FAS2/YPL231W Protein Information Help

Standard Name Fas2p 1
Systematic Name Ypl231wp
ORF Classification Verified
Description Alpha subunit of fatty acid synthetase, which catalyzes the synthesis of long-chain saturated fatty acids; contains the acyl-carrier protein domain and beta-ketoacyl reductase, beta-ketoacyl synthase and self-pantetheinylation activities (2, 3, 4)
Name Description Fatty Acid Synthetase
Experimental Data
Molecules/cell 17000 5
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 1,887
Molecular Weight (Da) 206,945
Isoelectric Point (pI) 5.21

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Fas2p (InterPro)
Physical Interactions There are 39 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI0000052E03 | P19097
MIPS: YPL231W
NCBI: 1181257 | 1370478 | 152149307 | 152149310 | 152149313 | 171502 | 196049652 | 196049653 | 196049654 | 20981695 | 2326840 | 256599488 | 256599489 | 256599490 | 256599491 | 256599492 | 256599493 | 256599494 | 256599495 | 256599496 | 256599497 | 256599498 | 256599499 | 257097280 | 257097281 | 257097282 | 402715407 | 402715408 | 402715409 | 6325025 | 854531 | NP_015093.1 | NM_001184045.1
GenBank/EMBL/DDBJ: DAA11205.1 | J03936 | X76890 | X94561 | Z73586 | Z73587
External Classifications EC: 1.1.1.100 [3-oxoacyl-[acyl-carrier-protein] reductase]
EC: 2.3.1.41 [Beta-ketoacyl-[acyl-carrier-protein] synthase I]
EC: 2.3.1.86 [Fatty-acyl-CoA synthase]
Amino Acid Sequence (or in FASTA format)
       1  MKPEVEQELA HILLTELLAY QFASPVRWIE TQDVFLKDFN TERVVEIGPS
      51  PTLAGMAQRT LKNKYESYDA ALSLHREILC YSKDAKEIYY TPDPSELAAK
     101  EEPAKEEAPA PTPAASAPAP AAAAPAPVAA AAPAAAAAEI ADEPVKASLL
     151  LHVLVAHKLK KSLDSIPMSK TIKDLVGGKS TVQNEILGDL GKEFGTTPEK
     201  PEETPLEELA ETFQDTFSGA LGKQSSSLLS RLISSKMPGG FTITVARKYL
     251  QTRWGLPSGR QDGVLLVALS NEPAARLGSE ADAKAFLDSM AQKYASIVGV
     301  DLSSAASASG AAGAGAAAGA AMIDAGALEE ITKDHKVLAR QQLQVLARYL
     351  KMDLDNGERK FLKEKDTVAE LQAQLDYLNA ELGEFFVNGV ATSFSRKKAR
     401  TFDSSWNWAK QSLLSLYFEI IHGVLKNVDR EVVSEAINIM NRSNDALIKF
     451  MEYHISNTDE TKGENYQLVK TLGEQLIENC KQVLDVDPVY KDVAKPTGPK
     501  TAIDKNGNIT YSEEPREKVR KLSQYVQEMA LGGPITKESQ PTIEEDLTRV
     551  YKAISAQADK QDISSSTRVE FEKLYSDLMK FLESSKEIDP SQTTQLAGMD
     601  VEDALDKDST KEVASLPNKS TISKTVSSTI PRETIPFLHL RKKTPAGDWK
     651  YDRQLSSLFL DGLEKAAFNG VTFKDKYVLI TGAGKGSIGA EVLQGLLQGG
     701  AKVVVTTSRF SKQVTDYYQS IYAKYGAKGS TLIVVPFNQG SKQDVEALIE
     751  FIYDTEKNGG LGWDLDAIIP FAAIPEQGIE LEHIDSKSEF AHRIMLTNIL
     801  RMMGCVKKQK SARGIETRPA QVILPMSPNH GTFGGDGMYS ESKLSLETLF
     851  NRWHSESWAN QLTVCGAIIG WTRGTGLMSA NNIIAEGIEK MGVRTFSQKE
     901  MAFNLLGLLT PEVVELCQKS PVMADLNGGL QFVPELKEFT AKLRKELVET
     951  SEVRKAVSIE TALEHKVVNG NSADAAYAQV EIQPRANIQL DFPELKPYKQ
    1001  VKQIAPAELE GLLDLERVIV VTGFAEVGPW GSARTRWEME AFGEFSLEGC
    1051  VEMAWIMGFI SYHNGNLKGR PYTGWVDSKT KEPVDDKDVK AKYETSILEH
    1101  SGIRLIEPEL FNGYNPEKKE MIQEVIVEED LEPFEASKET AEQFKHQHGD
    1151  KVDIFEIPET GEYSVKLLKG ATLYIPKALR FDRLVAGQIP TGWNAKTYGI
    1201  SDDIISQVDP ITLFVLVSVV EAFIASGITD PYEMYKYVHV SEVGNCSGSG
    1251  MGGVSALRGM FKDRFKDEPV QNDILQESFI NTMSAWVNML LISSSGPIKT
    1301  PVGACATSVE SVDIGVETIL SGKARICIVG GYDDFQEEGS FEFGNMKATS
    1351  NTLEEFEHGR TPAEMSRPAT TTRNGFMEAQ GAGIQIIMQA DLALKMGVPI
    1401  YGIVAMAATA TDKIGRSVPA PGKGILTTAR EHHSSVKYAS PNLNMKYRKR
    1451  QLVTREAQIK DWVENELEAL KLEAEEIPSE DQNEFLLERT REIHNEAESQ
    1501  LRAAQQQWGN DFYKRDPRIA PLRGALATYG LTIDDLGVAS FHGTSTKAND
    1551  KNESATINEM MKHLGRSEGN PVIGVFQKFL TGHPKGAAGA WMMNGALQIL
    1601  NSGIIPGNRN ADNVDKILEQ FEYVLYPSKT LKTDGVRAVS ITSFGFGQKG
    1651  GQAIVVHPDY LYGAITEDRY NEYVAKVSAR EKSAYKFFHN GMIYNKLFVS
    1701  KEHAPYTDEL EEDVYLDPLA RVSKDKKSGS LTFNSKNIQS KDSYINANTI
    1751  ETAKMIENMT KEKVSNGGVG VDVELITSIN VENDTFIERN FTPQEIEYCS
    1801  AQPSVQSSFA GTWSAKEAVF KSLGVKSLGG GAALKDIEIV RVNKNAPAVE
    1851  LHGNAKKAAE EAGVTDVKVS ISHDDLQAVA VAVSTKK*             

external links for Fas2p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily Organelle DB
Ashbya (AGD) BOND GPMdb (Mass Spec.) YPL+
Aspergillus (AspGD) BioPIXIE MIPS YeastGFP
Candida (CGD) CYC2008 (complexes) Pfam domains YeastRC Public Image Repository
Candida (CandidaDB) Complexome YeastRC Structure Prediction (Seattle)
YGOB DIP

YOGY GeneMANIA

References cited on this page View Complete Literature Guide for Fas2p
1) Schweizer, E.  (1989) Personal Communication, Mortimer Map Edition 10
2) Mohamed AH, et al.  (1988) Primary structure of the multifunctional alpha subunit protein of yeast fatty acid synthase derived from FAS2 gene sequence. J Biol Chem 263(25):12315-25
3) Fichtlscherer F, et al.  (2000) A novel function of yeast fatty acid synthase. Subunit alpha is capable of self-pantetheinylation. Eur J Biochem 267(9):2666-71
4) Reinders J, et al.  (2007) Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase. Mol Cell Proteomics 6(11):1896-906
5) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41