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Conserved oligomeric Golgi complex subunit 4 (COG complex subunit 4) (Component of oligomeric Golgi complex 4)

 COG4_HUMAN              Reviewed;         785 AA.
Q9H9E3; B4DMN8; C9JS23; Q96D40; Q9BRF0; Q9BVZ2; Q9H5Y4; Q9Y3W3;
30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
02-NOV-2010, sequence version 3.
12-SEP-2018, entry version 150.
RecName: Full=Conserved oligomeric Golgi complex subunit 4;
Short=COG complex subunit 4;
AltName: Full=Component of oligomeric Golgi complex 4;
Name=COG4;
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 2), AND VARIANT ILE-158.
TISSUE=T-cell;
Ariga H.;
"Cog4S, a splicing variant of Cog4.";
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
ILE-158.
TISSUE=Brain, Ileal mucosa, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ILE-158.
TISSUE=Muscle, Placenta, Skin, and 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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 229-785 (ISOFORM 1).
TISSUE=Uterus;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
SUBCELLULAR LOCATION.
PubMed=11703943; DOI=10.1016/S1534-5807(01)00063-6;
Whyte J.R., Munro S.;
"The Sec34/35 Golgi transport complex is related to the exocyst,
defining a family of complexes involved in multiple steps of membrane
traffic.";
Dev. Cell 1:527-537(2001).
[7]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:R8.1-R8.16(2004).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[9]
FUNCTION, AND INTERACTION WITH SCFD1 AND STX5.
PubMed=19536132; DOI=10.1038/emboj.2009.168;
Laufman O., Kedan A., Hong W., Lev S.;
"Direct interaction between the COG complex and the SM protein, Sly1,
is required for Golgi SNARE pairing.";
EMBO J. 28:2006-2017(2009).
[10]
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).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, 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).
[13]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 525-785, SUBUNIT,
IDENTIFICATION OF DOMAINS D AND E, CHARACTERIZATION OF VARIANT CDG2J
TRP-729, AND MUTAGENESIS OF ARG-729 AND GLU-764.
PubMed=19651599; DOI=10.1073/pnas.0901966106;
Richardson B.C., Smith R.D., Ungar D., Nakamura A., Jeffrey P.D.,
Lupashin V.V., Hughson F.M.;
"Structural basis for a human glycosylation disorder caused by
mutation of the COG4 gene.";
Proc. Natl. Acad. Sci. U.S.A. 106:13329-13334(2009).
[14]
VARIANT CDG2J TRP-729.
PubMed=19494034; DOI=10.1093/hmg/ddp262;
Reynders E., Foulquier F., Leao Teles E., Quelhas D., Morelle W.,
Rabouille C., Annaert W., Matthijs G.;
"Golgi function and dysfunction in the first COG4-deficient CDG type
II patient.";
Hum. Mol. Genet. 18:3244-3256(2009).
-!- FUNCTION: Required for normal Golgi function. Plays a role in
SNARE-pin assembly and Golgi-to-ER retrograde transport via its
interaction with SCFD1. {ECO:0000269|PubMed:19536132}.
-!- SUBUNIT: Monomer. Component of the conserved oligomeric Golgi
(COG) complex which is composed of eight different subunits and is
required for normal Golgi morphology and localization. Mediates
interaction of SCFD1 with the COG complex. Interacts with STX5.
{ECO:0000269|PubMed:19536132, ECO:0000269|PubMed:19651599}.
-!- INTERACTION:
Q8WTW3:COG1; NbExp=2; IntAct=EBI-368382, EBI-368371;
Q14746:COG2; NbExp=2; IntAct=EBI-368382, EBI-389449;
Q9UP83:COG5; NbExp=2; IntAct=EBI-368382, EBI-389502;
P83436:COG7; NbExp=4; IntAct=EBI-368382, EBI-389534;
Q8WVM8:SCFD1; NbExp=10; IntAct=EBI-368382, EBI-722569;
Q13190:STX5; NbExp=2; IntAct=EBI-368382, EBI-714206;
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane
{ECO:0000305|PubMed:11703943}; Peripheral membrane protein
{ECO:0000305|PubMed:11703943}; Cytoplasmic side
{ECO:0000305|PubMed:11703943}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9H9E3-1; Sequence=Displayed;
Name=2; Synonyms=Cog4S;
IsoId=Q9H9E3-2; Sequence=VSP_001127, VSP_001128;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=3;
IsoId=Q9H9E3-3; Sequence=VSP_037551;
Note=No experimental confirmation available.;
-!- DISEASE: Congenital disorder of glycosylation 2J (CDG2J)
[MIM:613489]: 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. {ECO:0000269|PubMed:19494034,
ECO:0000269|PubMed:19651599}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the COG4 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB15483.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AB088369; BAC05682.1; -; mRNA.
EMBL; AK022874; BAB14286.1; -; mRNA.
EMBL; AK026435; BAB15483.1; ALT_INIT; mRNA.
EMBL; AK297557; BAG59950.1; -; mRNA.
EMBL; AC106804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000796; AAH00796.1; -; mRNA.
EMBL; BC006306; AAH06306.2; -; mRNA.
EMBL; BC013347; AAH13347.2; -; mRNA.
EMBL; BC072438; AAH72438.1; -; mRNA.
EMBL; AL050101; CAB43272.1; -; mRNA.
RefSeq; NP_001182068.1; NM_001195139.1.
RefSeq; NP_056201.2; NM_015386.2.
UniGene; Hs.208680; -.
PDB; 3HR0; X-ray; 1.90 A; A/B=525-785.
PDBsum; 3HR0; -.
ProteinModelPortal; Q9H9E3; -.
SMR; Q9H9E3; -.
BioGrid; 117365; 40.
CORUM; Q9H9E3; -.
DIP; DIP-32635N; -.
IntAct; Q9H9E3; 25.
MINT; Q9H9E3; -.
STRING; 9606.ENSP00000315775; -.
iPTMnet; Q9H9E3; -.
PhosphoSitePlus; Q9H9E3; -.
BioMuta; COG4; -.
DMDM; 311033464; -.
EPD; Q9H9E3; -.
MaxQB; Q9H9E3; -.
PaxDb; Q9H9E3; -.
PeptideAtlas; Q9H9E3; -.
PRIDE; Q9H9E3; -.
ProteomicsDB; 81316; -.
ProteomicsDB; 81317; -. [Q9H9E3-2]
ProteomicsDB; 81318; -. [Q9H9E3-3]
DNASU; 25839; -.
Ensembl; ENST00000482252; ENSP00000432802; ENSG00000103051. [Q9H9E3-2]
GeneID; 25839; -.
KEGG; hsa:25839; -.
UCSC; uc059wqe.1; human. [Q9H9E3-1]
CTD; 25839; -.
DisGeNET; 25839; -.
EuPathDB; HostDB:ENSG00000103051.18; -.
GeneCards; COG4; -.
GeneReviews; COG4; -.
H-InvDB; HIX0013201; -.
HGNC; HGNC:18620; COG4.
HPA; HPA040924; -.
HPA; HPA042539; -.
MalaCards; COG4; -.
MIM; 606976; gene.
MIM; 613489; phenotype.
neXtProt; NX_Q9H9E3; -.
OpenTargets; ENSG00000103051; -.
Orphanet; 263501; COG4-CDG.
PharmGKB; PA38603; -.
eggNOG; KOG0412; Eukaryota.
eggNOG; ENOG410XS60; LUCA.
GeneTree; ENSGT00390000003662; -.
HOVERGEN; HBG031403; -.
InParanoid; Q9H9E3; -.
KO; K20291; -.
PhylomeDB; Q9H9E3; -.
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; COG4; human.
EvolutionaryTrace; Q9H9E3; -.
GeneWiki; COG4; -.
GenomeRNAi; 25839; -.
PRO; PR:Q9H9E3; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000103051; Expressed in 217 organ(s), highest expression level in right testis.
CleanEx; HS_COG4; -.
ExpressionAtlas; Q9H9E3; baseline and differential.
Genevisible; Q9H9E3; HS.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0017119; C:Golgi transport complex; IDA:UniProtKB.
GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:Reactome.
GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
GO; GO:0048213; P:Golgi vesicle prefusion complex stabilization; IMP:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0000301; P:retrograde transport, vesicle recycling within Golgi; IBA:GO_Central.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; IMP:UniProtKB.
InterPro; IPR013167; COG_su4.
Pfam; PF08318; COG4; 1.
SMART; SM00762; Cog4; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Congenital disorder of glycosylation; Disease mutation;
Golgi apparatus; Membrane; Phosphoprotein; Polymorphism;
Protein transport; Reference proteome; Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
CHAIN 2 785 Conserved oligomeric Golgi complex
subunit 4.
/FTId=PRO_0000213504.
REGION 2 84 Interaction with SCFD1.
{ECO:0000269|PubMed:19536132}.
REGION 85 153 Interaction with STX5.
{ECO:0000269|PubMed:19536132}.
REGION 618 740 D domain.
REGION 741 785 E domain; essential for proper cell
surface glycosylation.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
MOD_RES 6 6 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 73 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_037551.
VAR_SEQ 331 337 FRHVQNN -> NFVFSFF (in isoform 2).
{ECO:0000303|Ref.1}.
/FTId=VSP_001127.
VAR_SEQ 338 785 Missing (in isoform 2).
{ECO:0000303|Ref.1}.
/FTId=VSP_001128.
VARIANT 158 158 T -> I (in dbSNP:rs3931036).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.1}.
/FTId=VAR_058009.
VARIANT 729 729 R -> W (in CDG2J; severe defects in
glycosylation).
{ECO:0000269|PubMed:19494034,
ECO:0000269|PubMed:19651599}.
/FTId=VAR_063767.
MUTAGEN 729 729 R->A: Severe defects in glycosylation.
{ECO:0000269|PubMed:19651599}.
MUTAGEN 764 764 E->A: Severe defects in glycosylation.
{ECO:0000269|PubMed:19651599}.
CONFLICT 177 177 E -> G (in Ref. 2; BAB14286).
{ECO:0000305}.
CONFLICT 234 234 K -> R (in Ref. 2; BAB14286).
{ECO:0000305}.
CONFLICT 285 285 T -> A (in Ref. 2; BAB14286).
{ECO:0000305}.
CONFLICT 486 486 E -> G (in Ref. 2; BAB15483).
{ECO:0000305}.
CONFLICT 588 588 S -> G (in Ref. 2; BAB14286/BAG59950).
{ECO:0000305}.
CONFLICT 644 644 A -> S (in Ref. 4; AAH06306).
{ECO:0000305}.
HELIX 537 572 {ECO:0000244|PDB:3HR0}.
TURN 573 575 {ECO:0000244|PDB:3HR0}.
HELIX 580 615 {ECO:0000244|PDB:3HR0}.
HELIX 617 625 {ECO:0000244|PDB:3HR0}.
HELIX 626 629 {ECO:0000244|PDB:3HR0}.
HELIX 636 644 {ECO:0000244|PDB:3HR0}.
HELIX 649 666 {ECO:0000244|PDB:3HR0}.
HELIX 669 691 {ECO:0000244|PDB:3HR0}.
HELIX 698 716 {ECO:0000244|PDB:3HR0}.
HELIX 723 726 {ECO:0000244|PDB:3HR0}.
HELIX 728 737 {ECO:0000244|PDB:3HR0}.
HELIX 742 747 {ECO:0000244|PDB:3HR0}.
HELIX 750 753 {ECO:0000244|PDB:3HR0}.
HELIX 762 769 {ECO:0000244|PDB:3HR0}.
HELIX 777 782 {ECO:0000244|PDB:3HR0}.
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


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EIAAB08492 COG complex subunit 1,Cog1,Component of oligomeric Golgi complex 1,Conserved oligomeric Golgi complex subunit 1,Ldlb,Low density lipoprotein receptor defect B-complementing protein,Mouse,Mus musculus
EIAAB08494 COG complex subunit 2,COG2,Component of oligomeric Golgi complex 2,Conserved oligomeric Golgi complex subunit 2,Homo sapiens,Human,LDLC,Low density lipoprotein receptor defect C-complementing protein
EIAAB08493 COG complex subunit 1,COG1,Component of oligomeric Golgi complex 1,Conserved oligomeric Golgi complex subunit 1,Homo sapiens,Human,KIAA1381,LDLB
EIAAB08512 COG complex subunit 8,Cog8,Component of oligomeric Golgi complex 8,Conserved oligomeric Golgi complex subunit 8,MNCb-5704,Mouse,Mus musculus
EIAAB08509 COG complex subunit 7,COG7,Component of oligomeric Golgi complex 7,Conserved oligomeric Golgi complex subunit 7,Homo sapiens,Human,UNQ3082_PRO10013
EIAAB08505 COG complex subunit 6,COG6,Component of oligomeric Golgi complex 6,Conserved oligomeric Golgi complex subunit 6,Homo sapiens,Human,KIAA1134
EIAAB08507 COG complex subunit 6,Cog6,Component of oligomeric Golgi complex 6,Conserved oligomeric Golgi complex subunit 6,Kiaa1134,Mouse,Mus musculus
EIAAB08500 COG complex subunit 4,COG4,Component of oligomeric Golgi complex 4,Conserved oligomeric Golgi complex subunit 4,Homo sapiens,Human
EIAAB08514 COG complex subunit 8,COG8,Component of oligomeric Golgi complex 8,Conserved oligomeric Golgi complex subunit 8,Homo sapiens,Human
EIAAB08506 COG complex subunit 6,Cog6,Component of oligomeric Golgi complex 6,Conserved oligomeric Golgi complex subunit 6,Rat,Rattus norvegicus
EIAAB08513 Bos taurus,Bovine,COG complex subunit 8,COG8,Component of oligomeric Golgi complex 8,Conserved oligomeric Golgi complex subunit 8
EIAAB08499 COG complex subunit 4,Cog4,Component of oligomeric Golgi complex 4,Conserved oligomeric Golgi complex subunit 4,Mouse,Mus musculus
EIAAB08511 Bos taurus,Bovine,COG complex subunit 7,COG7,Component of oligomeric Golgi complex 7,Conserved oligomeric Golgi complex subunit 7
EIAAB08508 COG complex subunit 7,Cog7,Component of oligomeric Golgi complex 7,Conserved oligomeric Golgi complex subunit 7,Rat,Rattus norvegicus
EIAAB08498 Bos taurus,Bovine,COG complex subunit 4,COG4,Component of oligomeric Golgi complex 4,Conserved oligomeric Golgi complex subunit 4
EIAAB08510 COG complex subunit 7,Cog7,Component of oligomeric Golgi complex 7,Conserved oligomeric Golgi complex subunit 7,Mouse,Mus musculus
EIAAB08497 COG complex subunit 3,Cog3,Component of oligomeric Golgi complex 3,Conserved oligomeric Golgi complex subunit 3,Mouse,Mus musculus
EIAAB08504 Bos taurus,Bovine,COG complex subunit 6,COG6,Component of oligomeric Golgi complex 6,Conserved oligomeric Golgi complex subunit 6
EIAAB08502 COG complex subunit 5,Cog5,Component of oligomeric Golgi complex 5,Conserved oligomeric Golgi complex subunit 5,Mouse,Mus musculus
EIAAB08496 COG complex subunit 3,COG3,Component of oligomeric Golgi complex 3,Conserved oligomeric Golgi complex subunit 3,Homo sapiens,Human,p94,SEC34,Vesicle-docking protein SEC34 homolog
E10812c Rat ELISA Kit FOR Conserved oligomeric Golgi complex subunit 6 96T
E1305h Rat ELISA Kit FOR Conserved oligomeric Golgi complex subunit 7 96T


 

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