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Protein
Submitted name:

Stearoyl-CoA desaturase variant

Gene
N/A
Organism
Homo sapiens (Human)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at transcript leveli

Functioni

Cofactori

Fe2+UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotation

Keywords - Biological processi

Fatty acid biosynthesisUniRule annotation, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Names & Taxonomyi

Protein namesi
Submitted name:
Stearoyl-CoA desaturase variantImported
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei79 – 10022HelicalSequence analysisAdd
BLAST
Transmembranei112 – 13019HelicalSequence analysisAdd
BLAST
Transmembranei229 – 24618HelicalSequence analysisAdd
BLAST
Transmembranei258 – 28023HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Proteomic databases

PaxDbiQ59GX7.
PRIDEiQ59GX7.

Interactioni

Protein-protein interaction databases

STRINGi9606.ENSP00000359380.

Family & Domainsi

Domaini

The histidine box domains are involved in binding the catalytic metal ions.UniRule annotation

Sequence similaritiesi

Belongs to the fatty acid desaturase type 1 family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helixSequence analysis

Phylogenomic databases

eggNOGiKOG1600. Eukaryota.
COG1398. LUCA.
HOGENOMiHOG000270352.
HOVERGENiHBG003367.

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: Fragment.

Q59GX7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
SRHPRAKMPA HLLQDDISSS YTTTTTITAP PSRVLQNGGD KLETMPLYLE
60 70 80 90 100
DDIRPDIKDD IYDPTYKDKE GPSPKVEYVW RNIILMSLLH LGALYGITLI
110 120 130 140 150
PTCKFYTWLW GVFYYFVSAL GITAGAHRLW SHRSYKARLP LRLFLIIANT
160 170 180 190 200
MAFQNDVYEW ARDHRAHHKF SETHADPHNS RRGFFFSHVG WLLVRKHPAV
210 220 230 240 250
KEKGSTLDLS DLEAEKLVMF QRRYYKPGLL LMCFILPTLV PWYFWGETFQ
260 270 280 290 300
NSVFVATFLR YAVVLNATWL VNSAAHLFGY RPYDKNISPR ENILVSLGAV
310 320 330 340 350
GEGFHNYHHS FPYDYSASEY RWHINFTTFF IDCMAALGLA YDRKKVSKAA
360
ILARIKRTGD GNYKSG
Length:366
Mass (Da):42,338
Last modified:April 26, 2005 - v1
Checksum:iA549E1EC77C826AF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11Imported

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB208982 mRNA. Translation: BAD92219.1.
UniGeneiHs.558396.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB208982 mRNA. Translation: BAD92219.1.
UniGeneiHs.558396.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000359380.

Proteomic databases

PaxDbiQ59GX7.
PRIDEiQ59GX7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1600. Eukaryota.
COG1398. LUCA.
HOGENOMiHOG000270352.
HOVERGENiHBG003367.

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...

Entry informationi

Entry nameiQ59GX7_HUMAN
AccessioniPrimary (citable) accession number: Q59GX7
Entry historyi
Integrated into UniProtKB/TrEMBL: April 26, 2005
Last sequence update: April 26, 2005
Last modified: May 11, 2016
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)
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.

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.