ID COPB_HUMAN Reviewed; 953 AA. AC P53618; D3DQX0; Q6GTT7; Q9NTK2; Q9UNW7; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 3. DT 27-MAR-2024, entry version 205. DE RecName: Full=Coatomer subunit beta; DE AltName: Full=Beta-coat protein; DE Short=Beta-COP {ECO:0000303|PubMed:7982906, ECO:0000303|Ref.1}; GN Name=COPB1 {ECO:0000312|HGNC:HGNC:2231}; Synonyms=COPB; GN ORFNames=MSTP026; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Zhang J., Liu T., Fu G., Li W., Ye M., Zhou J., Wu J., Shen Y., Yu M., RA Chen S., Mao M., Chen Z.; RT "Human beta-cop homolog gene, complete CDS."; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Aorta; RA Xu Y.Y., Sun L.Z., Wu Q.Y., Liu Y.Q., Liu B., Zhao B., Wang X.Y., Song L., RA Ye J., Sheng H., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Sun Y.H., RA Jiang Y.X., Zhao X.W., Liu S., Liu L.S., Ding J.F., Gao R.L., Qiang B.Q., RA Yuan J.G., Liew C.C., Zhao M.S., Hui R.T.; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Amygdala; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 651-953, AND INTERACTION WITH HIV-1 NEF RP (MICROBIAL INFECTION). RC TISSUE=Lymphoid tissue; RX PubMed=7982906; DOI=10.1016/s0021-9258(18)43773-8; RA Benichou S., Bomsel M., Bodeus M., Durand H., Doute M., Letourneur F., RA Camonis J., Benarous R.; RT "Physical interaction of the HIV-1 Nef protein with beta-COP, a component RT of non-clathrin-coated vesicles essential for membrane traffic."; RL J. Biol. Chem. 269:30073-30076(1994). RN [7] RP SUBCELLULAR LOCATION. RX PubMed=7573041; RA Olivos-Glander I.M., Janne P.A., Nussbaum R.L.; RT "The oculocerebrorenal syndrome gene product is a 105-kD protein localized RT to the Golgi complex."; RL Am. J. Hum. Genet. 57:817-823(1995). RN [8] RP INTERACTION WITH COPG1, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=11056392; DOI=10.1093/oxfordjournals.jbchem.a022817; RA Futatsumori M., Kasai K., Takatsu H., Shin H.-W., Nakayama K.; RT "Identification and characterization of novel isoforms of COP I subunits."; RL J. Biochem. 128:793-801(2000). RN [9] RP SUBUNIT. RX PubMed=11520457; DOI=10.1016/s1074-7613(01)00179-0; RA Park B., Lee S., Kim E., Chang S., Jin M., Ahn K.; RT "The truncated cytoplasmic tail of HLA-G serves a quality-control function RT in post-ER compartments."; RL Immunity 15:213-224(2001). RN [10] RP SUBUNIT. RX PubMed=12582157; DOI=10.1074/jbc.m212882200; RA Park B., Ahn K.; RT "An essential function of tapasin in quality control of HLA-G molecules."; RL J. Biol. Chem. 278:14337-14345(2003). RN [11] RP INTERACTION WITH ARF1, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=17451557; DOI=10.1111/j.1600-0854.2007.00554.x; RA Sun Z., Anderl F., Frohlich K., Zhao L., Hanke S., Brugger B., Wieland F., RA Bethune J.; RT "Multiple and stepwise interactions between coatomer and ADP-ribosylation RT factor-1 (Arf1)-GTP."; RL Traffic 8:582-593(2007). RN [12] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=18385291; DOI=10.1152/ajpcell.00010.2008; RA Styers M.L., O'Connor A.K., Grabski R., Cormet-Boyaka E., Sztul E.; RT "Depletion of beta-COP reveals a role for COP-I in compartmentalization of RT secretory compartments and in biosynthetic transport of caveolin-1."; RL Am. J. Physiol. 294:C1485-C1498(2008). RN [13] RP INTERACTION WITH SCYL1. RX PubMed=18556652; DOI=10.1074/jbc.m801869200; RA Burman J.L., Bourbonniere L., Philie J., Stroh T., Dejgaard S.Y., RA Presley J.F., McPherson P.S.; RT "Scyl1, mutated in a recessive form of spinocerebellar neurodegeneration, RT regulates COPI-mediated retrograde traffic."; RL J. Biol. Chem. 283:22774-22786(2008). RN [14] RP FUNCTION, AND INTERACTION WITH HIV-1 NEF (MICROBIAL INFECTION). RX PubMed=18725938; DOI=10.1371/journal.ppat.1000131; RA Schaefer M.R., Wonderlich E.R., Roeth J.F., Leonard J.A., Collins K.L.; RT "HIV-1 Nef targets MHC-I and CD4 for degradation via a final common beta- RT COP-dependent pathway in T cells."; RL PLoS Pathog. 4:E1000131-E1000131(2008). RN [15] RP INTERACTION WITH ANTHRAX LETHAL FACTOR. RX PubMed=18356299; DOI=10.1073/pnas.0710100105; RA Tamayo A.G., Bharti A., Trujillo C., Harrison R., Murphy J.R.; RT "COPI coatomer complex proteins facilitate the translocation of anthrax RT lethal factor across vesicular membranes in vitro."; RL Proc. Natl. Acad. Sci. U.S.A. 105:5254-5259(2008). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [17] RP FUNCTION. RX PubMed=19364919; DOI=10.1083/jcb.200810098; RA Razi M., Chan E.Y., Tooze S.A.; RT "Early endosomes and endosomal coatomer are required for autophagy."; RL J. Cell Biol. 185:305-321(2009). RN [18] RP INTERACTION WITH KCNK2, AND SUBCELLULAR LOCATION. RX PubMed=20362547; DOI=10.1016/j.bbrc.2010.03.171; RA Kim E., Hwang E.M., Yarishkin O., Yoo J.C., Kim D., Park N., Cho M., RA Lee Y.S., Sun C.H., Yi G.S., Yoo J., Kang D., Han J., Hong S.G., Park J.Y.; RT "Enhancement of TREK1 channel surface expression by protein-protein RT interaction with beta-COP."; RL Biochem. Biophys. Res. Commun. 395:244-250(2010). RN [19] RP FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=20056612; DOI=10.1074/jbc.m109.047084; RA Chen X., Simon E.S., Xiang Y., Kachman M., Andrews P.C., Wang Y.; RT "Quantitative proteomics analysis of cell cycle-regulated Golgi disassembly RT and reassembly."; RL J. Biol. Chem. 285:7197-7207(2010). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [21] RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [22] RP INTERACTION WITH TMEM115. RX PubMed=24806965; DOI=10.1242/jcs.136754; RA Ong Y.S., Tran T.H., Gounko N.V., Hong W.; RT "TMEM115 is an integral membrane protein of the Golgi complex involved in RT retrograde transport."; RL J. Cell Sci. 127:2825-2839(2014). RN [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [24] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [25] RP INTERACTION WITH TMEM41B. RX PubMed=30352685; DOI=10.1016/j.bbrc.2018.10.073; RA Van Alstyne M., Lotti F., Dal Mas A., Area-Gomez E., Pellizzoni L.; RT "Stasimon/Tmem41b localizes to mitochondria-associated ER membranes and is RT essential for mouse embryonic development."; RL Biochem. Biophys. Res. Commun. 506:463-470(2018). RN [26] RP VARIANT BARMACS VAL-551, AND INVOLVEMENT IN BARMACS. RX PubMed=33632302; DOI=10.1186/s13073-021-00850-w; RA Macken W.L., Godwin A., Wheway G., Stals K., Nazlamova L., Ellard S., RA Alfares A., Aloraini T., AlSubaie L., Alfadhel M., Alajaji S., Wai H.A., RA Self J., Douglas A.G.L., Kao A.P., Guille M., Baralle D.; RT "Biallelic variants in COPB1 cause a novel, severe intellectual disability RT syndrome with cataracts and variable microcephaly."; RL Genome Med. 13:34-34(2021). CC -!- FUNCTION: The coatomer is a cytosolic protein complex that binds to CC dilysine motifs and reversibly associates with Golgi non-clathrin- CC coated vesicles, which further mediate biosynthetic protein transport CC from the ER, via the Golgi up to the trans Golgi network. Coatomer CC complex is required for budding from Golgi membranes, and is essential CC for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. CC In mammals, the coatomer can only be recruited by membranes associated CC to ADP-ribosylation factors (ARFs), which are small GTP-binding CC proteins; the complex also influences the Golgi structural integrity, CC as well as the processing, activity, and endocytic recycling of LDL CC receptors. Plays a functional role in facilitating the transport of CC kappa-type opioid receptor mRNAs into axons and enhances translation of CC these proteins. Required for limiting lipid storage in lipid droplets. CC Involved in lipid homeostasis by regulating the presence of perilipin CC family members PLIN2 and PLIN3 at the lipid droplet surface and CC promoting the association of adipocyte surface triglyceride lipase CC (PNPLA2) with the lipid droplet to mediate lipolysis (By similarity). CC Involved in the Golgi disassembly and reassembly processes during cell CC cycle. Involved in autophagy by playing a role in early endosome CC function. Plays a role in organellar compartmentalization of secretory CC compartments including endoplasmic reticulum (ER)-Golgi intermediate CC compartment (ERGIC), Golgi, trans-Golgi network (TGN) and recycling CC endosomes, and in biosynthetic transport of CAV1. Promotes degradation CC of Nef cellular targets CD4 and MHC class I antigens by facilitating CC their trafficking to degradative compartments. {ECO:0000250, CC ECO:0000269|PubMed:18385291, ECO:0000269|PubMed:18725938, CC ECO:0000269|PubMed:19364919, ECO:0000269|PubMed:20056612}. CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta, CC beta', gamma, delta, epsilon and zeta subunits. Interacts with SCYL1. CC Interacts with COPG1. Interacts (via trunk domain) with ARF1 (via CC switch I region); the interaction is direct. Interacts with KCNK2/TREK CC (via N-terminus); this interaction increases the channel-mediated whole CC cell currents and promotes plasma membrane expression of KCNK2/TREK. CC Interacts with anthrax lethal factor (LF); this interaction may CC facilitate endosomal vesicle membrane translocation of LF and its CC release from the lumen of endosomal vesicles to external milieu. CC Interacts with CAPN8 and PRKCE (By similarity). Interacts with ARF1 CC (myristoylated); this interaction is required for binding of COPB1 to CC Golgi membranes (By similarity). Interacts with STX17 (By similarity). CC Interacts with TMEM115. Interacts with HLA-G-B2M complex; this CC interaction mediates the endoplasmic reticulum (ER) retrieval of HLA-E- CC B2M complexes that bind low affinity peptides. Interacts with TMEM41B CC (PubMed:30352685). {ECO:0000250|UniProtKB:P23514, CC ECO:0000250|UniProtKB:Q9JIF7, ECO:0000269|PubMed:11520457, CC ECO:0000269|PubMed:12582157, ECO:0000269|PubMed:24806965, CC ECO:0000269|PubMed:30352685}. CC -!- SUBUNIT: (Microbial infection) Interacts (via C-terminus) with HIV-1 CC Nef; the interaction is direct. {ECO:0000269|PubMed:18725938, CC ECO:0000269|PubMed:7982906}. CC -!- INTERACTION: CC P53618; P48444: ARCN1; NbExp=3; IntAct=EBI-359063, EBI-1044491; CC P53618; P56945: BCAR1; NbExp=3; IntAct=EBI-359063, EBI-702093; CC P53618; Q9BZE4: GTPBP4; NbExp=3; IntAct=EBI-359063, EBI-1056249; CC P53618; P42858: HTT; NbExp=6; IntAct=EBI-359063, EBI-466029; CC P53618; Q86T90: KIAA1328; NbExp=3; IntAct=EBI-359063, EBI-3437878; CC P53618; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-359063, EBI-1216080; CC P53618; Q96RS6: NUDCD1; NbExp=3; IntAct=EBI-359063, EBI-2512429; CC P53618; Q9UH99: SUN2; NbExp=3; IntAct=EBI-359063, EBI-1044964; CC P53618; O94972: TRIM37; NbExp=4; IntAct=EBI-359063, EBI-741602; CC P53618; Q9BSA4: TTYH2; NbExp=7; IntAct=EBI-359063, EBI-3959652; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus membrane CC {ECO:0000269|PubMed:11056392, ECO:0000269|PubMed:17451557, CC ECO:0000269|PubMed:7573041}; Peripheral membrane protein CC {ECO:0000269|PubMed:17451557, ECO:0000269|PubMed:18385291, CC ECO:0000269|PubMed:20056612}; Cytoplasmic side {ECO:0000305}. CC Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane CC protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell membrane CC {ECO:0000269|PubMed:20362547}. Endoplasmic reticulum-Golgi intermediate CC compartment {ECO:0000250|UniProtKB:Q9JIF7}. Note=The coatomer is CC cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as CC well as on the vesicles/buds originating from it (By similarity). CC Proteolytic cleavage by CAPN8 triggers translocation from Golgi to CC cytoplasm (By similarity). Found in perinuclear vesicular-tubular CC clusters (VTCs) and in the Golgi region where associated with vesicles, CC buds and rims of the Golgi stack (By similarity). Occasionally present CC at the trans-side of Golgi, but mainly present at the cis-Golgi side in CC transitional areas (TA), on so-called peripheral elements (PE) CC consisting of tubules and vesicles located between the cup-shaped CC transitional elements (TE) of the rough endoplasmic reticulum (RER) and CC the cis-most Golgi cisternae (By similarity). Present in cytoplasm, not CC associated with visible coats or membranes, with a minor fraction CC present on small clusters of tubules and vesicles (By similarity). Some CC association with high-density and low-density microsomes and CC mitochondria/nuclei fraction (By similarity). Very little found in CC plasma membrane fraction (PubMed:20362547). CC {ECO:0000250|UniProtKB:P23514, ECO:0000269|PubMed:20362547}. CC -!- PTM: Proteolytically cleaved between Ser-528 and Ser-529 by CAPN8. CC {ECO:0000250}. CC -!- DISEASE: Baralle-Macken syndrome (BARMACS) [MIM:619255]: An autosomal CC recessive disorder characterized by global developmental delay, CC impaired intellectual development, poor or absent speech, and CC difficulty walking or inability to walk. Affected individuals have CC early-onset cataracts. Additional variable features are microcephaly, CC facial dysmorphism, metabolic abnormalities, spasticity, and CC lymphopenia. {ECO:0000269|PubMed:33632302}. Note=The disease is caused CC by variants affecting the gene represented in this entry. CC -!- MISCELLANEOUS: Brefeldin A induces dissociation from the Golgi of the CC beta-COP and presumably the other coatomer subunits. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF084457; AAD41240.1; -; mRNA. DR EMBL; AF111807; AAL39009.1; -; mRNA. DR EMBL; AL136593; CAB66528.1; -; mRNA. DR EMBL; CH471064; EAW68481.1; -; Genomic_DNA. DR EMBL; CH471064; EAW68482.1; -; Genomic_DNA. DR EMBL; CH471064; EAW68483.1; -; Genomic_DNA. DR EMBL; CH471064; EAW68484.1; -; Genomic_DNA. DR EMBL; CH471064; EAW68485.1; -; Genomic_DNA. DR EMBL; BC037280; AAH37280.1; -; mRNA. DR EMBL; X82103; CAA57622.1; -; mRNA. DR CCDS; CCDS7815.1; -. DR PIR; A55136; A55136. DR PIR; T46913; T46913. DR RefSeq; NP_001137533.1; NM_001144061.1. DR RefSeq; NP_001137534.1; NM_001144062.1. DR RefSeq; NP_057535.1; NM_016451.4. DR AlphaFoldDB; P53618; -. DR SMR; P53618; -. DR BioGRID; 107710; 276. DR ComplexPortal; CPX-7803; COPI vesicle coat complex, COPG1-COPZ1 variant. DR ComplexPortal; CPX-7969; COPI vesicle coat complex, COPG2-COPZ1 variant. DR ComplexPortal; CPX-7970; COPI vesicle coat complex, COPG1-COPZ2 variant. DR DIP; DIP-265N; -. DR IntAct; P53618; 115. DR MINT; P53618; -. DR STRING; 9606.ENSP00000249923; -. DR ChEMBL; CHEMBL4295782; -. DR GlyGen; P53618; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P53618; -. DR MetOSite; P53618; -. DR PhosphoSitePlus; P53618; -. DR SwissPalm; P53618; -. DR BioMuta; COPB1; -. DR DMDM; 116241311; -. DR EPD; P53618; -. DR jPOST; P53618; -. DR MassIVE; P53618; -. DR MaxQB; P53618; -. DR PaxDb; 9606-ENSP00000249923; -. DR PeptideAtlas; P53618; -. DR PRIDE; P53618; -. DR ProteomicsDB; 56592; -. DR Pumba; P53618; -. DR Antibodypedia; 3231; 261 antibodies from 32 providers. DR DNASU; 1315; -. DR Ensembl; ENST00000249923.7; ENSP00000249923.3; ENSG00000129083.13. DR Ensembl; ENST00000439561.7; ENSP00000397873.2; ENSG00000129083.13. DR GeneID; 1315; -. DR KEGG; hsa:1315; -. DR MANE-Select; ENST00000439561.7; ENSP00000397873.2; NM_001144061.2; NP_001137533.1. DR UCSC; uc001mlh.3; human. DR AGR; HGNC:2231; -. DR CTD; 1315; -. DR DisGeNET; 1315; -. DR GeneCards; COPB1; -. DR HGNC; HGNC:2231; COPB1. DR HPA; ENSG00000129083; Low tissue specificity. DR MalaCards; COPB1; -. DR MIM; 600959; gene. DR MIM; 619255; phenotype. DR neXtProt; NX_P53618; -. DR OpenTargets; ENSG00000129083; -. DR Orphanet; 633035; Intellectual disability-early-onset cataract-microcephaly syndrome. DR PharmGKB; PA26747; -. DR VEuPathDB; HostDB:ENSG00000129083; -. DR eggNOG; KOG1058; Eukaryota. DR GeneTree; ENSGT00390000005270; -. DR HOGENOM; CLU_006949_0_0_1; -. DR InParanoid; P53618; -. DR OMA; MDYIIPA; -. DR OrthoDB; 151169at2759; -. DR PhylomeDB; P53618; -. DR TreeFam; TF105737; -. DR PathwayCommons; P53618; -. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport. DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic. DR SignaLink; P53618; -. DR BioGRID-ORCS; 1315; 821 hits in 1158 CRISPR screens. DR ChiTaRS; COPB1; human. DR GeneWiki; COPB1; -. DR GenomeRNAi; 1315; -. DR Pharos; P53618; Tbio. DR PRO; PR:P53618; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; P53618; Protein. DR Bgee; ENSG00000129083; Expressed in choroid plexus epithelium and 216 other cell types or tissues. DR ExpressionAtlas; P53618; baseline and differential. DR GO; GO:0030126; C:COPI vesicle coat; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell. DR GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0005798; C:Golgi-associated vesicle; TAS:ProtInc. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome. DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome. DR GO; GO:0030133; C:transport vesicle; TAS:Reactome. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IBA:GO_Central. DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; ISS:UniProtKB. DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N. DR InterPro; IPR011710; Coatomer_bsu_C. DR InterPro; IPR016460; COPB1. DR InterPro; IPR029446; COPB1_appendage_platform_dom. DR PANTHER; PTHR10635; COATOMER SUBUNIT BETA; 1. DR PANTHER; PTHR10635:SF0; COATOMER SUBUNIT BETA; 1. DR Pfam; PF01602; Adaptin_N; 1. DR Pfam; PF07718; Coatamer_beta_C; 1. DR Pfam; PF14806; Coatomer_b_Cpla; 1. DR PIRSF; PIRSF005727; Coatomer_beta_subunit; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR Genevisible; P53618; HS. PE 1: Evidence at protein level; KW Acetylation; Cataract; Cell membrane; Cytoplasm; Cytoplasmic vesicle; KW Disease variant; ER-Golgi transport; Golgi apparatus; KW Host-virus interaction; Intellectual disability; Membrane; KW Protein transport; Reference proteome; Repeat; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895" FT CHAIN 2..953 FT /note="Coatomer subunit beta" FT /id="PRO_0000193833" FT REPEAT 96..131 FT /note="HEAT 1" FT REPEAT 132..168 FT /note="HEAT 2" FT REPEAT 240..276 FT /note="HEAT 3" FT REPEAT 277..314 FT /note="HEAT 4" FT REPEAT 316..353 FT /note="HEAT 5" FT REPEAT 396..433 FT /note="HEAT 6" FT MOD_RES 2 FT /note="N-acetylthreonine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895" FT MOD_RES 494 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9JIF7" FT VARIANT 551 FT /note="F -> V (in BARMACS)" FT /evidence="ECO:0000269|PubMed:33632302" FT /id="VAR_085552" FT CONFLICT 825 FT /note="D -> E (in Ref. 1; AAD41240 and 6; CAA57622)" FT /evidence="ECO:0000305" FT CONFLICT 847 FT /note="F -> L (in Ref. 1; AAD41240 and 6; CAA57622)" FT /evidence="ECO:0000305" FT CONFLICT 911 FT /note="I -> S (in Ref. 1; AAD41240 and 6; CAA57622)" FT /evidence="ECO:0000305" FT CONFLICT 915 FT /note="I -> L (in Ref. 1; AAD41240 and 6; CAA57622)" FT /evidence="ECO:0000305" FT CONFLICT 925 FT /note="G -> V (in Ref. 1; AAD41240 and 6; CAA57622)" FT /evidence="ECO:0000305" FT CONFLICT 950 FT /note="K -> E (in Ref. 1; AAD41240 and 6; CAA57622)" FT /evidence="ECO:0000305" SQ SEQUENCE 953 AA; 107142 MW; BE916C1C5A599D79 CRC64; MTAAENVCYT LINVPMDSEP PSEISLKNDL EKGDVKSKTE ALKKVIIMIL NGEKLPGLLM TIIRFVLPLQ DHTIKKLLLV FWEIVPKTTP DGRLLHEMIL VCDAYRKDLQ HPNEFIRGST LRFLCKLKEA ELLEPLMPAI RACLEHRHSY VRRNAVLAIY TIYRNFEHLI PDAPELIHDF LVNEKDASCK RNAFMMLIHA DQDRALDYLS TCIDQVQTFG DILQLVIVEL IYKVCHANPS ERARFIRCIY NLLQSSSPAV KYEAAGTLVT LSSAPTAIKA AAQCYIDLII KESDNNVKLI VLDRLIELKE HPAHERVLQD LVMDILRVLS TPDLEVRKKT LQLALDLVSS RNVEELVIVL KKEVIKTNNV SEHEDTDKYR QLLVRTLHSC SVRFPDMAAN VIPVLMEFLS DNNEAAAADV LEFVREAIQR FDNLRMLIVE KMLEVFHAIK SVKIYRGALW ILGEYCSTKE DIQSVMTEIR RSLGEIPIVE SEIKKEAGEL KPEEEITVGP VQKLVTEMGT YATQSALSSS RPTKKEEDRP PLRGFLLDGD FFVAASLATT LTKIALRYVA LVQEKKKQNS FVAEAMLLMA TILHLGKSSL PKKPITDDDV DRISLCLKVL SECSPLMNDI FNKECRQSLS HMLSAKLEEE KLSQKKESEK RNVTVQPDDP ISFMQLTAKN EMNCKEDQFQ LSLLAAMGNT QRKEAADPLA SKLNKVTQLT GFSDPVYAEA YVHVNQYDIV LDVLVVNQTS DTLQNCTLEL ATLGDLKLVE KPSPLTLAPH DFANIKANVK VASTENGIIF GNIVYDVSGA ASDRNCVVLS DIHIDIMDYI QPATCTDAEF RQMWAEFEWE NKVTVNTNMV DLNDYLQHIL KSTNMKCLTP EKALSGYCGF MAANLYARSI FGEDALANVS IEKPIHQGPD AAVTGHIRIR AKSQGMALSL GDKINLSQKK TSI //