COPB_HUMAN
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 03-AUG-2022, entry version 196.
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; 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.
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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; 197.
DR DIP; DIP-265N; -.
DR IntAct; P53618; 103.
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; P53618; -.
DR PeptideAtlas; P53618; -.
DR PRIDE; P53618; -.
DR ProteomicsDB; 56592; -.
DR Antibodypedia; 3231; 244 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 CTD; 1315; -.
DR DisGeNET; 1315; -.
DR GeneCards; COPB1; -.
DR HGNC; HGNC:2231; COPB1.
DR HPA; ENSG00000129083; Low tissue specificity.
DR MIM; 600959; gene.
DR MIM; 619255; phenotype.
DR neXtProt; NX_P53618; -.
DR OpenTargets; ENSG00000129083; -.
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; QCGFMAA; -.
DR OrthoDB; 195812at2759; -.
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; 790 hits in 1080 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 214 other tissues.
DR ExpressionAtlas; P53618; baseline and differential.
DR Genevisible; P53618; HS.
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; -; 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; PTHR10635; 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; SSF48371; 1.
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
