ID COG3_HUMAN Reviewed; 828 AA. AC Q96JB2; B2RAW5; Q5VT70; Q8IXX4; Q9BZ92; DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 02-SEP-2026, entry version 181. DE RecName: Full=Conserved oligomeric Golgi complex subunit 3; DE Short=COG complex subunit 3; DE AltName: Full=Component of oligomeric Golgi complex 3; DE AltName: Full=Vesicle-docking protein SEC34 homolog; DE AltName: Full=p94; GN Name=COG3; Synonyms=SEC34; 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), SUBCELLULAR LOCATION, AND TISSUE RP SPECIFICITY. RC TISSUE=Fetal brain; RX PubMed=11292827; DOI=10.1074/jbc.m011624200; RA Suvorova E.S., Kurten R.C., Lupashin V.V.; RT "Identification of a human ortholog of Sec34p as a component of the cis- RT Golgi vesicle tethering machinery."; RL J. Biol. Chem. 276:22810-22818(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND VARIANT SER-747. RX PubMed=11929878; DOI=10.1074/jbc.m202326200; RA Loh E., Hong W.; RT "Sec34 is implicated in traffic from the endoplasmic reticulum to the Golgi RT and exists in a complex with GTC-90 and ldlBp."; RL J. Biol. Chem. 277:21955-21961(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Placenta; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Leukocyte; 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 2-16, AND ACETYLATION AT ALA-2. 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, AND IDENTIFICATION BY RP 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, 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 [10] 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 [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [14] 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 [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [16] RP VARIANT [LARGE SCALE ANALYSIS] CYS-620. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [17] RP VARIANTS CDG2BB HIS-37 AND PRO-42, CHARACTERIZATION OF VARIANT CDG2BB RP PRO-42, INVOLVEMENT IN CDG2BB, AND FUNCTION. RX PubMed=37711075; DOI=10.1002/jimd.12679; RA Duan R., Marafi D., Xia Z.J., Ng B.G., Maroofian R., Sumya F.T., Saad A.K., RA Du H., Fatih J.M., Hunter J.V., Elbendary H.M., Baig S.M., Abdullah U., RA Ali Z., Efthymiou S., Murphy D., Mitani T., Withers M.A., Jhangiani S.N., RA Coban-Akdemir Z., Calame D.G., Pehlivan D., Gibbs R.A., Posey J.E., RA Houlden H., Lupashin V.V., Zaki M.S., Freeze H.H., Lupski J.R.; RT "Biallelic missense variants in COG3 cause a congenital disorder of RT glycosylation with impairment of retrograde vesicular trafficking."; RL J. Inherit. Metab. Dis. 46:1195-1205(2023). CC -!- FUNCTION: Involved in ER-Golgi transport (PubMed:11929878). Also CC involved in retrograde (Golgi to ER) transport (PubMed:37711075). CC {ECO:0000269|PubMed:11929878, ECO:0000269|PubMed:37711075}. CC -!- SUBUNIT: Component of the conserved oligomeric Golgi complex which is CC composed of eight different subunits and is required for normal Golgi CC morphology and localization. Interacts with TMEM115. {ECO:0000250, CC ECO:0000269|PubMed:24806965}. CC -!- INTERACTION: CC Q96JB2-2; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-9091495, EBI-11096309; CC Q96JB2-2; Q9BW66: CINP; NbExp=3; IntAct=EBI-9091495, EBI-739784; CC Q96JB2-2; Q13561: DCTN2; NbExp=3; IntAct=EBI-9091495, EBI-715074; CC Q96JB2-2; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-9091495, EBI-14069005; CC Q96JB2-2; O14901: KLF11; NbExp=3; IntAct=EBI-9091495, EBI-948266; CC Q96JB2-2; Q9BVL2: NUP58; NbExp=6; IntAct=EBI-9091495, EBI-2811583; CC Q96JB2-2; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-9091495, EBI-742688; CC Q96JB2-2; Q9C040: TRIM2; NbExp=3; IntAct=EBI-9091495, EBI-749840; CC Q96JB2-2; Q9NRE2: TSHZ2; NbExp=3; IntAct=EBI-9091495, EBI-10687282; CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane CC {ECO:0000269|PubMed:11292827}; Peripheral membrane protein CC {ECO:0000269|PubMed:11292827}. Note=Associated with the peripheral CC membrane of cis/medial cisternae. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q96JB2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96JB2-2; Sequence=VSP_013652, VSP_013653; CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in pancreas CC and testis and lowest levels in lung. {ECO:0000269|PubMed:11292827}. CC -!- DISEASE: Congenital disorder of glycosylation 2BB (CDG2BB) CC [MIM:620546]: A multisystem disorder caused by a defect in glycoprotein CC biosynthesis and characterized by under-glycosylated serum CC glycoproteins. Congenital disorders of glycosylation result in a wide CC variety of clinical features, such as defects in the nervous system CC development, psychomotor retardation, dysmorphic features, hypotonia, CC coagulation disorders, and immunodeficiency. The broad spectrum of CC features reflects the critical role of N-glycoproteins during embryonic CC development, differentiation, and maintenance of cell functions. CDG2BB CC is an autosomal recessive form characterized by global developmental CC delay, severe intellectual disability, microcephaly, epilepsy, facial CC dysmorphism, and variable neurological findings. CC {ECO:0000269|PubMed:37711075}. Note=The disease may be caused by CC variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the COG3 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; AF349676; AAK66974.1; -; mRNA. DR EMBL; AF332595; AAK06848.1; -; mRNA. DR EMBL; AK314387; BAG37012.1; -; mRNA. DR EMBL; AL139326; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL606514; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC038953; AAH38953.1; -; mRNA. DR CCDS; CCDS9398.1; -. [Q96JB2-1] DR RefSeq; NP_113619.3; NM_031431.4. [Q96JB2-1] DR AlphaFoldDB; Q96JB2; -. DR SMR; Q96JB2; -. DR BioGRID; 123680; 130. DR ComplexPortal; CPX-6199; COG tethering complex. DR CORUM; Q96JB2; -. DR FunCoup; Q96JB2; 3443. DR IntAct; Q96JB2; 72. DR MINT; Q96JB2; -. DR NDEx; IQUERY-CP-COG3; 1 NDEx IQuery Curated Pathway. DR STRING; 9606.ENSP00000258654; -. DR BindingDB; Q96JB2; -. DR ChEMBL; CHEMBL4105842; -. DR GlyCosmos; Q96JB2; 3 sites, 1 glycan. DR GlyGen; Q96JB2; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q96JB2; -. DR PhosphoSitePlus; Q96JB2; -. DR BioMuta; COG3; -. DR DMDM; 85701302; -. DR jPOST; Q96JB2; -. DR MassIVE; Q96JB2; -. DR PaxDb; 9606-ENSP00000258654; -. DR PeptideAtlas; Q96JB2; -. DR ProteomicsDB; 76926; -. [Q96JB2-1] DR ProteomicsDB; 76927; -. [Q96JB2-2] DR Pumba; Q96JB2; -. DR Antibodypedia; 23637; 162 antibodies from 26 providers. DR DNASU; 83548; -. DR Ensembl; ENST00000349995.10; ENSP00000258654.8; ENSG00000136152.16. [Q96JB2-1] DR Ensembl; ENST00000617493.1; ENSP00000481332.1; ENSG00000136152.16. [Q96JB2-2] DR GeneID; 83548; -. DR KEGG; hsa:83548; -. DR MANE-Select; ENST00000349995.10; ENSP00000258654.8; NM_031431.4; NP_113619.3. DR UCSC; uc001vai.4; human. [Q96JB2-1] DR AGR; HGNC:18619; -. DR ClinPGx; PA38602; -. DR CTD; 83548; -. DR DisGeNET; 83548; -. DR GeneCards; COG3; -. DR HGNC; HGNC:18619; COG3. DR HPA; ENSG00000136152; Low tissue specificity. DR MalaCards; COG3; -. DR MIM; 606975; gene. DR MIM; 620546; phenotype. DR OpenTargets; ENSG00000136152; -. DR VEuPathDB; HostDB:ENSG00000136152; -. DR eggNOG; KOG2604; Eukaryota. DR GeneTree; ENSGT00390000015682; -. DR HOGENOM; CLU_011639_1_1_1; -. DR InParanoid; Q96JB2; -. DR OMA; DEFELWG; -. DR OrthoDB; 296793at2759; -. DR PAN-GO; Q96JB2; 4 GO annotations based on evolutionary models. DR PhylomeDB; Q96JB2; -. DR PathwayCommons; Q96JB2; -. DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport. DR Reactome; R-HSA-6811438; Intra-Golgi traffic. DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network. DR SignaLink; Q96JB2; -. DR SIGNOR; Q96JB2; -. DR Agora; ENSG00000136152; -. DR BioGRID-ORCS; 83548; 626 hits in 1183 CRISPR screens. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR ChiTaRS; COG3; human. DR GeneWiki; COG3; -. DR GenomeRNAi; 83548; -. DR Pharos; Q96JB2; Tbio. DR PRO; PR:Q96JB2; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; Q96JB2; protein. DR Bgee; ENSG00000136152; Expressed in body of pancreas and 161 other cell types or tissues. DR ExpressionAtlas; Q96JB2; baseline and differential. DR GO; GO:0005801; C:cis-Golgi network; IEA:InterPro. DR GO; GO:0017119; C:COG complex; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0140312; F:cargo adaptor activity; IBA:GO_Central. DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA:UniProtKB. DR GO; GO:0009101; P:glycoprotein biosynthetic process; IMP:UniProtKB. DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB. DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IDA:UniProtKB. DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro. DR GO; GO:0033365; P:protein localization to organelle; IMP:UniProtKB. DR GO; GO:0050821; P:protein stabilization; IMP:UniProtKB. DR GO; GO:0000301; P:retrograde transport, vesicle recycling within Golgi; IMP:ComplexPortal. DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IMP:UniProtKB. DR InterPro; IPR048685; COG3_C. DR InterPro; IPR063408; COG3_Ccap. DR InterPro; IPR048320; COG3_N. DR InterPro; IPR007265; COG_su3. DR PANTHER; PTHR13302; CONSERVED OLIGOMERIC GOLGI COMPLEX COMPONENT 3; 1. DR PANTHER; PTHR13302:SF8; CONSERVED OLIGOMERIC GOLGI COMPLEX SUBUNIT 3; 1. DR Pfam; PF20671; COG3_C; 1. DR Pfam; PF31184; COG3_Ccap; 1. DR Pfam; PF04136; COG3_N; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Congenital disorder of glycosylation; KW Direct protein sequencing; Golgi apparatus; Membrane; Phosphoprotein; KW Protein transport; Proteomics identification; Reference proteome; KW Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:12665801, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, FT ECO:0007744|PubMed:25944712" FT CHAIN 2..828 FT /note="Conserved oligomeric Golgi complex subunit 3" FT /id="PRO_0000213500" FT REGION 504..543 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 525..543 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|PubMed:12665801, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, FT ECO:0007744|PubMed:25944712" FT MOD_RES 663 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT VAR_SEQ 443..444 FT /note="AE -> GK (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_013652" FT VAR_SEQ 445..828 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_013653" FT VARIANT 37 FT /note="D -> H (in CDG2BB; uncertain significance; FT dbSNP:rs755933277)" FT /evidence="ECO:0000269|PubMed:37711075" FT /id="VAR_089066" FT VARIANT 42 FT /note="S -> P (in CDG2BB; uncertain significance; decreased FT retrograde (Golgi to ER) transport in homozygous patient FT cells; decreased protein levels in homozygous patient FT cells)" FT /evidence="ECO:0000269|PubMed:37711075" FT /id="VAR_089067" FT VARIANT 620 FT /note="R -> C (in a breast cancer sample; somatic mutation; FT dbSNP:rs747042102)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036454" FT VARIANT 747 FT /note="N -> S (in dbSNP:rs2274285)" FT /evidence="ECO:0000269|PubMed:11929878" FT /id="VAR_055663" FT CONFLICT 106..107 FT /note="QQ -> HE (in Ref. 1; AAK66974)" FT /evidence="ECO:0000305" FT CONFLICT 825 FT /note="L -> S (in Ref. 1; AAK66974, 2; AAK06848 and 3; FT BAG37012)" FT /evidence="ECO:0000305" SQ SEQUENCE 828 AA; 94096 MW; B3DCF03FD4DC6A60 CRC64; MAEAALLLLP EAAAERDARE KLALWDRRPD TTAPLTDRQT DSVLELKAAA ENLPVPAELP IEDLCSLTSQ SLPIELTSVV PESTEDILLK GFTSLGMEEE RIETAQQFFS WFAKLQTQMD QDEGTKYRQM RDYLSGFQEQ CDAILNDVNS ALQHLESLQK QYLFVSNKTG TLHEACEQLL KEQSELVDLA ENIQQKLSYF NELETINTKL NSPTLSVNSD GFIPMLAKLD DCITYISSHP NFKDYPIYLL KFKQCLSKAL HLMKTYTVNT LQTLTSQLLK RDPSSVPNAD NAFTLFYVKF RAAAPKVRTL IEQIELRSEK IPEYQQLLND IHQCYLDQRE LLLGPSIACT VAELTSQNNR DHCALVRSGC AFMVHVCQDE HQLYNEFFTK PTSKLDELLE KLCVSLYDVF RPLIIHVIHL ETLSELCGIL KNEVLEDHVQ NNAEQLGAFA AGVKQMLEDV QERLVYRTHI YIQTDITGYK PAPGDLAYPD KLVMMEQIAQ SLKDEQKKVP SEASFSDVHL EEGESNSLTK SGSTESLNPR PQTTISPADL HGMWYPTVRR TLVCLSKLYR CIDRAVFQGL SQEALSACIQ SLLGASESIS KNKTQIDGQL FLIKHLLILR EQIAPFHTEF TIKEISLDLK KTRDAAFKIL NPMTVPRFFR LNSNNALIEF LLEGTPEIRE HYLDSKKDVD RHLKSACEQF IQQQTKLFVE QLEEFMTKVS ALKTMASQGG PKYTLSQQPW AQPAKVNDLA ATAYKTIKTK LPVTLRSMSL YLSNKDTEFI LFKPVRNNIQ QVFQKFHALL KEEFSPEDIQ IIACPSMEQL SLLLLVSK //