CERT1
entrez
10087
canonical
uniprot
Q9Y5P4
canonical
ensembl
ENSG00000113163
resolver
ensp
ENSP00000261415
resolver
ensp
ENSP00000383996
resolver
ensp
ENSP00000493563
resolver
ensp
ENSP00000494110
resolver
ensp
ENSP00000495760
resolver
ensp
ENSP00000496016
resolver
ensp
ENSP00000496243
resolver
enst
ENST00000642556
resolver
genesymbol
CERT1
resolver
genesymbol_syn
CERT
resolver
genesymbol_syn
COL4A3BP
resolver
genesymbol_syn
STARD11
resolver
hgnc
HGNC:2205
resolver
uniprot
A0A2R8Y7C5
resolver
uniprot
A8K7S2
resolver
uniprot
B3KUB7
resolver
uniprot
Q53YV1
resolver
uniprot
Q53YV2
resolver
uniprot
Q96Q85
resolver
uniprot
Q96Q88
resolver
uniprot
Q9H2S7
resolver
uniprot
Q9H2S8
resolver
uniprot_entry
A0A2R8Y7C5_HUMAN
resolver
uniprot_entry
CERT_HUMAN
resolver
uniprot_sec
A8K7S2
resolver
uniprot_sec
B3KUB7
resolver
uniprot_sec
Q53YV1
resolver
uniprot_sec
Q53YV2
resolver
uniprot_sec
Q96Q85
resolver
uniprot_sec
Q96Q88
resolver
uniprot_sec
Q9H2S7
resolver
uniprot_sec
Q9H2S8
resolver
amino_acid_sequence
MSDNQSWNSSGSEEDPETESGPPVERCGVLSKWTNYIHGWQDRWVVLKNNALSYYKSEDETEYGCRGSICLSKAVITPHDFDECRFDISVNDSVWYLRAQDPDHRQQWIDAIEQHKTESGYGSESSLRRHGSMVSLVSGASGYSATSTSSFKKGHSLREKLAEMETFRDILCRQVDTLQKYFDACADAVSKDELQRDKVVEDDEDDFPTTRSDGDFLHSTNGNKEKLFPHVTPKGINGIDFKGEAITFKATTAGILATLSHCIELMVKREDSWQKRLDKETEKKRRTEEAYKNAMTELKKKSHFGGPDYEEGPNSLINEEEFFDAVEAALDRQDKIEEQSQSEKVRLHWPTSLPSGDAFSSVGTHRFVQKPYSRSSSMSSIDLVSASDDVHRFSSQVEEMVQNHMTYSLQDVGGDANWQLVVEEGEMKVYRREVEENGIVLDPLKATHAVKGVTGHEVCNYFWNVDVRNDWETTIENFHVVETLADNAIIIYQTHKRVWPASQRDVLYLSVIRKIPALTENDPETWIVCNFSVDHDSAPLNNRCVRAKINVAMICQTLVSPPEGNQEISRDNILCKITYVANVNPGGWAPASVLRAVAKREYPKFLKRFTSYVQEKTAGKPILF
uniprot
proteins
disease_involvement
DISEASE: Neurodevelopmental disorder with hypotonia, speech delay, and dysmorphic facies (NEDHSF) [MIM:616351]: An autosomal dominant disorder characterized by mild to profound developmental delay with hypotonia, delayed motor skills, impaired intellectual development, poor or absent speech, and behavioral abnormalities. Some patients are non-verbal and non-ambulatory. Additional features may include early feeding difficulties, poor overall growth, seizures, brain imaging abnormalities, and dysmorphic facial features. {ECO:0000269|PubMed:25356899, ECO:0000269|PubMed:25533962}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Shelters ceramides inside its steroidogenic acute regulatory lipid transfer (START) domain and mediates their intracellular trafficking in a non-vesicular manner from the endoplasmic reticulum to the Golgi apparatus for conversion to sphingomyelin (PubMed:14685229, PubMed:15596449, PubMed:17392267, PubMed:17591919, PubMed:18184806, PubMed:20036255). Efficiently transfers ceramide molecules having long-chain fatty chains, but not those with very long acyl chains (PubMed:15596449, PubMed:18184806). Capable of transferring diacylglycerol, although with very low efficiency (PubMed:18184806). {ECO:0000269|PubMed:14685229, ECO:0000269|PubMed:15596449, ECO:0000269|PubMed:17392267, ECO:0000269|PubMed:17591919, ECO:0000269|PubMed:18184806, ECO:0000269|PubMed:20036255}.
uniprot
proteins
mass_dalton
70835
uniprot
proteins
mutagenesis
MUTAGEN 132; /note="S->A: Abolishes the phosphorylation. Strongly reduces the interaction with phosphatidylinositol 4-phosphate. Increases the ceramide transfer activity."; /evidence="ECO:0000269|PubMed:17591919"; MUTAGEN 324; /note="D->A: Impairs the endoplasmic reticulum-to-Golgi ceramide trafficking and abolishes the interaction with VAPA and MOSPD2."; /evidence="ECO:0000269|PubMed:16895911, ECO:0000269|PubMed:29858488"; MUTAGEN 472; /note="E->A: Reduces ceramide transfer."; /evidence="ECO:0000269|PubMed:18184806"; MUTAGEN 493; /note="Q->A: No effect on ceramide transfer activity."; /evidence="ECO:0000269|PubMed:18184806"; MUTAGEN 499; /note="W->A: Reduces affinity for membranes. Abolishes ceramide transfer; when associated with A-588."; /evidence="ECO:0000269|PubMed:20036255"; MUTAGEN 530; /note="N->A: Reduces ceramide transfer."; /evidence="ECO:0000269|PubMed:18184806"; MUTAGEN 588; /note="W->A: Abolishes ceramide transfer; when associated with A-499.
uniprot
proteins
post_translational_modification
PTM: Phosphorylation on Ser-132 decreases the affinity toward phosphatidylinositol 4-phosphate at Golgi membranes and reduces ceramide transfer activity. Inactivated by hyperphosphorylation of serine residues by CSNK1G2/CK1 that triggers dissociation from the Golgi complex, thus down-regulating ER-to-Golgi transport of ceramide and sphingomyelin synthesis. {ECO:0000269|PubMed:17591919, ECO:0000269|PubMed:19005213}.
uniprot
proteins
pubmed
10212244
uniprot
proteins
pubmed
11007769
uniprot
proteins
pubmed
14685229
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15596449
uniprot
proteins
pubmed
16895911
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17392267
uniprot
proteins
pubmed
17591919
uniprot
proteins
pubmed
18184806
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19005213
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20036255
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23033978
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25356899
uniprot
proteins
pubmed
25533962
uniprot
proteins
pubmed
29858488
uniprot
proteins
sequence_length
624
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16895911, ECO:0000269|PubMed:18184806}. Golgi apparatus {ECO:0000269|PubMed:16895911, ECO:0000269|PubMed:18184806, ECO:0000269|PubMed:29858488}. Endoplasmic reticulum {ECO:0000269|PubMed:16895911, ECO:0000269|PubMed:18184806}. Note=Preferentially localized to the Golgi apparatus. {ECO:0000305|PubMed:16895911}.
uniprot
proteins