CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018321
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Fatty acyl-CoA reductase 1 
Protein Synonyms/Alias
 Male sterility domain-containing protein 2 
Gene Name
 FAR1 
Gene Synonyms/Alias
 MLSTD2; UNQ2423/PRO4981 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
11IPEYYEGKNVLLTGAubiquitination[1]
29LGKVLLEKLLRSCPKubiquitination[1, 2, 3]
36KLLRSCPKVNSVYVLubiquitination[1]
63VEEVLSGKLFDRLRDubiquitination[1, 2, 3, 4, 5]
78ENPDFREKIIAINSEubiquitination[1, 4]
90NSELTQPKLALSEEDubiquitination[4, 5]
161AYAYCNRKHIDEVVYubiquitination[1, 2, 3, 4]
176PPPVDPKKLIDSLEWubiquitination[4, 5]
208PNTYIYTKALAEYVVubiquitination[1, 2, 3, 4, 5]
259GLFIAAGKGILRTIRubiquitination[5]
379GRSPRMMKTITRLHKubiquitination[2, 3, 4]
443NYCLGTKKYVLNEEMubiquitination[1, 2, 3, 4, 5]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 
Functional Description
 Catalyzes the reduction of saturated fatty acyl-CoA with chain length C16 or C18 to fatty alcohols. 
Sequence Annotation
  
Keyword
 Complete proteome; Lipid biosynthesis; Lipid metabolism; Membrane; NADP; Oxidoreductase; Peroxisome; Polymorphism; Reference proteome; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 515 AA 
Protein Sequence
MVSIPEYYEG KNVLLTGATG FLGKVLLEKL LRSCPKVNSV YVLVRQKAGQ TPQERVEEVL 60
SGKLFDRLRD ENPDFREKII AINSELTQPK LALSEEDKEV IIDSTNIIFH CAATVRFNEN 120
LRDAVQLNVI ATRQLILLAQ QMKNLEVFMH VSTAYAYCNR KHIDEVVYPP PVDPKKLIDS 180
LEWMDDGLVN DITPKLIGDR PNTYIYTKAL AEYVVQQEGA KLNVAIVRPS IVGASWKEPF 240
PGWIDNFNGP SGLFIAAGKG ILRTIRASNN ALADLVPVDV VVNMSLAAAW YSGVNRPRNI 300
MVYNCTTGST NPFHWGEVEY HVISTFKRNP LEQAFRRPNV NLTSNHLLYH YWIAVSHKAP 360
AFLYDIYLRM TGRSPRMMKT ITRLHKAMVF LEYFTSNSWV WNTENVNMLM NQLNPEDKKT 420
FNIDVRQLHW AEYIENYCLG TKKYVLNEEM SGLPAARKHL NKLRNIRYGF NTILVILIWR 480
IFIARSQMAR NIWYFVVSLC YKFLSYFRAS STMRY 515 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005782; C:peroxisomal matrix; TAS:Reactome.
 GO:0005778; C:peroxisomal membrane; IDA:UniProtKB.
 GO:0080019; F:fatty-acyl-CoA reductase (alcohol-forming) activity; IDA:UniProtKB.
 GO:0050062; F:long-chain-fatty-acyl-CoA reductase activity; IEA:Compara.
 GO:0008611; P:ether lipid biosynthetic process; IMP:UniProtKB.
 GO:0046474; P:glycerophospholipid biosynthetic process; IDA:UniProtKB.
 GO:0035336; P:long-chain fatty-acyl-CoA metabolic process; IDA:UniProtKB.
 GO:0010025; P:wax biosynthetic process; IEA:Compara. 
Interpro
 IPR026055; FAR.
 IPR013120; Male_sterile_NAD-bd.
 IPR016040; NAD(P)-bd_dom. 
Pfam
 PF07993; NAD_binding_4
 PF03015; Sterile 
SMART
  
PROSITE
  
PRINTS