Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

26S proteasome non-ATPase regulatory subunit 4 (26S proteasome regulatory subunit RPN10) (26S proteasome regulatory subunit S5A) (Antisecretory factor 1) (AF) (ASF) (Multiubiquitin chain-binding protein)

 PSMD4_HUMAN             Reviewed;         377 AA.
P55036; D3DV16; Q5VWC5; Q9NS92;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-OCT-2017, entry version 183.
RecName: Full=26S proteasome non-ATPase regulatory subunit 4;
AltName: Full=26S proteasome regulatory subunit RPN10;
AltName: Full=26S proteasome regulatory subunit S5A;
AltName: Full=Antisecretory factor 1;
Short=AF;
Short=ASF;
AltName: Full=Multiubiquitin chain-binding protein;
Name=PSMD4; Synonyms=MCB1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 63-75 AND 130-140.
TISSUE=Pituitary;
PubMed=7657640; DOI=10.1074/jbc.270.35.20615;
Johansson E., Loennroth I., Lange S., Jonson I., Jennische E.,
Loennroth C.;
"Molecular cloning and expression of a pituitary gland protein
modulating intestinal fluid secretion.";
J. Biol. Chem. 270:20615-20620(1995).
[2]
SEQUENCE REVISION.
Loennroth I.;
Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=8641424; DOI=10.1016/0014-5793(96)00101-9;
Ferrell K., Deveraux Q., van Nocker S., Rechsteiner M.;
"Molecular cloning and expression of a multiubiquitin chain binding
subunit of the human 26S protease.";
FEBS Lett. 381:143-148(1996).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
TISSUE=Fetal brain;
PubMed=10921894; DOI=10.1093/emboj/19.15.4144;
Kawahara H., Kasahara M., Nishiyama A., Ohsumi K., Goto T.,
Kishimoto T., Saeki Y., Yokosawa H., Shimbara N., Murata S., Chiba T.,
Suzuki K., Tanaka K.;
"Developmentally regulated, alternative splicing of the Rpn10 gene
generates multiple forms of 26S proteasomes.";
EMBO J. 19:4144-4153(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
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.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver, and Lung;
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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 70-377.
TISSUE=Brain;
Fraser P.E., Levesque G., Rogaeva E.A., Yu G., St George-Hyslop P.H.;
"Proteolysis of presenilin 1 is associated with the 26S proteasome and
is altered in Alzheimer's disease.";
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
[9]
CHARACTERIZATION.
PubMed=3524692;
Loennroth I., Lange S.;
"Purification and characterization of the antisecretory factor: a
protein in the central nervous system and in the gut which inhibits
intestinal hypersecretion induced by cholera toxin.";
Biochim. Biophys. Acta 883:138-144(1986).
[10]
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).
[11]
POLYUBIQUITIN BINDING SITES.
PubMed=9488668; DOI=10.1074/jbc.273.10.5461;
Young P., Deveraux Q., Beal R.E., Pickart C.M., Rechsteiner M.;
"Characterization of two polyubiquitin binding sites in the 26 S
protease subunit 5a.";
J. Biol. Chem. 273:5461-5467(1998).
[12]
INTERACTION WITH NUB1.
PubMed=11585840; DOI=10.1074/jbc.M108636200;
Kamitani T., Kito K., Fukuda-Kamitani T., Yeh E.T.H.;
"Targeting of NEDD8 and its conjugates for proteasomal degradation by
NUB1.";
J. Biol. Chem. 276:46655-46660(2001).
[13]
INTERACTION WITH UBQLN1.
PubMed=15147878; DOI=10.1016/j.febslet.2004.04.031;
Ko H.S., Uehara T., Tsuruma K., Nomura Y.;
"Ubiquilin interacts with ubiquitylated proteins and proteasome
through its ubiquitin-associated and ubiquitin-like domains.";
FEBS Lett. 566:110-114(2004).
[14]
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).
[15]
INTERACTION WITH UBQLN4.
PubMed=15280365; DOI=10.1074/jbc.M406284200;
Riley B.E., Xu Y., Zoghbi H.Y., Orr H.T.;
"The effects of the polyglutamine repeat protein ataxin-1 on the UbL-
UBA protein A1Up.";
J. Biol. Chem. 279:42290-42301(2004).
[16]
INTERACTION WITH SQSTM1.
PubMed=15340068; DOI=10.1128/MCB.24.18.8055-8068.2004;
Seibenhener M.L., Babu J.R., Geetha T., Wong H.C., Krishna N.R.,
Wooten M.W.;
"Sequestosome 1/p62 is a polyubiquitin chain binding protein involved
in ubiquitin proteasome degradation.";
Mol. Cell. Biol. 24:8055-8068(2004).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358 AND SER-361, AND
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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[21]
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).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[23]
INTERACTION WITH UBE3A.
PubMed=22645313; DOI=10.1128/MCB.00201-12;
Martinez-Noel G., Galligan J.T., Sowa M.E., Arndt V., Overton T.M.,
Harper J.W., Howley P.M.;
"Identification and proteomic analysis of distinct UBE3A/E6AP protein
complexes.";
Mol. Cell. Biol. 32:3095-3106(2012).
[24]
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).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266; SER-358 AND
SER-361, 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).
[26]
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).
[27]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-122, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[28]
STRUCTURE BY NMR OF 263-306 IN COMPLEX WITH HR23A UBIQUITIN-LIKE
DOMAIN.
PubMed=12970176; DOI=10.1093/emboj/cdg467;
Mueller T.D., Feigon J.;
"Structural determinants for the binding of ubiquitin-like domains to
the proteasome.";
EMBO J. 22:4634-4645(2003).
[29]
STRUCTURE BY NMR OF 260-307 IN COMPLEX WITH HR23B UBIQUITIN-LIKE
DOMAIN.
PubMed=14585839; DOI=10.1074/jbc.M309448200;
Fujiwara K., Tenno T., Sugasawa K., Jee J.-G., Ohki I., Kojima C.,
Tochio H., Hiroaki H., Hanaoka F., Shirakawa M.;
"Structure of the ubiquitin-interacting motif of S5a bound to the
ubiquitin-like domain of HR23B.";
J. Biol. Chem. 279:4760-4767(2004).
[30]
STRUCTURE BY NMR OF 192-306, FUNCTION, AND DOMAIN.
PubMed=15826667; DOI=10.1016/j.jmb.2005.03.007;
Wang Q., Young P., Walters K.J.;
"Structure of S5a bound to monoubiquitin provides a model for
polyubiquitin recognition.";
J. Mol. Biol. 348:727-739(2005).
[31]
STRUCTURE BY NMR OF 196-306, AND DOMAIN.
PubMed=19683493; DOI=10.1016/j.molcel.2009.06.010;
Zhang N., Wang Q., Ehlinger A., Randles L., Lary J.W., Kang Y.,
Haririnia A., Storaska A.J., Cole J.L., Fushman D., Walters K.J.;
"Structure of the s5a:k48-linked diubiquitin complex and its
interactions with rpn13.";
Mol. Cell 35:280-290(2009).
[32]
STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), 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).
[33]
STRUCTURE BY ELECTRON MICROSCOPY (4.50 ANGSTROMS), 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. PSMD4 acts as an
ubiquitin receptor subunit through ubiquitin-interacting motifs
and selects ubiquitin-conjugates for destruction. Displays a
preferred selectivity for longer polyubiquitin chains.
{ECO:0000269|PubMed:1317798, ECO:0000269|PubMed:15826667}.
-!- 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, a base containing 6 ATPases
and few additional components including PSMD4 (PubMed:27428775,
PubMed:27342858). Interacts with NUB1 (PubMed:11585840). Interacts
with SQSTM1 (PubMed:15340068). Interacts with UBQLN4
(PubMed:15280365). Interacts with UBE3A (PubMed:22645313).
Interacts with UBQLN1 (via ubiquitin-like domain)
(PubMed:15147878). {ECO:0000269|PubMed:11585840,
ECO:0000269|PubMed:12970176, ECO:0000269|PubMed:14585839,
ECO:0000269|PubMed:15147878, ECO:0000269|PubMed:15280365,
ECO:0000269|PubMed:15340068, ECO:0000269|PubMed:22645313,
ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-359318, EBI-359318;
Q16186:ADRM1; NbExp=4; IntAct=EBI-359318, EBI-954387;
P48510:DSK2 (xeno); NbExp=2; IntAct=EBI-359318, EBI-6174;
Q9SII8:DSK2B (xeno); NbExp=3; IntAct=EBI-359318, EBI-4433040;
P24610:Pax3 (xeno); NbExp=3; IntAct=EBI-359318, EBI-1208116;
P62191:PSMC1; NbExp=2; IntAct=EBI-359318, EBI-357598;
Q13200:PSMD2; NbExp=3; IntAct=EBI-359318, EBI-357648;
P54725:RAD23A; NbExp=5; IntAct=EBI-359318, EBI-746453;
Q84L32:RAD23A (xeno); NbExp=3; IntAct=EBI-359318, EBI-6394924;
P54727:RAD23B; NbExp=12; IntAct=EBI-359318, EBI-954531;
Q62921:Rbck1 (xeno); NbExp=3; IntAct=EBI-359318, EBI-7266339;
Q9P0W5:SCHIP1; NbExp=2; IntAct=EBI-359318, EBI-1397509;
P0CG48:UBC; NbExp=8; IntAct=EBI-359318, EBI-3390054;
Q9UMX0:UBQLN1; NbExp=6; IntAct=EBI-359318, EBI-741480;
Q9UHD9:UBQLN2; NbExp=3; IntAct=EBI-359318, EBI-947187;
Q9Y5K5:UCHL5; NbExp=5; IntAct=EBI-359318, EBI-1051183;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Additional isoforms seem to exist.;
Name=Rpn10A;
IsoId=P55036-1; Sequence=Displayed;
Name=Rpn10E;
IsoId=P55036-2; Sequence=VSP_005291, VSP_005292;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
-!- DOMAIN: The 2 UIM motifs are involved in the binding to a multi-
ubiquitin chain in a cooperative way.
{ECO:0000269|PubMed:15826667, ECO:0000269|PubMed:19683493}.
-!- SIMILARITY: Belongs to the proteasome subunit S5A family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U51007; AAC50433.1; -; mRNA.
EMBL; U24704; AAB54057.1; -; mRNA.
EMBL; AB033605; BAA97581.1; -; mRNA.
EMBL; AL391069; CAH70329.1; -; Genomic_DNA.
EMBL; AL592424; CAH70329.1; JOINED; Genomic_DNA.
EMBL; AL592424; CAI16390.1; -; Genomic_DNA.
EMBL; AL391069; CAI16390.1; JOINED; Genomic_DNA.
EMBL; CH471121; EAW53457.1; -; Genomic_DNA.
EMBL; CH471121; EAW53458.1; -; Genomic_DNA.
EMBL; BC002365; AAH02365.1; -; mRNA.
EMBL; BC072008; AAH72008.1; -; mRNA.
EMBL; U72664; AAB68598.1; -; mRNA.
CCDS; CCDS991.1; -. [P55036-1]
PIR; S63671; S63671.
RefSeq; NP_002801.1; NM_002810.2. [P55036-1]
UniGene; Hs.505059; -.
PDB; 1P9C; NMR; -; A=263-307.
PDB; 1P9D; NMR; -; S=263-307.
PDB; 1UEL; NMR; -; B=263-307.
PDB; 1YX4; NMR; -; A=196-306.
PDB; 1YX5; NMR; -; A=192-306.
PDB; 1YX6; NMR; -; A=196-306.
PDB; 2KDE; NMR; -; A=196-306.
PDB; 2KDF; NMR; -; A=196-306.
PDB; 5GJQ; EM; 4.50 A; W=1-377.
PDB; 5GJR; EM; 3.50 A; AA/W=1-377.
PDB; 5L4K; EM; 4.50 A; W=1-377.
PDB; 5LN3; EM; 6.80 A; W=1-377.
PDB; 5M32; EM; 3.80 A; p=1-377.
PDB; 5T0C; EM; 3.80 A; Ab/Bb=1-377.
PDB; 5T0G; EM; 4.40 A; b=1-377.
PDB; 5T0H; EM; 6.80 A; b=1-377.
PDB; 5T0I; EM; 8.00 A; b=1-377.
PDB; 5T0J; EM; 8.00 A; b=1-377.
PDB; 5VGZ; EM; 3.70 A; b=1-191.
PDB; 5VHF; EM; 5.70 A; b=1-191.
PDB; 5VHH; EM; 6.10 A; b=1-191.
PDB; 5VHI; EM; 6.80 A; b=1-191.
PDB; 5VHS; EM; 8.80 A; b=1-191.
PDBsum; 1P9C; -.
PDBsum; 1P9D; -.
PDBsum; 1UEL; -.
PDBsum; 1YX4; -.
PDBsum; 1YX5; -.
PDBsum; 1YX6; -.
PDBsum; 2KDE; -.
PDBsum; 2KDF; -.
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; P55036; -.
SMR; P55036; -.
BioGrid; 111683; 184.
CORUM; P55036; -.
DIP; DIP-38189N; -.
IntAct; P55036; 86.
MINT; MINT-105366; -.
STRING; 9606.ENSP00000357879; -.
ChEMBL; CHEMBL2364701; -.
iPTMnet; P55036; -.
PhosphoSitePlus; P55036; -.
BioMuta; PSMD4; -.
DMDM; 1709796; -.
EPD; P55036; -.
MaxQB; P55036; -.
PaxDb; P55036; -.
PeptideAtlas; P55036; -.
PRIDE; P55036; -.
DNASU; 5710; -.
Ensembl; ENST00000368884; ENSP00000357879; ENSG00000159352. [P55036-1]
GeneID; 5710; -.
KEGG; hsa:5710; -.
UCSC; uc001exl.4; human. [P55036-1]
CTD; 5710; -.
DisGeNET; 5710; -.
EuPathDB; HostDB:ENSG00000159352.15; -.
GeneCards; PSMD4; -.
HGNC; HGNC:9561; PSMD4.
HPA; CAB047300; -.
HPA; HPA038807; -.
HPA; HPA039252; -.
MIM; 601648; gene.
neXtProt; NX_P55036; -.
OpenTargets; ENSG00000159352; -.
PharmGKB; PA33907; -.
eggNOG; KOG2884; Eukaryota.
eggNOG; COG5148; LUCA.
GeneTree; ENSGT00530000064050; -.
HOGENOM; HOG000165630; -.
HOVERGEN; HBG000425; -.
InParanoid; P55036; -.
KO; K03029; -.
PhylomeDB; P55036; -.
TreeFam; TF106232; -.
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-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; PSMD4; human.
EvolutionaryTrace; P55036; -.
GeneWiki; PSMD4; -.
GenomeRNAi; 5710; -.
PRO; PR:P55036; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000159352; -.
CleanEx; HS_PSMD4; -.
ExpressionAtlas; P55036; baseline and differential.
Genevisible; P55036; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; 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: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:0043248; P:proteasome assembly; IBA:GO_Central.
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.
Gene3D; 3.40.50.410; -; 1.
InterPro; IPR003903; UIM_dom.
InterPro; IPR002035; VWF_A.
InterPro; IPR036465; vWFA_dom_sf.
Pfam; PF02809; UIM; 2.
Pfam; PF13519; VWA_2; 1.
SMART; SM00726; UIM; 2.
SMART; SM00327; VWA; 1.
SUPFAM; SSF53300; SSF53300; 1.
PROSITE; PS50330; UIM; 2.
PROSITE; PS50234; VWFA; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Direct protein sequencing; Isopeptide bond; Phosphoprotein;
Proteasome; Reference proteome; Repeat; Ubl conjugation.
CHAIN 1 377 26S proteasome non-ATPase regulatory
subunit 4.
/FTId=PRO_0000173828.
DOMAIN 5 188 VWFA. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
DOMAIN 211 230 UIM 1. {ECO:0000255|PROSITE-
ProRule:PRU00213}.
DOMAIN 282 301 UIM 2. {ECO:0000255|PROSITE-
ProRule:PRU00213}.
REGION 197 262 Interaction with UBQLN1.
{ECO:0000269|PubMed:15147878}.
REGION 216 220 Essential for ubiquitin-binding.
REGION 287 291 Essential for ubiquitin-binding.
COMPBIAS 238 246 Poly-Ala.
MOD_RES 250 250 Phosphothreonine.
{ECO:0000250|UniProtKB:O35226}.
MOD_RES 253 253 Phosphothreonine.
{ECO:0000250|UniProtKB:O35226}.
MOD_RES 256 256 Phosphoserine.
{ECO:0000250|UniProtKB:O35226}.
MOD_RES 266 266 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 358 358 Phosphoserine.
{ECO:0000244|PubMed:17323924,
ECO:0000244|PubMed:23186163}.
MOD_RES 361 361 Phosphoserine.
{ECO:0000244|PubMed:17323924,
ECO:0000244|PubMed:23186163}.
CROSSLNK 122 122 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 255 268 DSDDALLKMTISQQ -> GERGGIRSPGTAGC (in
isoform Rpn10E). {ECO:0000305}.
/FTId=VSP_005291.
VAR_SEQ 269 377 Missing (in isoform Rpn10E).
{ECO:0000305}.
/FTId=VSP_005292.
STRAND 201 203 {ECO:0000244|PDB:1YX4}.
STRAND 205 208 {ECO:0000244|PDB:2KDE}.
HELIX 210 212 {ECO:0000244|PDB:1YX4}.
HELIX 214 244 {ECO:0000244|PDB:1YX4}.
STRAND 245 249 {ECO:0000244|PDB:1YX4}.
STRAND 268 270 {ECO:0000244|PDB:1P9C}.
STRAND 273 275 {ECO:0000244|PDB:1P9C}.
HELIX 278 294 {ECO:0000244|PDB:1P9C}.
STRAND 296 300 {ECO:0000244|PDB:1P9C}.
STRAND 302 304 {ECO:0000244|PDB:2KDE}.
SEQUENCE 377 AA; 40737 MW; EC712EC4DB1CE9AB CRC64;
MVLESTMVCV DNSEYMRNGD FLPTRLQAQQ DAVNIVCHSK TRSNPENNVG LITLANDCEV
LTTLTPDTGR ILSKLHTVQP KGKITFCTGI RVAHLALKHR QGKNHKMRII AFVGSPVEDN
EKDLVKLAKR LKKEKVNVDI INFGEEEVNT EKLTAFVNTL NGKDGTGSHL VTVPPGPSLA
DALISSPILA GEGGAMLGLG ASDFEFGVDP SADPELALAL RVSMEEQRQR QEEEARRAAA
ASAAEAGIAT TGTEDSDDAL LKMTISQQEF GRTGLPDLSS MTEEEQIAYA MQMSLQGAEF
GQAESADIDA SSAMDTSEPA KEEDDYDVMQ DPEFLQSVLE NLPGVDPNNE AIRNAMGSLA
SQATKDGKKD KKEEDKK


Related products :

Catalog number Product name Quantity
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-
18-003-42186 26S proteasome non-ATPase regulatory subunit 4 - 26S proteasome regulatory subunit S5A; Rpn10; Multiubiquitin chain-binding protein; Antisecretory factor 1; AF; ASF Polyclonal 0.05 mg Aff Pur
18-003-42187 26S proteasome non-ATPase regulatory subunit 4 - 26S proteasome regulatory subunit S5A; Rpn10; Multiubiquitin chain-binding protein; Antisecretory factor 1; AF; ASF Polyclonal 0.1 mg Protein A
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
EIAAB32808 26S proteasome non-ATPase regulatory subunit 7,26S proteasome regulatory subunit RPN8,26S proteasome regulatory subunit S12,Homo sapiens,Human,Mov34 protein homolog,MOV34L,Proteasome subunit p40,PSMD7
EIAAB32846 26S proteasome non-ATPase regulatory subunit 2,26S proteasome regulatory subunit RPN1,26S proteasome regulatory subunit S2,26S proteasome subunit p97,Homo sapiens,Human,Protein 55.11,PSMD2,TRAP2,Tumor
EIAAB32847 26S proteasome non-ATPase regulatory subunit 2,26S proteasome regulatory subunit RPN1,26S proteasome regulatory subunit S2,26S proteasome subunit p97,Bos taurus,Bovine,PSMD2,TRAP2,Tumor necrosis facto
EIAAB32850 26S proteasome non-ATPase regulatory subunit 3,26S proteasome regulatory subunit RPN3,26S proteasome regulatory subunit S3,Mouse,Mus musculus,P91a,Proteasome subunit p58,Psmd3,Transplantation antigen
EIAAB32798 26S proteasome non-ATPase regulatory subunit 13,26S proteasome regulatory subunit p40.5,26S proteasome regulatory subunit RPN9,26S proteasome regulatory subunit S11,Homo sapiens,Human,PSMD13
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
EIAAB32842 26S proteasome non-ATPase regulatory subunit 1,26S proteasome regulatory subunit RPN2,26S proteasome regulatory subunit S1,26S proteasome subunit p112,Homo sapiens,Human,PSMD1
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
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
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
EIAAB32807 26S proteasome non-ATPase regulatory subunit 7,26S proteasome regulatory subunit RPN8,26S proteasome regulatory subunit S12,Mouse,Mov34,Mov-34,Mov34 protein,Mus musculus,Proteasome subunit p40,Psmd7
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
EIAAB32793 26S proteasome non-ATPase regulatory subunit 12,26S proteasome regulatory subunit p55,26S proteasome regulatory subunit RPN5,Homo sapiens,Human,PSMD12
EIAAB32862 26S proteasome non-ATPase regulatory subunit 8,26S proteasome regulatory subunit RPN12,26S proteasome regulatory subunit S14,Homo sapiens,Human,p31,PSMD8
EIAAB32859 26S proteasome non-ATPase regulatory subunit 6,26S proteasome regulatory subunit RPN7,26S proteasome regulatory subunit S10,Mouse,Mus musculus,p42A,Psmd6
EIAAB32853 26S proteasome non-ATPase regulatory subunit 4,26S proteasome regulatory subunit RPN10,Bos taurus,Bovine,PSMD4
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


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur