P53618 · COPB_HUMAN
- ProteinCoatomer subunit beta
- GeneCOPB1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids953 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. Plays a functional role in facilitating the transport of kappa-type opioid receptor mRNAs into axons and enhances translation of these proteins. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte surface triglyceride lipase (PNPLA2) with the lipid droplet to mediate lipolysis (By similarity).
Involved in the Golgi disassembly and reassembly processes during cell cycle. Involved in autophagy by playing a role in early endosome function. Plays a role in organellar compartmentalization of secretory compartments including endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC), Golgi, trans-Golgi network (TGN) and recycling endosomes, and in biosynthetic transport of CAV1. Promotes degradation of Nef cellular targets CD4 and MHC class I antigens by facilitating their trafficking to degradative compartments
Involved in the Golgi disassembly and reassembly processes during cell cycle. Involved in autophagy by playing a role in early endosome function. Plays a role in organellar compartmentalization of secretory compartments including endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC), Golgi, trans-Golgi network (TGN) and recycling endosomes, and in biosynthetic transport of CAV1. Promotes degradation of Nef cellular targets CD4 and MHC class I antigens by facilitating their trafficking to degradative compartments
Miscellaneous
Brefeldin A induces dissociation from the Golgi of the beta-COP and presumably the other coatomer subunits.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | COPI vesicle coat | |
Cellular Component | cytosol | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | endoplasmic reticulum-Golgi intermediate compartment | |
Cellular Component | ficolin-1-rich granule membrane | |
Cellular Component | Golgi apparatus | |
Cellular Component | Golgi membrane | |
Cellular Component | Golgi-associated vesicle | |
Cellular Component | intracellular membrane-bounded organelle | |
Cellular Component | membrane | |
Cellular Component | plasma membrane | |
Cellular Component | secretory granule membrane | |
Cellular Component | tertiary granule membrane | |
Cellular Component | transport vesicle | |
Molecular Function | structural molecule activity | |
Biological Process | endoplasmic reticulum to Golgi vesicle-mediated transport | |
Biological Process | intra-Golgi vesicle-mediated transport | |
Biological Process | intracellular protein transport |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCoatomer subunit beta
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP53618
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Golgi apparatus membrane ; Peripheral membrane protein
Cytoplasmic vesicle, COPI-coated vesicle membrane ; Peripheral membrane protein
Note: The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it (By similarity).
Proteolytic cleavage by CAPN8 triggers translocation from Golgi to cytoplasm (By similarity).
Found in perinuclear vesicular-tubular clusters (VTCs) and in the Golgi region where associated with vesicles, buds and rims of the Golgi stack (By similarity).
Occasionally present at the trans-side of Golgi, but mainly present at the cis-Golgi side in transitional areas (TA), on so-called peripheral elements (PE) consisting of tubules and vesicles located between the cup-shaped transitional elements (TE) of the rough endoplasmic reticulum (RER) and the cis-most Golgi cisternae (By similarity).
Present in cytoplasm, not associated with visible coats or membranes, with a minor fraction present on small clusters of tubules and vesicles (By similarity).
Some association with high-density and low-density microsomes and mitochondria/nuclei fraction (By similarity).
Very little found in plasma membrane fraction (PubMed:20362547).
Proteolytic cleavage by CAPN8 triggers translocation from Golgi to cytoplasm (By similarity).
Found in perinuclear vesicular-tubular clusters (VTCs) and in the Golgi region where associated with vesicles, buds and rims of the Golgi stack (By similarity).
Occasionally present at the trans-side of Golgi, but mainly present at the cis-Golgi side in transitional areas (TA), on so-called peripheral elements (PE) consisting of tubules and vesicles located between the cup-shaped transitional elements (TE) of the rough endoplasmic reticulum (RER) and the cis-most Golgi cisternae (By similarity).
Present in cytoplasm, not associated with visible coats or membranes, with a minor fraction present on small clusters of tubules and vesicles (By similarity).
Some association with high-density and low-density microsomes and mitochondria/nuclei fraction (By similarity).
Very little found in plasma membrane fraction (PubMed:20362547).
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Baralle-Macken syndrome (BARMACS)
- Note
- DescriptionAn autosomal recessive disorder characterized by global developmental delay, impaired intellectual development, poor or absent speech, and difficulty walking or inability to walk. Affected individuals have early-onset cataracts. Additional variable features are microcephaly, facial dysmorphism, metabolic abnormalities, spasticity, and lymphopenia.
- See alsoMIM:619255
Natural variants in BARMACS
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_085552 | 551 | F>V | in BARMACS |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_085552 | 551 | in BARMACS | |||
Sequence: F → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 938 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylthreonine | ||||
Sequence: T | |||||||
Chain | PRO_0000193833 | 2-953 | UniProt | Coatomer subunit beta | |||
Sequence: TAAENVCYTLINVPMDSEPPSEISLKNDLEKGDVKSKTEALKKVIIMILNGEKLPGLLMTIIRFVLPLQDHTIKKLLLVFWEIVPKTTPDGRLLHEMILVCDAYRKDLQHPNEFIRGSTLRFLCKLKEAELLEPLMPAIRACLEHRHSYVRRNAVLAIYTIYRNFEHLIPDAPELIHDFLVNEKDASCKRNAFMMLIHADQDRALDYLSTCIDQVQTFGDILQLVIVELIYKVCHANPSERARFIRCIYNLLQSSSPAVKYEAAGTLVTLSSAPTAIKAAAQCYIDLIIKESDNNVKLIVLDRLIELKEHPAHERVLQDLVMDILRVLSTPDLEVRKKTLQLALDLVSSRNVEELVIVLKKEVIKTNNVSEHEDTDKYRQLLVRTLHSCSVRFPDMAANVIPVLMEFLSDNNEAAAADVLEFVREAIQRFDNLRMLIVEKMLEVFHAIKSVKIYRGALWILGEYCSTKEDIQSVMTEIRRSLGEIPIVESEIKKEAGELKPEEEITVGPVQKLVTEMGTYATQSALSSSRPTKKEEDRPPLRGFLLDGDFFVAASLATTLTKIALRYVALVQEKKKQNSFVAEAMLLMATILHLGKSSLPKKPITDDDVDRISLCLKVLSECSPLMNDIFNKECRQSLSHMLSAKLEEEKLSQKKESEKRNVTVQPDDPISFMQLTAKNEMNCKEDQFQLSLLAAMGNTQRKEAADPLASKLNKVTQLTGFSDPVYAEAYVHVNQYDIVLDVLVVNQTSDTLQNCTLELATLGDLKLVEKPSPLTLAPHDFANIKANVKVASTENGIIFGNIVYDVSGAASDRNCVVLSDIHIDIMDYIQPATCTDAEFRQMWAEFEWENKVTVNTNMVDLNDYLQHILKSTNMKCLTPEKALSGYCGFMAANLYARSIFGEDALANVSIEKPIHQGPDAAVTGHIRIRAKSQGMALSLGDKINLSQKKTSI | |||||||
Modified residue (large scale data) | 371 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 494 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 507 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 521 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 523 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 528 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 530 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 638 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 773 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 933 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Proteolytically cleaved between Ser-528 and Ser-529 by CAPN8.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Oligomeric complex that consists of at least the alpha, beta, beta', gamma, delta, epsilon and zeta subunits. Interacts with SCYL1. Interacts with COPG1. Interacts (via trunk domain) with ARF1 (via switch I region); the interaction is direct. Interacts with KCNK2/TREK (via N-terminus); this interaction increases the channel-mediated whole cell currents and promotes plasma membrane expression of KCNK2/TREK. Interacts with anthrax lethal factor (LF); this interaction may facilitate endosomal vesicle membrane translocation of LF and its release from the lumen of endosomal vesicles to external milieu. Interacts with CAPN8 and PRKCE (By similarity).
Interacts with ARF1 (myristoylated); this interaction is required for binding of COPB1 to Golgi membranes (By similarity).
Interacts with STX17 (By similarity).
Interacts with TMEM115. Interacts with HLA-G-B2M complex; this interaction mediates the endoplasmic reticulum (ER) retrieval of HLA-E-B2M complexes that bind low affinity peptides. Interacts with TMEM41B (PubMed:30352685).
Interacts with ARF1 (myristoylated); this interaction is required for binding of COPB1 to Golgi membranes (By similarity).
Interacts with STX17 (By similarity).
Interacts with TMEM115. Interacts with HLA-G-B2M complex; this interaction mediates the endoplasmic reticulum (ER) retrieval of HLA-E-B2M complexes that bind low affinity peptides. Interacts with TMEM41B (PubMed:30352685).
(Microbial infection) Interacts (via C-terminus) with HIV-1 Nef; the interaction is direct.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P53618 | ARCN1 P48444 | 3 | EBI-359063, EBI-1044491 | |
BINARY | P53618 | BCAR1 P56945 | 3 | EBI-359063, EBI-702093 | |
BINARY | P53618 | GTPBP4 Q9BZE4 | 3 | EBI-359063, EBI-1056249 | |
BINARY | P53618 | HTT P42858 | 6 | EBI-359063, EBI-466029 | |
BINARY | P53618 | KIAA1328 Q86T90 | 3 | EBI-359063, EBI-3437878 | |
BINARY | P53618 | LZTS1 Q9Y250 | 3 | EBI-359063, EBI-1216080 | |
BINARY | P53618 | NUDCD1 Q96RS6 | 3 | EBI-359063, EBI-2512429 | |
BINARY | P53618 | SUN2 Q9UH99 | 3 | EBI-359063, EBI-1044964 | |
BINARY | P53618 | TRIM37 O94972 | 4 | EBI-359063, EBI-741602 | |
BINARY | P53618 | TTYH2 Q9BSA4 | 7 | EBI-359063, EBI-3959652 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 96-131 | HEAT 1 | ||||
Sequence: HEMILVCDAYRKDLQHPNEFIRGSTLRFLCKLKEAE | ||||||
Repeat | 132-168 | HEAT 2 | ||||
Sequence: LLEPLMPAIRACLEHRHSYVRRNAVLAIYTIYRNFEH | ||||||
Repeat | 240-276 | HEAT 3 | ||||
Sequence: SERARFIRCIYNLLQSSSPAVKYEAAGTLVTLSSAPT | ||||||
Repeat | 277-314 | HEAT 4 | ||||
Sequence: AIKAAAQCYIDLIIKESDNNVKLIVLDRLIELKEHPAH | ||||||
Repeat | 316-353 | HEAT 5 | ||||
Sequence: RVLQDLVMDILRVLSTPDLEVRKKTLQLALDLVSSRNV | ||||||
Repeat | 396-433 | HEAT 6 | ||||
Sequence: DMAANVIPVLMEFLSDNNEAAAADVLEFVREAIQRFDN |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length953
- Mass (Da)107,142
- Last updated2006-10-17 v3
- ChecksumBE916C1C5A599D79
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 825 | in Ref. 1; AAD41240 and 6; CAA57622 | ||||
Sequence: D → E | ||||||
Sequence conflict | 847 | in Ref. 1; AAD41240 and 6; CAA57622 | ||||
Sequence: F → L | ||||||
Sequence conflict | 911 | in Ref. 1; AAD41240 and 6; CAA57622 | ||||
Sequence: I → S | ||||||
Sequence conflict | 915 | in Ref. 1; AAD41240 and 6; CAA57622 | ||||
Sequence: I → L | ||||||
Sequence conflict | 925 | in Ref. 1; AAD41240 and 6; CAA57622 | ||||
Sequence: G → V | ||||||
Sequence conflict | 950 | in Ref. 1; AAD41240 and 6; CAA57622 | ||||
Sequence: K → E |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF084457 EMBL· GenBank· DDBJ | AAD41240.1 EMBL· GenBank· DDBJ | mRNA | ||
AF111807 EMBL· GenBank· DDBJ | AAL39009.1 EMBL· GenBank· DDBJ | mRNA | ||
AL136593 EMBL· GenBank· DDBJ | CAB66528.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471064 EMBL· GenBank· DDBJ | EAW68481.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471064 EMBL· GenBank· DDBJ | EAW68482.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471064 EMBL· GenBank· DDBJ | EAW68483.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471064 EMBL· GenBank· DDBJ | EAW68484.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471064 EMBL· GenBank· DDBJ | EAW68485.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC037280 EMBL· GenBank· DDBJ | AAH37280.1 EMBL· GenBank· DDBJ | mRNA | ||
X82103 EMBL· GenBank· DDBJ | CAA57622.1 EMBL· GenBank· DDBJ | mRNA |