O94855 · SC24D_HUMAN
- ProteinProtein transport protein Sec24D
- GeneSEC24D
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1032 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Plays a central role in cargo selection within the COPII complex and together with SEC24C may have a different specificity compared to SEC24A and SEC24B (PubMed:17499046, PubMed:18843296, PubMed:20427317).
May more specifically package GPI-anchored proteins through the cargo receptor TMED10 (PubMed:20427317).
May also be specific for IxM motif-containing cargos like the SNAREs GOSR2 and STX5 (PubMed:18843296).
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | COPII vesicle coat | |
Cellular Component | cytosol | |
Cellular Component | endoplasmic reticulum exit site | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | ER to Golgi transport vesicle membrane | |
Cellular Component | intracellular membrane-bounded organelle | |
Molecular Function | SNARE binding | |
Molecular Function | zinc ion binding | |
Biological Process | COPII-coated vesicle cargo loading | |
Biological Process | endoplasmic reticulum to Golgi vesicle-mediated transport | |
Biological Process | in utero embryonic development | |
Biological Process | intracellular protein transport |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein transport protein Sec24D
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO94855
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Cole-Carpenter syndrome 2 (CLCRP2)
- Note
- DescriptionA form of Cole-Carpenter syndrome, a disorder characterized by features of osteogenesis imperfecta such as bone deformities and severe bone fragility with frequent fractures, in association with craniosynostosis, ocular proptosis, hydrocephalus, growth failure and distinctive facial features. Craniofacial findings include marked frontal bossing, midface hypoplasia, and micrognathia. Despite the craniosynostosis and hydrocephalus, intellectual development is normal. CLCRP2 inheritance is autosomal recessive.
- See alsoMIM:616294
Natural variants in CLCRP2
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_073658 | 978 | Q>P | in CLCRP2; dbSNP:rs786204846 | |
VAR_073659 | 1015 | S>F | in CLCRP2; dbSNP:rs760670617 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_047472 | 42 | in dbSNP:rs10029206 | |||
Sequence: M → T | ||||||
Natural variant | VAR_047473 | 193 | in dbSNP:rs6844109 | |||
Sequence: P → L | ||||||
Natural variant | VAR_047474 | 496 | in dbSNP:rs11723368 | |||
Sequence: F → I | ||||||
Natural variant | VAR_073658 | 978 | in CLCRP2; dbSNP:rs786204846 | |||
Sequence: Q → P | ||||||
Natural variant | VAR_073659 | 1015 | in CLCRP2; dbSNP:rs760670617 | |||
Sequence: S → F |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,125 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000205157 | 1-1032 | UniProt | Protein transport protein Sec24D | |||
Sequence: MSQQGYVATPPYSQPQPGIGLSPPHYGHYGDPSHTASPTGMMKPAGPLGATATRGMLPPGPPPPGPHQFGQNGAHATGHPPQRFPGPPPVNNVASSHAPYQPSAQSSYPGPISTSSVTQLGSQLSAMQINSYGSGMAPPSQGPPGPLSATSLQTPPRPPQPSILQPGSQVLPPPPTTLNGPGASPLPLPMYRPDGLSGPPPPNAQYQPPPLPGQTLGAGYPPQQANSGPQMAGAQLSYPGGFPGGPAQMAGPPQPQKKLDPDSIPSPIQVIENDRASRGGQVYATNTRGQIPPLVTTDCMIQDQGNASPRFIRCTTYCFPCTSDMAKQAQIPLAAVIKPFATIPSNESPLYLVNHGESGPVRCNRCKAYMCPFMQFIEGGRRYQCGFCNCVNDVPPFYFQHLDHIGRRLDHYEKPELSLGSYEYVATLDYCRKSKPPNPPAFIFMIDVSYSNIKNGLVKLICEELKTMLEKIPKEEQEETSAIRVGFITYNKVLHFFNVKSNLAQPQMMVVTDVGEVFVPLLDGFLVNYQESQSVIHNLLDQIPDMFADSNENETVFAPVIQAGMEALKAADCPGKLFIFHSSLPTAEAPGKLKNRDDKKLVNTDKEKILFQPQTNVYDSLAKDCVAHGCSVTLFLFPSQYVDVASLGLVPQLTGGTLYKYNNFQMHLDRQQFLNDLRNDIEKKIGFDAIMRVRTSTGFRATDFFGGILMNNTTDVEMAAIDCDKAVTVEFKHDDKLSEDSGALIQCAVLYTTISGQRRLRIHNLGLNCSSQLADLYKSCETDALINFFAKSAFKAVLHQPLKVIREILVNQTAHMLACYRKNCASPSAASQLILPDSMKVLPVYMNCLLKNCVLLSRPEISTDERAYQRQLVMTMGVADSQLFFYPQLLPIHTLDVKSTMLPAAVRCSESRLSEEGIFLLANGLHMFLWLGVSSPPELIQGIFNVPSFAHINTDMTLLPEVGNPYSQQLRMIMGIIQQKRPYSMKLTIVKQREQPEMVFRQFLVEDKGLYGGSSYVDFLCCVHKEICQLLN | |||||||
Modified residue (large scale data) | 2 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 22 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 266 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 266 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 826 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 828 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with TMED2 and TMED10 (PubMed:20427317).
Interacts with CNIH4 (PubMed:24405750).
Interacts with GOSR2 (via IxM motif) and STX5 (via IxM motif); recruits GOSR2 and STX5 into COPII-coated vesicles (PubMed:18843296).
Interacts with KCNA3; this interaction is reduced in the presence of KCNE4 (PubMed:27802162).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O94855 | EWSR1 Q01844 | 3 | EBI-748817, EBI-739737 | |
BINARY | O94855 | SEC23A Q15436 | 5 | EBI-748817, EBI-81088 | |
BINARY | O94855 | SEC23B Q15437 | 9 | EBI-748817, EBI-742673 | |
BINARY | O94855 | SF3B4 Q15427 | 3 | EBI-748817, EBI-348469 | |
BINARY | O94855-2 | SEC23A Q15436 | 3 | EBI-12081096, EBI-81088 | |
BINARY | O94855-2 | SEC23B Q15437 | 3 | EBI-12081096, EBI-742673 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-260 | Disordered | ||||
Sequence: MSQQGYVATPPYSQPQPGIGLSPPHYGHYGDPSHTASPTGMMKPAGPLGATATRGMLPPGPPPPGPHQFGQNGAHATGHPPQRFPGPPPVNNVASSHAPYQPSAQSSYPGPISTSSVTQLGSQLSAMQINSYGSGMAPPSQGPPGPLSATSLQTPPRPPQPSILQPGSQVLPPPPTTLNGPGASPLPLPMYRPDGLSGPPPPNAQYQPPPLPGQTLGAGYPPQQANSGPQMAGAQLSYPGGFPGGPAQMAGPPQPQKKLD | ||||||
Compositional bias | 94-137 | Polar residues | ||||
Sequence: ASSHAPYQPSAQSSYPGPISTSSVTQLGSQLSAMQINSYGSGMA | ||||||
Compositional bias | 139-209 | Pro residues | ||||
Sequence: PSQGPPGPLSATSLQTPPRPPQPSILQPGSQVLPPPPTTLNGPGASPLPLPMYRPDGLSGPPPPNAQYQPP | ||||||
Compositional bias | 219-233 | Polar residues | ||||
Sequence: GYPPQQANSGPQMAG | ||||||
Region | 363-388 | Zinc finger-like | ||||
Sequence: CNRCKAYMCPFMQFIEGGRRYQCGFC | ||||||
Repeat | 901-974 | Gelsolin-like | ||||
Sequence: MLPAAVRCSESRLSEEGIFLLANGLHMFLWLGVSSPPELIQGIFNVPSFAHINTDMTLLPEVGNPYSQQLRMIM |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
O94855-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length1,032
- Mass (Da)113,010
- Last updated2008-11-25 v2
- ChecksumB46E566F096F37F0
O94855-2
- Name2
- Differences from canonical
- 224-224: Q → QA
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 94-137 | Polar residues | ||||
Sequence: ASSHAPYQPSAQSSYPGPISTSSVTQLGSQLSAMQINSYGSGMA | ||||||
Compositional bias | 139-209 | Pro residues | ||||
Sequence: PSQGPPGPLSATSLQTPPRPPQPSILQPGSQVLPPPPTTLNGPGASPLPLPMYRPDGLSGPPPPNAQYQPP | ||||||
Compositional bias | 219-233 | Polar residues | ||||
Sequence: GYPPQQANSGPQMAG | ||||||
Alternative sequence | VSP_035761 | 224 | in isoform 2 | |||
Sequence: Q → QA | ||||||
Sequence conflict | 559 | in Ref. 1; AAD28756 and 2; BAA34475 | ||||
Sequence: P → S |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF130464 EMBL· GenBank· DDBJ | AAD28756.2 EMBL· GenBank· DDBJ | mRNA | ||
AB018298 EMBL· GenBank· DDBJ | BAA34475.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
CH471229 EMBL· GenBank· DDBJ | EAW73656.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC035761 EMBL· GenBank· DDBJ | AAH35761.1 EMBL· GenBank· DDBJ | mRNA |