COG1_HUMAN
ID COG1_HUMAN Reviewed; 980 AA.
AC Q8WTW3; Q9NPV9; Q9P2G6;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Conserved oligomeric Golgi complex subunit 1;
DE Short=COG complex subunit 1;
DE AltName: Full=Component of oligomeric Golgi complex 1;
GN Name=COG1; Synonyms=KIAA1381, LDLB;
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 [LARGE SCALE MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-980.
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 543-980.
RC TISSUE=Melanoma;
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 [4]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=11980916; DOI=10.1083/jcb.200202016;
RA Ungar D., Oka T., Brittle E.E., Vasile E., Lupashin V.V., Chatterton J.E.,
RA Heuser J.E., Krieger M., Waters M.G.;
RT "Characterization of a mammalian Golgi-localized protein complex, COG, that
RT is required for normal Golgi morphology and function.";
RL J. Cell Biol. 157:405-415(2002).
RN [5]
RP INVOLVEMENT IN CDG2G.
RX PubMed=16537452; DOI=10.1073/pnas.0507685103;
RA Foulquier F., Vasile E., Schollen E., Callewaert N., Raemaekers T.,
RA Quelhas D., Jaeken J., Mills P., Winchester B., Krieger M., Annaert W.,
RA Matthijs G.;
RT "Conserved oligomeric Golgi complex subunit 1 deficiency reveals a
RT previously uncharacterized congenital disorder of glycosylation type II.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3764-3769(2006).
RN [6]
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 [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [9]
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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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).
CC -!- FUNCTION: Required for normal Golgi function. {ECO:0000250}.
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. {ECO:0000269|PubMed:11980916}.
CC -!- INTERACTION:
CC Q8WTW3; Q9H9E3: COG4; NbExp=2; IntAct=EBI-368371, EBI-368382;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000305|PubMed:11980916}; Peripheral membrane protein
CC {ECO:0000305|PubMed:11980916}; Cytoplasmic side
CC {ECO:0000305|PubMed:11980916}.
CC -!- DISEASE: Congenital disorder of glycosylation 2G (CDG2G) [MIM:611209]:
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 Clinical features of CDG2G include failure to thrive, generalized
CC hypotonia, growth retardation and mild psychomotor retardation. CDG2G
CC is biochemically characterized by a defect in O-glycosylation as well
CC as N-glycosylation. {ECO:0000269|PubMed:16537452}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the COG1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92619.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BC021985; AAH21985.1; -; mRNA.
DR EMBL; AB037802; BAA92619.1; ALT_FRAME; mRNA.
DR EMBL; AL359611; CAB94881.1; -; mRNA.
DR CCDS; CCDS11692.1; -.
DR PIR; T50629; T50629.
DR RefSeq; NP_061184.1; NM_018714.2.
DR AlphaFoldDB; Q8WTW3; -.
DR SMR; Q8WTW3; -.
DR BioGRID; 114783; 92.
DR ComplexPortal; CPX-6199; COG tethering complex.
DR CORUM; Q8WTW3; -.
DR IntAct; Q8WTW3; 26.
DR MINT; Q8WTW3; -.
DR STRING; 9606.ENSP00000299886; -.
DR ChEMBL; CHEMBL4105805; -.
DR iPTMnet; Q8WTW3; -.
DR PhosphoSitePlus; Q8WTW3; -.
DR BioMuta; COG1; -.
DR DMDM; 22653695; -.
DR EPD; Q8WTW3; -.
DR jPOST; Q8WTW3; -.
DR MassIVE; Q8WTW3; -.
DR MaxQB; Q8WTW3; -.
DR PaxDb; Q8WTW3; -.
DR PeptideAtlas; Q8WTW3; -.
DR PRIDE; Q8WTW3; -.
DR ProteomicsDB; 74609; -.
DR Antibodypedia; 31901; 132 antibodies from 28 providers.
DR DNASU; 9382; -.
DR Ensembl; ENST00000299886.9; ENSP00000299886.4; ENSG00000166685.13.
DR GeneID; 9382; -.
DR KEGG; hsa:9382; -.
DR MANE-Select; ENST00000299886.9; ENSP00000299886.4; NM_018714.3; NP_061184.1.
DR UCSC; uc002jjg.4; human.
DR CTD; 9382; -.
DR DisGeNET; 9382; -.
DR GeneCards; COG1; -.
DR GeneReviews; COG1; -.
DR HGNC; HGNC:6545; COG1.
DR HPA; ENSG00000166685; Low tissue specificity.
DR MalaCards; COG1; -.
DR MIM; 606973; gene.
DR MIM; 611209; phenotype.
DR neXtProt; NX_Q8WTW3; -.
DR OpenTargets; ENSG00000166685; -.
DR Orphanet; 263508; COG1-CDG.
DR PharmGKB; PA26696; -.
DR VEuPathDB; HostDB:ENSG00000166685; -.
DR eggNOG; KOG2033; Eukaryota.
DR GeneTree; ENSGT00390000017136; -.
DR InParanoid; Q8WTW3; -.
DR OMA; CSWFRHL; -.
DR OrthoDB; 221637at2759; -.
DR PhylomeDB; Q8WTW3; -.
DR TreeFam; TF314678; -.
DR PathwayCommons; Q8WTW3; -.
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; Q8WTW3; -.
DR BioGRID-ORCS; 9382; 382 hits in 1089 CRISPR screens.
DR ChiTaRS; COG1; human.
DR GeneWiki; COG1; -.
DR GenomeRNAi; 9382; -.
DR Pharos; Q8WTW3; Tbio.
DR PRO; PR:Q8WTW3; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8WTW3; protein.
DR Bgee; ENSG00000166685; Expressed in right hemisphere of cerebellum and 171 other tissues.
DR ExpressionAtlas; Q8WTW3; baseline and differential.
DR Genevisible; Q8WTW3; HS.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
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:0070085; P:glycosylation; IMP:ComplexPortal.
DR GO; GO:0007030; P:Golgi organization; IMP:ComplexPortal.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; NAS: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 InterPro; IPR033370; COG1.
DR PANTHER; PTHR31658; PTHR31658; 1.
PE 1: Evidence at protein level;
KW Acetylation; Congenital disorder of glycosylation; Golgi apparatus;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..980
FT /note="Conserved oligomeric Golgi complex subunit 1"
FT /id="PRO_0000213491"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 357
FT /note="M -> L (in dbSNP:rs4375725)"
FT /id="VAR_059231"
FT VARIANT 392
FT /note="N -> S (in dbSNP:rs1026128)"
FT /id="VAR_020415"
FT VARIANT 744
FT /note="Y -> C (in dbSNP:rs7208207)"
FT /id="VAR_048756"
SQ SEQUENCE 980 AA; 108978 MW; 68C066504260E36E CRC64;
MATAATSPAL KRLDLRDPAA LFETHGAEEI RGLERQVRAE IEHKKEELRQ MVGERYRDLI
EAADTIGQMR RCAVGLVDAV KATDQYCARL RQAGSAAPRP PRAQQPQQPS QEKFYSMAAQ
IKLLLEIPEK IWSSMEASQC LHATQLYLLC CHLHSLLQLD SSSSRYSPVL SRFPILIRQV
AAASHFRSTI LHESKMLLKC QGVSDQAVAE ALCSIMLLEE SSPRQALTDF LLARKATIQK
LLNQPHHGAG IKAQICSLVE LLATTLKQAH ALFYTLPEGL LPDPALPCGL LFSTLETITG
QHPAGKGTGV LQEEMKLCSW FKHLPASIVE FQPTLRTLAH PISQEYLKDT LQKWIHMCNE
DIKNGITNLL MYVKSMKGLA GIRDAMWELL TNESTNHSWD VLCRRLLEKP LLFWEDMMQQ
LFLDRLQTLT KEGFDSISSS SKELLVSALQ ELESSTSNSP SNKHIHFEYN MSLFLWSESP
NDLPSDAAWV SVANRGQFAS SGLSMKAQAI SPCVQNFCSA LDSKLKVKLD DLLAYLPSDD
SSLPKDVSPT QAKSSAFDRY ADAGTVQEML RTQSVACIKH IVDCIRAELQ SIEEGVQGQQ
DALNSAKLHS VLFMARLCQS LGELCPHLKQ CILGKSESSE KPAREFRALR KQGKVKTQEI
IPTQAKWQEV KEVLLQQSVM GYQVWSSAVV KVLIHGFTQS LLLDDAGSVL ATATSWDELE
IQEEAESGSS VTSKIRLPAQ PSWYVQSFLF SLCQEINRVG GHALPKVTLQ EMLKSCMVQV
VAAYEKLSEE KQIKKEGAFP VTQNRALQLL YDLRYLNIVL TAKGDEVKSG RSKPDSRIEK
VTDHLEALID PFDLDVFTPH LNSNLHRLVQ RTSVLFGLVT GTENQLAPRS STFNSQEPHN
ILPLASSQIR FGLLPLSMTS TRKAKSTRNI ETKAQVVPPA RSTAGDPTVP GSLFRQLVSE
EDNTSAPSLF KLGWLSSMTK
