conflict16471D → H in CAA27616. Ref.5
Sequence conflict16611V → G in AAB59310. Ref.1
Sequence conflict16611V → G in CAA27616. Ref.5
Sequence conflict18761E → K in AAA34602. Ref.6
Sequence conflict19801Y → T in AAA34602. Ref.6

Secondary structure

.......................................................................................................................................................................................................................................................................................................................................................... 2051
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07149 [UniParc].

Last modified February 1, 1994. Version 2.
Checksum: 43AA85A6071D8EAA

FASTA2,051228,691
        10         20         30         40         50         60 
MDAYSTRPLT LSHGSLEHVL LVPTASFFIA SQLQEQFNKI LPEPTEGFAA DDEPTTPAEL 

        70         80         90        100        110        120 
VGKFLGYVSS LVEPSKVGQF DQVLNLCLTE FENCYLEGND IHALAAKLLQ ENDTTLVKTK 

       130        140        150        160        170        180 
ELIKNYITAR IMAKRPFDKK SNSALFRAVG EGNAQLVAIF GGQGNTDDYF EELRDLYQTY 

       190        200        210        220        230        240 
HVLVGDLIKF SAETLSELIR TTLDAEKVFT QGLNILEWLE NPSNTPDKDY LLSIPISCPL 

       250        260        270        280        290        300 
IGVIQLAHYV VTAKLLGFTP GELRSYLKGA TGHSQGLVTA VAIAETDSWE SFFVSVRKAI 

       310        320        330        340        350        360 
TVLFFIGVRC YEAYPNTSLP PSILEDSLEN NEGVPSPMLS ISNLTQEQVQ DYVNKTNSHL 

       370        380        390        400        410        420 
PAGKQVEISL VNGAKNLVVS GPPQSLYGLN LTLRKAKAPS GLDQSRIPFS ERKLKFSNRF 

       430        440        450        460        470        480 
LPVASPFHSH LLVPASDLIN KDLVKNNVSF NAKDIQIPVY DTFDGSDLRV LSGSISERIV 

       490        500        510        520        530        540 
DCIIRLPVKW ETTTQFKATH ILDFGPGGAS GLGVLTHRNK DGTGVRVIVA GTLDINPDDD 

       550        560        570        580        590        600 
YGFKQEIFDV TSNGLKKNPN WLEEYHPKLI KNKSGKIFVE TKFSKLIGRP PLLVPGMTPC 

       610        620        630        640        650        660 
TVSPDFVAAT TNAGYTIELA GGGYFSAAGM TAAIDSVVSQ IEKGSTFGIN LIYVNPFMLQ 

       670        680        690        700        710        720 
WGIPLIKELR SKGYPIQFLT IGAGVPSLEV ASEYIETLGL KYLGLKPGSI DAISQVINIA 

       730        740        750        760        770        780 
KAHPNFPIAL QWTGGRGGGH HSFEDAHTPM LQMYSKIRRH PNIMLIFGSG FGSADDTYPY 

       790        800        810        820        830        840 
LTGEWSTKFD YPPMPFDGFL FGSRVMIAKE VKTSPDAKKC IAACTGVPDD KWEQTYKKPT 

       850        860        870        880        890        900 
GGIVTVRSEM GEPIHKIATR GVMLWKEFDE TIFNLPKNKL VPTLEAKRDY IISRLNADFQ 

       910        920        930        940        950        960 
KPWFATVNGQ ARDLATMTYE EVAKRLVELM FIRSTNSWFD VTWRTFTGDF LRRVEERFTK 

       970        980        990       1000       1010       1020 
SKTLSLIQSY SLLDKPDEAI EKVFNAYPAA REQFLNAQDI DHFLSMCQNP MQKPVPFVPV 

      1030       1040       1050       1060       1070       1080 
LDRRFEIFFK KDSLWQSEHL EAVVDQDVQR TCILHGPVAA QFTKVIDEPI KSIMDGIHDG 

      1090       1100       1110       1120       1130       1140 
HIKKLLHQYY GDDESKIPAV EYFGGESPVD VQSQVDSSSV SEDSAVFKAT SSTDEESWFK 

      1150       1160       1170       1180       1190       1200 
ALAGSEINWR HASFLCSFIT QDKMFVSNPI RKVFKPSQGM VVEISNGNTS SKTVVTLSEP 

      1210       1220       1230       1240       1250       1260 
VQGELKPTVI LKLLKENIIQ MEMIENRTMD GKPVSLPLLY NFNPDNGFAP ISEVMEDRNQ 

      1270       1280       1290       1300       1310       1320 
RIKEMYWKLW IDEPFNLDFD PRDVIKGKDF EITAKEVYDF THAVGNNCED FVSRPDRTML 

      1330       1340       1350       1360       1370       1380 
APMDFAIVVG WRAIIKAIFP NTVDGDLLKL VHLSNGYKMI PGAKPLQVGD VVSTTAVIES 

      1390       1400       1410       1420       1430       1440 
VVNQPTGKIV DVVGTLSRNG KPVMEVTSSF FYRGNYTDFE NTFQKTVEPV YQMHIKTSKD 

      1450       1460       1470       1480       1490       1500 
IAVLRSKEWF QLDDEDFDLL NKTLTFETET EVTFKNANIF SSVKCFGPIK VELPTKETVE 

      1510       1520       1530       1540       1550       1560 
IGIVDYEAGA SHGNPVVDFL KRNGSTLEQK VNLENPIPIA VLDSYTPSTN EPYARVSGDL 

      1570       1580       1590       1600       1610       1620 
NPIHVSRHFA SYANLPGTIT HGMFSSASVR ALIENWAADS VSSRVRGYTC QFVDMVLPNT 

      1630       1640       1650       1660       1670       1680 
ALKTSIQHVG MINGRKLIKF ETRNEDDVVV LTGEAEIEQP VTTFVFTGQG SQEQGMGMDL 

      1690       1700       1710       1720       1730       1740 
YKTSKAAQDV WNRADNHFKD TYGFSILDIV INNPVNLTIH FGGEKGKRIR ENYSAMIFET 

      1750       1760       1770       1780       1790       1800 
IVDGKLKTEK IFKEINEHST SYTFRSEKGL LSATQFTQPA LTLMEKAAFE DLKSKGLIPA 

      1810       1820       1830       1840       1850       1860 
DATFAGHSLG EYAALASLAD VMSIESLVEV VFYRGMTMQV AVPRDELGRS NYGMIAINPG 

      1870       1880       1890       1900       1910       1920 
RVAASFSQEA LQYVVERVGK RTGWLVEIVN YNVENQQYVA AGDLRALDTV TNVLNFIKLQ 

      1930       1940       1950       1960       1970       1980 
KIDIIELQKS LSLEEVEGHL FEIIDEASKK SAVKPRPLKL ERGFACIPLV GISVPFHSTY 

      1990       2000       2010       2020       2030       2040 
LMNGVKPFKS FLKKNIIKEN VKVARLAGKY IPNLTAKPFQ VTKEYFQDVY DLTGSEPIKE 

      2050 
IIDNWEKYEQ S 

« Hide

References

« Hide 'large scale' references
[1]"The pentafunctional FAS1 genes of Saccharomyces cerevisiae and Yarrowia lipolytica are co-linear and considerably longer than previously estimated."
Koettig H., Rottner G., Beck K.-F., Schweizer M., Schweizer E.
Mol. Gen. Genet. 226:310-314(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequencing and analysis of 51.6 kilobases on the left arm of chromosome XI from Saccharomyces cerevisiae reveals 23 open reading frames including the FAS1 gene."
Wiemann S., Voss H., Schwager C., Rupp T., Stegemann J., Zimmermann J., Grothues D., Sensen C., Erfle H., Hewitt N., Banrevi A., Ansorge W.
Yeast 9:1343-1348(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Complete DNA sequence of yeast chromosome XI."
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C. expand/collapse author list , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"The pentafunctional FAS1 gene of yeast: its nucleotide sequence and order of the catalytic domains."
Schweizer M., Roberts L.M., Hoeltke H.-J., Takabayashi K., Hoellerer E., Hoffmann B., Mueller G., Koettig H., Schweizer E.
Mol. Gen. Genet. 203:479-486(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-2025.
[6]"Complementation of mutations and nucleotide sequence of FAS1 gene encoding beta subunit of yeast fatty acid synthase."
Chirala S.S., Kuziora M.A., Spector D.M., Wakil S.J.
J. Biol. Chem. 262:4231-4240(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1980.
Strain: ATCC 26787 / X2180-1B.
[7]"Phosphoribosylpyrophosphate synthetase (PRS): a new gene family in Saccharomyces cerevisiae."
Carter A.T., Narbad A., Pearson B.M., Beck K.-F., Logghe M., Contreras R., Schweizer M.
Yeast 10:1031-1044(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1947-2051.
Strain: ATCC 26786 / X2180-1A.
[8]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-733 AND SER-1121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Sites of ubiquitin attachment in Saccharomyces cerevisiae."
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS34688.
RefSeqNP_012739.1. NM_001179748.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2PFFX-ray4.00B/E/H1-1940[»]
2UV8X-ray3.10G/H/I1-2051[»]
2VKZX-ray4.00G/H/I1-2051[»]
3HMJX-ray4.00G/H/I1-2051[»]
ProteinModelPortalP07149.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33940. 66 interactions.
DIPDIP-742N.
IntActP07149. 77 interactions.
MINTMINT-1325736.
STRING4932.YKL182W.

Proteomic databases

PaxDbP07149.
PeptideAtlasP07149.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYKL182W; YKL182W; YKL182W.
GeneID853653.
KEGGsce:YKL182W.

Organism-specific databases

CYGDYKL182w.
SGDS000001665. FAS1.

Phylogenomic databases

eggNOGCOG0331.
HOGENOMHOG000177963.
KOK00668.
OMAKLQHVGM.
OrthoDBEOG76QFRJ.

Enzyme and pathway databases

BioCycMetaCyc:YKL182W-MONOMER.
YEAST:YKL182W-MONOMER.
SABIO-RKP07149.

Gene expression databases

GenevestigatorP07149.

Family and domain databases

Gene3D3.40.366.10. 5 hits.
InterProIPR001227. Ac_transferase_dom.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR013565. DUF1729.
IPR003965. Fatty_acid_synthase.
IPR016452. Fatty_acid_Synthase_bsu_fun.
IPR002539. MaoC_dom.
[Graphical view]
PfamPF00698. Acyl_transf_1. 1 hit.
PF08354. DUF1729. 1 hit.
PF01575. MaoC_dehydratas. 1 hit.
[Graphical view]
PIRSFPIRSF005562. FAS_yeast_beta. 1 hit.
PRINTSPR01483. FASYNTHASE.
SUPFAMSSF52151. SSF52151. 5 hits.
ProtoNetSearch...

Other

EvolutionaryTraceP07149.
NextBio974569.

Entry information

Entry nameFAS1_YEAST
AccessionPrimary (citable) accession number: P07149
Secondary accession number(s): D6VX19, Q05747
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: February 1, 1994
Last modified: April 16, 2014
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XI

Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references