PRS8_HUMAN
ID PRS8_HUMAN Reviewed; 406 AA.
AC P62195; A8K3Z3; A8K763; O35051; O43208; P47210; P52915; P52916;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=26S proteasome regulatory subunit 8;
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT6;
DE AltName: Full=Proteasome 26S subunit ATPase 5;
DE AltName: Full=Proteasome subunit p45;
DE AltName: Full=Thyroid hormone receptor-interacting protein 1;
DE Short=TRIP1;
DE AltName: Full=p45/SUG;
GN Name=PSMC5; Synonyms=SUG1;
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).
RC TISSUE=Hepatoma;
RX PubMed=7729537; DOI=10.1016/0014-5793(95)00304-r;
RA Akiyama K., Yokota K., Kagawa S., Shimbara N., Demartino G.N.,
RA Slaughter C.A., Noda C., Tanaka K.;
RT "cDNA cloning of a new putative ATPase subunit p45 of the human 26S
RT proteasome, a homolog of yeast transcriptional factor Sug1p.";
RL FEBS Lett. 363:151-156(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7776974; DOI=10.1210/mend.9.2.7776974;
RA Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.;
RT "Two classes of proteins dependent on either the presence or absence of
RT thyroid hormone for interaction with the thyroid hormone receptor.";
RL Mol. Endocrinol. 9:243-254(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Skeletal muscle;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung carcinoma;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-406.
RC TISSUE=Brain;
RX PubMed=9110174; DOI=10.1101/gr.7.4.353;
RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT "Large-scale concatenation cDNA sequencing.";
RL Genome Res. 7:353-358(1997).
RN [7]
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 [8]
RP INTERACTION WITH NDC80.
RX PubMed=9295362; DOI=10.1074/jbc.272.38.24081;
RA Chen Y., Sharp Z.D., Lee W.-H.;
RT "HEC binds to the seventh regulatory subunit of the 26 S proteasome and
RT modulates the proteolysis of mitotic cyclins.";
RL J. Biol. Chem. 272:24081-24087(1997).
RN [9]
RP INTERACTION WITH NDC80.
RX PubMed=10409732; DOI=10.1128/mcb.19.8.5417;
RA Zheng L., Chen Y., Lee W.-H.;
RT "Hec1p, an evolutionarily conserved coiled-coil protein, modulates
RT chromosome segregation through interaction with SMC proteins.";
RL Mol. Cell. Biol. 19:5417-5428(1999).
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 ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-222, AND IDENTIFICATION BY MASS
RP 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 [14]
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 [15]
RP INTERACTION WITH TRIM5.
RX PubMed=22078707; DOI=10.1186/1742-4690-8-93;
RA Lukic Z., Hausmann S., Sebastian S., Rucci J., Sastri J., Robia S.L.,
RA Luban J., Campbell E.M.;
RT "TRIM5alpha associates with proteasomal subunits in cells while in complex
RT with HIV-1 virions.";
RL Retrovirology 8:93-93(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, ACETYLATION [LARGE SCALE
RP ANALYSIS] AT MET-1 (ISOFORM 2), CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP IDENTIFICATION IN A COMPLEX WITH USP49 AND RUVBL1.
RX PubMed=23824326; DOI=10.1101/gad.211037.112;
RA Zhang Z., Jones A., Joo H.Y., Zhou D., Cao Y., Chen S.,
RA Erdjument-Bromage H., Renfrow M., He H., Tempst P., Townes T.M.,
RA Giles K.E., Ma L., Wang H.;
RT "USP49 deubiquitinates histone H2B and regulates cotranscriptional pre-mRNA
RT splicing.";
RL Genes Dev. 27:1581-1595(2013).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [20]
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 [21]
RP ACETYLATION AT ALA-2, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=25489052; DOI=10.1093/hmg/ddu611;
RA Myklebust L.M., Van Damme P., Stoeve S.I., Doerfel M.J., Abboud A.,
RA Kalvik T.V., Grauffel C., Jonckheere V., Wu Y., Swensen J., Kaasa H.,
RA Liszczak G., Marmorstein R., Reuter N., Lyon G.J., Gevaert K., Arnesen T.;
RT "Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-
RT acetylation defects.";
RL Hum. Mol. Genet. 24:1956-1976(2015).
RN [22]
RP INTERACTION WITH ERCC6.
RX PubMed=26030138; DOI=10.1371/journal.pone.0128558;
RA Nicolai S., Filippi S., Caputo M., Cipak L., Gregan J., Ammerer G.,
RA Frontini M., Willems D., Prantera G., Balajee A.S., Proietti-De-Santis L.;
RT "Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group
RT B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin
RT Dynamics.";
RL PLoS ONE 10:E0128558-E0128558(2015).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 318-395, AND STRUCTURE BY NMR OF
RP 320-395.
RG Northeast structural genomics consortium (NESG);
RT "Crystal structure of a domain of 26s proteasome regulatory subunit 8 from
RT Homo sapiens. Northeast structural genomics consortium target ID HR3102A.";
RL Submitted (JAN-2010) to the PDB data bank.
RN [24]
RP VARIANT [LARGE SCALE ANALYSIS] GLN-60.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [25]
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 [26]
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. PSMC5 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 PSMC5 and
CC few additional components (PubMed:27428775, PubMed:27342858). Component
CC of a complex with USP49 and RUVBL1 (PubMed:23824326). Interacts with
CC PRPF19. Interacts with TRIM5 (PubMed:22078707). Interacts with NDC80
CC (PubMed:9295362, PubMed:10409732). Interacts with PAAF1
CC (PubMed:15831487). Interacts, in vitro, with the thyroid hormone
CC receptor (in a thyroid hormone T3-dependent manner) and with retinoid X
CC receptor (RXR) (By similarity). Interacts with ERCC6 (PubMed:26030138).
CC {ECO:0000250|UniProtKB:P62196, ECO:0000269|PubMed:10409732,
CC ECO:0000269|PubMed:15831487, ECO:0000269|PubMed:22078707,
CC ECO:0000269|PubMed:23824326, ECO:0000269|PubMed:26030138,
CC ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775,
CC ECO:0000269|PubMed:9295362}.
CC -!- INTERACTION:
CC P62195; Q9BYV9: BACH2; NbExp=3; IntAct=EBI-357745, EBI-1642333;
CC P62195; Q13515: BFSP2; NbExp=3; IntAct=EBI-357745, EBI-10229433;
CC P62195; Q8IYR0: CFAP206; NbExp=3; IntAct=EBI-357745, EBI-749051;
CC P62195; P19447: ERCC3; NbExp=4; IntAct=EBI-357745, EBI-1183307;
CC P62195; P62508-3: ESRRG; NbExp=3; IntAct=EBI-357745, EBI-12001340;
CC P62195; Q6FG41: FOS; NbExp=3; IntAct=EBI-357745, EBI-10198738;
CC P62195; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-357745, EBI-3044087;
CC P62195; Q15323: KRT31; NbExp=3; IntAct=EBI-357745, EBI-948001;
CC P62195; O76015: KRT38; NbExp=6; IntAct=EBI-357745, EBI-1047263;
CC P62195; Q6A162: KRT40; NbExp=5; IntAct=EBI-357745, EBI-10171697;
CC P62195; Q9BRP4: PAAF1; NbExp=2; IntAct=EBI-357745, EBI-1056358;
CC P62195; Q13371: PDCL; NbExp=16; IntAct=EBI-357745, EBI-5772890;
CC P62195; Q53GL0: PLEKHO1; NbExp=10; IntAct=EBI-357745, EBI-949945;
CC P62195; P35998: PSMC2; NbExp=11; IntAct=EBI-357745, EBI-359710;
CC P62195; P43686: PSMC4; NbExp=15; IntAct=EBI-357745, EBI-743997;
CC P62195; P62333: PSMC6; NbExp=14; IntAct=EBI-357745, EBI-357669;
CC P62195; Q13200: PSMD2; NbExp=10; IntAct=EBI-357745, EBI-357648;
CC P62195; P55036: PSMD4; NbExp=2; IntAct=EBI-357745, EBI-359318;
CC P62195; P10826-2: RARB; NbExp=3; IntAct=EBI-357745, EBI-8583223;
CC P62195; Q92753-1: RORB; NbExp=3; IntAct=EBI-357745, EBI-18560266;
CC P62195; P51449: RORC; NbExp=3; IntAct=EBI-357745, EBI-3908771;
CC P62195; Q96BD8: SKA1; NbExp=7; IntAct=EBI-357745, EBI-741854;
CC P62195; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-357745, EBI-1105213;
CC P62195; P48788: TNNI2; NbExp=3; IntAct=EBI-357745, EBI-7746394;
CC P62195; P09493-10: TPM1; NbExp=3; IntAct=EBI-357745, EBI-12123928;
CC P62195; P06753: TPM3; NbExp=3; IntAct=EBI-357745, EBI-355607;
CC P62195; Q01831: XPC; NbExp=2; IntAct=EBI-357745, EBI-372610;
CC P62195; P11275: Camk2a; Xeno; NbExp=4; IntAct=EBI-357745, EBI-2640645;
CC P62195; P08413: Camk2b; Xeno; NbExp=3; IntAct=EBI-357745, EBI-916155;
CC P62195; P03255-1; Xeno; NbExp=2; IntAct=EBI-357745, EBI-6692439;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P62195-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P62195-2; Sequence=VSP_045441;
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; D44467; BAA07919.1; -; mRNA.
DR EMBL; L38810; AAC41735.1; -; mRNA.
DR EMBL; AK290758; BAF83447.1; -; mRNA.
DR EMBL; AK291878; BAF84567.1; -; mRNA.
DR EMBL; AC015651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94270.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94271.1; -; Genomic_DNA.
DR EMBL; CH471109; EAW94272.1; -; Genomic_DNA.
DR EMBL; BC001932; AAH01932.1; -; mRNA.
DR EMBL; BC002367; AAH02367.3; -; mRNA.
DR EMBL; AF035309; AAB88187.1; -; mRNA.
DR CCDS; CCDS11645.1; -. [P62195-1]
DR CCDS; CCDS56043.1; -. [P62195-2]
DR PIR; S60343; S60343.
DR PIR; S65536; S65536.
DR RefSeq; NP_001186092.1; NM_001199163.1. [P62195-2]
DR RefSeq; NP_002796.4; NM_002805.5. [P62195-1]
DR PDB; 2KRK; NMR; -; A=320-395.
DR PDB; 3KW6; X-ray; 2.10 A; A=318-395.
DR PDB; 5GJQ; EM; 4.50 A; J=1-406.
DR PDB; 5GJR; EM; 3.50 A; J/x=1-406.
DR PDB; 5L4G; EM; 4.02 A; J=1-406.
DR PDB; 5LN3; EM; 6.80 A; J=1-406.
DR PDB; 5M32; EM; 3.80 A; h=38-392.
DR PDB; 5T0C; EM; 3.80 A; AC/BC=1-406.
DR PDB; 5T0G; EM; 4.40 A; C=9-406.
DR PDB; 5T0H; EM; 6.80 A; C=9-406.
DR PDB; 5T0I; EM; 8.00 A; C=9-406.
DR PDB; 5T0J; EM; 8.00 A; C=9-406.
DR PDB; 5VFP; EM; 4.20 A; C=11-402.
DR PDB; 5VFQ; EM; 4.20 A; C=11-402.
DR PDB; 5VFR; EM; 4.90 A; C=11-402.
DR PDB; 5VFS; EM; 3.60 A; C=9-397.
DR PDB; 5VFT; EM; 7.00 A; C=11-394.
DR PDB; 5VFU; EM; 5.80 A; C=11-394.
DR PDB; 5VGZ; EM; 3.70 A; C=11-128.
DR PDB; 5VHF; EM; 5.70 A; C=11-395.
DR PDB; 5VHH; EM; 6.10 A; C=11-395.
DR PDB; 5VHI; EM; 6.80 A; C=11-395.
DR PDB; 5VHJ; EM; 8.50 A; C=130-395.
DR PDB; 5VHM; EM; 8.30 A; C=130-395.
DR PDB; 5VHN; EM; 7.30 A; C=130-395.
DR PDB; 5VHO; EM; 8.30 A; C=130-395.
DR PDB; 5VHP; EM; 7.90 A; C=130-395.
DR PDB; 5VHQ; EM; 8.90 A; C=130-395.
DR PDB; 5VHR; EM; 7.70 A; C=130-395.
DR PDB; 5VHS; EM; 8.80 A; C=11-395.
DR PDB; 6MSB; EM; 3.00 A; C=9-406.
DR PDB; 6MSD; EM; 3.20 A; C=9-406.
DR PDB; 6MSG; EM; 3.50 A; C=9-406.
DR PDB; 6MSH; EM; 3.60 A; C=9-406.
DR PDB; 6MSJ; EM; 3.30 A; C=9-406.
DR PDB; 6MSK; EM; 3.20 A; C=9-406.
DR PDB; 6WJD; EM; 4.80 A; C=9-406.
DR PDB; 6WJN; EM; 5.70 A; C=11-402.
DR PDBsum; 2KRK; -.
DR PDBsum; 3KW6; -.
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; 6MSG; -.
DR PDBsum; 6MSH; -.
DR PDBsum; 6MSJ; -.
DR PDBsum; 6MSK; -.
DR PDBsum; 6WJD; -.
DR PDBsum; 6WJN; -.
DR AlphaFoldDB; P62195; -.
DR BMRB; P62195; -.
DR SMR; P62195; -.
DR BioGRID; 111678; 365.
DR ComplexPortal; CPX-5993; 26S Proteasome complex.
DR CORUM; P62195; -.
DR DIP; DIP-36645N; -.
DR IntAct; P62195; 158.
DR MINT; P62195; -.
DR STRING; 9606.ENSP00000310572; -.
DR ChEMBL; CHEMBL2364701; -.
DR GlyGen; P62195; 1 site.
DR iPTMnet; P62195; -.
DR MetOSite; P62195; -.
DR PhosphoSitePlus; P62195; -.
DR SwissPalm; P62195; -.
DR BioMuta; PSMC5; -.
DR DMDM; 49065819; -.
DR EPD; P62195; -.
DR jPOST; P62195; -.
DR MassIVE; P62195; -.
DR MaxQB; P62195; -.
DR PaxDb; P62195; -.
DR PeptideAtlas; P62195; -.
DR PRIDE; P62195; -.
DR ProteomicsDB; 1859; -.
DR ProteomicsDB; 57371; -. [P62195-1]
DR Antibodypedia; 18742; 313 antibodies from 35 providers.
DR DNASU; 5705; -.
DR Ensembl; ENST00000310144.11; ENSP00000310572.6; ENSG00000087191.13. [P62195-1]
DR Ensembl; ENST00000375812.8; ENSP00000364970.4; ENSG00000087191.13. [P62195-2]
DR Ensembl; ENST00000580864.5; ENSP00000462495.1; ENSG00000087191.13. [P62195-2]
DR Ensembl; ENST00000581882.5; ENSP00000463938.1; ENSG00000087191.13. [P62195-2]
DR GeneID; 5705; -.
DR KEGG; hsa:5705; -.
DR MANE-Select; ENST00000310144.11; ENSP00000310572.6; NM_002805.6; NP_002796.4.
DR UCSC; uc002jcb.4; human. [P62195-1]
DR CTD; 5705; -.
DR DisGeNET; 5705; -.
DR GeneCards; PSMC5; -.
DR HGNC; HGNC:9552; PSMC5.
DR HPA; ENSG00000087191; Low tissue specificity.
DR MIM; 601681; gene.
DR neXtProt; NX_P62195; -.
DR NIAGADS; ENSG00000087191; -.
DR OpenTargets; ENSG00000087191; -.
DR PharmGKB; PA33897; -.
DR VEuPathDB; HostDB:ENSG00000087191; -.
DR eggNOG; KOG0728; Eukaryota.
DR GeneTree; ENSGT01020000230346; -.
DR HOGENOM; CLU_000688_2_0_1; -.
DR InParanoid; P62195; -.
DR OMA; TANCRVA; -.
DR OrthoDB; 571919at2759; -.
DR PhylomeDB; P62195; -.
DR PathwayCommons; P62195; -.
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; P62195; -.
DR SIGNOR; P62195; -.
DR BioGRID-ORCS; 5705; 596 hits in 1054 CRISPR screens.
DR ChiTaRS; PSMC5; human.
DR EvolutionaryTrace; P62195; -.
DR GeneWiki; PSMC5; -.
DR GenomeRNAi; 5705; -.
DR Pharos; P62195; Tbio.
DR PRO; PR:P62195; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P62195; protein.
DR Bgee; ENSG00000087191; Expressed in tendon of biceps brachii and 213 other tissues.
DR ExpressionAtlas; P62195; baseline and differential.
DR Genevisible; P62195; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031597; C:cytosolic proteasome complex; IEA:Ensembl.
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:0031595; C:nuclear proteasome complex; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0098794; C:postsynapse; IEA:Ensembl.
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:Ensembl.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0140296; F:general transcription initiation factor binding; IPI:UniProtKB.
DR GO; GO:0036402; F:proteasome-activating activity; ISS:UniProtKB.
DR GO; GO:0017025; F:TBP-class protein binding; IEA:Ensembl.
DR GO; GO:0031531; F:thyrotropin-releasing hormone receptor binding; IPI:UniProtKB.
DR GO; GO:0008134; F:transcription factor binding; IDA:GO_Central.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0043069; P:negative regulation of programmed cell death; NAS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
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:0045893; P:positive regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA: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 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; Alternative splicing; ATP-binding; Cytoplasm;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Proteasome;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25489052,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..406
FT /note="26S proteasome regulatory subunit 8"
FT /id="PRO_0000084721"
FT REGION 186..406
FT /note="May mediate interaction with PRPF9"
FT /evidence="ECO:0000250|UniProtKB:P62196"
FT BINDING 190..197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:25489052,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 222
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..8
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045441"
FT VARIANT 60
FT /note="R -> Q (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035901"
FT VARIANT 258
FT /note="R -> W (in dbSNP:rs11543211)"
FT /id="VAR_048119"
FT CONFLICT 61
FT /note="E -> R (in Ref. 1; BAA07919)"
FT /evidence="ECO:0000305"
FT CONFLICT 127..128
FT /note="LP -> ML (in Ref. 6; AAB88187)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="D -> S (in Ref. 2; AAC41735)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="T -> Q (in Ref. 2; AAC41735)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="I -> M (in Ref. 2; AAC41735)"
FT /evidence="ECO:0000305"
FT HELIX 322..333
FT /evidence="ECO:0007829|PDB:3KW6"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:3KW6"
FT HELIX 344..349
FT /evidence="ECO:0007829|PDB:3KW6"
FT HELIX 356..372
FT /evidence="ECO:0007829|PDB:3KW6"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:3KW6"
FT HELIX 380..391
FT /evidence="ECO:0007829|PDB:3KW6"
FT MOD_RES P62195-2:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 406 AA; 45626 MW; 29C6410C4A85A7F7 CRC64;
MALDGPEQME LEEGKAGSGL RQYYLSKIEE LQLIVNDKSQ NLRRLQAQRN ELNAKVRLLR
EELQLLQEQG SYVGEVVRAM DKKKVLVKVH PEGKFVVDVD KNIDINDVTP NCRVALRNDS
YTLHKILPNK VDPLVSLMMV EKVPDSTYEM IGGLDKQIKE IKEVIELPVK HPELFEALGI
AQPKGVLLYG PPGTGKTLLA RAVAHHTDCT FIRVSGSELV QKFIGEGARM VRELFVMARE
HAPSIIFMDE IDSIGSSRLE GGSGGDSEVQ RTMLELLNQL DGFEATKNIK VIMATNRIDI
LDSALLRPGR IDRKIEFPPP NEEARLDILK IHSRKMNLTR GINLRKIAEL MPGASGAEVK
GVCTEAGMYA LRERRVHVTQ EDFEMAVAKV MQKDSEKNMS IKKLWK
