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26S proteasome non-ATPase regulatory subunit 7 (26S proteasome regulatory subunit RPN8) (26S proteasome regulatory subunit S12) (Mov34 protein homolog) (Proteasome subunit p40)

 PSMD7_HUMAN             Reviewed;         324 AA.
P51665; D3DWS9; Q6PKI2; Q96E97;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
10-MAY-2002, sequence version 2.
25-OCT-2017, entry version 169.
RecName: Full=26S proteasome non-ATPase regulatory subunit 7;
AltName: Full=26S proteasome regulatory subunit RPN8;
AltName: Full=26S proteasome regulatory subunit S12;
AltName: Full=Mov34 protein homolog;
AltName: Full=Proteasome subunit p40;
Name=PSMD7; Synonyms=MOV34L;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7755639; DOI=10.1006/bbrc.1995.1701;
Tsurumi C., DeMartino G.N., Slaughter C., Shimbara N., Tanaka K.;
"cDNA cloning of p40, a regulatory subunit of the human 26S
proteasome, and a homolog of the Mov-34 gene product.";
Biochem. Biophys. Res. Commun. 210:600-608(1995).
[2]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, and Skin;
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).
[4]
FUNCTION.
PubMed=1317798; DOI=10.1111/j.1432-1033.1992.tb16961.x;
Kanayama H.O., Tamura T., Ugai S., Kagawa S., Tanahashi N.,
Yoshimura T., Tanaka K., Ichihara A.;
"Demonstration that a human 26S proteolytic complex consists of a
proteasome and multiple associated protein components and hydrolyzes
ATP and ubiquitin-ligated proteins by closely linked mechanisms.";
Eur. J. Biochem. 206:567-578(1992).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17323924; DOI=10.1021/bi061994u;
Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
"Mass spectrometric characterization of the affinity-purified human
26S proteasome complex.";
Biochemistry 46:3553-3565(2007).
[6]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-204 AND LYS-214, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[7]
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).
[8]
INTERACTION WITH TRIM5.
PubMed=22078707; DOI=10.1186/1742-4690-8-93;
Lukic Z., Hausmann S., Sebastian S., Rucci J., Sastri J., Robia S.L.,
Luban J., Campbell E.M.;
"TRIM5alpha associates with proteasomal subunits in cells while in
complex with HIV-1 virions.";
Retrovirology 8:93-93(2011).
[9]
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).
[10]
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).
[11]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1-186, AND LACK OF
METAL-BINDING.
PubMed=17559875; DOI=10.1016/j.jmb.2007.04.084;
Sanches M., Alves B.S.C., Zanchin N.I.T., Guimaraes B.G.;
"The crystal structure of the human Mov34 MPN domain reveals a metal-
free dimer.";
J. Mol. Biol. 370:846-855(2007).
[12]
STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) OF 1-389, AND
SUBUNIT.
PubMed=27428775; DOI=10.1038/nsmb.3273;
Huang X., Luan B., Wu J., Shi Y.;
"An atomic structure of the human 26S proteasome.";
Nat. Struct. Mol. Biol. 23:778-785(2016).
[13]
STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS) OF 1-389, AND
SUBUNIT.
PubMed=27342858; DOI=10.1073/pnas.1608050113;
Schweitzer A., Aufderheide A., Rudack T., Beck F., Pfeifer G.,
Plitzko J.M., Sakata E., Schulten K., Foerster F., Baumeister W.;
"Structure of the human 26S proteasome at a resolution of 3.9 Aa.";
Proc. Natl. Acad. Sci. U.S.A. 113:7816-7821(2016).
-!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
involved in the ATP-dependent degradation of ubiquitinated
proteins. This complex plays a key role in the maintenance of
protein homeostasis by removing misfolded or damaged proteins,
which could impair cellular functions, and by removing proteins
whose functions are no longer required. Therefore, the proteasome
participates in numerous cellular processes, including cell cycle
progression, apoptosis, or DNA damage repair.
{ECO:0000269|PubMed:1317798}.
-!- SUBUNIT: Component of the 19S proteasome regulatory particle
complex. The 26S proteasome consists of a 20S core particle (CP)
and two 19S regulatory subunits (RP). The regulatory particle is
made of a lid composed of 9 subunits including PSMD7, a base
containing 6 ATPases and few additional components
(PubMed:27428775, PubMed:27342858). Within the complex, PSMD7
interacts with subunit PSMD4 through their respective MPN domain.
Interacts with TRIM5 (PubMed:22078707).
{ECO:0000269|PubMed:22078707, ECO:0000269|PubMed:27342858,
ECO:0000269|PubMed:27428775}.
-!- INTERACTION:
O00487:PSMD14; NbExp=8; IntAct=EBI-357659, EBI-722193;
-!- MISCELLANEOUS: Does not bind a metal ion.
-!- SIMILARITY: Belongs to the peptidase M67A family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH00338.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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EMBL; D50063; BAA08780.1; -; mRNA.
EMBL; CH471166; EAW59162.1; -; Genomic_DNA.
EMBL; CH471166; EAW59163.1; -; Genomic_DNA.
EMBL; BC000338; AAH00338.1; ALT_SEQ; mRNA.
EMBL; BC012606; AAH12606.1; -; mRNA.
CCDS; CCDS10910.1; -.
PIR; JC4154; JC4154.
PIR; S65491; S65491.
RefSeq; NP_002802.2; NM_002811.4.
UniGene; Hs.440604; -.
PDB; 2O95; X-ray; 1.95 A; A/B=1-186.
PDB; 2O96; X-ray; 3.00 A; A/B=1-177.
PDB; 5GJQ; EM; 4.50 A; U=1-324.
PDB; 5GJR; EM; 3.50 A; 8/U=1-324.
PDB; 5L4K; EM; 4.50 A; U=1-324.
PDB; 5LN3; EM; 6.80 A; U=1-324.
PDB; 5M32; EM; 3.80 A; n=1-324.
PDB; 5T0C; EM; 3.80 A; AZ/BZ=1-324.
PDB; 5T0G; EM; 4.40 A; Z=1-324.
PDB; 5T0H; EM; 6.80 A; Z=1-324.
PDB; 5T0I; EM; 8.00 A; Z=1-324.
PDB; 5T0J; EM; 8.00 A; Z=1-324.
PDB; 5VGZ; EM; 3.70 A; Z=5-290.
PDB; 5VHF; EM; 5.70 A; Z=5-290.
PDB; 5VHH; EM; 6.10 A; Z=5-290.
PDB; 5VHI; EM; 6.80 A; Z=5-290.
PDB; 5VHS; EM; 8.80 A; Z=5-290.
PDBsum; 2O95; -.
PDBsum; 2O96; -.
PDBsum; 5GJQ; -.
PDBsum; 5GJR; -.
PDBsum; 5L4K; -.
PDBsum; 5LN3; -.
PDBsum; 5M32; -.
PDBsum; 5T0C; -.
PDBsum; 5T0G; -.
PDBsum; 5T0H; -.
PDBsum; 5T0I; -.
PDBsum; 5T0J; -.
PDBsum; 5VGZ; -.
PDBsum; 5VHF; -.
PDBsum; 5VHH; -.
PDBsum; 5VHI; -.
PDBsum; 5VHS; -.
ProteinModelPortal; P51665; -.
SMR; P51665; -.
BioGrid; 111685; 118.
CORUM; P51665; -.
DIP; DIP-27572N; -.
IntAct; P51665; 52.
MINT; MINT-5002613; -.
STRING; 9606.ENSP00000219313; -.
ChEMBL; CHEMBL2364701; -.
MEROPS; M67.973; -.
iPTMnet; P51665; -.
PhosphoSitePlus; P51665; -.
BioMuta; PSMD7; -.
DMDM; 20532412; -.
EPD; P51665; -.
MaxQB; P51665; -.
PaxDb; P51665; -.
PeptideAtlas; P51665; -.
PRIDE; P51665; -.
DNASU; 5713; -.
Ensembl; ENST00000219313; ENSP00000219313; ENSG00000103035.
GeneID; 5713; -.
KEGG; hsa:5713; -.
UCSC; uc002fcq.3; human.
CTD; 5713; -.
DisGeNET; 5713; -.
EuPathDB; HostDB:ENSG00000103035.10; -.
GeneCards; PSMD7; -.
HGNC; HGNC:9565; PSMD7.
HPA; CAB019379; -.
HPA; HPA049824; -.
HPA; HPA056069; -.
MIM; 157970; gene.
neXtProt; NX_P51665; -.
OpenTargets; ENSG00000103035; -.
PharmGKB; PA33911; -.
eggNOG; KOG1556; Eukaryota.
eggNOG; COG1310; LUCA.
GeneTree; ENSGT00530000063075; -.
HOGENOM; HOG000209236; -.
HOVERGEN; HBG035951; -.
InParanoid; P51665; -.
KO; K03038; -.
OMA; DAYFAVE; -.
OrthoDB; EOG091G0DX6; -.
PhylomeDB; P51665; -.
Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
Reactome; R-HSA-446652; Interleukin-1 family signaling.
Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
Reactome; R-HSA-4641257; Degradation of AXIN.
Reactome; R-HSA-4641258; Degradation of DVL.
Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
Reactome; R-HSA-5362768; Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-HSA-5632684; Hedgehog 'on' state.
Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-68827; CDT1 association with the CDC6:ORC:origin complex.
Reactome; R-HSA-68949; Orc1 removal from chromatin.
Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-HSA-69229; Ubiquitin-dependent degradation of Cyclin D1.
Reactome; R-HSA-69481; G2/M Checkpoints.
Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
ChiTaRS; PSMD7; human.
EvolutionaryTrace; P51665; -.
GeneWiki; PSMD7; -.
GenomeRNAi; 5713; -.
PRO; PR:P51665; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000103035; -.
CleanEx; HS_PSMD7; -.
ExpressionAtlas; P51665; baseline and differential.
Genevisible; P51665; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
GO; GO:0005838; C:proteasome regulatory particle; TAS:ProtInc.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition; TAS:Reactome.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
CDD; cd08062; MPN_RPN7_8; 1.
InterPro; IPR000555; JAMM/MPN+_dom.
InterPro; IPR033858; MPN_RPN7_8.
InterPro; IPR024969; Rpn11/EIF3F_C.
PANTHER; PTHR10540:SF7; PTHR10540:SF7; 1.
Pfam; PF01398; JAB; 1.
Pfam; PF13012; MitMem_reg; 1.
SMART; SM00232; JAB_MPN; 1.
PROSITE; PS50249; MPN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Isopeptide bond;
Proteasome; Reference proteome; Ubl conjugation.
CHAIN 1 324 26S proteasome non-ATPase regulatory
subunit 7.
/FTId=PRO_0000213943.
DOMAIN 9 144 MPN. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
COMPBIAS 286 324 Glu/Lys-rich.
MOD_RES 204 204 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 214 214 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 316 316 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26516}.
MOD_RES 317 317 N6-acetyllysine.
{ECO:0000250|UniProtKB:P26516}.
CROSSLNK 180 180 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
CONFLICT 27 27 G -> V (in Ref. 1; BAA08780).
{ECO:0000305}.
CONFLICT 144 145 VH -> DQ (in Ref. 1; BAA08780).
{ECO:0000305}.
CONFLICT 216 216 A -> G (in Ref. 1; BAA08780).
{ECO:0000305}.
STRAND 7 11 {ECO:0000244|PDB:2O95}.
HELIX 13 28 {ECO:0000244|PDB:2O95}.
STRAND 36 56 {ECO:0000244|PDB:2O95}.
STRAND 58 60 {ECO:0000244|PDB:2O95}.
STRAND 67 70 {ECO:0000244|PDB:2O95}.
HELIX 72 83 {ECO:0000244|PDB:2O95}.
STRAND 86 88 {ECO:0000244|PDB:2O95}.
STRAND 90 96 {ECO:0000244|PDB:2O95}.
HELIX 105 112 {ECO:0000244|PDB:2O95}.
TURN 113 115 {ECO:0000244|PDB:2O95}.
STRAND 120 124 {ECO:0000244|PDB:2O95}.
STRAND 134 143 {ECO:0000244|PDB:2O95}.
STRAND 152 162 {ECO:0000244|PDB:2O95}.
HELIX 166 178 {ECO:0000244|PDB:2O95}.
SEQUENCE 324 AA; 37025 MW; 3F7B343996B102B7 CRC64;
MPELAVQKVV VHPLVLLSVV DHFNRIGKVG NQKRVVGVLL GSWQKKVLDV SNSFAVPFDE
DDKDDSVWFL DHDYLENMYG MFKKVNARER IVGWYHTGPK LHKNDIAINE LMKRYCPNSV
LVIIDVKPKD LGLPTEAYIS VEEVHDDGTP TSKTFEHVTS EIGAEEAEEV GVEHLLRDIK
DTTVGTLSQR ITNQVHGLKG LNSKLLDIRS YLEKVATGKL PINHQIIYQL QDVFNLLPDV
SLQEFVKAFY LKTNDQMVVV YLASLIRSVV ALHNLINNKI ANRDAEKKEG QEKEESKKDR
KEDKEKDKDK EKSDVKKEEK KEKK


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EIAAB32789 26S proteasome non-ATPase regulatory subunit 11,26S proteasome regulatory subunit p44.5,26S proteasome regulatory subunit RPN6,26S proteasome regulatory subunit S9,Homo sapiens,Human,PSMD11
EIAAB32858 26S proteasome non-ATPase regulatory subunit 6,26S proteasome regulatory subunit RPN7,26S proteasome regulatory subunit S10,Breast cancer-associated protein SGA-113M,Homo sapiens,Human,KIAA0107,p42A,P
EIAAB32852 26S proteasome non-ATPase regulatory subunit 4,26S proteasome regulatory subunit RPN10,26S proteasome regulatory subunit S5A,Mcb1,Mouse,Multiubiquitin chain-binding protein,Mus musculus,Psmd4
EIAAB32841 26S proteasome non-ATPase regulatory subunit 1,26S proteasome regulatory subunit RPN2,26S proteasome regulatory subunit S1,26S proteasome subunit p112,Psmd1,Rat,Rattus norvegicus
EIAAB32848 26S proteasome non-ATPase regulatory subunit 3,26S proteasome regulatory subunit RPN3,26S proteasome regulatory subunit S3,Homo sapiens,Human,Proteasome subunit p58,PSMD3
EIAAB32797 26S proteasome non-ATPase regulatory subunit 13,26S proteasome regulatory subunit p40.5,26S proteasome regulatory subunit RPN9,26S proteasome regulatory subunit S11,Mouse,Mus musculus,Psmd13
EIAAB32796 26S proteasome non-ATPase regulatory subunit 13,26S proteasome regulatory subunit p40.5,26S proteasome regulatory subunit RPN9,26S proteasome regulatory subunit S11,Psmd13,Rat,Rattus norvegicus
EIAAB32799 26S proteasome non-ATPase regulatory subunit 13,26S proteasome regulatory subunit p40.5,26S proteasome regulatory subunit RPN9,26S proteasome regulatory subunit S11,Bos taurus,Bovine,PSMD13
EIAAB32791 26S proteasome non-ATPase regulatory subunit 11,26S proteasome regulatory subunit p44.5,26S proteasome regulatory subunit RPN6,26S proteasome regulatory subunit S9,Mouse,Mus musculus,Psmd11
EIAAB32851 26S proteasome non-ATPase regulatory subunit 4,26S proteasome regulatory subunit RPN10,26S proteasome regulatory subunit S5A,AF,Antisecretory factor 1,ASF,Homo sapiens,Human,MCB1,Multiubiquitin chain-
EIAAB32844 26S proteasome non-ATPase regulatory subunit 2,26S proteasome regulatory subunit RPN1,26S proteasome regulatory subunit S2,26S proteasome subunit p97,Mouse,Mus musculus,Psmd2
EIAAB32669 26S protease regulatory subunit 8,26S proteasome AAA-ATPase subunit RPT6,p45_SUG,Pig,Proteasome 26S subunit ATPase 5,Proteasome subunit p45,PSMC5,Sus scrofa,Tat-binding protein homolog 10,TBP10
EIAAB32809 26S proteasome non-ATPase regulatory subunit 14,26S proteasome regulatory subunit RPN11,26S proteasome-associated PAD1 homolog 1,Homo sapiens,Human,POH1,PSMD14
EIAAB32793 26S proteasome non-ATPase regulatory subunit 12,26S proteasome regulatory subunit p55,26S proteasome regulatory subunit RPN5,Homo sapiens,Human,PSMD12
EIAAB32859 26S proteasome non-ATPase regulatory subunit 6,26S proteasome regulatory subunit RPN7,26S proteasome regulatory subunit S10,Mouse,Mus musculus,p42A,Psmd6
EIAAB32862 26S proteasome non-ATPase regulatory subunit 8,26S proteasome regulatory subunit RPN12,26S proteasome regulatory subunit S14,Homo sapiens,Human,p31,PSMD8
15-288-22830 26S proteasome non-ATPase regulatory subunit 1 - 26S proteasome regulatory subunit RPN2; 26S proteasome regulatory subunit S1; 26S proteasome subunit p112 Polyclonal 0.05 mg
15-288-22830 26S proteasome non-ATPase regulatory subunit 1 - 26S proteasome regulatory subunit RPN2; 26S proteasome regulatory subunit S1; 26S proteasome subunit p112 Polyclonal 0.1 mg


 

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