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Protein

Acyl-CoA desaturase

Gene

SCD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Stearyl-CoA desaturase that utilizes O2 and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates (PubMed:15907797, PubMed:18765284). Catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA (PubMed:15907797, PubMed:18765284). Gives rise to a mixture of 16:1 and 18:1 unsaturated fatty acids (PubMed:15610069). Plays an important role in lipid biosynthesis. Plays an important role in regulating the expression of genes that are involved in lipogenesis and in regulating mitochondrial fatty acid oxidation (By similarity). Plays an important role in body energy homeostasis (By similarity). Contributes to the biosynthesis of membrane phospholipids, cholesterol esters and triglycerides (By similarity).By similarity3 Publications

Catalytic activityi

Stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O.3 Publications

Cofactori

Fe2+1 Publication1 PublicationNote: Expected to bind 2 Fe2+ ions per subunit, instead of the Zn2+ ions seen in the 3D-structure.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei75 – 751Substrate1 Publication
Metal bindingi120 – 1201Iron 11 Publication
Metal bindingi125 – 1251Iron 11 Publication
Binding sitei148 – 1481Substrate1 Publication
Binding sitei155 – 1551Substrate1 Publication
Binding sitei156 – 1561Substrate1 Publication
Metal bindingi157 – 1571Iron 11 Publication
Metal bindingi160 – 1601Iron 21 Publication
Metal bindingi161 – 1611Iron 11 Publication
Binding sitei188 – 1881Substrate1 Publication
Binding sitei189 – 1891Substrate1 Publication
Binding sitei262 – 2621Substrate1 Publication
Metal bindingi269 – 2691Iron 21 Publication
Metal bindingi298 – 2981Iron 21 Publication
Metal bindingi301 – 3011Iron 11 Publication
Metal bindingi302 – 3021Iron 21 Publication

GO - Molecular functioni

  • iron ion binding Source: UniProtKB
  • oxidoreductase activity Source: UniProtKB
  • stearoyl-CoA 9-desaturase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.14.19.1. 2681.
ReactomeiR-HSA-75105. Fatty Acyl-CoA Biosynthesis.

Chemistry

SwissLipidsiSLP:000000465.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA desaturase (EC:1.14.19.13 Publications)
Alternative name(s):
Delta(9)-desaturase
Short name:
Delta-9 desaturase
Fatty acid desaturase
Stearoyl-CoA desaturase1 Publication
Short name:
hSCD11 Publication
Gene namesi
Name:SCD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:10571. SCD.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 7272Cytoplasmic1 PublicationAdd
BLAST
Transmembranei73 – 9321Helical1 PublicationAdd
BLAST
Topological domaini94 – 974Lumenal1 Publication
Transmembranei98 – 11821Helical1 PublicationAdd
BLAST
Topological domaini119 – 21799Cytoplasmic1 PublicationAdd
BLAST
Transmembranei218 – 23720Helical1 PublicationAdd
BLAST
Topological domaini238 – 2414Lumenal1 Publication
Transmembranei242 – 26322Helical1 PublicationAdd
BLAST
Topological domaini264 – 35996Cytoplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: HPA
  • endoplasmic reticulum membrane Source: UniProtKB
  • integral component of membrane Source: UniProtKB
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

MalaCardsiSCD.
PharmGKBiPA34984.

Chemistry

ChEMBLiCHEMBL5555.

Polymorphism and mutation databases

BioMutaiSCD.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 359359Acyl-CoA desaturasePRO_0000185395Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei203 – 2031PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO00767.
PaxDbiO00767.
PRIDEiO00767.

PTM databases

iPTMnetiO00767.
PhosphoSiteiO00767.

Expressioni

Tissue specificityi

Detected in fetal liver, lung and brain. Highly expressed in adult adipose tissue, and at lower levels in adult brain and lung.1 Publication

Gene expression databases

BgeeiO00767.
GenevisibleiO00767. HS.

Organism-specific databases

HPAiHPA012107.

Interactioni

Subunit structurei

May self-associate and form homodimers.1 Publication

Protein-protein interaction databases

BioGridi112225. 14 interactions.
IntActiO00767. 4 interactions.
MINTiMINT-2997962.
STRINGi9606.ENSP00000359380.

Chemistry

BindingDBiO00767.

Structurei

Secondary structure

1
359
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi57 – 593Combined sources
Beta strandi63 – 653Combined sources
Helixi73 – 9119Combined sources
Turni92 – 954Combined sources
Helixi98 – 11518Combined sources
Helixi116 – 1249Combined sources
Helixi132 – 14413Combined sources
Helixi150 – 16213Combined sources
Turni163 – 1653Combined sources
Helixi173 – 1753Combined sources
Helixi177 – 1815Combined sources
Helixi183 – 1853Combined sources
Helixi192 – 1965Combined sources
Helixi203 – 2064Combined sources
Helixi209 – 2168Combined sources
Helixi218 – 2269Combined sources
Helixi228 – 23710Combined sources
Helixi242 – 2476Combined sources
Turni248 – 2503Combined sources
Helixi251 – 26212Combined sources
Turni263 – 2664Combined sources
Helixi267 – 2693Combined sources
Beta strandi271 – 2733Combined sources
Beta strandi278 – 2803Combined sources
Helixi286 – 2916Combined sources
Beta strandi292 – 2943Combined sources
Helixi298 – 3036Combined sources
Beta strandi308 – 3136Combined sources
Helixi319 – 32911Combined sources
Helixi341 – 3466Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ZYOX-ray3.25A45-359[»]
ProteinModelPortaliO00767.
SMRiO00767. Positions 53-350.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi120 – 1256Histidine box-1Curated
Motifi157 – 1615Histidine box-2Curated
Motifi298 – 3025Histidine box-3Curated

Domaini

The histidine box domains are involved in binding the catalytic metal ions.1 Publication

Sequence similaritiesi

Belongs to the fatty acid desaturase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1600. Eukaryota.
COG1398. LUCA.
GeneTreeiENSGT00530000063158.
HOVERGENiHBG003367.
InParanoidiO00767.
KOiK00507.
OMAiLIPTCKF.
OrthoDBiEOG7ZPNKS.
PhylomeDBiO00767.
TreeFamiTF313251.

Family and domain databases

InterProiIPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
[Graphical view]
PRINTSiPR00075. FACDDSATRASE.
PROSITEiPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O00767-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAHLLQDDI SSSYTTTTTI TAPPSRVLQN GGDKLETMPL YLEDDIRPDI
60 70 80 90 100
KDDIYDPTYK DKEGPSPKVE YVWRNIILMS LLHLGALYGI TLIPTCKFYT
110 120 130 140 150
WLWGVFYYFV SALGITAGAH RLWSHRSYKA RLPLRLFLII ANTMAFQNDV
160 170 180 190 200
YEWARDHRAH HKFSETHADP HNSRRGFFFS HVGWLLVRKH PAVKEKGSTL
210 220 230 240 250
DLSDLEAEKL VMFQRRYYKP GLLMMCFILP TLVPWYFWGE TFQNSVFVAT
260 270 280 290 300
FLRYAVVLNA TWLVNSAAHL FGYRPYDKNI SPRENILVSL GAVGEGFHNY
310 320 330 340 350
HHSFPYDYSA SEYRWHINFT TFFIDCMAAL GLAYDRKKVS KAAILARIKR

TGDGNYKSG
Length:359
Mass (Da):41,523
Last modified:June 6, 2002 - v2
Checksum:iED56A63DBD850F05
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51L → M in AAB30631 (PubMed:7909540).Curated
Sequence conflicti8 – 81D → E in AAB30631 (PubMed:7909540).Curated
Sequence conflicti25 – 262SR → PG in CAA73998 (Ref. 1) Curated
Sequence conflicti25 – 262SR → PG in AAB30631 (PubMed:7909540).Curated
Sequence conflicti237 – 2371F → C in AAB30631 (PubMed:7909540).Curated
Sequence conflicti269 – 2691H → L in BAD96582 (Ref. 5) Curated
Sequence conflicti320 – 3201T → N in CAA73998 (Ref. 1) Curated
Sequence conflicti326 – 3261C → W in CAA73998 (Ref. 1) Curated
Sequence conflicti333 – 3331A → T in CAA73998 (Ref. 1) Curated
Sequence conflicti356 – 3594Missing in AAH05807 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti224 – 2241M → L.4 Publications
Corresponds to variant rs2234970 [ dbSNP | Ensembl ].
VAR_025994

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13647 mRNA. Translation: CAA73998.1.
AF097514 mRNA. Translation: AAD29870.1.
AB032261 mRNA. Translation: BAA93510.1.
AK312312 mRNA. Translation: BAG35237.1.
AK222862 mRNA. Translation: BAD96582.1.
AL139819 Genomic DNA. Translation: CAH72823.1.
AL139819 Genomic DNA. Translation: CAH72824.1.
CH471066 Genomic DNA. Translation: EAW49829.1.
CH471066 Genomic DNA. Translation: EAW49830.1.
BC005807 mRNA. Translation: AAH05807.1.
BC062303 mRNA. Translation: AAH62303.1.
AF320307 Genomic DNA. Translation: AAK54510.1.
S70284 mRNA. Translation: AAB30631.1.
CCDSiCCDS7493.1.
PIRiI54779.
RefSeqiNP_005054.3. NM_005063.4.
UniGeneiHs.558396.

Genome annotation databases

EnsembliENST00000370355; ENSP00000359380; ENSG00000099194.
GeneIDi6319.
KEGGihsa:6319.
UCSCiuc001kqy.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13647 mRNA. Translation: CAA73998.1.
AF097514 mRNA. Translation: AAD29870.1.
AB032261 mRNA. Translation: BAA93510.1.
AK312312 mRNA. Translation: BAG35237.1.
AK222862 mRNA. Translation: BAD96582.1.
AL139819 Genomic DNA. Translation: CAH72823.1.
AL139819 Genomic DNA. Translation: CAH72824.1.
CH471066 Genomic DNA. Translation: EAW49829.1.
CH471066 Genomic DNA. Translation: EAW49830.1.
BC005807 mRNA. Translation: AAH05807.1.
BC062303 mRNA. Translation: AAH62303.1.
AF320307 Genomic DNA. Translation: AAK54510.1.
S70284 mRNA. Translation: AAB30631.1.
CCDSiCCDS7493.1.
PIRiI54779.
RefSeqiNP_005054.3. NM_005063.4.
UniGeneiHs.558396.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ZYOX-ray3.25A45-359[»]
ProteinModelPortaliO00767.
SMRiO00767. Positions 53-350.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112225. 14 interactions.
IntActiO00767. 4 interactions.
MINTiMINT-2997962.
STRINGi9606.ENSP00000359380.

Chemistry

BindingDBiO00767.
ChEMBLiCHEMBL5555.
SwissLipidsiSLP:000000465.

PTM databases

iPTMnetiO00767.
PhosphoSiteiO00767.

Polymorphism and mutation databases

BioMutaiSCD.

Proteomic databases

MaxQBiO00767.
PaxDbiO00767.
PRIDEiO00767.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000370355; ENSP00000359380; ENSG00000099194.
GeneIDi6319.
KEGGihsa:6319.
UCSCiuc001kqy.3. human.

Organism-specific databases

CTDi6319.
GeneCardsiSCD.
H-InvDBHIX0009123.
HGNCiHGNC:10571. SCD.
HPAiHPA012107.
MalaCardsiSCD.
MIMi604031. gene.
neXtProtiNX_O00767.
PharmGKBiPA34984.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1600. Eukaryota.
COG1398. LUCA.
GeneTreeiENSGT00530000063158.
HOVERGENiHBG003367.
InParanoidiO00767.
KOiK00507.
OMAiLIPTCKF.
OrthoDBiEOG7ZPNKS.
PhylomeDBiO00767.
TreeFamiTF313251.

Enzyme and pathway databases

BRENDAi1.14.19.1. 2681.
ReactomeiR-HSA-75105. Fatty Acyl-CoA Biosynthesis.

Miscellaneous databases

ChiTaRSiSCD. human.
GeneWikiiStearoyl-CoA_desaturase-1.
GenomeRNAii6319.
NextBioi24520.
PROiO00767.
SOURCEiSearch...

Gene expression databases

BgeeiO00767.
GenevisibleiO00767. HS.

Family and domain databases

InterProiIPR001522. Fatty_acid_desaturase-1_C.
IPR015876. Fatty_acid_desaturase-1_core.
[Graphical view]
PRINTSiPR00075. FACDDSATRASE.
PROSITEiPS00476. FATTY_ACID_DESATUR_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization and expression of a stearoyl CoA desaturase from human liver."
    Al-Jeryan L., McCord A., Pierotti A.R., Craft J.A.
    Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Human stearoyl-CoA desaturase: alternative transcripts generated from a single gene by usage of tandem polyadenylation sites."
    Zhang L., Ge L., Parimoo S., Stenn K., Prouty S.M.
    Biochem. J. 340:255-264(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-224.
    Tissue: Brain, Liver and Skin.
  3. "Cloning, sequencing and expression of human stearoyl-CoA desaturase."
    Hoshino T., Ohtsu K.
    Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-224.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Cerebellum.
  5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  6. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LEU-224.
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LEU-224.
    Tissue: Mammary gland and Placenta.
  9. "Isolation and characterization of the human stearoyl-CoA desaturase gene promoter: requirement of a conserved CCAAT cis-element."
    Zhang L., Ge L., Tran T., Stenn K., Prouty S.M.
    Biochem. J. 357:183-193(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
  10. "Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini."
    Xu G., Shin S.B., Jaffrey S.R.
    Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 2-27.
    Tissue: Leukemic T-cell.
  11. "Partial characterization of a cDNA for human stearoyl-CoA desaturase and changes in its mRNA expression in some normal and malignant tissues."
    Li J., Ding S.-F., Habib N.A., Fermor B.F., Wood C.B., Gilmour R.S.
    Int. J. Cancer 57:348-352(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-239.
    Tissue: Adipose tissue.
  12. "Characterization of HSCD5, a novel human stearoyl-CoA desaturase unique to primates."
    Wang J., Yu L., Schmidt R.E., Su C., Huang X., Gould K., Cao G.
    Biochem. Biophys. Res. Commun. 332:735-742(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  13. "Characterization of human SCD2, an oligomeric desaturase with improved stability and enzyme activity by cross-linking in intact cells."
    Zhang S., Yang Y., Shi Y.
    Biochem. J. 388:135-142(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
  14. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "Wheat germ cell-free translation, purification, and assembly of a functional human stearoyl-CoA desaturase complex."
    Goren M.A., Fox B.G.
    Protein Expr. Purif. 62:171-178(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Crystal structure of human stearoyl-coenzyme A desaturase in complex with substrate."
    Wang H., Klein M.G., Zou H., Lane W., Snell G., Levin I., Li K., Sang B.C.
    Nat. Struct. Mol. Biol. 22:581-585(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS) OF 45-359 IN COMPLEX WITH STEAROYL-COENZYME A AND ZINC IONS, TOPOLOGY.

Entry informationi

Entry nameiACOD_HUMAN
AccessioniPrimary (citable) accession number: O00767
Secondary accession number(s): B2R5U0
, D3DR68, Q16150, Q53GR9, Q5W037, Q5W038, Q6GSS4, Q96KF6, Q9BS07, Q9Y695
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: June 6, 2002
Last modified: January 20, 2016
This is version 155 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.