PSD10_HUMAN
ID PSD10_HUMAN Reviewed; 226 AA.
AC O75832; Q5U0B2; Q8IZK9;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=26S proteasome non-ATPase regulatory subunit 10;
DE AltName: Full=26S proteasome regulatory subunit p28;
DE AltName: Full=Gankyrin;
DE AltName: Full=p28(GANK);
GN Name=PSMD10;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9714768; DOI=10.1016/s0378-1119(98)00309-6;
RA Hori T., Kato S., Saeki M., DeMartino G.N., Slaughter C.A., Takeuchi J.,
RA Toh-e A., Tanaka K.;
RT "cDNA cloning and functional analysis of p28 (Nas6p) and p40.5 (Nas7p), two
RT novel regulatory subunits of the 26S proteasome.";
RL Gene 216:113-122(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RA Higashitsuji H., Fujita J.;
RT "Enhanced expression of a novel tumour marker in the human hepatomas.";
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Liver;
RA Wang H., Fu X., Wu M.;
RT "Involvement of p28-II in hepatocellular carcinoma.";
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Subthalamic nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP FUNCTION AS POTENTIAL PROTO-ONCOGENE, INTERACTION WITH RB1, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF GLU-182.
RX PubMed=10613832; DOI=10.1038/71600;
RA Higashitsuji H., Itoh K., Nagao T., Dawson S., Nonoguchi K., Kido T.,
RA Mayer R.J., Arii S., Fujita J.;
RT "Reduced stability of retinoblastoma protein by gankyrin, an oncogenic
RT ankyrin-repeat protein overexpressed in hepatomas.";
RL Nat. Med. 6:96-99(2000).
RN [9]
RP FUNCTION, AND INTERACTION WITH CDK4.
RX PubMed=11900540; DOI=10.1021/bi011550s;
RA Li J., Tsai M.D.;
RT "Novel insights into the INK4-CDK4/6-Rb pathway: counter action of gankyrin
RT against INK4 proteins regulates the CDK4-mediated phosphorylation of Rb.";
RL Biochemistry 41:3977-3983(2002).
RN [10]
RP FUNCTION, AND INTERACTION WITH PSMC4.
RX PubMed=11779854; DOI=10.1074/jbc.m107313200;
RA Dawson S., Apcher S., Mee M., Higashitsuji H., Baker R., Uhle S.,
RA Dubiel W., Fujita J., Mayer R.J.;
RT "Gankyrin is an ankyrin-repeat oncoprotein that interacts with CDK4 kinase
RT and the S6 ATPase of the 26 S proteasome.";
RL J. Biol. Chem. 277:10893-10902(2002).
RN [11]
RP FUNCTION IN DEGRADATION OF TP53, AND INTERACTION WITH MDM2.
RX PubMed=16023600; DOI=10.1016/j.ccr.2005.06.006;
RA Higashitsuji H., Higashitsuji H., Itoh K., Sakurai T., Nagao T.,
RA Sumitomo Y., Masuda T., Dawson S., Shimada Y., Mayer R.J., Fujita J.;
RT "The oncoprotein gankyrin binds to MDM2/HDM2, enhancing ubiquitylation and
RT degradation of p53.";
RL Cancer Cell 8:75-87(2005).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17323924; DOI=10.1021/bi061994u;
RA Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
RT "Mass spectrometric characterization of the affinity-purified human 26S
RT proteasome complex.";
RL Biochemistry 46:3553-3565(2007).
RN [13]
RP FUNCTION IN REGULATION OF NF-KAPPA-B, INTERACTION WITH RELY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=18040287; DOI=10.1038/cr.2007.99;
RA Chen Y., Li H.H., Fu J., Wang X.F., Ren Y.B., Dong L.W., Tang S.H.,
RA Liu S.Q., Wu M.C., Wang H.Y.;
RT "Oncoprotein p28 GANK binds to RelA and retains NF-kappaB in the cytoplasm
RT through nuclear export.";
RL Cell Res. 17:1020-1029(2007).
RN [14]
RP FUNCTION AS PROTEASOME CHAPERONE, AND SUBUNIT.
RX PubMed=19490896; DOI=10.1016/j.cell.2009.05.008;
RA Kaneko T., Hamazaki J., Iemura S., Sasaki K., Furuyama K., Natsume T.,
RA Tanaka K., Murata S.;
RT "Assembly pathway of the Mammalian proteasome base subcomplex is mediated
RT by multiple specific chaperones.";
RL Cell 137:914-925(2009).
RN [15]
RP FUNCTION IN APOPTOSIS.
RX PubMed=19729910; DOI=10.1159/000227831;
RA Wang J., Wang X.F., Zhang L.G., Xie S.Y., Li Z.L., Li Y.J., Li H.H.,
RA Jiao F.;
RT "Involvement of the mitochondrial pathway in p53-independent apoptosis
RT induced by p28GANK knockdown in Hep3B cells.";
RL Cytogenet. Genome Res. 125:87-97(2009).
RN [16]
RP FUNCTION IN AKT ACTIVATION, INTERACTION WITH ARHGDIA, AND TISSUE
RP SPECIFICITY.
RX PubMed=20628200; DOI=10.1172/jci42542;
RA Man J.H., Liang B., Gu Y.X., Zhou T., Li A.L., Li T., Jin B.F., Bai B.,
RA Zhang H.Y., Zhang W.N., Li W.H., Gong W.L., Li H.Y., Zhang X.M.;
RT "Gankyrin plays an essential role in Ras-induced tumorigenesis through
RT regulation of the RhoA/ROCK pathway in mammalian cells.";
RL J. Clin. Invest. 120:2829-2841(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP STRUCTURE BY NMR, AND DOMAINS ANK REPEATS.
RX PubMed=15379554; DOI=10.1021/bi049116o;
RA Yuan C., Li J., Mahajan A., Poi M.J., Byeon I.-J., Tsai M.-D.;
RT "Solution structure of the human oncogenic protein gankyrin containing
RT seven ankyrin repeats and analysis of its structure-function
RT relationship.";
RL Biochemistry 43:12152-12161(2004).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND DOMAIN ANK REPEATS.
RX PubMed=14573599; DOI=10.1074/jbc.m310265200;
RA Krzywda S., Brzozowski A.M., Higashitsuji H., Fujita J., Welchman R.,
RA Dawson S., Mayer R.J., Wilkinson A.J.;
RT "The crystal structure of gankyrin, an oncoprotein found in complexes with
RT cyclin-dependent kinase 4, a 19 S proteasomal ATPase regulator, and the
RT tumor suppressors Rb and p53.";
RL J. Biol. Chem. 279:1541-1545(2004).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-226.
RX PubMed=14997555; DOI=10.1002/prot.20028;
RA Manjasetty B.A., Quedenau C., Sievert V., Bussow K., Niesen F.,
RA Delbruck H., Heinemann U.;
RT "X-ray structure of human gankyrin, the product of a gene linked to
RT hepatocellular carcinoma.";
RL Proteins 55:214-217(2004).
CC -!- FUNCTION: Acts as a chaperone during the assembly of the 26S
CC proteasome, specifically of the PA700/19S regulatory complex (RC). In
CC the initial step of the base subcomplex assembly is part of an
CC intermediate PSMD10:PSMC4:PSMC5:PAAF1 module which probably assembles
CC with a PSMD5:PSMC2:PSMC1:PSMD2 module. Independently of the proteasome,
CC regulates EGF-induced AKT activation through inhibition of the
CC RHOA/ROCK/PTEN pathway, leading to prolonged AKT activation. Plays an
CC important role in RAS-induced tumorigenesis.
CC -!- FUNCTION: Acts as an proto-oncoprotein by being involved in negative
CC regulation of tumor suppressors RB1 and p53/TP53. Overexpression is
CC leading to phosphorylation of RB1 and proteasomal degradation of RB1.
CC Regulates CDK4-mediated phosphorylation of RB1 by competing with CDKN2A
CC for binding with CDK4. Facilitates binding of MDM2 to p53/TP53 and the
CC mono- and polyubiquitination of p53/TP53 by MDM2 suggesting a function
CC in targeting the TP53:MDM2 complex to the 26S proteasome. Involved in
CC p53-independent apoptosis. Involved in regulation of NF-kappa-B by
CC retaining it in the cytoplasm. Binds to the NF-kappa-B component RELA
CC and accelerates its XPO1/CRM1-mediated nuclear export.
CC -!- SUBUNIT: Part of transient complex containing PSMD10, PSMC4, PSMC5 and
CC PAAF1 formed during the assembly of the 26S proteasome. Stays
CC associated throughout the assembly of the PA700/19S RC and is released
CC upon association with the 20S core. Interacts with PSMC4. Interacts
CC with RB1. Interacts with CDK4. Interacts with MDM2. Interacts with
CC RELA. Associates with a CDK4:CCND2 serine/threonine kinase complex.
CC Interacts with ARHGDIA and increases the interaction between ARHGDIA
CC and RHOA, hence promotes ARHGDIA inactivation of RHOA and ROCK.
CC {ECO:0000269|PubMed:10613832, ECO:0000269|PubMed:11779854,
CC ECO:0000269|PubMed:11900540, ECO:0000269|PubMed:16023600,
CC ECO:0000269|PubMed:18040287, ECO:0000269|PubMed:19490896,
CC ECO:0000269|PubMed:20628200}.
CC -!- INTERACTION:
CC O75832; O00299: CLIC1; NbExp=9; IntAct=EBI-752185, EBI-347404;
CC O75832; Q12849: GRSF1; NbExp=4; IntAct=EBI-752185, EBI-1054150;
CC O75832; Q9NWT6: HIF1AN; NbExp=2; IntAct=EBI-752185, EBI-745632;
CC O75832; P0DMV8: HSPA1A; NbExp=2; IntAct=EBI-752185, EBI-11052499;
CC O75832; P43358: MAGEA4; NbExp=5; IntAct=EBI-752185, EBI-743122;
CC O75832; O43639: NCK2; NbExp=2; IntAct=EBI-752185, EBI-713635;
CC O75832; P43686: PSMC4; NbExp=23; IntAct=EBI-752185, EBI-743997;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18040287}. Nucleus
CC {ECO:0000269|PubMed:18040287}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75832-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75832-2; Sequence=VSP_043043;
CC -!- TISSUE SPECIFICITY: Tends to be up-regulated in cancer cells with RAS
CC mutations, including lung cancers and adenocarconimas (at protein
CC level). {ECO:0000269|PubMed:10613832, ECO:0000269|PubMed:20628200}.
CC -!- CAUTION: Was initially identified as a genuine component of the 26S
CC proteasome. {ECO:0000305}.
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DR EMBL; AB009619; BAA33215.1; -; mRNA.
DR EMBL; D83197; BAA34594.1; -; mRNA.
DR EMBL; AY057056; AAL25260.1; -; mRNA.
DR EMBL; AK295996; BAG58771.1; -; mRNA.
DR EMBL; BT019689; AAV38495.1; -; mRNA.
DR EMBL; AL031177; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011960; AAH11960.1; -; mRNA.
DR CCDS; CCDS14536.1; -. [O75832-1]
DR CCDS; CCDS14537.1; -. [O75832-2]
DR RefSeq; NP_002805.1; NM_002814.3. [O75832-1]
DR RefSeq; NP_736606.1; NM_170750.2. [O75832-2]
DR PDB; 1QYM; X-ray; 2.80 A; A=2-226.
DR PDB; 1TR4; NMR; -; A=1-226.
DR PDB; 1UOH; X-ray; 2.00 A; A=1-226.
DR PDB; 4NIK; X-ray; 2.50 A; A=1-226.
DR PDB; 5VHF; EM; 5.70 A; G=4-226.
DR PDB; 5VHH; EM; 6.10 A; G=4-226.
DR PDB; 5VHI; EM; 6.80 A; G=1-226.
DR PDB; 5VHJ; EM; 8.50 A; G=4-226.
DR PDB; 5VHM; EM; 8.30 A; G=4-226.
DR PDB; 5VHN; EM; 7.30 A; G=4-226.
DR PDB; 5VHO; EM; 8.30 A; G=4-226.
DR PDB; 5VHP; EM; 7.90 A; G=3-226.
DR PDB; 5VHQ; EM; 8.90 A; G=4-226.
DR PDB; 5VHR; EM; 7.70 A; G=4-226.
DR PDBsum; 1QYM; -.
DR PDBsum; 1TR4; -.
DR PDBsum; 1UOH; -.
DR PDBsum; 4NIK; -.
DR PDBsum; 5VHF; -.
DR PDBsum; 5VHH; -.
DR PDBsum; 5VHI; -.
DR PDBsum; 5VHJ; -.
DR PDBsum; 5VHM; -.
DR PDBsum; 5VHN; -.
DR PDBsum; 5VHO; -.
DR PDBsum; 5VHP; -.
DR PDBsum; 5VHQ; -.
DR PDBsum; 5VHR; -.
DR AlphaFoldDB; O75832; -.
DR BMRB; O75832; -.
DR SMR; O75832; -.
DR BioGRID; 111688; 105.
DR CORUM; O75832; -.
DR DIP; DIP-39026N; -.
DR IntAct; O75832; 44.
DR MINT; O75832; -.
DR STRING; 9606.ENSP00000217958; -.
DR ChEMBL; CHEMBL2331054; -.
DR GlyGen; O75832; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75832; -.
DR MetOSite; O75832; -.
DR PhosphoSitePlus; O75832; -.
DR BioMuta; PSMD10; -.
DR OGP; O75832; -.
DR EPD; O75832; -.
DR jPOST; O75832; -.
DR MassIVE; O75832; -.
DR MaxQB; O75832; -.
DR PaxDb; O75832; -.
DR PeptideAtlas; O75832; -.
DR PRIDE; O75832; -.
DR ProteomicsDB; 50220; -. [O75832-1]
DR ProteomicsDB; 50221; -. [O75832-2]
DR TopDownProteomics; O75832-1; -. [O75832-1]
DR ABCD; O75832; 1 sequenced antibody.
DR Antibodypedia; 496; 433 antibodies from 33 providers.
DR DNASU; 5716; -.
DR Ensembl; ENST00000217958.8; ENSP00000217958.3; ENSG00000101843.19. [O75832-1]
DR Ensembl; ENST00000361815.9; ENSP00000354906.5; ENSG00000101843.19. [O75832-2]
DR GeneID; 5716; -.
DR KEGG; hsa:5716; -.
DR MANE-Select; ENST00000217958.8; ENSP00000217958.3; NM_002814.4; NP_002805.1.
DR UCSC; uc004enp.3; human. [O75832-1]
DR CTD; 5716; -.
DR DisGeNET; 5716; -.
DR GeneCards; PSMD10; -.
DR HGNC; HGNC:9555; PSMD10.
DR HPA; ENSG00000101843; Low tissue specificity.
DR MIM; 300880; gene.
DR neXtProt; NX_O75832; -.
DR OpenTargets; ENSG00000101843; -.
DR PharmGKB; PA33900; -.
DR VEuPathDB; HostDB:ENSG00000101843; -.
DR eggNOG; KOG4412; Eukaryota.
DR GeneTree; ENSGT00940000153404; -.
DR HOGENOM; CLU_000134_18_2_1; -.
DR InParanoid; O75832; -.
DR OMA; WAVAYNR; -.
DR OrthoDB; 1514637at2759; -.
DR PhylomeDB; O75832; -.
DR TreeFam; TF106234; -.
DR PathwayCommons; O75832; -.
DR Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
DR Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
DR Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-HSA-202424; Downstream TCR signaling.
DR Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-HSA-4641257; Degradation of AXIN.
DR Reactome; R-HSA-4641258; Degradation of DVL.
DR Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD.
DR Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
DR Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
DR Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex.
DR Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-HSA-69481; G2/M Checkpoints.
DR Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-HSA-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-HSA-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; O75832; -.
DR BioGRID-ORCS; 5716; 23 hits in 701 CRISPR screens.
DR ChiTaRS; PSMD10; human.
DR EvolutionaryTrace; O75832; -.
DR GeneWiki; PSMD10; -.
DR GenomeRNAi; 5716; -.
DR Pharos; O75832; Tbio.
DR PRO; PR:O75832; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; O75832; protein.
DR Bgee; ENSG00000101843; Expressed in epithelium of nasopharynx and 207 other tissues.
DR ExpressionAtlas; O75832; baseline and differential.
DR Genevisible; O75832; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
DR GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007253; P:cytoplasmic sequestering of NF-kappaB; IDA:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IDA:UniProtKB.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IMP:UniProtKB.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0030307; P:positive regulation of cell growth; IDA:UniProtKB.
DR GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IMP:UniProtKB.
DR GO; GO:0070682; P:proteasome regulatory particle assembly; IMP:UniProtKB.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR039334; PSMD10-like.
DR PANTHER; PTHR24126:SF24; PTHR24126:SF24; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 2.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 5.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ANK repeat; Apoptosis; Chaperone;
KW Cytoplasm; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..226
FT /note="26S proteasome non-ATPase regulatory subunit 10"
FT /id="PRO_0000067045"
FT REPEAT 3..36
FT /note="ANK 1"
FT REPEAT 37..69
FT /note="ANK 2"
FT REPEAT 70..102
FT /note="ANK 3"
FT REPEAT 103..135
FT /note="ANK 4"
FT REPEAT 136..168
FT /note="ANK 5"
FT REPEAT 169..201
FT /note="ANK 6"
FT REPEAT 202..226
FT /note="ANK 7"
FT REGION 1..71
FT /note="Interaction with RB1"
FT /evidence="ECO:0000269|PubMed:10613832"
FT REGION 1..37
FT /note="Required for nuclear localization"
FT REGION 39..226
FT /note="Interaction with RELA"
FT REGION 171..226
FT /note="Interaction with RB1"
FT /evidence="ECO:0000269|PubMed:10613832"
FT VAR_SEQ 150..226
FT /note="GNLKMIHILLYYKASTNIQDTEGNTPLHLACDEERVEEAKLLVSQGASIYIE
FT NKEEKTPLQVAKGGLGLILKRMVEG -> DT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.3"
FT /id="VSP_043043"
FT MUTAGEN 182
FT /note="E->A: Abolishes interaction with RB1."
FT /evidence="ECO:0000269|PubMed:10613832"
FT CONFLICT 196
FT /note="A -> T (in Ref. 5; AAV38495)"
FT /evidence="ECO:0000305"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:1UOH"
FT HELIX 9..15
FT /evidence="ECO:0007829|PDB:1UOH"
FT HELIX 19..28
FT /evidence="ECO:0007829|PDB:1UOH"
FT HELIX 30..34
FT /evidence="ECO:0007829|PDB:1UOH"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:1TR4"
FT HELIX 43..50
FT /evidence="ECO:0007829|PDB:1UOH"
FT HELIX 53..62
FT /evidence="ECO:0007829|PDB:1UOH"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:1TR4"
FT HELIX 76..83
FT /evidence="ECO:0007829|PDB:1UOH"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:1UOH"
FT HELIX 109..115
FT /evidence="ECO:0007829|PDB:1UOH"
FT HELIX 119..127
FT /evidence="ECO:0007829|PDB:1UOH"
FT HELIX 142..148
FT /evidence="ECO:0007829|PDB:1UOH"
FT HELIX 152..160
FT /evidence="ECO:0007829|PDB:1UOH"
FT HELIX 175..181
FT /evidence="ECO:0007829|PDB:1UOH"
FT HELIX 185..193
FT /evidence="ECO:0007829|PDB:1UOH"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:1UOH"
FT HELIX 216..224
FT /evidence="ECO:0007829|PDB:1UOH"
SQ 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
