COG4_HUMAN
ID COG4_HUMAN Reviewed; 785 AA.
AC Q9H9E3; B4DMN8; C9JS23; Q96D40; Q9BRF0; Q9BVZ2; Q9H5Y4; Q9Y3W3;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Conserved oligomeric Golgi complex subunit 4;
DE Short=COG complex subunit 4;
DE AltName: Full=Component of oligomeric Golgi complex 4;
GN Name=COG4;
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 2), AND VARIANT ILE-158.
RC TISSUE=T-cell;
RA Ariga H.;
RT "Cog4S, a splicing variant of Cog4.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP ILE-158.
RC TISSUE=Brain, Ileal mucosa, and 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=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-158.
RC TISSUE=Muscle, Placenta, Skin, and 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 229-785 (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=11703943; DOI=10.1016/s1534-5807(01)00063-6;
RA Whyte J.R., Munro S.;
RT "The Sec34/35 Golgi transport complex is related to the exocyst, defining a
RT family of complexes involved in multiple steps of membrane traffic.";
RL Dev. Cell 1:527-537(2001).
RN [7]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [8]
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=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 [9]
RP FUNCTION, AND INTERACTION WITH SCFD1 AND STX5.
RX PubMed=19536132; DOI=10.1038/emboj.2009.168;
RA Laufman O., Kedan A., Hong W., Lev S.;
RT "Direct interaction between the COG complex and the SM protein, Sly1, is
RT required for Golgi SNARE pairing.";
RL EMBO J. 28:2006-2017(2009).
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=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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND IDENTIFICATION BY MASS
RP 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 [13]
RP INVOLVEMENT IN SWILS, VARIANT SWILS ARG-512, CHARACTERIZATION OF VARIANT
RP SWILS ARG-512, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=30290151; DOI=10.1016/j.ajhg.2018.09.003;
RA Ferreira C.R., Xia Z.J., Clement A., Parry D.A., Davids M., Taylan F.,
RA Sharma P., Turgeon C.T., Blanco-Sanchez B., Ng B.G., Logan C.V.,
RA Wolfe L.A., Solomon B.D., Cho M.T., Douglas G., Carvalho D.R., Bratke H.,
RA Haug M.G., Phillips J.B., Wegner J., Tiemeyer M., Aoki K., Nordgren A.,
RA Hammarsjoe A., Duker A.L., Rohena L., Hove H.B., Ek J., Adams D.,
RA Tifft C.J., Onyekweli T., Weixel T., Macnamara E., Radtke K., Powis Z.,
RA Earl D., Gabriel M., Russi A.H.S., Brick L., Kozenko M., Tham E.,
RA Raymond K.M., Phillips J.A. III, Tiller G.E., Wilson W.G., Hamid R.,
RA Malicdan M.C.V., Nishimura G., Grigelioniene G., Jackson A.,
RA Westerfield M., Bober M.B., Gahl W.A., Freeze H.H.;
RT "A recurrent de novo heterozygous COG4 substitution leads to Saul-Wilson
RT syndrome, disrupted vesicular trafficking, and altered proteoglycan
RT glycosylation.";
RL Am. J. Hum. Genet. 103:553-567(2018).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 525-785, SUBUNIT, IDENTIFICATION
RP OF DOMAINS D AND E, CHARACTERIZATION OF VARIANT CDG2J TRP-729, AND
RP MUTAGENESIS OF ARG-729 AND GLU-764.
RX PubMed=19651599; DOI=10.1073/pnas.0901966106;
RA Richardson B.C., Smith R.D., Ungar D., Nakamura A., Jeffrey P.D.,
RA Lupashin V.V., Hughson F.M.;
RT "Structural basis for a human glycosylation disorder caused by mutation of
RT the COG4 gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:13329-13334(2009).
RN [15]
RP VARIANT CDG2J TRP-729.
RX PubMed=19494034; DOI=10.1093/hmg/ddp262;
RA Reynders E., Foulquier F., Leao Teles E., Quelhas D., Morelle W.,
RA Rabouille C., Annaert W., Matthijs G.;
RT "Golgi function and dysfunction in the first COG4-deficient CDG type II
RT patient.";
RL Hum. Mol. Genet. 18:3244-3256(2009).
CC -!- FUNCTION: Required for normal Golgi function (PubMed:19536132,
CC PubMed:30290151). Plays a role in SNARE-pin assembly and Golgi-to-ER
CC retrograde transport via its interaction with SCFD1 (PubMed:19536132).
CC {ECO:0000269|PubMed:19536132, ECO:0000269|PubMed:30290151}.
CC -!- SUBUNIT: Monomer. Component of the conserved oligomeric Golgi (COG)
CC complex which is composed of eight different subunits and is required
CC for normal Golgi morphology and localization (PubMed:19651599).
CC Mediates interaction of SCFD1 with the COG complex (PubMed:19536132).
CC Interacts with STX5 (PubMed:19536132). {ECO:0000269|PubMed:19536132,
CC ECO:0000269|PubMed:19651599}.
CC -!- INTERACTION:
CC Q9H9E3; X5D778: ANKRD11; NbExp=3; IntAct=EBI-368382, EBI-17183751;
CC Q9H9E3; Q9BXY8: BEX2; NbExp=3; IntAct=EBI-368382, EBI-745073;
CC Q9H9E3; Q8WTW3: COG1; NbExp=2; IntAct=EBI-368382, EBI-368371;
CC Q9H9E3; Q14746: COG2; NbExp=2; IntAct=EBI-368382, EBI-389449;
CC Q9H9E3; Q9UP83: COG5; NbExp=2; IntAct=EBI-368382, EBI-389502;
CC Q9H9E3; P83436: COG7; NbExp=4; IntAct=EBI-368382, EBI-389534;
CC Q9H9E3; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-368382, EBI-11962928;
CC Q9H9E3; Q9BQ89: FAM110A; NbExp=3; IntAct=EBI-368382, EBI-1752811;
CC Q9H9E3; Q9Y285: FARSA; NbExp=3; IntAct=EBI-368382, EBI-725361;
CC Q9H9E3; P25786: PSMA1; NbExp=3; IntAct=EBI-368382, EBI-359352;
CC Q9H9E3; Q8WVM8: SCFD1; NbExp=10; IntAct=EBI-368382, EBI-722569;
CC Q9H9E3; O60504: SORBS3; NbExp=3; IntAct=EBI-368382, EBI-741237;
CC Q9H9E3; Q13190: STX5; NbExp=2; IntAct=EBI-368382, EBI-714206;
CC Q9H9E3; O14530: TXNDC9; NbExp=5; IntAct=EBI-368382, EBI-707554;
CC Q9H9E3-1; Q9H9E3-1: COG4; NbExp=2; IntAct=EBI-15796331, EBI-15796331;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:30290151}.
CC Golgi apparatus membrane {ECO:0000305|PubMed:11703943}; Peripheral
CC membrane protein {ECO:0000305|PubMed:11703943}; Cytoplasmic side
CC {ECO:0000305|PubMed:11703943}. Note=Mosty cytosolic, with about 5%
CC membrane-bound. {ECO:0000269|PubMed:30290151}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9H9E3-1; Sequence=Displayed;
CC Name=2; Synonyms=Cog4S;
CC IsoId=Q9H9E3-2; Sequence=VSP_001127, VSP_001128;
CC Name=3;
CC IsoId=Q9H9E3-3; Sequence=VSP_037551;
CC -!- DISEASE: Congenital disorder of glycosylation 2J (CDG2J) [MIM:613489]:
CC A multisystem disorder caused by a defect in glycoprotein biosynthesis
CC and characterized by under-glycosylated serum glycoproteins. Congenital
CC disorders of glycosylation result in a wide variety of clinical
CC features, such as defects in the nervous system development,
CC psychomotor retardation, dysmorphic features, hypotonia, coagulation
CC disorders, and immunodeficiency. The broad spectrum of features
CC reflects the critical role of N-glycoproteins during embryonic
CC development, differentiation, and maintenance of cell functions.
CC {ECO:0000269|PubMed:19494034, ECO:0000269|PubMed:19651599}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Saul-Wilson syndrome (SWILS) [MIM:618150]: A rare skeletal
CC dysplasia with characteristic dysmorphic and radiographic findings, as
CC well as early developmental delay, primarily involving speech, with
CC eventual normal cognition. Clinical findings include marked short
CC stature, prominent forehead with an enlarged anterior fontanel,
CC prominent eyes with cataracts, narrow nasal bridge with a convex nasal
CC ridge, micrognathia, clubfoot, brachydactyly, and short distal
CC phalanges of fingers. Radiographic changes include platyspondyly,
CC irregular end plates of vertebral bodies, and hypoplasia of the
CC odontoid process with cervical instability in the spine, coxa valga,
CC overtubulation, metaphyseal flaring and megaepiphyses in the long
CC bones, while the hands and feet exhibit short phalanges, metacarpals
CC and metatarsals, cone-shaped epiphyses of phalanges, and accessory
CC ossification centers of metacarpals and metatarsals.
CC {ECO:0000269|PubMed:30290151}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the COG4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15483.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AB088369; BAC05682.1; -; mRNA.
DR EMBL; AK022874; BAB14286.1; -; mRNA.
DR EMBL; AK026435; BAB15483.1; ALT_INIT; mRNA.
DR EMBL; AK297557; BAG59950.1; -; mRNA.
DR EMBL; AC106804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000796; AAH00796.1; -; mRNA.
DR EMBL; BC006306; AAH06306.2; -; mRNA.
DR EMBL; BC013347; AAH13347.2; -; mRNA.
DR EMBL; BC072438; AAH72438.1; -; mRNA.
DR EMBL; AL050101; CAB43272.1; -; mRNA.
DR RefSeq; NP_001182068.1; NM_001195139.1.
DR RefSeq; NP_056201.2; NM_015386.2.
DR PDB; 3HR0; X-ray; 1.90 A; A/B=525-785.
DR PDBsum; 3HR0; -.
DR AlphaFoldDB; Q9H9E3; -.
DR SMR; Q9H9E3; -.
DR BioGRID; 117365; 100.
DR ComplexPortal; CPX-6199; COG tethering complex.
DR CORUM; Q9H9E3; -.
DR DIP; DIP-32635N; -.
DR IntAct; Q9H9E3; 43.
DR MINT; Q9H9E3; -.
DR STRING; 9606.ENSP00000315775; -.
DR ChEMBL; CHEMBL4105733; -.
DR iPTMnet; Q9H9E3; -.
DR PhosphoSitePlus; Q9H9E3; -.
DR BioMuta; COG4; -.
DR DMDM; 311033464; -.
DR EPD; Q9H9E3; -.
DR jPOST; Q9H9E3; -.
DR MassIVE; Q9H9E3; -.
DR MaxQB; Q9H9E3; -.
DR PaxDb; Q9H9E3; -.
DR PeptideAtlas; Q9H9E3; -.
DR PRIDE; Q9H9E3; -.
DR ProteomicsDB; 81316; -. [Q9H9E3-1]
DR ProteomicsDB; 81317; -. [Q9H9E3-2]
DR ProteomicsDB; 81318; -. [Q9H9E3-3]
DR DNASU; 25839; -.
DR Ensembl; ENST00000482252.5; ENSP00000432802.1; ENSG00000103051.20. [Q9H9E3-2]
DR GeneID; 25839; -.
DR KEGG; hsa:25839; -.
DR UCSC; uc059wqe.1; human. [Q9H9E3-1]
DR CTD; 25839; -.
DR DisGeNET; 25839; -.
DR GeneCards; COG4; -.
DR GeneReviews; COG4; -.
DR HGNC; HGNC:18620; COG4.
DR MalaCards; COG4; -.
DR MIM; 606976; gene.
DR MIM; 613489; phenotype.
DR MIM; 618150; phenotype.
DR neXtProt; NX_Q9H9E3; -.
DR OpenTargets; ENSG00000103051; -.
DR Orphanet; 263501; COG4-CDG.
DR Orphanet; 85172; Microcephalic osteodysplastic dysplasia, Saul-Wilson type.
DR PharmGKB; PA38603; -.
DR VEuPathDB; HostDB:ENSG00000103051; -.
DR eggNOG; KOG0412; Eukaryota.
DR GeneTree; ENSGT00940000154065; -.
DR HOGENOM; CLU_014853_0_0_1; -.
DR InParanoid; Q9H9E3; -.
DR OrthoDB; 376278at2759; -.
DR PhylomeDB; Q9H9E3; -.
DR PathwayCommons; Q9H9E3; -.
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; Q9H9E3; -.
DR BioGRID-ORCS; 25839; 399 hits in 1087 CRISPR screens.
DR ChiTaRS; COG4; human.
DR EvolutionaryTrace; Q9H9E3; -.
DR GeneWiki; COG4; -.
DR GenomeRNAi; 25839; -.
DR Pharos; Q9H9E3; Tbio.
DR PRO; PR:Q9H9E3; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9H9E3; protein.
DR Bgee; ENSG00000103051; Expressed in lower esophagus mucosa and 189 other tissues.
DR ExpressionAtlas; Q9H9E3; baseline and differential.
DR Genevisible; Q9H9E3; HS.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0017119; C:Golgi transport complex; IDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0070085; P:glycosylation; IMP:ComplexPortal.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0048213; P:Golgi vesicle prefusion complex stabilization; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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; IPR013167; COG_su4.
DR Pfam; PF08318; COG4; 1.
DR SMART; SM00762; Cog4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing;
KW Congenital disorder of glycosylation; Cytoplasm; Disease variant; Dwarfism;
KW Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..785
FT /note="Conserved oligomeric Golgi complex subunit 4"
FT /id="PRO_0000213504"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..84
FT /note="Interaction with SCFD1"
FT /evidence="ECO:0000269|PubMed:19536132"
FT REGION 85..153
FT /note="Interaction with STX5"
FT /evidence="ECO:0000269|PubMed:19536132"
FT REGION 618..740
FT /note="D domain"
FT /evidence="ECO:0000269|PubMed:19651599"
FT REGION 741..785
FT /note="E domain; essential for proper cell surface
FT glycosylation"
FT /evidence="ECO:0000269|PubMed:19651599"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..73
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037551"
FT VAR_SEQ 331..337
FT /note="FRHVQNN -> NFVFSFF (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_001127"
FT VAR_SEQ 338..785
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_001128"
FT VARIANT 158
FT /note="T -> I (in dbSNP:rs3931036)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.1"
FT /id="VAR_058009"
FT VARIANT 512
FT /note="G -> R (in SWILS; delayed anterograde vesicular
FT trafficking from the ER to the Golgi and accelerated
FT retrograde vesicular recycling from the Golgi to the ER,
FT leading to a decrease in Golgi volume, as well as
FT morphologic abnormalities with collapse of the Golgi stacks
FT in affected fibroblasts; altered decorin/DCN Golgi-
FT dependent glycosylation; no effect on protein expression;
FT dbSNP:rs1555575860)"
FT /evidence="ECO:0000269|PubMed:30290151"
FT /id="VAR_081564"
FT VARIANT 729
FT /note="R -> W (in CDG2J; severe defects in glycosylation)"
FT /evidence="ECO:0000269|PubMed:19494034,
FT ECO:0000269|PubMed:19651599"
FT /id="VAR_063767"
FT MUTAGEN 729
FT /note="R->A: Severe defects in glycosylation."
FT /evidence="ECO:0000269|PubMed:19651599"
FT MUTAGEN 764
FT /note="E->A: Severe defects in glycosylation."
FT /evidence="ECO:0000269|PubMed:19651599"
FT CONFLICT 177
FT /note="E -> G (in Ref. 2; BAB14286)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="K -> R (in Ref. 2; BAB14286)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="T -> A (in Ref. 2; BAB14286)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="E -> G (in Ref. 2; BAB15483)"
FT /evidence="ECO:0000305"
FT CONFLICT 588
FT /note="S -> G (in Ref. 2; BAB14286/BAG59950)"
FT /evidence="ECO:0000305"
FT CONFLICT 644
FT /note="A -> S (in Ref. 4; AAH06306)"
FT /evidence="ECO:0000305"
FT HELIX 537..572
FT /evidence="ECO:0007829|PDB:3HR0"
FT TURN 573..575
FT /evidence="ECO:0007829|PDB:3HR0"
FT HELIX 580..615
FT /evidence="ECO:0007829|PDB:3HR0"
FT HELIX 617..625
FT /evidence="ECO:0007829|PDB:3HR0"
FT HELIX 626..629
FT /evidence="ECO:0007829|PDB:3HR0"
FT HELIX 636..644
FT /evidence="ECO:0007829|PDB:3HR0"
FT HELIX 649..666
FT /evidence="ECO:0007829|PDB:3HR0"
FT HELIX 669..691
FT /evidence="ECO:0007829|PDB:3HR0"
FT HELIX 698..716
FT /evidence="ECO:0007829|PDB:3HR0"
FT HELIX 723..726
FT /evidence="ECO:0007829|PDB:3HR0"
FT HELIX 728..737
FT /evidence="ECO:0007829|PDB:3HR0"
FT HELIX 742..747
FT /evidence="ECO:0007829|PDB:3HR0"
FT HELIX 750..753
FT /evidence="ECO:0007829|PDB:3HR0"
FT HELIX 762..769
FT /evidence="ECO:0007829|PDB:3HR0"
FT HELIX 777..782
FT /evidence="ECO:0007829|PDB:3HR0"
SQ SEQUENCE 785 AA; 89083 MW; 93E8597991934AD2 CRC64;
MADLDSPPKL SGVQQPSEGV GGGRCSEISA ELIRSLTELQ ELEAVYERLC GEEKVVEREL
DALLEQQNTI ESKMVTLHRM GPNLQLIEGD AKQLAGMITF TCNLAENVSS KVRQLDLAKN
RLYQAIQRAD DILDLKFCMD GVQTALRSED YEQAAAHTHR YLCLDKSVIE LSRQGKEGSM
IDANLKLLQE AEQRLKAIVA EKFAIATKEG DLPQVERFFK IFPLLGLHEE GLRKFSEYLC
KQVASKAEEN LLMVLGTDMS DRRAAVIFAD TLTLLFEGIA RIVETHQPIV ETYYGPGRLY
TLIKYLQVEC DRQVEKVVDK FIKQRDYHQQ FRHVQNNLMR NSTTEKIEPR ELDPILTEVT
LMNARSELYL RFLKKRISSD FEVGDSMASE EVKQEHQKCL DKLLNNCLLS CTMQELIGLY
VTMEEYFMRE TVNKAVALDT YEKGQLTSSM VDDVFYIVKK CIGRALSSSS IDCLCAMINL
ATTELESDFR DVLCNKLRMG FPATTFQDIQ RGVTSAVNIM HSSLQQGKFD TKGIESTDEA
KMSFLVTLNN VEVCSENIST LKKTLESDCT KLFSQGIGGE QAQAKFDSCL SDLAAVSNKF
RDLLQEGLTE LNSTAIKPQV QPWINSFFSV SHNIEEEEFN DYEANDPWVQ QFILNLEQQM
AEFKASLSPV IYDSLTGLMT SLVAVELEKV VLKSTFNRLG GLQFDKELRS LIAYLTTVTT
WTIRDKFARL SQMATILNLE RVTEILDYWG PNSGPLTWRL TPAEVRQVLA LRIDFRSEDI
KRLRL
