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Conserved oligomeric Golgi complex subunit 5 (COG complex subunit 5) (13S Golgi transport complex 90 kDa subunit) (GTC-90) (Component of oligomeric Golgi complex 5) (Golgi transport complex 1)

 COG5_HUMAN              Reviewed;         839 AA.
Q9UP83; A4D0R6; A4D0R7; O14555; O95008; Q6NUL5;
30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 3.
12-SEP-2018, entry version 140.
RecName: Full=Conserved oligomeric Golgi complex subunit 5;
Short=COG complex subunit 5;
AltName: Full=13S Golgi transport complex 90 kDa subunit;
Short=GTC-90;
AltName: Full=Component of oligomeric Golgi complex 5;
AltName: Full=Golgi transport complex 1;
Name=COG5; Synonyms=GOLTC1, GTC90;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
VARIANTS LEU-330 AND PRO-558.
TISSUE=Brain;
PubMed=9792665; DOI=10.1074/jbc.273.45.29565;
Walter D.M., Paul K.S., Waters M.G.;
"Purification and characterization of a novel 13 S hetero-oligomeric
protein complex that stimulates in vitro Golgi transport.";
J. Biol. Chem. 273:29565-29576(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANT
LEU-330.
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[8]
INVOLVEMENT IN CDG2I.
PubMed=19690088; DOI=10.1093/hmg/ddp389;
Paesold-Burda P., Maag C., Troxler H., Foulquier F., Kleinert P.,
Schnabel S., Baumgartner M., Hennet T.;
"Deficiency in COG5 causes a moderate form of congenital disorders of
glycosylation.";
Hum. Mol. Genet. 18:4350-4356(2009).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- FUNCTION: Required for normal Golgi function. {ECO:0000250}.
-!- SUBUNIT: Component of the conserved oligomeric Golgi complex which
is composed of eight different subunits and is required for normal
Golgi morphology and localization. {ECO:0000250}.
-!- INTERACTION:
Q9H9E3:COG4; NbExp=2; IntAct=EBI-389502, EBI-368382;
A0A0S2Z604:COG7; NbExp=3; IntAct=EBI-16431689, EBI-16430119;
P83436:COG7; NbExp=2; IntAct=EBI-389502, EBI-389534;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:9792665}. Golgi apparatus membrane
{ECO:0000269|PubMed:9792665}; Peripheral membrane protein
{ECO:0000269|PubMed:9792665}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9UP83-1; Sequence=Displayed;
Name=2;
IsoId=Q9UP83-2; Sequence=VSP_031610;
Name=3;
IsoId=Q9UP83-3; Sequence=VSP_031610, VSP_031611;
Note=No experimental confirmation available.;
-!- DISEASE: Congenital disorder of glycosylation 2I (CDG2I)
[MIM:613612]: A multisystem disorder caused by a defect in
glycoprotein biosynthesis and characterized by under-glycosylated
serum glycoproteins. Congenital disorders of glycosylation result
in a wide variety of clinical features, such as defects in the
nervous system development, psychomotor retardation, dysmorphic
features, hypotonia, coagulation disorders, and immunodeficiency.
The broad spectrum of features reflects the critical role of N-
glycoproteins during embryonic development, differentiation, and
maintenance of cell functions. Congenital disorder of
glycosylation type 2I is characterized by mild neurological
impairments. {ECO:0000269|PubMed:19690088}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the COG5 family. {ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-32 is the initiator.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF058718; AAC69276.1; -; mRNA.
EMBL; AC002381; AAB63816.2; -; Genomic_DNA.
EMBL; AC004855; AAC83406.1; -; Genomic_DNA.
EMBL; CH236947; EAL24392.1; -; Genomic_DNA.
EMBL; CH236947; EAL24393.1; -; Genomic_DNA.
EMBL; CH471070; EAW83395.1; -; Genomic_DNA.
EMBL; CH471070; EAW83396.1; -; Genomic_DNA.
EMBL; BC068540; AAH68540.1; -; mRNA.
CCDS; CCDS55152.1; -. [Q9UP83-3]
CCDS; CCDS5742.1; -. [Q9UP83-2]
CCDS; CCDS5743.1; -. [Q9UP83-1]
RefSeq; NP_001154992.1; NM_001161520.1. [Q9UP83-3]
RefSeq; NP_006339.3; NM_006348.3. [Q9UP83-2]
RefSeq; NP_859422.2; NM_181733.2. [Q9UP83-1]
UniGene; Hs.239631; -.
ProteinModelPortal; Q9UP83; -.
SMR; Q9UP83; -.
BioGrid; 115729; 41.
CORUM; Q9UP83; -.
IntAct; Q9UP83; 14.
MINT; Q9UP83; -.
STRING; 9606.ENSP00000297135; -.
iPTMnet; Q9UP83; -.
PhosphoSitePlus; Q9UP83; -.
BioMuta; COG5; -.
DMDM; 296439390; -.
EPD; Q9UP83; -.
PaxDb; Q9UP83; -.
PeptideAtlas; Q9UP83; -.
PRIDE; Q9UP83; -.
ProteomicsDB; 85357; -.
ProteomicsDB; 85358; -. [Q9UP83-2]
ProteomicsDB; 85359; -. [Q9UP83-3]
DNASU; 10466; -.
Ensembl; ENST00000297135; ENSP00000297135; ENSG00000164597. [Q9UP83-2]
Ensembl; ENST00000347053; ENSP00000334703; ENSG00000164597. [Q9UP83-1]
Ensembl; ENST00000393603; ENSP00000377228; ENSG00000164597. [Q9UP83-3]
GeneID; 10466; -.
KEGG; hsa:10466; -.
UCSC; uc003vec.3; human. [Q9UP83-1]
CTD; 10466; -.
DisGeNET; 10466; -.
EuPathDB; HostDB:ENSG00000164597.13; -.
GeneCards; COG5; -.
GeneReviews; COG5; -.
HGNC; HGNC:14857; COG5.
HPA; HPA020300; -.
HPA; HPA041583; -.
MalaCards; COG5; -.
MIM; 606821; gene.
MIM; 613612; phenotype.
neXtProt; NX_Q9UP83; -.
OpenTargets; ENSG00000164597; -.
Orphanet; 263487; COG5-CDG.
PharmGKB; PA26698; -.
eggNOG; KOG2211; Eukaryota.
eggNOG; ENOG410XWH0; LUCA.
GeneTree; ENSGT00390000004586; -.
HOGENOM; HOG000170357; -.
HOVERGEN; HBG051063; -.
InParanoid; Q9UP83; -.
KO; K20292; -.
OMA; KDSLQPY; -.
OrthoDB; EOG091G048P; -.
PhylomeDB; Q9UP83; -.
TreeFam; TF313139; -.
Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
Reactome; R-HSA-6811438; Intra-Golgi traffic.
Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
ChiTaRS; COG5; human.
GeneWiki; COG5; -.
GenomeRNAi; 10466; -.
PRO; PR:Q9UP83; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000164597; Expressed in 235 organ(s), highest expression level in secondary oocyte.
CleanEx; HS_COG5; -.
ExpressionAtlas; Q9UP83; baseline and differential.
Genevisible; Q9UP83; HS.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0017119; C:Golgi transport complex; IDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:Reactome.
GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IBA:GO_Central.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
InterPro; IPR019465; Cog5.
PANTHER; PTHR13228; PTHR13228; 1.
Pfam; PF10392; COG5; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome;
Congenital disorder of glycosylation; Cytoplasm; Golgi apparatus;
Membrane; Phosphoprotein; Polymorphism; Protein transport;
Reference proteome; Transport.
CHAIN 1 839 Conserved oligomeric Golgi complex
subunit 5.
/FTId=PRO_0000213510.
MOD_RES 197 197 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 593 593 K -> KVVSSQSSFPLAAEQTIISALK (in isoform 2
and isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_031610.
VAR_SEQ 803 839 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_031611.
VARIANT 330 330 F -> L (in dbSNP:rs2269970).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9792665}.
/FTId=VAR_039142.
VARIANT 365 365 I -> V (in dbSNP:rs34087251).
/FTId=VAR_039182.
VARIANT 452 452 H -> R (in dbSNP:rs35393416).
/FTId=VAR_055664.
VARIANT 558 558 S -> P. {ECO:0000269|PubMed:9792665}.
/FTId=VAR_039143.
CONFLICT 112 112 A -> V (in Ref. 1; AAC69276).
{ECO:0000305}.
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


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