COPB2_HUMAN
ID COPB2_HUMAN Reviewed; 906 AA.
AC P35606; B4DZI8;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Coatomer subunit beta';
DE AltName: Full=Beta'-coat protein;
DE Short=Beta'-COP;
DE AltName: Full=p102;
GN Name=COPB2;
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] (ISOFORM 1).
RX PubMed=8335000; DOI=10.1002/j.1460-2075.1993.tb05946.x;
RA Harrison-Lavoie K.J., Lewis V.A., Hynes G.M., Collison K.S., Nutland E.,
RA Willison K.R.;
RT "A 102 kDa subunit of a Golgi-associated particle has homology to beta
RT subunits of trimeric G proteins.";
RL EMBO J. 12:2847-2853(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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] (ISOFORM 1).
RC TISSUE=Lung;
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 PROTEIN SEQUENCE OF 2-9.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-627, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859 AND THR-861, AND
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 [18]
RP INTERACTION WITH JAGN1.
RX PubMed=25129144; DOI=10.1038/ng.3069;
RA Boztug K., Jaervinen P.M., Salzer E., Racek T., Moench S., Garncarz W.,
RA Gertz E.M., Schaeffer A.A., Antonopoulos A., Haslam S.M., Schieck L.,
RA Puchalka J., Diestelhorst J., Appaswamy G., Lescoeur B., Giambruno R.,
RA Bigenzahn J.W., Elling U., Pfeifer D., Conde C.D., Albert M.H., Welte K.,
RA Brandes G., Sherkat R., van der Werff Ten Bosch J., Rezaei N., Etzioni A.,
RA Bellanne-Chantelot C., Superti-Furga G., Penninger J.M., Bennett K.L.,
RA von Blume J., Dell A., Donadieu J., Klein C.;
RT "JAGN1 deficiency causes aberrant myeloid cell homeostasis and congenital
RT neutropenia.";
RL Nat. Genet. 46:1021-1027(2014).
RN [19]
RP INVOLVEMENT IN MCPH19, AND VARIANT MCPH19 CYS-254.
RX PubMed=29036432; DOI=10.1093/hmg/ddx362;
RA DiStasio A., Driver A., Sund K., Donlin M., Muraleedharan R.M., Pooya S.,
RA Kline-Fath B., Kaufman K.M., Prows C.A., Schorry E., Dasgupta B.,
RA Stottmann R.W.;
RT "Copb2 is essential for embryogenesis and hypomorphic mutations cause human
RT microcephaly.";
RL Hum. Mol. Genet. 26:4836-4848(2017).
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 (By similarity). {ECO:0000250}.
CC -!- FUNCTION: This coatomer complex protein, essential for Golgi budding
CC and vesicular trafficking, is a selective binding protein (RACK) for
CC protein kinase C, epsilon type. It binds to Golgi membranes in a GTP-
CC dependent manner (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Oligomeric complex that consists of at least the alpha, beta,
CC beta', gamma, delta, epsilon and zeta subunits. Probably interacts with
CC PEX11A. Interacts with SCYL1 (By similarity). Interacts with JAGN1
CC (PubMed:25129144). {ECO:0000250, ECO:0000269|PubMed:25129144}.
CC -!- INTERACTION:
CC P35606; P19838: NFKB1; NbExp=5; IntAct=EBI-1056534, EBI-300010;
CC P35606; P0DTC2: S; Xeno; NbExp=3; IntAct=EBI-1056534, EBI-25474821;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Golgi apparatus
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated
CC vesicle membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. 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. Shows only a slight
CC preference for the cis-Golgi apparatus, compared with the trans-Golgi.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P35606-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P35606-2; Sequence=VSP_056165;
CC -!- DISEASE: Microcephaly 19, primary, autosomal recessive (MCPH19)
CC [MIM:617800]: A form of microcephaly, a disease defined as a head
CC circumference more than 3 standard deviations below the age, sex and
CC ethnically matched mean. Brain weight is markedly reduced and the
CC cerebral cortex is disproportionately small. MCPH19 affected
CC individuals manifest severe developmental delay, failure to thrive,
CC cortical blindness, and spasticity. Brain imaging show a simplified
CC gyral pattern, thin corpus callosum, slight ventricular dilation, and
CC delayed myelination. {ECO:0000269|PubMed:29036432}. Note=The disease
CC may be caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the WD repeat COPB2 family. {ECO:0000305}.
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DR EMBL; X70476; CAA49900.1; -; mRNA.
DR EMBL; AK302943; BAG64100.1; -; mRNA.
DR EMBL; AC024933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW79040.1; -; Genomic_DNA.
DR EMBL; BC000326; AAH00326.1; -; mRNA.
DR CCDS; CCDS3108.1; -. [P35606-1]
DR PIR; S35342; S35342.
DR RefSeq; NP_004757.1; NM_004766.2. [P35606-1]
DR RefSeq; XP_016863001.1; XM_017007512.1.
DR AlphaFoldDB; P35606; -.
DR SMR; P35606; -.
DR BioGRID; 114693; 163.
DR CORUM; P35606; -.
DR DIP; DIP-27603N; -.
DR IntAct; P35606; 63.
DR MINT; P35606; -.
DR STRING; 9606.ENSP00000329419; -.
DR GlyGen; P35606; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P35606; -.
DR MetOSite; P35606; -.
DR PhosphoSitePlus; P35606; -.
DR SwissPalm; P35606; -.
DR BioMuta; COPB2; -.
DR DMDM; 544076; -.
DR EPD; P35606; -.
DR jPOST; P35606; -.
DR MassIVE; P35606; -.
DR MaxQB; P35606; -.
DR PaxDb; P35606; -.
DR PeptideAtlas; P35606; -.
DR PRIDE; P35606; -.
DR ProteomicsDB; 55099; -. [P35606-1]
DR ProteomicsDB; 5603; -.
DR Antibodypedia; 33460; 126 antibodies from 25 providers.
DR DNASU; 9276; -.
DR Ensembl; ENST00000333188.10; ENSP00000329419.4; ENSG00000184432.11. [P35606-1]
DR Ensembl; ENST00000507777.6; ENSP00000422295.1; ENSG00000184432.11. [P35606-2]
DR Ensembl; ENST00000512242.6; ENSP00000427185.2; ENSG00000184432.11. [P35606-2]
DR Ensembl; ENST00000514508.2; ENSP00000422469.2; ENSG00000184432.11. [P35606-2]
DR GeneID; 9276; -.
DR KEGG; hsa:9276; -.
DR MANE-Select; ENST00000333188.10; ENSP00000329419.4; NM_004766.3; NP_004757.1.
DR UCSC; uc003etf.5; human. [P35606-1]
DR CTD; 9276; -.
DR DisGeNET; 9276; -.
DR GeneCards; COPB2; -.
DR HGNC; HGNC:2232; COPB2.
DR HPA; ENSG00000184432; Low tissue specificity.
DR MalaCards; COPB2; -.
DR MIM; 606990; gene.
DR MIM; 617800; phenotype.
DR neXtProt; NX_P35606; -.
DR OpenTargets; ENSG00000184432; -.
DR Orphanet; 2512; Autosomal recessive primary microcephaly.
DR PharmGKB; PA26748; -.
DR VEuPathDB; HostDB:ENSG00000184432; -.
DR eggNOG; KOG0276; Eukaryota.
DR GeneTree; ENSGT00900000141083; -.
DR HOGENOM; CLU_005507_1_0_1; -.
DR OrthoDB; 139008at2759; -.
DR PhylomeDB; P35606; -.
DR TreeFam; TF300688; -.
DR PathwayCommons; P35606; -.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR SignaLink; P35606; -.
DR BioGRID-ORCS; 9276; 800 hits in 1084 CRISPR screens.
DR ChiTaRS; COPB2; human.
DR GeneWiki; COPB2; -.
DR GenomeRNAi; 9276; -.
DR Pharos; P35606; Tbio.
DR PRO; PR:P35606; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P35606; protein.
DR Bgee; ENSG00000184432; Expressed in parotid gland and 208 other tissues.
DR ExpressionAtlas; P35606; baseline and differential.
DR Genevisible; P35606; HS.
DR GO; GO:0030126; C:COPI vesicle coat; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0000139; C:Golgi 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; IDA:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:1901998; P:toxin transport; IEA:Ensembl.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR006692; Coatomer_WD-assoc_reg.
DR InterPro; IPR016453; COPB2.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF04053; Coatomer_WDAD; 1.
DR Pfam; PF00400; WD40; 4.
DR PIRSF; PIRSF005567; Coatomer_beta'_subunit; 1.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Direct protein sequencing; Disease variant;
KW ER-Golgi transport; Golgi apparatus; Membrane; Phosphoprotein;
KW Primary microcephaly; Protein transport; Reference proteome; Repeat;
KW Transport; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801"
FT CHAIN 2..906
FT /note="Coatomer subunit beta'"
FT /id="PRO_0000050912"
FT REPEAT 13..52
FT /note="WD 1"
FT REPEAT 55..94
FT /note="WD 2"
FT REPEAT 97..136
FT /note="WD 3"
FT REPEAT 140..180
FT /note="WD 4"
FT REPEAT 183..224
FT /note="WD 5"
FT REPEAT 227..266
FT /note="WD 6"
FT REGION 837..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 866..891
FT /evidence="ECO:0000255"
FT COMPBIAS 841..855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 627
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 859
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 861
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..29
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056165"
FT VARIANT 254
FT /note="R -> C (in MCPH19; unknown pathological
FT significance; dbSNP:rs1229568621)"
FT /evidence="ECO:0000269|PubMed:29036432"
FT /id="VAR_080601"
SQ SEQUENCE 906 AA; 102487 MW; 824BB63BEFAA53F6 CRC64;
MPLRLDIKRK LTARSDRVKS VDLHPTEPWM LASLYNGSVC VWNHETQTLV KTFEVCDLPV
RAAKFVARKN WVVTGADDMQ IRVFNYNTLE RVHMFEAHSD YIRCIAVHPT QPFILTSSDD
MLIKLWDWDK KWSCSQVFEG HTHYVMQIVI NPKDNNQFAS ASLDRTIKVW QLGSSSPNFT
LEGHEKGVNC IDYYSGGDKP YLISGADDRL VKIWDYQNKT CVQTLEGHAQ NVSCASFHPE
LPIIITGSED GTVRIWHSST YRLESTLNYG MERVWCVASL RGSNNVALGY DEGSIIVKLG
REEPAMSMDA NGKIIWAKHS EVQQANLKAM GDAEIKDGER LPLAVKDMGS CEIYPQTIQH
NPNGRFVVVC GDGEYIIYTA MALRNKSFGS AQEFAWAHDS SEYAIRESNS IVKIFKNFKE
KKSFKPDFGA ESIYGGFLLG VRSVNGLAFY DWDNTELIRR IEIQPKHIFW SDSGELVCIA
TEESFFILKY LSEKVLAAQE THEGVTEDGI EDAFEVLGEI QEIVKTGLWV GDCFIYTSSV
NRLNYYVGGE IVTIAHLDRT MYLLGYIPKD NRLYLGDKEL NIISYSLLVS VLEYQTAVMR
RDFSMADKVL PTIPKEQRTR VAHFLEKQGF KQQALTVSTD PEHRFELALQ LGELKIAYQL
AVEAESEQKW KQLAELAISK CQFGLAQECL HHAQDYGGLL LLATASGNAN MVNKLAEGAE
RDGKNNVAFM SYFLQGKVDA CLELLIRTGR LPEAAFLART YLPSQVSRVV KLWRENLSKV
NQKAAESLAD PTEYENLFPG LKEAFVVEEW VKETHADLWP AKQYPLVTPN EERNVMEEGK
DFQPSRSTAQ QELDGKPASP TPVIVASHTA NKEEKSLLEL EVDLDNLELE DIDTTDINLD
EDILDD
