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Coatomer subunit zeta-1 (Zeta-1-coat protein) (Zeta-1 COP)

 COPZ1_HUMAN             Reviewed;         177 AA.
P61923; B4DDX8; B4DHZ0; F8VS17; F8VWL5; Q549N6; Q9Y3C3;
07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
07-JUN-2004, sequence version 1.
18-JUL-2018, entry version 132.
RecName: Full=Coatomer subunit zeta-1;
AltName: Full=Zeta-1-coat protein;
Short=Zeta-1 COP;
Name=COPZ1; Synonyms=COPZ; ORFNames=CGI-120, HSPC181;
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).
PubMed=11056392; DOI=10.1093/oxfordjournals.jbchem.a022817;
Futatsumori M., Kasai K., Takatsu H., Shin H.-W., Nakayama K.;
"Identification and characterization of novel isoforms of COP I
subunits.";
J. Biochem. 128:793-801(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=10810093; DOI=10.1101/gr.10.5.703;
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
"Identification of novel human genes evolutionarily conserved in
Caenorhabditis elegans by comparative proteomics.";
Genome Res. 10:703-713(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Umbilical cord blood;
PubMed=11042152; DOI=10.1101/gr.140200;
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
"Cloning and functional analysis of cDNAs with open reading frames for
300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells.";
Genome Res. 10:1546-1560(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tu Q., Yu L., Hu P.R., Zhang H.L., Huang J., Zhao S.Y.;
"Cloning and expression of a new human cDNA homology to B.taurus z-cop
mRNA.";
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Caudate nucleus, and Urinary bladder;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[7]
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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
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).
[9]
PROTEIN SEQUENCE OF 1-14, ACETYLATION AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Colon carcinoma;
Bienvenut W.V., Zebisch A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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).
[11]
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).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[15]
STRUCTURE BY NMR, SUBUNIT, AND MUTAGENESIS OF 58-LYS-ILE-59 AND
87-GLU-LEU-88.
PubMed=19167404; DOI=10.1016/j.jmb.2008.12.083;
Yu W., Lin J., Jin C., Xia B.;
"Solution structure of human zeta-COP: direct evidences for structural
similarity between COP I and clathrin-adaptor coats.";
J. Mol. Biol. 386:903-912(2009).
-!- FUNCTION: The coatomer is a cytosolic protein complex that binds
to dilysine motifs and reversibly associates with Golgi non-
clathrin-coated vesicles, which further mediate biosynthetic
protein transport from the ER, via the Golgi up to the trans Golgi
network. Coatomer complex is required for budding from Golgi
membranes, and is essential for the retrograde Golgi-to-ER
transport of dilysine-tagged proteins. In mammals, the coatomer
can only be recruited by membranes associated to ADP-ribosylation
factors (ARFs), which are small GTP-binding proteins; the complex
also influences the Golgi structural integrity, as well as the
processing, activity, and endocytic recycling of LDL receptors (By
similarity). {ECO:0000250}.
-!- FUNCTION: The zeta subunit may be involved in regulating the coat
assembly and, hence, the rate of biosynthetic protein transport
due to its association-dissociation properties with the coatomer
complex.
-!- SUBUNIT: Oligomeric complex that consists of at least the alpha,
beta, beta', gamma, delta, epsilon and zeta subunits.
{ECO:0000269|PubMed:19167404}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Golgi apparatus
membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated
vesicle membrane {ECO:0000250}; Peripheral membrane protein
{ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer
is cytoplasmic or polymerized on the cytoplasmic side of the
Golgi, as well as on the vesicles/buds originating from it.
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=P61923-1; Sequence=Displayed;
Name=2;
IsoId=P61923-2; Sequence=VSP_053675, VSP_053676;
Note=No experimental confirmation available.;
Name=3;
IsoId=P61923-3; Sequence=VSP_055050;
Note=No experimental confirmation available.;
Name=4;
IsoId=P61923-4; Sequence=VSP_055049;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
Name=5;
IsoId=P61923-5; Sequence=VSP_055051;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
-!- SIMILARITY: Belongs to the adaptor complexes small subunit family.
{ECO:0000305}.
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EMBL; AB047848; BAB17659.1; -; mRNA.
EMBL; AF151878; AAD34115.1; -; mRNA.
EMBL; AF161529; AAF29144.1; -; mRNA.
EMBL; AF086911; AAP97141.1; -; mRNA.
EMBL; AK293377; BAG56889.1; -; mRNA.
EMBL; AK295325; BAG58302.1; -; mRNA.
EMBL; AC078778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471054; EAW96774.1; -; Genomic_DNA.
EMBL; BC002849; AAH02849.1; -; mRNA.
CCDS; CCDS61137.1; -. [P61923-5]
CCDS; CCDS61138.1; -. [P61923-3]
CCDS; CCDS61139.1; -. [P61923-4]
CCDS; CCDS8877.1; -. [P61923-1]
RefSeq; NP_001258663.1; NM_001271734.1. [P61923-3]
RefSeq; NP_001258664.1; NM_001271735.1. [P61923-5]
RefSeq; NP_001258665.1; NM_001271736.1. [P61923-4]
RefSeq; NP_057141.1; NM_016057.2. [P61923-1]
UniGene; Hs.505652; -.
PDB; 2HF6; NMR; -; A=1-149.
PDB; 5MC7; X-ray; 1.60 A; A/B=7-150.
PDBsum; 2HF6; -.
PDBsum; 5MC7; -.
ProteinModelPortal; P61923; -.
SMR; P61923; -.
BioGrid; 116495; 49.
DIP; DIP-29873N; -.
IntAct; P61923; 22.
STRING; 9606.ENSP00000262061; -.
iPTMnet; P61923; -.
PhosphoSitePlus; P61923; -.
DMDM; 48428830; -.
EPD; P61923; -.
MaxQB; P61923; -.
PaxDb; P61923; -.
PeptideAtlas; P61923; -.
PRIDE; P61923; -.
ProteomicsDB; 57338; -.
TopDownProteomics; P61923-1; -. [P61923-1]
DNASU; 22818; -.
Ensembl; ENST00000262061; ENSP00000262061; ENSG00000111481. [P61923-1]
Ensembl; ENST00000455864; ENSP00000410620; ENSG00000111481. [P61923-3]
Ensembl; ENST00000549043; ENSP00000449270; ENSG00000111481. [P61923-4]
Ensembl; ENST00000552362; ENSP00000448444; ENSG00000111481. [P61923-5]
GeneID; 22818; -.
KEGG; hsa:22818; -.
UCSC; uc001sfs.3; human. [P61923-1]
CTD; 22818; -.
DisGeNET; 22818; -.
EuPathDB; HostDB:ENSG00000111481.9; -.
GeneCards; COPZ1; -.
HGNC; HGNC:2243; COPZ1.
MIM; 615472; gene.
neXtProt; NX_P61923; -.
OpenTargets; ENSG00000111481; -.
PharmGKB; PA26760; -.
eggNOG; KOG3343; Eukaryota.
eggNOG; COG5541; LUCA.
GeneTree; ENSGT00390000004405; -.
HOGENOM; HOG000214428; -.
HOVERGEN; HBG051077; -.
InParanoid; P61923; -.
KO; K20472; -.
PhylomeDB; P61923; -.
TreeFam; TF300262; -.
Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
ChiTaRS; COPZ1; human.
EvolutionaryTrace; P61923; -.
GeneWiki; COPZ1; -.
GenomeRNAi; 22818; -.
PRO; PR:P61923; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000111481; -.
CleanEx; HS_COPZ1; -.
ExpressionAtlas; P61923; baseline and differential.
Genevisible; P61923; HS.
GO; GO:0030126; C:COPI vesicle coat; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0030133; C:transport vesicle; TAS:Reactome.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:Reactome.
GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; IDA:UniProtKB.
GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; TAS:UniProtKB.
GO; GO:1901998; P:toxin transport; IEA:Ensembl.
InterPro; IPR022775; AP_mu_sigma_su.
InterPro; IPR000804; Clathrin_sm-chain_CS.
InterPro; IPR011012; Longin-like_dom_sf.
Pfam; PF01217; Clat_adaptor_s; 1.
SUPFAM; SSF64356; SSF64356; 1.
PROSITE; PS00989; CLAT_ADAPTOR_S; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing;
ER-Golgi transport; Golgi apparatus; Membrane; Protein transport;
Reference proteome; Transport.
CHAIN 1 177 Coatomer subunit zeta-1.
/FTId=PRO_0000193825.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000269|Ref.9}.
VAR_SEQ 1 36 MEALILEPSLYTVKAILILDNDGDRLFAKYYDDTYP -> M
MEIDFLPSTMTTPTPVSRSKRPLRRTFSTRPIGLT (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_053675.
VAR_SEQ 1 6 MEALIL -> MGGFRTEGMFVSLQ (in isoform 4).
{ECO:0000305}.
/FTId=VSP_055049.
VAR_SEQ 7 29 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055050.
VAR_SEQ 37 87 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_053676.
VAR_SEQ 147 163 Missing (in isoform 5). {ECO:0000305}.
/FTId=VSP_055051.
MUTAGEN 58 59 EI->KA: Reduced interaction with gamma
subunit. {ECO:0000269|PubMed:19167404}.
MUTAGEN 87 88 EL->KA: Reduced interaction with gamma
subunit. {ECO:0000269|PubMed:19167404}.
STRAND 15 20 {ECO:0000244|PDB:5MC7}.
STRAND 25 30 {ECO:0000244|PDB:5MC7}.
STRAND 32 35 {ECO:0000244|PDB:5MC7}.
HELIX 38 50 {ECO:0000244|PDB:5MC7}.
STRAND 58 62 {ECO:0000244|PDB:5MC7}.
STRAND 65 71 {ECO:0000244|PDB:5MC7}.
STRAND 73 82 {ECO:0000244|PDB:5MC7}.
HELIX 87 104 {ECO:0000244|PDB:5MC7}.
TURN 105 107 {ECO:0000244|PDB:5MC7}.
HELIX 111 115 {ECO:0000244|PDB:5MC7}.
HELIX 118 128 {ECO:0000244|PDB:5MC7}.
HELIX 139 149 {ECO:0000244|PDB:5MC7}.
SEQUENCE 177 AA; 20198 MW; 355530D032D3A049 CRC64;
MEALILEPSL YTVKAILILD NDGDRLFAKY YDDTYPSVKE QKAFEKNIFN KTHRTDSEIA
LLEGLTVVYK SSIDLYFYVI GSSYENELML MAVLNCLFDS LSQMLRKNVE KRALLENMEG
LFLAVDEIVD GGVILESDPQ QVVHRVALRG EDVPLTEQTV SQVLQSAKEQ IKWSLLR


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EIAAB41784 CCT6,CCTZ,CCT-zeta,Pig,Sus scrofa,T-complex protein 1 subunit zeta,TCP-1-zeta
EIAAB41777 Bos taurus,Bovine,CCT6B,CCT-zeta-2,T-complex protein 1 subunit zeta-2,TCP-1-zeta-2
EIAAB41783 Acute morphine dependence-related protein 2,CCT6,CCT6A,CCTZ,CCT-zeta-1,Homo sapiens,HTR3,Human,T-complex protein 1 subunit zeta,TCP-1-zeta,Tcp20
EIAAB31476 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase zeta-1,Homo sapiens,Human,Phosphoinositide phospholipase C-zeta-1,Phospholipase C-zeta-1,PLCZ1,PLC-zeta-1,Testis-development protein NYD-SP27
EIAAB41781 CCT6,CCT-zeta,Chicken,Gallus gallus,RCJMB04_20k5,T-complex protein 1 subunit zeta,TCP-1-zeta
EIAAB31479 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase zeta-1,Bos taurus,Bovine,Phosphoinositide phospholipase C-zeta-1,Phospholipase C-zeta-1,PLCZ,PLCZ1,PLC-zeta-1
EIAAB31475 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase zeta-1,Phosphoinositide phospholipase C-zeta-1,Phospholipase C-zeta-1,Plcz1,PLC-zeta-1,Rat,Rattus norvegicus
EIAAB31478 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase zeta-1,Mouse,Mus musculus,Phosphoinositide phospholipase C-zeta-1,Phospholipase C-zeta-1,Plcz1,PLC-zeta-1
EIAAB31474 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase zeta-1,Phosphoinositide phospholipase C-zeta-1,Phospholipase C-zeta-1,Pig,PLCZ,PLC-zeta-1,Sus scrofa
EIAAB11076 DAG kinase zeta,DAGK6,DGKZ,DGK-zeta,Diacylglycerol kinase zeta,Diglyceride kinase zeta,Homo sapiens,Human
EIAAB31477 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase zeta-1,Chicken,Gallus gallus,Phosphoinositide phospholipase C-zeta-1,Phospholipase C-zeta-1,PLCZ1,PLC-zeta-1
EIAAB11077 DAG kinase zeta,Dgkz,DGK-zeta,Diacylglycerol kinase zeta,Diglyceride kinase zeta,Mouse,Mus musculus
EIAAB32722 Homo sapiens,Human,Macropain zeta chain,Multicatalytic endopeptidase complex zeta chain,Proteasome subunit alpha type-5,Proteasome zeta chain,PSMA5
EIAAB32721 Macropain zeta chain,Mouse,Multicatalytic endopeptidase complex zeta chain,Mus musculus,Proteasome subunit alpha type-5,Proteasome zeta chain,Psma5
EIAAB32720 Macropain zeta chain,Multicatalytic endopeptidase complex zeta chain,Proteasome subunit alpha type-5,Proteasome zeta chain,Psma5,Rat,Rattus norvegicus


 

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