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 27-MAR-2024, entry version 221. 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). RN [20] RP INVOLVEMENT IN OPDD, AND FUNCTION. RX PubMed=34450031; DOI=10.1016/j.ajhg.2021.08.002; RG Undiagnosed Diseases Network; RA Marom R., Burrage L.C., Venditti R., Clement A., Blanco-Sanchez B., RA Jain M., Scott D.A., Rosenfeld J.A., Sutton V.R., Shinawi M., Mirzaa G., RA DeVile C., Roberts R., Calder A.D., Allgrove J., Grafe I., Lanza D.G., RA Li X., Joeng K.S., Lee Y.C., Song I.W., Sliepka J.M., Batkovskyte D., RA Washington M., Dawson B.C., Jin Z., Jiang M.M., Chen S., Chen Y., RA Tran A.A., Emrick L.T., Murdock D.R., Hanchard N.A., Zapata G.E., RA Mehta N.R., Weis M.A., Scott A.A., Tremp B.A., Phillips J.B., Wegner J., RA Taylor-Miller T., Gibbs R.A., Muzny D.M., Jhangiani S.N., Hicks J., RA Stottmann R.W., Dickinson M.E., Seavitt J.R., Heaney J.D., Eyre D.R., RA Westerfield M., De Matteis M.A., Lee B.; RT "COPB2 loss of function causes a coatopathy with osteoporosis and RT developmental delay."; RL Am. J. Hum. Genet. 108:1710-1724(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. {ECO:0000269|PubMed:34450031}. 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 -!- DISEASE: Osteoporosis, childhood- or juvenile-onset, with developmental CC delay (OPDD) [MIM:619884]: An autosomal dominant disorder characterized CC by decreased bone mass and deterioration of bone microarchitecture, CC fragile bones, recurrent fractures following minor trauma, and CC developmental delay of variable severity. CC {ECO:0000269|PubMed:34450031}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the WD repeat COPB2 family. {ECO:0000305}. 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; 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 CCDS; CCDS93395.1; -. [P35606-2] DR PIR; S35342; S35342. DR RefSeq; NP_004757.1; NM_004766.2. [P35606-1] DR RefSeq; XP_016863001.1; XM_017007512.1. DR PDB; 8D30; X-ray; 2.40 A; A/B=1-597. DR PDB; 8D41; X-ray; 2.00 A; A/B=1-300. DR PDBsum; 8D30; -. DR PDBsum; 8D41; -. DR AlphaFoldDB; P35606; -. DR SMR; P35606; -. DR BioGRID; 114693; 357. 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 CORUM; P35606; -. DR DIP; DIP-27603N; -. DR IntAct; P35606; 76. DR MINT; P35606; -. DR STRING; 9606.ENSP00000329419; -. DR GlyCosmos; P35606; 2 sites, 1 glycan. 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; 9606-ENSP00000329419; -. DR PeptideAtlas; P35606; -. DR ProteomicsDB; 55099; -. [P35606-1] DR ProteomicsDB; 5603; -. DR Pumba; P35606; -. DR Antibodypedia; 33460; 141 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 AGR; HGNC:2232; -. 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 MIM; 619884; 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 InParanoid; P35606; -. DR OrthoDB; 20819at2759; -. 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; 831 hits in 1160 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 210 other cell types or tissues. DR ExpressionAtlas; P35606; baseline and differential. 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; IMP:UniProtKB. DR CDD; cd22947; Coatomer_WDAD_beta-like; 1. DR CDD; cd00200; WD40; 1. DR Gene3D; 1.25.40.470; -; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 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; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR19876; COATOMER; 1. DR PANTHER; PTHR19876:SF2; COATOMER SUBUNIT BETA; 1. DR Pfam; PF04053; Coatomer_WDAD; 1. DR Pfam; PF00400; WD40; 6. DR PIRSF; PIRSF005567; Coatomer_beta'_subunit; 1. DR PRINTS; PR00320; GPROTEINBRPT. DR SMART; SM00320; WD40; 6. DR SUPFAM; SSF50978; WD40 repeat-like; 2. DR PROSITE; PS50082; WD_REPEATS_2; 5. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. DR Genevisible; P35606; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Coiled coil; Cytoplasm; KW Cytoplasmic vesicle; Direct protein sequencing; ER-Golgi transport; KW Golgi apparatus; Membrane; Phosphoprotein; Primary microcephaly; KW Protein transport; Reference proteome; Repeat; 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; uncertain significance; FT dbSNP:rs1229568621)" FT /evidence="ECO:0000269|PubMed:29036432" FT /id="VAR_080601" FT STRAND 7..14 FT /evidence="ECO:0007829|PDB:8D41" FT STRAND 18..23 FT /evidence="ECO:0007829|PDB:8D41" FT STRAND 25..34 FT /evidence="ECO:0007829|PDB:8D41" FT STRAND 37..43 FT /evidence="ECO:0007829|PDB:8D41" FT TURN 44..47 FT /evidence="ECO:0007829|PDB:8D41" FT STRAND 48..54 FT /evidence="ECO:0007829|PDB:8D41" FT STRAND 62..66 FT /evidence="ECO:0007829|PDB:8D41" FT HELIX 67..69 FT /evidence="ECO:0007829|PDB:8D41" FT STRAND 71..75 FT /evidence="ECO:0007829|PDB:8D41" FT STRAND 79..85 FT /evidence="ECO:0007829|PDB:8D41" FT TURN 86..88 FT /evidence="ECO:0007829|PDB:8D41" FT STRAND 91..96 FT /evidence="ECO:0007829|PDB:8D41" FT STRAND 102..107 FT /evidence="ECO:0007829|PDB:8D41" FT STRAND 109..118 FT /evidence="ECO:0007829|PDB:8D41" FT STRAND 123..127 FT /evidence="ECO:0007829|PDB:8D41" FT TURN 128..132 FT /evidence="ECO:0007829|PDB:8D41" FT STRAND 134..138 FT /evidence="ECO:0007829|PDB:8D41" FT STRAND 145..151 FT /evidence="ECO:0007829|PDB:8D41" FT STRAND 154..162 FT /evidence="ECO:0007829|PDB:8D41" FT STRAND 167..171 FT /evidence="ECO:0007829|PDB:8D41" FT STRAND 178..181 FT /evidence="ECO:0007829|PDB:8D41" FT STRAND 188..193 FT /evidence="ECO:0007829|PDB:8D41" FT STRAND 201..206 FT /evidence="ECO:0007829|PDB:8D41" FT STRAND 211..215 FT /evidence="ECO:0007829|PDB:8D41" FT TURN 216..219 FT /evidence="ECO:0007829|PDB:8D41" FT STRAND 220..225 FT /evidence="ECO:0007829|PDB:8D41" FT STRAND 232..237 FT /evidence="ECO:0007829|PDB:8D41" FT STRAND 239..248 FT /evidence="ECO:0007829|PDB:8D41" FT STRAND 251..257 FT /evidence="ECO:0007829|PDB:8D41" FT TURN 258..260 FT /evidence="ECO:0007829|PDB:8D41" FT STRAND 263..268 FT /evidence="ECO:0007829|PDB:8D41" FT STRAND 270..272 FT /evidence="ECO:0007829|PDB:8D41" FT STRAND 274..279 FT /evidence="ECO:0007829|PDB:8D41" FT STRAND 285..290 FT /evidence="ECO:0007829|PDB:8D41" FT STRAND 293..299 FT /evidence="ECO:0007829|PDB:8D41" FT STRAND 306..308 FT /evidence="ECO:0007829|PDB:8D30" FT STRAND 314..318 FT /evidence="ECO:0007829|PDB:8D30" FT STRAND 321..327 FT /evidence="ECO:0007829|PDB:8D30" FT TURN 332..334 FT /evidence="ECO:0007829|PDB:8D30" FT STRAND 343..350 FT /evidence="ECO:0007829|PDB:8D30" FT STRAND 356..360 FT /evidence="ECO:0007829|PDB:8D30" FT STRAND 364..371 FT /evidence="ECO:0007829|PDB:8D30" FT STRAND 374..379 FT /evidence="ECO:0007829|PDB:8D30" FT TURN 380..383 FT /evidence="ECO:0007829|PDB:8D30" FT STRAND 384..390 FT /evidence="ECO:0007829|PDB:8D30" FT STRAND 392..407 FT /evidence="ECO:0007829|PDB:8D30" FT TURN 408..410 FT /evidence="ECO:0007829|PDB:8D30" FT STRAND 411..416 FT /evidence="ECO:0007829|PDB:8D30" FT STRAND 419..424 FT /evidence="ECO:0007829|PDB:8D30" FT STRAND 431..434 FT /evidence="ECO:0007829|PDB:8D30" FT STRAND 436..442 FT /evidence="ECO:0007829|PDB:8D30" FT STRAND 447..450 FT /evidence="ECO:0007829|PDB:8D30" FT TURN 452..454 FT /evidence="ECO:0007829|PDB:8D30" FT STRAND 457..461 FT /evidence="ECO:0007829|PDB:8D30" FT STRAND 466..470 FT /evidence="ECO:0007829|PDB:8D30" FT STRAND 474..480 FT /evidence="ECO:0007829|PDB:8D30" FT STRAND 485..490 FT /evidence="ECO:0007829|PDB:8D30" FT HELIX 492..501 FT /evidence="ECO:0007829|PDB:8D30" FT STRAND 513..522 FT /evidence="ECO:0007829|PDB:8D30" FT STRAND 524..530 FT /evidence="ECO:0007829|PDB:8D30" FT STRAND 533..538 FT /evidence="ECO:0007829|PDB:8D30" FT STRAND 541..547 FT /evidence="ECO:0007829|PDB:8D30" FT STRAND 550..556 FT /evidence="ECO:0007829|PDB:8D30" FT STRAND 562..567 FT /evidence="ECO:0007829|PDB:8D30" FT TURN 568..571 FT /evidence="ECO:0007829|PDB:8D30" FT STRAND 572..576 FT /evidence="ECO:0007829|PDB:8D30" FT STRAND 582..586 FT /evidence="ECO:0007829|PDB:8D30" 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 //