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 10 (26S proteasome regulatory subunit p28) (Gankyrin) (p28(GANK))

 PSD10_HUMAN             Reviewed;         226 AA.
O75832; Q5U0B2; Q8IZK9;
10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
25-OCT-2017, entry version 178.
RecName: Full=26S proteasome non-ATPase regulatory subunit 10;
AltName: Full=26S proteasome regulatory subunit p28;
AltName: Full=Gankyrin;
AltName: Full=p28(GANK);
Name=PSMD10;
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=9714768; DOI=10.1016/S0378-1119(98)00309-6;
Hori T., Kato S., Saeki M., DeMartino G.N., Slaughter C.A.,
Takeuchi J., Toh-e A., Tanaka K.;
"cDNA cloning and functional analysis of p28 (Nas6p) and p40.5
(Nas7p), two novel regulatory subunits of the 26S proteasome.";
Gene 216:113-122(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
Higashitsuji H., Fujita J.;
"Enhanced expression of a novel tumour marker in the human
hepatomas.";
Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Liver;
Wang H., Fu X., Wu M.;
"Involvement of p28-II in hepatocellular carcinoma.";
Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Subthalamic nucleus;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=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]
FUNCTION AS POTENTIAL PROTO-ONCOGENE, INTERACTION WITH RB1, TISSUE
SPECIFICITY, AND MUTAGENESIS OF GLU-182.
PubMed=10613832; DOI=10.1038/71600;
Higashitsuji H., Itoh K., Nagao T., Dawson S., Nonoguchi K., Kido T.,
Mayer R.J., Arii S., Fujita J.;
"Reduced stability of retinoblastoma protein by gankyrin, an oncogenic
ankyrin-repeat protein overexpressed in hepatomas.";
Nat. Med. 6:96-99(2000).
[9]
FUNCTION, AND INTERACTION WITH CDK4.
PubMed=11900540; DOI=10.1021/bi011550s;
Li J., Tsai M.D.;
"Novel insights into the INK4-CDK4/6-Rb pathway: counter action of
gankyrin against INK4 proteins regulates the CDK4-mediated
phosphorylation of Rb.";
Biochemistry 41:3977-3983(2002).
[10]
FUNCTION, AND INTERACTION WITH PSMC4.
PubMed=11779854; DOI=10.1074/jbc.M107313200;
Dawson S., Apcher S., Mee M., Higashitsuji H., Baker R., Uhle S.,
Dubiel W., Fujita J., Mayer R.J.;
"Gankyrin is an ankyrin-repeat oncoprotein that interacts with CDK4
kinase and the S6 ATPase of the 26 S proteasome.";
J. Biol. Chem. 277:10893-10902(2002).
[11]
FUNCTION IN DEGRADATION OF TP53, AND INTERACTION WITH MDM2.
PubMed=16023600; DOI=10.1016/j.ccr.2005.06.006;
Higashitsuji H., Higashitsuji H., Itoh K., Sakurai T., Nagao T.,
Sumitomo Y., Masuda T., Dawson S., Shimada Y., Mayer R.J., Fujita J.;
"The oncoprotein gankyrin binds to MDM2/HDM2, enhancing ubiquitylation
and degradation of p53.";
Cancer Cell 8:75-87(2005).
[12]
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).
[13]
FUNCTION IN REGULATION OF NF-KAPPA-B, INTERACTION WITH RELY, AND
SUBCELLULAR LOCATION.
PubMed=18040287; DOI=10.1038/cr.2007.99;
Chen Y., Li H.H., Fu J., Wang X.F., Ren Y.B., Dong L.W., Tang S.H.,
Liu S.Q., Wu M.C., Wang H.Y.;
"Oncoprotein p28 GANK binds to RelA and retains NF-kappaB in the
cytoplasm through nuclear export.";
Cell Res. 17:1020-1029(2007).
[14]
FUNCTION AS PROTEASOME CHAPERONE, AND SUBUNIT.
PubMed=19490896; DOI=10.1016/j.cell.2009.05.008;
Kaneko T., Hamazaki J., Iemura S., Sasaki K., Furuyama K., Natsume T.,
Tanaka K., Murata S.;
"Assembly pathway of the Mammalian proteasome base subcomplex is
mediated by multiple specific chaperones.";
Cell 137:914-925(2009).
[15]
FUNCTION IN APOPTOSIS.
PubMed=19729910; DOI=10.1159/000227831;
Wang J., Wang X.F., Zhang L.G., Xie S.Y., Li Z.L., Li Y.J., Li H.H.,
Jiao F.;
"Involvement of the mitochondrial pathway in p53-independent apoptosis
induced by p28GANK knockdown in Hep3B cells.";
Cytogenet. Genome Res. 125:87-97(2009).
[16]
FUNCTION IN AKT ACTIVATION, INTERACTION WITH ARHGDIA, AND TISSUE
SPECIFICITY.
PubMed=20628200; DOI=10.1172/JCI42542;
Man J.H., Liang B., Gu Y.X., Zhou T., Li A.L., Li T., Jin B.F.,
Bai B., Zhang H.Y., Zhang W.N., Li W.H., Gong W.L., Li H.Y.,
Zhang X.M.;
"Gankyrin plays an essential role in Ras-induced tumorigenesis through
regulation of the RhoA/ROCK pathway in mammalian cells.";
J. Clin. Invest. 120:2829-2841(2010).
[17]
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).
[18]
STRUCTURE BY NMR, AND DOMAINS ANK REPEATS.
PubMed=15379554; DOI=10.1021/bi049116o;
Yuan C., Li J., Mahajan A., Poi M.J., Byeon I.-J., Tsai M.-D.;
"Solution structure of the human oncogenic protein gankyrin containing
seven ankyrin repeats and analysis of its structure-function
relationship.";
Biochemistry 43:12152-12161(2004).
[19]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND DOMAIN ANK REPEATS.
PubMed=14573599; DOI=10.1074/jbc.M310265200;
Krzywda S., Brzozowski A.M., Higashitsuji H., Fujita J., Welchman R.,
Dawson S., Mayer R.J., Wilkinson A.J.;
"The crystal structure of gankyrin, an oncoprotein found in complexes
with cyclin-dependent kinase 4, a 19 S proteasomal ATPase regulator,
and the tumor suppressors Rb and p53.";
J. Biol. Chem. 279:1541-1545(2004).
[20]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-226.
PubMed=14997555; DOI=10.1002/prot.20028;
Manjasetty B.A., Quedenau C., Sievert V., Bussow K., Niesen F.,
Delbruck H., Heinemann U.;
"X-ray structure of human gankyrin, the product of a gene linked to
hepatocellular carcinoma.";
Proteins 55:214-217(2004).
-!- FUNCTION: Acts as a chaperone during the assembly of the 26S
proteasome, specifically of the PA700/19S regulatory complex (RC).
In the initial step of the base subcomplex assembly is part of an
intermediate PSMD10:PSMC4:PSMC5:PAAF1 module which probably
assembles with a PSMD5:PSMC2:PSMC1:PSMD2 module. Independently of
the proteasome, regulates EGF-induced AKT activation through
inhibition of the RHOA/ROCK/PTEN pathway, leading to prolonged AKT
activation. Plays an important role in RAS-induced tumorigenesis.
-!- FUNCTION: Acts as an proto-oncoprotein by being involved in
negative regulation of tumor suppressors RB1 and p53/TP53.
Overexpression is leading to phosphorylation of RB1 and
proteasomal degradation of RB1. Regulates CDK4-mediated
phosphorylation of RB1 by competing with CDKN2A for binding with
CDK4. Facilitates binding of MDM2 to p53/TP53 and the mono- and
polyubiquitination of p53/TP53 by MDM2 suggesting a function in
targeting the TP53:MDM2 complex to the 26S proteasome. Involved in
p53-independent apoptosis. Involved in regulation of NF-kappa-B by
retaining it in the cytoplasm. Binds to the NF-kappa-B component
RELA and accelerates its XPO1/CRM1-mediated nuclear export.
-!- SUBUNIT: Part of transient complex containing PSMD10, PSMC4, PSMC5
and PAAF1 formed during the assembly of the 26S proteasome. Stays
associated throughout the assembly of the PA700/19S RC and is
released upon association with the 20S core. Interacts with PSMC4.
Interacts with RB1. Interacts with CDK4. Interacts with MDM2.
Interacts with RELA. Associates with a CDK4:CCND2 serine/threonine
kinase complex. Interacts with ARHGDIA and increases the
interaction between ARHGDIA and RHOA, hence promotes ARHGDIA
inactivation of RHOA and ROCK. {ECO:0000269|PubMed:10613832,
ECO:0000269|PubMed:11779854, ECO:0000269|PubMed:11900540,
ECO:0000269|PubMed:16023600, ECO:0000269|PubMed:18040287,
ECO:0000269|PubMed:19490896, ECO:0000269|PubMed:20628200}.
-!- INTERACTION:
Q9NWT6:HIF1AN; NbExp=2; IntAct=EBI-752185, EBI-745632;
P43358:MAGEA4; NbExp=5; IntAct=EBI-752185, EBI-743122;
P43686:PSMC4; NbExp=17; IntAct=EBI-752185, EBI-743997;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18040287}.
Nucleus {ECO:0000269|PubMed:18040287}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O75832-1; Sequence=Displayed;
Name=2;
IsoId=O75832-2; Sequence=VSP_043043;
-!- TISSUE SPECIFICITY: Tends to be up-regulated in cancer cells with
RAS mutations, including lung cancers and adenocarconimas (at
protein level). {ECO:0000269|PubMed:10613832,
ECO:0000269|PubMed:20628200}.
-!- CAUTION: Was initially identified as a genuine component of the
26S proteasome. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AB009619; BAA33215.1; -; mRNA.
EMBL; D83197; BAA34594.1; -; mRNA.
EMBL; AY057056; AAL25260.1; -; mRNA.
EMBL; AK295996; BAG58771.1; -; mRNA.
EMBL; BT019689; AAV38495.1; -; mRNA.
EMBL; AL031177; CAA20117.1; -; Genomic_DNA.
EMBL; AL031177; CAI43131.1; -; Genomic_DNA.
EMBL; BC011960; AAH11960.1; -; mRNA.
CCDS; CCDS14536.1; -. [O75832-1]
CCDS; CCDS14537.1; -. [O75832-2]
RefSeq; NP_002805.1; NM_002814.3. [O75832-1]
RefSeq; NP_736606.1; NM_170750.2. [O75832-2]
UniGene; Hs.522752; -.
PDB; 1QYM; X-ray; 2.80 A; A=2-226.
PDB; 1TR4; NMR; -; A=1-226.
PDB; 1UOH; X-ray; 2.00 A; A=1-226.
PDB; 4NIK; X-ray; 2.50 A; A=1-226.
PDB; 5VHF; EM; 5.70 A; G=4-226.
PDB; 5VHH; EM; 6.10 A; G=4-226.
PDB; 5VHI; EM; 6.80 A; G=1-226.
PDB; 5VHJ; EM; 8.50 A; G=4-226.
PDB; 5VHM; EM; 8.30 A; G=4-226.
PDB; 5VHN; EM; 7.30 A; G=4-226.
PDB; 5VHO; EM; 8.30 A; G=4-226.
PDB; 5VHP; EM; 7.90 A; G=3-226.
PDB; 5VHQ; EM; 8.90 A; G=4-226.
PDB; 5VHR; EM; 7.70 A; G=4-226.
PDBsum; 1QYM; -.
PDBsum; 1TR4; -.
PDBsum; 1UOH; -.
PDBsum; 4NIK; -.
PDBsum; 5VHF; -.
PDBsum; 5VHH; -.
PDBsum; 5VHI; -.
PDBsum; 5VHJ; -.
PDBsum; 5VHM; -.
PDBsum; 5VHN; -.
PDBsum; 5VHO; -.
PDBsum; 5VHP; -.
PDBsum; 5VHQ; -.
PDBsum; 5VHR; -.
ProteinModelPortal; O75832; -.
SMR; O75832; -.
BioGrid; 111688; 76.
CORUM; O75832; -.
DIP; DIP-39026N; -.
IntAct; O75832; 25.
MINT; MINT-254757; -.
STRING; 9606.ENSP00000217958; -.
ChEMBL; CHEMBL2331054; -.
iPTMnet; O75832; -.
PhosphoSitePlus; O75832; -.
BioMuta; PSMD10; -.
OGP; O75832; -.
EPD; O75832; -.
MaxQB; O75832; -.
PaxDb; O75832; -.
PeptideAtlas; O75832; -.
PRIDE; O75832; -.
TopDownProteomics; O75832-1; -. [O75832-1]
DNASU; 5716; -.
Ensembl; ENST00000217958; ENSP00000217958; ENSG00000101843. [O75832-1]
Ensembl; ENST00000361815; ENSP00000354906; ENSG00000101843. [O75832-2]
GeneID; 5716; -.
KEGG; hsa:5716; -.
UCSC; uc004enp.3; human. [O75832-1]
CTD; 5716; -.
DisGeNET; 5716; -.
EuPathDB; HostDB:ENSG00000101843.18; -.
GeneCards; PSMD10; -.
HGNC; HGNC:9555; PSMD10.
HPA; CAB010434; -.
HPA; HPA002920; -.
MIM; 300880; gene.
neXtProt; NX_O75832; -.
OpenTargets; ENSG00000101843; -.
PharmGKB; PA33900; -.
eggNOG; KOG4412; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00900000140840; -.
HOGENOM; HOG000158359; -.
HOVERGEN; HBG053737; -.
InParanoid; O75832; -.
KO; K06694; -.
OMA; SVNQNGC; -.
OrthoDB; EOG091G0KEZ; -.
PhylomeDB; O75832; -.
TreeFam; TF106234; -.
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; PSMD10; human.
EvolutionaryTrace; O75832; -.
GeneWiki; PSMD10; -.
GenomeRNAi; 5716; -.
PRO; PR:O75832; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000101843; -.
CleanEx; HS_PSMD10; -.
ExpressionAtlas; O75832; baseline and differential.
Genevisible; O75832; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
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:0008134; F:transcription factor binding; IPI: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:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007253; P:cytoplasmic sequestering of NF-kappaB; IDA:UniProtKB.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IDA:UniProtKB.
GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0043409; P:negative regulation of MAPK cascade; IMP:UniProtKB.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
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:0030307; P:positive regulation of cell growth; IDA:UniProtKB.
GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IMP:UniProtKB.
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:0070682; P:proteasome regulatory particle assembly; IMP:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; TAS:Reactome.
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; cd00204; ANK; 1.
Gene3D; 1.25.40.20; -; 3.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
Pfam; PF00023; Ank; 1.
Pfam; PF12796; Ank_2; 2.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 5.
SUPFAM; SSF48403; SSF48403; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 5.
1: Evidence at protein level;
3D-structure; Alternative splicing; ANK repeat; Apoptosis; Chaperone;
Complete proteome; Cytoplasm; Nucleus; Reference proteome; Repeat.
CHAIN 1 226 26S proteasome non-ATPase regulatory
subunit 10.
/FTId=PRO_0000067045.
REPEAT 3 36 ANK 1.
REPEAT 37 69 ANK 2.
REPEAT 70 102 ANK 3.
REPEAT 103 135 ANK 4.
REPEAT 136 168 ANK 5.
REPEAT 169 201 ANK 6.
REPEAT 202 226 ANK 7.
REGION 1 71 Interaction with RB1.
{ECO:0000269|PubMed:10613832}.
REGION 1 37 Required for nuclear localization.
REGION 39 226 Interaction with RELA.
REGION 171 226 Interaction with RB1.
{ECO:0000269|PubMed:10613832}.
VAR_SEQ 150 226 GNLKMIHILLYYKASTNIQDTEGNTPLHLACDEERVEEAKL
LVSQGASIYIENKEEKTPLQVAKGGLGLILKRMVEG -> D
T (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.3}.
/FTId=VSP_043043.
MUTAGEN 182 182 E->A: Abolishes interaction with RB1.
{ECO:0000269|PubMed:10613832}.
CONFLICT 196 196 A -> T (in Ref. 5; AAV38495).
{ECO:0000305}.
STRAND 6 8 {ECO:0000244|PDB:1UOH}.
HELIX 9 15 {ECO:0000244|PDB:1UOH}.
HELIX 19 28 {ECO:0000244|PDB:1UOH}.
HELIX 30 34 {ECO:0000244|PDB:1UOH}.
TURN 38 40 {ECO:0000244|PDB:1TR4}.
HELIX 43 50 {ECO:0000244|PDB:1UOH}.
HELIX 53 62 {ECO:0000244|PDB:1UOH}.
STRAND 71 73 {ECO:0000244|PDB:1TR4}.
HELIX 76 83 {ECO:0000244|PDB:1UOH}.
HELIX 86 94 {ECO:0000244|PDB:1UOH}.
HELIX 109 115 {ECO:0000244|PDB:1UOH}.
HELIX 119 127 {ECO:0000244|PDB:1UOH}.
HELIX 142 148 {ECO:0000244|PDB:1UOH}.
HELIX 152 160 {ECO:0000244|PDB:1UOH}.
HELIX 175 181 {ECO:0000244|PDB:1UOH}.
HELIX 185 193 {ECO:0000244|PDB:1UOH}.
HELIX 208 211 {ECO:0000244|PDB:1UOH}.
HELIX 216 224 {ECO:0000244|PDB:1UOH}.
SEQUENCE 226 AA; 24428 MW; 57158E33146EC7C8 CRC64;
MEGCVSNLMV CNLAYSGKLE ELKESILADK SLATRTDQDS RTALHWACSA GHTEIVEFLL
QLGVPVNDKD DAGWSPLHIA ASAGRDEIVK ALLGKGAQVN AVNQNGCTPL HYAASKNRHE
IAVMLLEGGA NPDAKDHYEA TAMHRAAAKG NLKMIHILLY YKASTNIQDT EGNTPLHLAC
DEERVEEAKL LVSQGASIYI ENKEEKTPLQ VAKGGLGLIL KRMVEG


Related products :

Catalog number Product name Quantity
EIAAB32787 26S proteasome non-ATPase regulatory subunit 10,26S proteasome regulatory subunit p28,Gankyrin,Homo sapiens,Human,p28(GANK),PSMD10
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
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
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
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
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
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
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
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
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
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
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
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-
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
EIAAB32786 26S proteasome non-ATPase regulatory subunit 10,26S proteasome regulatory subunit p28,Gankyrin,Psmd10,Rat,Rattus norvegicus
EIAAB32788 26S proteasome non-ATPase regulatory subunit 10,26S proteasome regulatory subunit p28,Gankyrin,Mouse,Mus musculus,Psmd10
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
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
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
EIAAB32793 26S proteasome non-ATPase regulatory subunit 12,26S proteasome regulatory subunit p55,26S proteasome regulatory subunit RPN5,Homo sapiens,Human,PSMD12
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