COG5_HUMAN
ID COG5_HUMAN Reviewed; 839 AA.
AC Q9UP83; A4D0R6; A4D0R7; O14555; O95008; Q6NUL5;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Conserved oligomeric Golgi complex subunit 5;
DE Short=COG complex subunit 5;
DE AltName: Full=13S Golgi transport complex 90 kDa subunit;
DE Short=GTC-90;
DE AltName: Full=Component of oligomeric Golgi complex 5;
DE AltName: Full=Golgi transport complex 1;
GN Name=COG5; Synonyms=GOLTC1, GTC90;
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 VARIANTS
RP LEU-330 AND PRO-558.
RC TISSUE=Brain;
RX PubMed=9792665; DOI=10.1074/jbc.273.45.29565;
RA Walter D.M., Paul K.S., Waters M.G.;
RT "Purification and characterization of a novel 13 S hetero-oligomeric
RT protein complex that stimulates in vitro Golgi transport.";
RL J. Biol. Chem. 273:29565-29576(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT LEU-330.
RC TISSUE=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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, 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 INVOLVEMENT IN CDG2I.
RX PubMed=19690088; DOI=10.1093/hmg/ddp389;
RA Paesold-Burda P., Maag C., Troxler H., Foulquier F., Kleinert P.,
RA Schnabel S., Baumgartner M., Hennet T.;
RT "Deficiency in COG5 causes a moderate form of congenital disorders of
RT glycosylation.";
RL Hum. Mol. Genet. 18:4350-4356(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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, 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).
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:0000250}.
CC -!- INTERACTION:
CC Q9UP83; Q9H9E3: COG4; NbExp=2; IntAct=EBI-389502, EBI-368382;
CC Q9UP83; P83436: COG7; NbExp=2; IntAct=EBI-389502, EBI-389534;
CC Q9UP83-3; A0A0S2Z604: COG7; NbExp=3; IntAct=EBI-16431689, EBI-16430119;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:9792665}.
CC Golgi apparatus membrane {ECO:0000269|PubMed:9792665}; Peripheral
CC membrane protein {ECO:0000269|PubMed:9792665}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UP83-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UP83-2; Sequence=VSP_031610;
CC Name=3;
CC IsoId=Q9UP83-3; Sequence=VSP_031610, VSP_031611;
CC -!- DISEASE: Congenital disorder of glycosylation 2I (CDG2I) [MIM:613612]:
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 Congenital disorder of glycosylation type 2I is characterized by mild
CC neurological impairments. {ECO:0000269|PubMed:19690088}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the COG5 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-32 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AF058718; AAC69276.1; -; mRNA.
DR EMBL; AC002381; AAB63816.2; -; Genomic_DNA.
DR EMBL; AC004855; AAC83406.1; -; Genomic_DNA.
DR EMBL; CH236947; EAL24392.1; -; Genomic_DNA.
DR EMBL; CH236947; EAL24393.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83395.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83396.1; -; Genomic_DNA.
DR EMBL; BC068540; AAH68540.1; -; mRNA.
DR RefSeq; NP_001154992.1; NM_001161520.1.
DR RefSeq; NP_006339.3; NM_006348.3.
DR RefSeq; NP_859422.2; NM_181733.2.
DR AlphaFoldDB; Q9UP83; -.
DR BioGRID; 115729; 67.
DR ComplexPortal; CPX-6199; COG tethering complex.
DR CORUM; Q9UP83; -.
DR IntAct; Q9UP83; 40.
DR MINT; Q9UP83; -.
DR STRING; 9606.ENSP00000297135; -.
DR GlyConnect; 2030; 1 N-Linked glycan (1 site).
DR GlyGen; Q9UP83; 1 site, 2 N-linked glycans (1 site).
DR iPTMnet; Q9UP83; -.
DR MetOSite; Q9UP83; -.
DR PhosphoSitePlus; Q9UP83; -.
DR BioMuta; COG5; -.
DR DMDM; 296439390; -.
DR EPD; Q9UP83; -.
DR jPOST; Q9UP83; -.
DR MassIVE; Q9UP83; -.
DR MaxQB; Q9UP83; -.
DR PaxDb; Q9UP83; -.
DR PeptideAtlas; Q9UP83; -.
DR PRIDE; Q9UP83; -.
DR ProteomicsDB; 85357; -. [Q9UP83-1]
DR ProteomicsDB; 85358; -. [Q9UP83-2]
DR ProteomicsDB; 85359; -. [Q9UP83-3]
DR Antibodypedia; 17176; 50 antibodies from 15 providers.
DR DNASU; 10466; -.
DR Ensembl; ENST00000297135.9; ENSP00000297135.4; ENSG00000164597.15.
DR Ensembl; ENST00000347053.8; ENSP00000334703.3; ENSG00000164597.15.
DR Ensembl; ENST00000393603.7; ENSP00000377228.3; ENSG00000164597.15.
DR GeneID; 10466; -.
DR KEGG; hsa:10466; -.
DR UCSC; uc003vec.3; human. [Q9UP83-1]
DR CTD; 10466; -.
DR DisGeNET; 10466; -.
DR GeneCards; COG5; -.
DR GeneReviews; COG5; -.
DR HGNC; HGNC:14857; COG5.
DR HPA; ENSG00000164597; Low tissue specificity.
DR MalaCards; COG5; -.
DR MIM; 606821; gene.
DR MIM; 613612; phenotype.
DR neXtProt; NX_Q9UP83; -.
DR Orphanet; 263487; COG5-CDG.
DR PharmGKB; PA26698; -.
DR VEuPathDB; HostDB:ENSG00000164597; -.
DR eggNOG; KOG2211; Eukaryota.
DR HOGENOM; CLU_009839_1_0_1; -.
DR InParanoid; Q9UP83; -.
DR OrthoDB; 871605at2759; -.
DR PhylomeDB; Q9UP83; -.
DR TreeFam; TF313139; -.
DR PathwayCommons; Q9UP83; -.
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; Q9UP83; -.
DR BioGRID-ORCS; 10466; 66 hits in 1084 CRISPR screens.
DR ChiTaRS; COG5; human.
DR GeneWiki; COG5; -.
DR GenomeRNAi; 10466; -.
DR Pharos; Q9UP83; Tbio.
DR PRO; PR:Q9UP83; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9UP83; protein.
DR Bgee; ENSG00000164597; Expressed in corpus callosum and 107 other tissues.
DR ExpressionAtlas; Q9UP83; baseline and differential.
DR Genevisible; Q9UP83; HS.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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:0048219; P:inter-Golgi cisterna vesicle-mediated transport; IDA:MGI.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
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; IPR019465; Cog5.
DR PANTHER; PTHR13228; PTHR13228; 1.
DR Pfam; PF10392; COG5; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Congenital disorder of glycosylation; Cytoplasm;
KW Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..839
FT /note="Conserved oligomeric Golgi complex subunit 5"
FT /id="PRO_0000213510"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 593
FT /note="K -> KVVSSQSSFPLAAEQTIISALK (in isoform 2 and
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031610"
FT VAR_SEQ 803..839
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031611"
FT VARIANT 330
FT /note="F -> L (in dbSNP:rs2269970)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9792665"
FT /id="VAR_039142"
FT VARIANT 365
FT /note="I -> V (in dbSNP:rs34087251)"
FT /id="VAR_039182"
FT VARIANT 452
FT /note="H -> R (in dbSNP:rs35393416)"
FT /id="VAR_055664"
FT VARIANT 558
FT /note="S -> P"
FT /evidence="ECO:0000269|PubMed:9792665"
FT /id="VAR_039143"
FT CONFLICT 112
FT /note="A -> V (in Ref. 1; AAC69276)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 839 AA; 92743 MW; 95BD2E254A0C3FF7 CRC64;
MGWVGGRRRD SASPPGRSRS AADDINPAPA NMEGGGGSVA VAGLGARGSG AAAATVRELL
QDGCYSDFLN EDFDVKTYTS QSIHQAVIAE QLAKLAQGIS QLDRELHLQV VARHEDLLAQ
ATGIESLEGV LQMMQTRIGA LQGAVDRIKA KIVEPYNKIV ARTAQLARLQ VACDLLRRII
RILNLSKRLQ GQLQGGSREI TKAAQSLNEL DYLSQGIDLS GIEVIENDLL FIARARLEVE
NQAKRLLEQG LETQNPTQVG TALQVFYNLG TLKDTITSVV DGYCATLEEN INSALDIKVL
TQPSQSAVRG GPGRSTMPTP GNTAALRASF WTNMEKLMDH IYAVCGQVQH LQKVLAKKRD
PVSHICFIEE IVKDGQPEIF YTFWNSVTQA LSSQFHMATN SSMFLKQAFE GEYPKLLRLY
NDLWKRLQQY SQHIQGNFNA SGTTDLYVDL QHMEDDAQDI FIPKKPDYDP EKALKDSLQP
YEAAYLSKSL SRLFDPINLV FPPGGRNPPS SDELDGIIKT IASELNVAAV DTNLTLAVSK
NVAKTIQLYS VKSEQLLSTQ GDASQVIGPL TEGQRRNVAV VNSLYKLHQS VTKAIHALME
NAVQPLLTSV GDAIEAIIIT MHQEDFSGSL SSSGKPDVPC SLYMKELQGF IARVMSDYFK
HFECLDFVFD NTEAIAQRAV ELFIRHASLI RPLGEGGKMR LAADFAQMEL AVGPFCRRVS
DLGKSYRMLR SFRPLLFQAS EHVASSPALG DVIPFSIIIQ FLFTRAPAEL KSPFQRAEWS
HTRFSQWLDD HPSEKDRLLL IRGALEAYVQ SVRSREGKEF APVYPIMVQL LQKAMSALQ
