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Protein

Squalene monooxygenase

Gene

SQLE

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

Functioni

Catalyzes the first oxygenation step in sterol biosynthesis and is suggested to be one of the rate-limiting enzymes in this pathway.

Catalytic activityi

Squalene + NADPH + O2 = (3S)-2,3-epoxy-2,3-dihydrosqualene + NADP+ + H2O.

Cofactori

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi126 – 15328FADSequence AnalysisAdd
BLAST

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: InterPro
  2. squalene monooxygenase activity Source: UniProtKB

GO - Biological processi

  1. cellular aromatic compound metabolic process Source: Ensembl
  2. cholesterol biosynthetic process Source: Reactome
  3. response to organic substance Source: Ensembl
  4. small molecule metabolic process Source: Reactome
  5. sterol biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein, NADP

Enzyme and pathway databases

BioCyciMetaCyc:HS02595-MONOMER.
ReactomeiREACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_9405. Cholesterol biosynthesis.
SABIO-RKQ14534.
UniPathwayiUPA00767; UER00752.

Names & Taxonomyi

Protein namesi
Recommended name:
Squalene monooxygenase (EC:1.14.13.132)
Alternative name(s):
Squalene epoxidase
Short name:
SE
Gene namesi
Name:SQLE
Synonyms:ERG1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:11279. SQLE.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei20 – 4021HelicalSequence AnalysisAdd
BLAST
Transmembranei61 – 8121HelicalSequence AnalysisAdd
BLAST
Transmembranei123 – 14321HelicalSequence AnalysisAdd
BLAST
Transmembranei546 – 56621HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: Reactome
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36108.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 574574Squalene monooxygenasePRO_0000209838Add
BLAST

Proteomic databases

MaxQBiQ14534.
PaxDbiQ14534.
PRIDEiQ14534.

PTM databases

PhosphoSiteiQ14534.

Expressioni

Gene expression databases

BgeeiQ14534.
CleanExiHS_SQLE.
ExpressionAtlasiQ14534. baseline and differential.
GenevestigatoriQ14534.

Organism-specific databases

HPAiHPA018038.
HPA020762.

Interactioni

Subunit structurei

May form a complex with squalene synthase.

Protein-protein interaction databases

BioGridi112591. 7 interactions.
IntActiQ14534. 3 interactions.
STRINGi9606.ENSP00000265896.

Structurei

3D structure databases

ProteinModelPortaliQ14534.
SMRiQ14534. Positions 124-185.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the squalene monooxygenase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0654.
HOGENOMiHOG000174713.
HOVERGENiHBG005603.
InParanoidiQ14534.
KOiK00511.
OMAiFYKKFGD.
OrthoDBiEOG7J446G.
PhylomeDBiQ14534.
TreeFamiTF331056.

Family and domain databases

InterProiIPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR003042. Rng_hydrolase-like.
IPR013698. Squalene_epoxidase.
[Graphical view]
PfamiPF00070. Pyr_redox. 1 hit.
PF08491. SE. 1 hit.
[Graphical view]
PRINTSiPR00420. RNGMNOXGNASE.

Sequencei

Sequence statusi: Complete.

Q14534-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWTFLGIATF TYFYKKFGDF ITLANREVLL CVLVFLSLGL VLSYRCRHRN
60 70 80 90 100
GGLLGRQQSG SQFALFSDIL SGLPFIGFFW AKSPPESENK EQLEARRRRK
110 120 130 140 150
GTNISETSLI GTAACTSTSS QNDPEVIIVG AGVLGSALAA VLSRDGRKVT
160 170 180 190 200
VIERDLKEPD RIVGEFLQPG GYHVLKDLGL GDTVEGLDAQ VVNGYMIHDQ
210 220 230 240 250
ESKSEVQIPY PLSENNQVQS GRAFHHGRFI MSLRKAAMAE PNAKFIEGVV
260 270 280 290 300
LQLLEEDDVV MGVQYKDKET GDIKELHAPL TVVADGLFSK FRKSLVSNKV
310 320 330 340 350
SVSSHFVGFL MKNAPQFKAN HAELILANPS PVLIYQISSS ETRVLVDIRG
360 370 380 390 400
EMPRNLREYM VEKIYPQIPD HLKEPFLEAT DNSHLRSMPA SFLPPSSVKK
410 420 430 440 450
RGVLLLGDAY NMRHPLTGGG MTVAFKDIKL WRKLLKGIPD LYDDAAIFEA
460 470 480 490 500
KKSFYWARKT SHSFVVNILA QALYELFSAT DDSLHQLRKA CFLYFKLGGE
510 520 530 540 550
CVAGPVGLLS VLSPNPLVLI GHFFAVAIYA VYFCFKSEPW ITKPRALLSS
560 570
GAVLYKACSV IFPLIYSEMK YMVH
Length:574
Mass (Da):63,923
Last modified:May 17, 2010 - v3
Checksum:i6957F5CF1F1624C8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 431S → F in BX647400 (PubMed:17974005).Curated
Sequence conflicti58 – 581Q → R in BAA22372 (PubMed:9286711).Curated
Sequence conflicti94 – 941E → G in BAA22372 (PubMed:9286711).Curated
Sequence conflicti139 – 1391A → V in BAA22372 (PubMed:9286711).Curated
Sequence conflicti247 – 2471E → G in BAA11209 (PubMed:8626488).Curated
Sequence conflicti334 – 3341I → T in BX647400 (PubMed:17974005).Curated
Sequence conflicti336 – 3361Q → R in BAA22372 (PubMed:9286711).Curated
Sequence conflicti379 – 3802AT → VA in BX647400 (PubMed:17974005).Curated
Sequence conflicti389 – 3891P → L in BAA22372 (PubMed:9286711).Curated
Sequence conflicti451 – 4511K → N in BAA22372 (PubMed:9286711).Curated
Sequence conflicti518 – 5181V → A in BAA22372 (PubMed:9286711).Curated
Sequence conflicti551 – 5511G → S in BAA22372 (PubMed:9286711).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78130 mRNA. Translation: BAA22372.1.
BX647400 mRNA. No translation available.
AC009908 Genomic DNA. No translation available.
FJ695197 Genomic DNA. No translation available.
D78129 mRNA. Translation: BAA11209.1.
CCDSiCCDS47918.1.
RefSeqiNP_003120.2. NM_003129.3.
UniGeneiHs.71465.

Genome annotation databases

EnsembliENST00000265896; ENSP00000265896; ENSG00000104549.
GeneIDi6713.
KEGGihsa:6713.
UCSCiuc011liq.2. human.

Polymorphism databases

DMDMi296439362.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D78130 mRNA. Translation: BAA22372.1.
BX647400 mRNA. No translation available.
AC009908 Genomic DNA. No translation available.
FJ695197 Genomic DNA. No translation available.
D78129 mRNA. Translation: BAA11209.1.
CCDSiCCDS47918.1.
RefSeqiNP_003120.2. NM_003129.3.
UniGeneiHs.71465.

3D structure databases

ProteinModelPortaliQ14534.
SMRiQ14534. Positions 124-185.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112591. 7 interactions.
IntActiQ14534. 3 interactions.
STRINGi9606.ENSP00000265896.

Chemistry

BindingDBiQ14534.
ChEMBLiCHEMBL3592.
DrugBankiDB01091. Butenafine.
DB00735. Naftifine.
DB00857. Terbinafine.

PTM databases

PhosphoSiteiQ14534.

Polymorphism databases

DMDMi296439362.

Proteomic databases

MaxQBiQ14534.
PaxDbiQ14534.
PRIDEiQ14534.

Protocols and materials databases

DNASUi6713.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265896; ENSP00000265896; ENSG00000104549.
GeneIDi6713.
KEGGihsa:6713.
UCSCiuc011liq.2. human.

Organism-specific databases

CTDi6713.
GeneCardsiGC08P126010.
H-InvDBHIX0007779.
HGNCiHGNC:11279. SQLE.
HPAiHPA018038.
HPA020762.
MIMi602019. gene.
neXtProtiNX_Q14534.
PharmGKBiPA36108.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0654.
HOGENOMiHOG000174713.
HOVERGENiHBG005603.
InParanoidiQ14534.
KOiK00511.
OMAiFYKKFGD.
OrthoDBiEOG7J446G.
PhylomeDBiQ14534.
TreeFamiTF331056.

Enzyme and pathway databases

UniPathwayiUPA00767; UER00752.
BioCyciMetaCyc:HS02595-MONOMER.
ReactomeiREACT_147904. Activation of gene expression by SREBF (SREBP).
REACT_9405. Cholesterol biosynthesis.
SABIO-RKQ14534.

Miscellaneous databases

ChiTaRSiSQLE. human.
GeneWikiiSqualene_monooxygenase.
GenomeRNAii6713.
NextBioi26182.
PROiQ14534.
SOURCEiSearch...

Gene expression databases

BgeeiQ14534.
CleanExiHS_SQLE.
ExpressionAtlasiQ14534. baseline and differential.
GenevestigatoriQ14534.

Family and domain databases

InterProiIPR001327. Pyr_OxRdtase_NAD-bd_dom.
IPR003042. Rng_hydrolase-like.
IPR013698. Squalene_epoxidase.
[Graphical view]
PfamiPF00070. Pyr_redox. 1 hit.
PF08491. SE. 1 hit.
[Graphical view]
PRINTSiPR00420. RNGMNOXGNASE.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Localization of the squalene epoxidase gene (SQLE) to human chromosome region 8q24.1."
    Nagai M., Sakakibara J., Wakui K., Fukushima Y., Igarashi S., Tsuji S., Arakawa M., Ono T.
    Genomics 44:141-143(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon endothelium.
  3. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Transcriptional regulation of squalene epoxidase by sterols and inhibitors in HeLa cells."
    Nakamura Y., Sakakibara J., Izumi T., Shibata A., Ono T.
    J. Biol. Chem. 271:8053-8056(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 187-535.
    Tissue: Liver.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiERG1_HUMAN
AccessioniPrimary (citable) accession number: Q14534
Secondary accession number(s): Q9UEK6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1997
Last sequence update: May 17, 2010
Last modified: March 3, 2015
This is version 128 of the entry and version 3 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.