UniProt Accession

 ACOD_HUMAN; O00767; B2R5U0; D3DR68; Q16150; Q53GR9; Q5W037; Q5W038; Q6GSS4; Q96KF6; Q9BS07; Q9Y695 

Genbank Protein ID

 Y13647; AF097514; AB032261; AK312312; AK222862; AL139819; AL139819; CH471066; CH471066; BC005807; BC062303; AF320307; S70284 

Genbank Nucleotide ID

 CAA73998.1; AAD29870.1; BAA93510.1; BAG35237.1; BAD96582.1; CAH72823.1; CAH72824.1; EAW49829.1; EAW49830.1; AAH05807.1; AAH62303.1; AAK54510.1; AAB30631.1 

Protein Name

 Acyl-CoA desaturase 

Protein Synonyms/Alias

 Delta(9)-desaturase; Delta-9 desaturase; Fatty acid desaturase; Stearoyl-CoA desaturase 

Gene Name

 SCD 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
34	VLQNGGDKLETMPLY	ubiquitination	[1, 2, 3]
51	DDIRPDIKDDIYDPT	ubiquitination	[1, 2, 3]
60	DIYDPTYKDKEGPSP	ubiquitination	[1, 2, 3]
62	YDPTYKDKEGPSPKV	ubiquitination	[1, 2, 3]
68	DKEGPSPKVEYVWRN	ubiquitination	[1, 2, 3, 4, 5]
162	RDHRAHHKFSETHAD	ubiquitination	[1, 2, 3, 6, 7, 8, 9]
189	VGWLLVRKHPAVKEK	ubiquitination	[1]
194	VRKHPAVKEKGSTLD	ubiquitination	[1, 2]
196	KHPAVKEKGSTLDLS	ubiquitination	[1, 2, 3, 4, 5, 7, 8, 9, 10, 11]
209	LSDLEAEKLVMFQRR	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11]
337	LGLAYDRKKVSKAAI	ubiquitination	[2]
338	GLAYDRKKVSKAAIL	ubiquitination	[1, 2, 4, 5]
341	YDRKKVSKAAILARI	ubiquitination	[1, 2, 3, 4, 5, 7, 8, 9, 11]
357	RTGDGNYKSG*****	ubiquitination	[1]

Reference

 [1] 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]
 [2] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [3] 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]
 [4] 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]
 [5] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [6] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [7] 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]
 [8] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [9] 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]
 [10] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [11] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 

Functional Description

 Terminal component of the liver microsomal stearyl-CoA desaturase system, that utilizes O(2) and electrons from reduced cytochrome b5 to catalyze the insertion of a double bond into a spectrum of fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA. 

Sequence Annotation

 MOTIF 120 125 Histidine box-1.
 MOTIF 157 161 Histidine box-2.
 MOTIF 298 302 Histidine box-3.
 MOD_RES 203 203 Phosphoserine.  

Keyword

 Complete proteome; Direct protein sequencing; Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism; Iron; Lipid biosynthesis; Lipid metabolism; Membrane; Oxidoreductase; Phosphoprotein; Polymorphism; Reference proteome; Transmembrane; Transmembrane helix. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 359 AA 

Protein Sequence

Gene Ontology

 GO:0005783; C:endoplasmic reticulum; IDA:HPA.
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005506; F:iron ion binding; IEA:InterPro.
 GO:0004768; F:stearoyl-CoA 9-desaturase activity; TAS:ProtInc.
 GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW. 

Interpro

 IPR005804; Fatty_acid_desaturase-1.
 IPR001522; Fatty_acid_desaturase-1_C.
 IPR015876; Fatty_acid_desaturase-1_core. 

Pfam

 PF00487; FA_desaturase 

SMART

  

PROSITE

 PS00476; FATTY_ACID_DESATUR_1 

PRINTS

 PR00075; FACDDSATRASE.