Q9Y5P4A8K7S2B3KUB7Q53YV1Q53YV2Q96Q85Q96Q88Q9H2S7Q9H2S8CERT_HUMANCeramide transfer proteinhCERTCollagen type IV alpha-3-binding proteinGoodpasture antigen-binding proteinGPBPSTART domain-containing protein 11StARD11StAR-related lipid transfer protein 11CERT1CERTCOL4A3BPSTARD11Homo sapiensHumanEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomoCharacterization of a novel type of serine/threonine kinase that specifically phosphorylates the human goodpasture antigen.NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1)CHARACTERIZATIONGoodpasture antigen-binding protein, the kinase that phosphorylates the Goodpasture antigen, is an alternatively spliced variant implicated in autoimmune pathogenesis.NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2)Molecular machinery for non-vesicular trafficking of ceramide.NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2)FUNCTIONDOMAIN STARTComplete sequencing and characterization of 21,243 full-length human cDNAs.NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3)The DNA sequence and comparative analysis of human chromosome 5.NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2)Homo sapiens genomic sequence, containing DINB1 and GPBP gene.NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Efficient trafficking of ceramide from the endoplasmic reticulum to the Golgi apparatus requires a VAMP-associated protein-interacting FFAT motif of CERT.INTERACTION WITH VAPA AND VAPBSUBCELLULAR LOCATIONMUTAGENESIS OF ASP-324DOMAIN FFAT MOTIFDOMAIN PHRegulation of secretory transport by protein kinase D-mediated phosphorylation of the ceramide transfer protein.PHOSPHORYLATION AT SER-132FUNCTIONMUTAGENESIS OF SER-132A quantitative atlas of mitotic phosphorylation.PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Casein kinase I{gamma}2 down-regulates trafficking of ceramide in the synthesis of sphingomyelin.PHOSPHORYLATION BY CSNK1G2/CK1Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Initial characterization of the human central proteome.IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Toward a comprehensive characterization of a human cancer cell phosphoproteome.PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126; TYR-372; SER-373 AND SER-380IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Large-scale discovery of novel genetic causes of developmental disorders.INVOLVEMENT IN MRD34VARIANT MRD34 LEU-132Identification of MOSPD2, a novel scaffold for endoplasmic reticulum membrane contact sites.IDENTIFICATION BY MASS SPECTROMETRYINTERACTION WITH MOSPD2SUBCELLULAR LOCATIONDOMAINFFAT MOTIFMUTAGENESIS OF ASP-324Structural basis for specific lipid recognition by CERT responsible for nonvesicular trafficking of ceramide.X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 347-624 IN COMPLEXES WITH CERAMIDES AND DIACYLGLYCEROLMUTAGENESIS OF GLU-472; GLN-493 AND ASN-530FUNCTIONSUBCELLULAR LOCATIONCERAMIDE-BINDINGCrystal structures of the CERT START domain with inhibitors provide insights into the mechanism of ceramide transfer.X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) OF 347-624 IN COMPLEXES WITH CERAMIDE AND INHIBITORMUTAGENESIS OF TRP-499FUNCTIONCERAMIDE-BINDINGDiagnostic exome sequencing in persons with severe intellectual disability.VARIANT CYS-138De novo mutations in moderate or severe intellectual disability.VARIANT MRD34 ARG-243Shelters ceramides and diacylglycerol lipids inside its START domain and mediates the intracellular trafficking of ceramides and diacylglycerol lipids in a non-vesicular manner.N-hexadecanoylsphing-4-enine(in) = N-hexadecanoylsphing-4-enine(out)Interacts with VAPA and VAPB. Interaction with VAPB is less efficient than with VAPA (PubMed:16895911). Interacts (via FFAT motif) with MOSPD2 (via MSP domain) (PubMed:29858488).Q9Y5P4Q9H568false3Q9Y5P4Q15041false5Q9Y5P4P78368false5Q9Y5P4Q13352false4Q9Y5P4O95197false3Q9Y5P4Q9NQC3false3Q9Y5P4-1P02743false6Q9Y5P4-2Q9H568false3Q9Y5P4-2P02743false4Q9Y5P4-2Q15041false3Q9Y5P4-2Q8WZ55false3Q9Y5P4-2Q9Y5P4-2false3Q9Y5P4-2P78368false4Q9Y5P4-2Q9UET6false3Q9Y5P4-2Q9UPX6false3Q9Y5P4-2Q8IYS1false3Q9Y5P4-2Q96HR9-2false3Q9Y5P4-2Q2TAY7false3Q9Y5P4-2P32856-2false3CytoplasmGolgi apparatusEndoplasmic reticulumPreferentially localized to the Golgi apparatus.Q9Y5P4-11CERTLQ9Y5P4-22Delta26GPBPD26CERTQ9Y5P4-33Widely expressed.The START domain recognizes ceramides and diacylglycerol lipids, interacts with membranes, and mediates the intermembrane transfer of ceramides and diacylglycerol lipids.The PH domain targets the Golgi apparatus.The FFAT motif is required for interaction with VAPA, VAPB and MOSPD2.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.Intellectual developmental disorder, autosomal dominant 34
MRD34
A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptive behavior and manifested during the developmental period.The disease is caused by variants affecting the gene represented in this entry.Was originally reported to have a protein kinase activity and to phosphorylate on Ser and Thr residues the Goodpasture autoantigen (in vitro).3D-structureAlternative splicingCoiled coilCytoplasmDisease variantEndoplasmic reticulumGolgi apparatusIntellectual disabilityLipid transportLipid-bindingPhosphoproteinReference proteomeTransportan N-acylsphing-4-eninean N-acylsphing-4-eninean N-acylsphing-4-eninean N-acylsphing-4-enineMMQHSCIPTPPSPFSAPPAFLPVVTRESRRGLSSGGSAGRNAGVTATAAAADGWKGRLPSPLVLLPRSARCQARRRRGGRTSSLLLLPPTPERALFASPSPDPSPRGLGASSGAAEGAGAGLLLGCRASMSLSCGRKRSADAEAQAWANAWAMSDNQSWNSSGSEEDPETESGPPVERCGVLSKWTNYIHGWQDRWVVLKNNALSYYKSEDETEYGCRGSICLSKAVITPHDFDECRFDISVNDSVWYLRAQDPDHRQQWIDAIEQHKTESGYGSESSLRRHGSMVSLVSGASGYSATSTSSFKKGHSLREKLAEMETFRDILCRQVDTLQKYFDACADAVSKDELQRDKVVEDDEDDFPTTRSDGDFLHSTNGNKEKLFPHVTPKGINGIDFKGEAITFKATTAGILATLSHCIELMVKREDSWQKRLDKETEKKRRTEEAYKNAMTELKKKSHFGGPDYEEGPNSLINEEEFFDAVEAALDRQDKIEEQSQSEKVRLHWPTSLPSGDAFSSVGTHRFVQKPYSRSSSMSSIDLVSASDDVHRFSSQVEEMVQNHMTYSLQDVGGDANWQLVVEEGEMKVYRREVEENGIVLDPLKATHAVKGVTGHEVCNYFWNVDVRNDWETTIENFHVVETLADNAIIIYQTHKRVWPASQRDVLYLSVIRKIPALTENDPETWIVCNFSVDHDSAPLNNRCVRAKINVAMICQTLVSPPEGNQEISRDNILCKITYVANVNPGGWAPASVLRAVAKREYPKFLKRFTSYVQEKTAGKPILF
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