EBP
entrez
10682
canonical
uniprot
Q15125
canonical
ensembl
ENSG00000147155
resolver
ensp
ENSP00000417052
resolver
ensp
ENSP00000552132
resolver
ensp
ENSP00000552134
resolver
ensp
ENSP00000552135
resolver
ensp
ENSP00000552136
resolver
ensp
ENSP00000552137
resolver
ensp
ENSP00000552138
resolver
ensp
ENSP00000552139
resolver
ensp
ENSP00000552140
resolver
ensp
ENSP00000552141
resolver
ensp
ENSP00000552142
resolver
ensp
ENSP00000606616
resolver
ensp
ENSP00000639182
resolver
enst
ENST00000495186
resolver
enst
ENST00000882073
resolver
enst
ENST00000882075
resolver
enst
ENST00000882076
resolver
enst
ENST00000882077
resolver
enst
ENST00000882078
resolver
enst
ENST00000882079
resolver
enst
ENST00000882080
resolver
enst
ENST00000882081
resolver
enst
ENST00000882082
resolver
enst
ENST00000882083
resolver
enst
ENST00000936557
resolver
enst
ENST00000969123
resolver
genesymbol
EBP
resolver
hgnc
HGNC:3133
resolver
uniprot
A0A024QYX0
resolver
uniprot
Q6FGL3
resolver
uniprot
Q6IBI9
resolver
uniprot_entry
A0A024QYX0_HUMAN
resolver
uniprot_entry
EBP_HUMAN
resolver
uniprot_sec
Q6FGL3
resolver
uniprot_sec
Q6IBI9
resolver
activity_regulation
ACTIVITY REGULATION: Cholestenol Delta-isomerase and cholesterol-5,6-epoxide hydrolase (ChEH) activities are inhibited by tamoxifen and the selective AEBS ligand (4-benzyl-phenoxy)-ethyl-N-pyrrolidine (PBPE) (PubMed:15175332, PubMed:20615952). ChEH activity is inhibited by oleic acid (PubMed:20615952). {ECO:0000269|PubMed:15175332, ECO:0000269|PubMed:20615952}.
uniprot
proteins
amino_acid_sequence
MTTNAGPLHPYWPQHLRLDNFVPNDRPTWHILAGLFSVTGVLVVTTWLLSGRAAVVPLGTWRRLSLCWFAVCGFIHLVIEGWFVLYYEDLLGDQAFLSQLWKEYAKGDSRYILGDNFTVCMETITACLWGPLSLWVVIAFLRQHPLRFILQLVVSVGQIYGDVLYFLTEHRDGFQHGELGHPLYFWFYFVFMNALWLVLPGVLVLDAVKHLTHAQSTLDAKATKAKSKKN
uniprot
proteins
disease_involvement
DISEASE: Chondrodysplasia punctata 2, X-linked dominant (CDPX2) [MIM:302960]: A clinically and genetically heterogeneous disorder characterized by punctiform calcification of the bones. The key clinical features of CDPX2 are chondrodysplasia punctata, linear ichthyosis, cataracts and short stature. CDPX2 is a rare disorder of defective cholesterol biosynthesis, biochemically characterized by an increased amount of 8-dehydrocholesterol and cholest-8(9)-en-3-beta-ol in the plasma and tissues. {ECO:0000269|PubMed:10391218, ECO:0000269|PubMed:10391219, ECO:0000269|PubMed:10942423, ECO:0000269|PubMed:11493318, ECO:0000269|PubMed:18176751, ECO:0000269|PubMed:25814754}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: MEND syndrome (MEND) [MIM:300960]: An X-linked recessive disorder associated with a defect in sterol biosynthesis. Disease manifestations and severity are highly variable. Clinical features include intellectual disability, short stature, scoliosis, digital abnormalities, cataracts, and dermatologic abnormalities. {ECO:0000269|PubMed:12503101, ECO:0000269|PubMed:20949533, ECO:0000269|PubMed:24459067, ECO:0000269|PubMed:24700572}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.3.2.11
uniprot
proteins
ec_number
5.3.3.5
uniprot
proteins
function
FUNCTION: Isomerase that catalyzes the conversion of Delta(8)-sterols to their corresponding Delta(7)-isomers a catalytic step in the postlanosterol biosynthesis of cholesterol. {ECO:0000269|PubMed:12760743, ECO:0000269|PubMed:8798407, ECO:0000269|PubMed:9894009}.; FUNCTION: Component of the microsomal antiestrogen binding site (AEBS), a multiproteic complex at the ER membrane that consists of an association between EBP and 7-dehydrocholesterol reductase/DHCR7 (PubMed:15175332, PubMed:20615952). This complex is responsible for cholesterol-5,6-epoxide hydrolase (ChEH) activity, which consists in the hydration of cholesterol-5,6-epoxides (5,6-EC) into cholestane-3beta,5alpha,6beta-triol (CT) (PubMed:20615952). The precise role of each component of this complex has not been described yet (PubMed:20615952). {ECO:0000269|PubMed:15175332, ECO:0000269|PubMed:20615952}.
uniprot
proteins
mass_dalton
26353
uniprot
proteins
mutagenesis
MUTAGEN 68; /note="W->A: Reduces catalytic activity to less than 35% of wild-type."; /evidence="ECO:0000269|PubMed:9894009"; MUTAGEN 75; /note="I->A: Reduces catalytic activity to less than 35% of wild-type."; /evidence="ECO:0000269|PubMed:9894009"; MUTAGEN 76; /note="H->A: Reduces catalytic activity to less than 10% of wild-type."; /evidence="ECO:0000269|PubMed:9894009"; MUTAGEN 80; /note="E->A: Reduces catalytic activity to less than 10% of wild-type."; /evidence="ECO:0000269|PubMed:9894009"; MUTAGEN 111; /note="Y->W: Reduces catalytic activity to less than 2% of wild-type."; /evidence="ECO:0000269|PubMed:12760743"; MUTAGEN 121; /note="M->A: Reduces catalytic activity to less than 35% of wild-type."; /evidence="ECO:0000269|PubMed:12760743"; MUTAGEN 121; /note="M->V: No effect on catalytic activity."; /evidence="ECO:0000269|PubMed:12760743"; MUTAGEN 122; /note="E->A: Reduces catalytic activity to less than 10% of wild-type."; /evidence="ECO:0000269|PubMed:9894009"; MUTAGEN 125; /note="T->A: Reduces catalytic activity to less than 10% of wild-type."; /evidence="ECO:0000269|PubMed:9894009"; MUTAGEN 188; /note="Y->A: Reduces catalytic activity to less than 35% of wild-type."; /evidence="ECO:0000269|PubMed:9894009"; MUTAGEN 189; /note="F->A: Reduces catalytic activity to less than 35% of wild-type."; /evidence="ECO:0000269|PubMed:12760743"; MUTAGEN 189; /note="F->L: No effect on catalytic activity."; /evidence="ECO:0000269|PubMed:12760743"; MUTAGEN 193; /note="N->A: Reduces catalytic activity to less than 10% of wild-type."; /evidence="ECO:0000269|PubMed:9894009"; MUTAGEN 196; /note="W->A: Reduces catalytic activity to less than 10% of wild-type."; /evidence="ECO:0000269|PubMed:9894009
uniprot
proteins
pathway_participation
PATHWAY: Steroid biosynthesis; cholesterol biosynthesis. {ECO:0000269|PubMed:12760743, ECO:0000269|PubMed:8798407, ECO:0000269|PubMed:9894009}.
uniprot
proteins
protein_family
EBP family
uniprot
proteins
pubmed
10391218
uniprot
proteins
pubmed
10391219
uniprot
proteins
pubmed
10406945
uniprot
proteins
pubmed
10942423
uniprot
proteins
pubmed
11493318
uniprot
proteins
pubmed
12503101
uniprot
proteins
pubmed
12760743
uniprot
proteins
pubmed
15175332
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
18176751
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
20615952
uniprot
proteins
pubmed
20949533
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
24459067
uniprot
proteins
pubmed
24700572
uniprot
proteins
pubmed
25814754
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
7706302
uniprot
proteins
pubmed
8798407
uniprot
proteins
pubmed
9894009
uniprot
proteins
sequence_length
230
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10406945}; Multi-pass membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000269|PubMed:10406945}. Cytoplasmic vesicle {ECO:0000269|PubMed:10406945}. Note=During interphase, detected on the endoplasmic reticulum and the nuclear envelope. During mitosis, detected on cytoplasmic vesicles. {ECO:0000269|PubMed:10406945}.
uniprot
proteins
transmembrane_region
TRANSMEM 29..49; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 66..86; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 121..141; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 185..205; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins