PRS10_HUMAN
ID PRS10_HUMAN Reviewed; 389 AA.
AC P62333; B2R975; P49719; Q6IBU3; Q92524;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=26S proteasome regulatory subunit 10B;
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT4;
DE AltName: Full=Proteasome 26S subunit ATPase 6;
DE AltName: Full=Proteasome subunit p42;
GN Name=PSMC6; Synonyms=SUG2;
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].
RC TISSUE=Aorta;
RX PubMed=8674546; DOI=10.1016/0014-5793(96)00489-9;
RA Fujiwara T., Watanabe T.K., Tanaka K., Slaughter C.A., Demartino G.N.;
RT "cDNA cloning of p42, a shared subunit of two proteasome regulatory
RT proteins, reveals a novel member of the AAA protein family.";
RL FEBS Lett. 387:184-188(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Li Y., Benezra R.;
RT "Human SUG2.";
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Caudate 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Urinary bladder;
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 PARTIAL PROTEIN SEQUENCE.
RX PubMed=8621709; DOI=10.1074/jbc.271.6.3112;
RA Demartino G.N., Proske R.J., Moomaw C.R., Strong A.A., Song X.,
RA Hisamatsu H., Tanaka K., Slaughter C.A.;
RT "Identification, purification, and characterization of a PA700-dependent
RT activator of the proteasome.";
RL J. Biol. Chem. 271:3112-3118(1996).
RN [9]
RP FUNCTION.
RX PubMed=1317798; DOI=10.1111/j.1432-1033.1992.tb16961.x;
RA Kanayama H.O., Tamura T., Ugai S., Kagawa S., Tanahashi N., Yoshimura T.,
RA Tanaka K., Ichihara A.;
RT "Demonstration that a human 26S proteolytic complex consists of a
RT proteasome and multiple associated protein components and hydrolyzes ATP
RT and ubiquitin-ligated proteins by closely linked mechanisms.";
RL Eur. J. Biochem. 206:567-578(1992).
RN [10]
RP INTERACTION WITH PAAF1.
RX PubMed=15831487; DOI=10.1128/mcb.25.9.3842-3853.2005;
RA Park Y., Hwang Y.-P., Lee J.-S., Seo S.-H., Yoon S.K., Yoon J.-B.;
RT "Proteasomal ATPase-associated factor 1 negatively regulates proteasome
RT activity by interacting with proteasomal ATPases.";
RL Mol. Cell. Biol. 25:3842-3853(2005).
RN [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-72 AND LYS-206, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [17]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS) OF 1-440, AND SUBUNIT.
RX PubMed=27428775; DOI=10.1038/nsmb.3273;
RA Huang X., Luan B., Wu J., Shi Y.;
RT "An atomic structure of the human 26S proteasome.";
RL Nat. Struct. Mol. Biol. 23:778-785(2016).
RN [18]
RP STRUCTURE BY ELECTRON MICROSCOPY (4.02 ANGSTROMS) OF 1-440, AND SUBUNIT.
RX PubMed=27342858; DOI=10.1073/pnas.1608050113;
RA Schweitzer A., Aufderheide A., Rudack T., Beck F., Pfeifer G.,
RA Plitzko J.M., Sakata E., Schulten K., Foerster F., Baumeister W.;
RT "Structure of the human 26S proteasome at a resolution of 3.9 Aa.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:7816-7821(2016).
CC -!- FUNCTION: Component of the 26S proteasome, a multiprotein complex
CC involved in the ATP-dependent degradation of ubiquitinated proteins.
CC This complex plays a key role in the maintenance of protein homeostasis
CC by removing misfolded or damaged proteins, which could impair cellular
CC functions, and by removing proteins whose functions are no longer
CC required. Therefore, the proteasome participates in numerous cellular
CC processes, including cell cycle progression, apoptosis, or DNA damage
CC repair. PSMC6 belongs to the heterohexameric ring of AAA (ATPases
CC associated with diverse cellular activities) proteins that unfolds
CC ubiquitinated target proteins that are concurrently translocated into a
CC proteolytic chamber and degraded into peptides.
CC {ECO:0000269|PubMed:1317798}.
CC -!- SUBUNIT: Component of the 19S proteasome regulatory particle complex.
CC The 26S proteasome consists of a 20S core particle (CP) and two 19S
CC regulatory subunits (RP). The regulatory particle is made of a lid
CC composed of 9 subunits, a base containing 6 ATPases including PSMC6 and
CC few additional components (PubMed:27428775, PubMed:27342858). Interacts
CC with PAAF1 (PubMed:15831487). {ECO:0000269|PubMed:15831487,
CC ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775}.
CC -!- INTERACTION:
CC P62333; Q13895: BYSL; NbExp=3; IntAct=EBI-357669, EBI-358049;
CC P62333; Q8TAB5: C1orf216; NbExp=4; IntAct=EBI-357669, EBI-747505;
CC P62333; Q8IYE0-2: CCDC146; NbExp=3; IntAct=EBI-357669, EBI-10247802;
CC P62333; Q16543: CDC37; NbExp=3; IntAct=EBI-357669, EBI-295634;
CC P62333; P46108: CRK; NbExp=10; IntAct=EBI-357669, EBI-886;
CC P62333; P46109: CRKL; NbExp=5; IntAct=EBI-357669, EBI-910;
CC P62333; Q6BCY4: CYB5R2; NbExp=3; IntAct=EBI-357669, EBI-744761;
CC P62333; P22607: FGFR3; NbExp=3; IntAct=EBI-357669, EBI-348399;
CC P62333; Q14957: GRIN2C; NbExp=3; IntAct=EBI-357669, EBI-8285963;
CC P62333; P52655: GTF2A1; NbExp=3; IntAct=EBI-357669, EBI-389518;
CC P62333; P04792: HSPB1; NbExp=3; IntAct=EBI-357669, EBI-352682;
CC P62333; P62191: PSMC1; NbExp=7; IntAct=EBI-357669, EBI-357598;
CC P62333; P17980: PSMC3; NbExp=16; IntAct=EBI-357669, EBI-359720;
CC P62333; P43686: PSMC4; NbExp=5; IntAct=EBI-357669, EBI-743997;
CC P62333; P62195: PSMC5; NbExp=14; IntAct=EBI-357669, EBI-357745;
CC P62333; P62333: PSMC6; NbExp=4; IntAct=EBI-357669, EBI-357669;
CC P62333; O00233: PSMD9; NbExp=15; IntAct=EBI-357669, EBI-750973;
CC P62333; O00560: SDCBP; NbExp=6; IntAct=EBI-357669, EBI-727004;
CC P62333; O43304: SEC14L5; NbExp=3; IntAct=EBI-357669, EBI-12224055;
CC P62333; Q969G3: SMARCE1; NbExp=3; IntAct=EBI-357669, EBI-455078;
CC P62333; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-357669, EBI-10180829;
CC P62333; O76024: WFS1; NbExp=3; IntAct=EBI-357669, EBI-720609;
CC P62333; P59595: N; Xeno; NbExp=3; IntAct=EBI-357669, EBI-7602718;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
CC -!- CAUTION: Alternative initiation from an upstream conserved methionine
CC cannot be fully excluded but is not experimentally supported while
CC initiation from the displayed methionine is supported by
CC PubMed:17323924. {ECO:0000305}.
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DR EMBL; D78275; BAA11338.1; -; mRNA.
DR EMBL; AF006305; AAB61616.1; -; mRNA.
DR EMBL; BT006843; AAP35489.1; -; mRNA.
DR EMBL; CR456709; CAG32990.1; -; mRNA.
DR EMBL; AK313670; BAG36422.1; -; mRNA.
DR EMBL; CH471078; EAW65645.1; -; Genomic_DNA.
DR EMBL; BC005390; AAH05390.1; -; mRNA.
DR CCDS; CCDS9710.2; -.
DR PIR; S71316; S71316.
DR RefSeq; NP_002797.3; NM_002806.3.
DR PDB; 5GJQ; EM; 4.50 A; L=1-389.
DR PDB; 5GJR; EM; 3.50 A; L/z=1-389.
DR PDB; 5L4G; EM; 4.02 A; L=1-389.
DR PDB; 5LN3; EM; 6.80 A; L=1-389.
DR PDB; 5M32; EM; 3.80 A; f=1-379.
DR PDB; 5T0C; EM; 3.80 A; AE/BE=1-389.
DR PDB; 5T0G; EM; 4.40 A; E=1-389.
DR PDB; 5T0H; EM; 6.80 A; E=1-389.
DR PDB; 5T0I; EM; 8.00 A; E=1-389.
DR PDB; 5T0J; EM; 8.00 A; E=1-389.
DR PDB; 5VFP; EM; 4.20 A; E=15-389.
DR PDB; 5VFQ; EM; 4.20 A; E=15-389.
DR PDB; 5VFR; EM; 4.90 A; E=15-389.
DR PDB; 5VFS; EM; 3.60 A; E=1-389.
DR PDB; 5VFT; EM; 7.00 A; E=37-389.
DR PDB; 5VFU; EM; 5.80 A; E=37-389.
DR PDB; 5VGZ; EM; 3.70 A; E=11-114.
DR PDB; 5VHF; EM; 5.70 A; E=11-389.
DR PDB; 5VHH; EM; 6.10 A; E=11-389.
DR PDB; 5VHI; EM; 6.80 A; E=11-389.
DR PDB; 5VHJ; EM; 8.50 A; E=128-389.
DR PDB; 5VHM; EM; 8.30 A; E=128-389.
DR PDB; 5VHN; EM; 7.30 A; E=115-389.
DR PDB; 5VHO; EM; 8.30 A; E=128-389.
DR PDB; 5VHP; EM; 7.90 A; E=128-389.
DR PDB; 5VHQ; EM; 8.90 A; E=128-389.
DR PDB; 5VHR; EM; 7.70 A; E=128-389.
DR PDB; 5VHS; EM; 8.80 A; E=11-389.
DR PDB; 6MSB; EM; 3.00 A; E=1-389.
DR PDB; 6MSD; EM; 3.20 A; E=1-389.
DR PDB; 6MSE; EM; 3.30 A; E=1-389.
DR PDB; 6MSG; EM; 3.50 A; E=1-389.
DR PDB; 6MSH; EM; 3.60 A; E=1-389.
DR PDB; 6MSJ; EM; 3.30 A; E=1-389.
DR PDB; 6MSK; EM; 3.20 A; E=1-389.
DR PDB; 6WJN; EM; 5.70 A; E=15-389.
DR PDBsum; 5GJQ; -.
DR PDBsum; 5GJR; -.
DR PDBsum; 5L4G; -.
DR PDBsum; 5LN3; -.
DR PDBsum; 5M32; -.
DR PDBsum; 5T0C; -.
DR PDBsum; 5T0G; -.
DR PDBsum; 5T0H; -.
DR PDBsum; 5T0I; -.
DR PDBsum; 5T0J; -.
DR PDBsum; 5VFP; -.
DR PDBsum; 5VFQ; -.
DR PDBsum; 5VFR; -.
DR PDBsum; 5VFS; -.
DR PDBsum; 5VFT; -.
DR PDBsum; 5VFU; -.
DR PDBsum; 5VGZ; -.
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 PDBsum; 5VHS; -.
DR PDBsum; 6MSB; -.
DR PDBsum; 6MSD; -.
DR PDBsum; 6MSE; -.
DR PDBsum; 6MSG; -.
DR PDBsum; 6MSH; -.
DR PDBsum; 6MSJ; -.
DR PDBsum; 6MSK; -.
DR PDBsum; 6WJN; -.
DR AlphaFoldDB; P62333; -.
DR SMR; P62333; -.
DR BioGRID; 111679; 231.
DR ComplexPortal; CPX-5993; 26S Proteasome complex.
DR CORUM; P62333; -.
DR DIP; DIP-38150N; -.
DR IntAct; P62333; 111.
DR MINT; P62333; -.
DR STRING; 9606.ENSP00000401802; -.
DR ChEMBL; CHEMBL2364701; -.
DR GlyGen; P62333; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62333; -.
DR MetOSite; P62333; -.
DR PhosphoSitePlus; P62333; -.
DR SwissPalm; P62333; -.
DR BioMuta; PSMC6; -.
DR DMDM; 51702772; -.
DR REPRODUCTION-2DPAGE; IPI00021926; -.
DR EPD; P62333; -.
DR jPOST; P62333; -.
DR MassIVE; P62333; -.
DR MaxQB; P62333; -.
DR PaxDb; P62333; -.
DR PeptideAtlas; P62333; -.
DR PRIDE; P62333; -.
DR ProteomicsDB; 57397; -.
DR Antibodypedia; 23885; 308 antibodies from 34 providers.
DR DNASU; 5706; -.
DR Ensembl; ENST00000445930.7; ENSP00000401802.3; ENSG00000100519.12.
DR GeneID; 5706; -.
DR KEGG; hsa:5706; -.
DR MANE-Select; ENST00000445930.7; ENSP00000401802.3; NM_002806.5; NP_002797.4.
DR UCSC; uc059bor.1; human.
DR CTD; 5706; -.
DR DisGeNET; 5706; -.
DR GeneCards; PSMC6; -.
DR HGNC; HGNC:9553; PSMC6.
DR HPA; ENSG00000100519; Low tissue specificity.
DR MIM; 602708; gene.
DR neXtProt; NX_P62333; -.
DR OpenTargets; ENSG00000100519; -.
DR PharmGKB; PA33898; -.
DR VEuPathDB; HostDB:ENSG00000100519; -.
DR eggNOG; KOG0651; Eukaryota.
DR GeneTree; ENSGT01020000230346; -.
DR HOGENOM; CLU_000688_2_2_1; -.
DR InParanoid; P62333; -.
DR OMA; YNMTTFE; -.
DR OrthoDB; 571919at2759; -.
DR PhylomeDB; P62333; -.
DR TreeFam; TF106229; -.
DR PathwayCommons; P62333; -.
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; P62333; -.
DR SIGNOR; P62333; -.
DR BioGRID-ORCS; 5706; 798 hits in 1051 CRISPR screens.
DR ChiTaRS; PSMC6; human.
DR GeneWiki; PSMC6; -.
DR GenomeRNAi; 5706; -.
DR Pharos; P62333; Tbio.
DR PRO; PR:P62333; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P62333; protein.
DR Bgee; ENSG00000100519; Expressed in esophagus squamous epithelium and 203 other tissues.
DR ExpressionAtlas; P62333; baseline and differential.
DR Genevisible; P62333; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031597; C:cytosolic proteasome complex; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016234; C:inclusion body; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0022624; C:proteasome accessory complex; ISS:UniProtKB.
DR GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0036402; F:proteasome-activating activity; IBA:GO_Central.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; NAS:UniProtKB.
DR GO; GO:0090261; P:positive regulation of inclusion body assembly; IEA:Ensembl.
DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IC:UniProtKB.
DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR005937; 26S_Psome_P45-like.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032501; Prot_ATP_ID_OB_C.
DR InterPro; IPR035263; PSMC6.
DR PANTHER; PTHR23073:SF76; PTHR23073:SF76; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01242; 26Sp45; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Proteasome; Reference proteome.
FT CHAIN 1..389
FT /note="26S proteasome regulatory subunit 10B"
FT /id="PRO_0000084732"
FT BINDING 174..181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 72
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 206
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CONFLICT 276
FT /note="I -> T (in Ref. 1; BAA11338)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 389 AA; 44173 MW; B26421295742CACD CRC64;
MADPRDKALQ DYRKKLLEHK EIDGRLKELR EQLKELTKQY EKSENDLKAL QSVGQIVGEV
LKQLTEEKFI VKATNGPRYV VGCRRQLDKS KLKPGTRVAL DMTTLTIMRY LPREVDPLVY
NMSHEDPGNV SYSEIGGLSE QIRELREVIE LPLTNPELFQ RVGIIPPKGC LLYGPPGTGK
TLLARAVASQ LDCNFLKVVS SSIVDKYIGE SARLIREMFN YARDHQPCII FMDEIDAIGG
RRFSEGTSAD REIQRTLMEL LNQMDGFDTL HRVKMIMATN RPDTLDPALL RPGRLDRKIH
IDLPNEQARL DILKIHAGPI TKHGEIDYEA IVKLSDGFNG ADLRNVCTEA GMFAIRADHD
FVVQEDFMKA VRKVADSKKL ESKLDYKPV
