PRS6B_HUMAN
ID PRS6B_HUMAN Reviewed; 418 AA.
AC P43686; Q96FV5; Q9UBM3; Q9UEX3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=26S proteasome regulatory subunit 6B;
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT3;
DE AltName: Full=MB67-interacting protein;
DE AltName: Full=MIP224;
DE AltName: Full=Proteasome 26S subunit ATPase 4;
DE AltName: Full=Tat-binding protein 7;
DE Short=TBP-7;
GN Name=PSMC4; Synonyms=MIP224, TBP7;
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=8419915; DOI=10.1073/pnas.90.1.138;
RA Ohana B., Moore P.A., Ruben S.M., Southgate C.D., Green M.R., Rosen C.A.;
RT "The type 1 human immunodeficiency virus Tat binding protein is a
RT transcriptional activator belonging to an additional family of
RT evolutionarily conserved genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:138-142(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH NR1I3.
RX PubMed=8603043; DOI=10.1016/0960-0760(95)00220-0;
RA Choi H.S., Seol W., Moore D.D.;
RT "A component of the 26S proteasome binds on orphan member of the nuclear
RT hormone receptor superfamily.";
RL J. Steroid Biochem. Mol. Biol. 56:23-30(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Bi A., Yu L., Zheng L.;
RT "Cloning and expression analysis of a novel human gene homologous to mouse
RT proteasomal ATPase (Tat-binding protein 7).";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung, Pancreas, and Skin;
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 PROTEIN SEQUENCE OF 1-10; 218-229; 307-313 AND 343-369, ACETYLATION AT
RP MET-1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.;
RL Submitted (JUL-2007) to UniProtKB.
RN [9]
RP PARTIAL PROTEIN SEQUENCE, AND FUNCTION.
RX PubMed=8060531; DOI=10.1515/bchm3.1994.375.4.237;
RA Dubiel W., Ferrell K., Rechsteiner M.;
RT "Tat-binding protein 7 is a subunit of the 26S protease.";
RL Biol. Chem. Hoppe-Seyler 375:237-240(1994).
RN [10]
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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND IDENTIFICATION BY
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-28, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-397 AND LYS-401, 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [19]
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 [20]
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 [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-25, AND IDENTIFICATION BY
RP 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 [24]
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 [25]
RP INTERACTION WITH ZFAND1.
RX PubMed=29804830; DOI=10.1016/j.molcel.2018.04.021;
RA Turakhiya A., Meyer S.R., Marincola G., Boehm S., Vanselow J.T.,
RA Schlosser A., Hofmann K., Buchberger A.;
RT "ZFAND1 recruits p97 and the 26S proteasome to promote the clearance of
RT arsenite-induced stress granules.";
RL Mol. Cell 70:906-919(2018).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 337-418 IN COMPLEX WITH MOUSE
RP PSMD10.
RX PubMed=17292836; DOI=10.1016/j.str.2006.11.015;
RA Nakamura Y., Nakano K., Umehara T., Kimura M., Hayashizaki Y., Tanaka A.,
RA Horikoshi M., Padmanabhan B., Yokoyama S.;
RT "Structure of the oncoprotein gankyrin in complex with S6 ATPase of the 26S
RT proteasome.";
RL Structure 15:179-189(2007).
RN [27]
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 [28]
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. PSMC4 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, ECO:0000269|PubMed:8060531}.
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 PSMC4 and
CC few additional components (PubMed:27428775,PubMed:27342858). Interacts
CC with NR1I3. Interacts with PAAF1 (PubMed:15831487). Interacts with
CC TRIM5 (PubMed:22078707). Interacts with ZFAND1 (PubMed:29804830).
CC {ECO:0000269|PubMed:15831487, ECO:0000269|PubMed:17292836,
CC ECO:0000269|PubMed:22078707, ECO:0000269|PubMed:27342858,
CC ECO:0000269|PubMed:27428775, ECO:0000269|PubMed:29804830,
CC ECO:0000269|PubMed:8603043}.
CC -!- INTERACTION:
CC P43686; P27797: CALR; NbExp=3; IntAct=EBI-743997, EBI-1049597;
CC P43686; P36957: DLST; NbExp=5; IntAct=EBI-743997, EBI-351007;
CC P43686; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-743997, EBI-1055945;
CC P43686; P62191: PSMC1; NbExp=2; IntAct=EBI-743997, EBI-357598;
CC P43686; P62195: PSMC5; NbExp=15; IntAct=EBI-743997, EBI-357745;
CC P43686; P62333: PSMC6; NbExp=5; IntAct=EBI-743997, EBI-357669;
CC P43686; O75832: PSMD10; NbExp=23; IntAct=EBI-743997, EBI-752185;
CC P43686; Q9Z2X2: Psmd10; Xeno; NbExp=4; IntAct=EBI-743997, EBI-8377084;
CC P43686-2; P00441: SOD1; NbExp=3; IntAct=EBI-21522939, EBI-990792;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P43686-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P43686-2; Sequence=VSP_000022;
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; AF038965; AAC26843.1; -; mRNA.
DR EMBL; U27515; AAC99817.1; -; mRNA.
DR EMBL; AF020736; AAC32612.1; -; mRNA.
DR EMBL; BT007232; AAP35896.1; -; mRNA.
DR EMBL; AC007842; AAD39267.1; -; Genomic_DNA.
DR EMBL; BC000343; AAH00343.1; -; mRNA.
DR EMBL; BC010396; AAH10396.1; -; mRNA.
DR EMBL; BC014488; AAH14488.1; -; mRNA.
DR CCDS; CCDS12547.1; -. [P43686-1]
DR CCDS; CCDS46076.1; -. [P43686-2]
DR RefSeq; NP_006494.1; NM_006503.3. [P43686-1]
DR RefSeq; NP_694546.1; NM_153001.2. [P43686-2]
DR PDB; 2DVW; X-ray; 2.30 A; B=337-418.
DR PDB; 5GJQ; EM; 4.50 A; K=1-418.
DR PDB; 5GJR; EM; 3.50 A; K/y=1-418.
DR PDB; 5L4G; EM; 4.02 A; K=1-418.
DR PDB; 5LN3; EM; 6.80 A; K=1-418.
DR PDB; 5M32; EM; 3.80 A; e=1-418.
DR PDB; 5T0C; EM; 3.80 A; AD/BD=1-418.
DR PDB; 5T0G; EM; 4.40 A; D=1-418.
DR PDB; 5T0H; EM; 6.80 A; D=1-418.
DR PDB; 5T0I; EM; 8.00 A; D=1-418.
DR PDB; 5T0J; EM; 8.00 A; D=1-418.
DR PDB; 5VFP; EM; 4.20 A; D=39-418.
DR PDB; 5VFQ; EM; 4.20 A; D=39-418.
DR PDB; 5VFR; EM; 4.90 A; D=39-418.
DR PDB; 5VFS; EM; 3.60 A; D=1-418.
DR PDB; 5VFT; EM; 7.00 A; D=39-418.
DR PDB; 5VFU; EM; 5.80 A; D=39-418.
DR PDB; 5VGZ; EM; 3.70 A; D=39-145.
DR PDB; 5VHF; EM; 5.70 A; D=39-406.
DR PDB; 5VHH; EM; 6.10 A; D=39-406.
DR PDB; 5VHI; EM; 6.80 A; D=39-406.
DR PDB; 5VHJ; EM; 8.50 A; D=145-406.
DR PDB; 5VHM; EM; 8.30 A; D=145-406.
DR PDB; 5VHN; EM; 7.30 A; D=145-406.
DR PDB; 5VHO; EM; 8.30 A; D=145-406.
DR PDB; 5VHP; EM; 7.90 A; D=145-406.
DR PDB; 5VHQ; EM; 8.90 A; D=145-406.
DR PDB; 5VHR; EM; 7.70 A; D=145-406.
DR PDB; 5VHS; EM; 8.80 A; D=39-406.
DR PDB; 6MSB; EM; 3.00 A; D=1-418.
DR PDB; 6MSD; EM; 3.20 A; D=1-418.
DR PDB; 6MSE; EM; 3.30 A; P/p=152-198.
DR PDB; 6MSG; EM; 3.50 A; D=1-418.
DR PDB; 6MSH; EM; 3.60 A; D=1-418.
DR PDB; 6MSJ; EM; 3.30 A; D=1-418.
DR PDB; 6MSK; EM; 3.20 A; D=1-418.
DR PDB; 6WJD; EM; 4.80 A; D=1-418.
DR PDB; 6WJN; EM; 5.70 A; D=39-418.
DR PDBsum; 2DVW; -.
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; 6WJD; -.
DR PDBsum; 6WJN; -.
DR AlphaFoldDB; P43686; -.
DR SMR; P43686; -.
DR BioGRID; 111677; 262.
DR ComplexPortal; CPX-5993; 26S Proteasome complex.
DR CORUM; P43686; -.
DR DIP; DIP-29274N; -.
DR IntAct; P43686; 99.
DR MINT; P43686; -.
DR STRING; 9606.ENSP00000157812; -.
DR BindingDB; P43686; -.
DR ChEMBL; CHEMBL3831205; -.
DR GlyGen; P43686; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P43686; -.
DR MetOSite; P43686; -.
DR PhosphoSitePlus; P43686; -.
DR SwissPalm; P43686; -.
DR BioMuta; PSMC4; -.
DR DMDM; 20532409; -.
DR OGP; P43686; -.
DR EPD; P43686; -.
DR jPOST; P43686; -.
DR MassIVE; P43686; -.
DR MaxQB; P43686; -.
DR PaxDb; P43686; -.
DR PeptideAtlas; P43686; -.
DR PRIDE; P43686; -.
DR ProteomicsDB; 55650; -. [P43686-1]
DR ProteomicsDB; 55651; -. [P43686-2]
DR Antibodypedia; 1215; 242 antibodies from 32 providers.
DR DNASU; 5704; -.
DR Ensembl; ENST00000157812.7; ENSP00000157812.1; ENSG00000013275.8. [P43686-1]
DR Ensembl; ENST00000455878.2; ENSP00000413869.1; ENSG00000013275.8. [P43686-2]
DR Ensembl; ENST00000629691.3; ENSP00000487367.1; ENSG00000281221.3. [P43686-1]
DR Ensembl; ENST00000630857.1; ENSP00000485851.1; ENSG00000281221.3. [P43686-2]
DR GeneID; 5704; -.
DR KEGG; hsa:5704; -.
DR MANE-Select; ENST00000157812.7; ENSP00000157812.1; NM_006503.4; NP_006494.1.
DR UCSC; uc002omq.5; human. [P43686-1]
DR CTD; 5704; -.
DR DisGeNET; 5704; -.
DR GeneCards; PSMC4; -.
DR HGNC; HGNC:9551; PSMC4.
DR HPA; ENSG00000013275; Low tissue specificity.
DR MIM; 602707; gene.
DR neXtProt; NX_P43686; -.
DR OpenTargets; ENSG00000013275; -.
DR PharmGKB; PA33896; -.
DR VEuPathDB; HostDB:ENSG00000013275; -.
DR eggNOG; KOG0727; Eukaryota.
DR GeneTree; ENSGT01020000230346; -.
DR HOGENOM; CLU_000688_2_0_1; -.
DR InParanoid; P43686; -.
DR OMA; AYAAQVK; -.
DR PhylomeDB; P43686; -.
DR TreeFam; TF106227; -.
DR PathwayCommons; P43686; -.
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; P43686; -.
DR SIGNOR; P43686; -.
DR BioGRID-ORCS; 5704; 738 hits in 1089 CRISPR screens.
DR ChiTaRS; PSMC4; human.
DR EvolutionaryTrace; P43686; -.
DR GeneWiki; PSMC4; -.
DR GenomeRNAi; 5704; -.
DR Pharos; P43686; Tchem.
DR PRO; PR:P43686; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P43686; protein.
DR Bgee; ENSG00000013275; Expressed in gastrocnemius and 103 other tissues.
DR ExpressionAtlas; P43686; baseline and differential.
DR Genevisible; P43686; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0031597; C:cytosolic proteasome complex; IEA:Ensembl.
DR GO; GO:0016234; C:inclusion body; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; HDA: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:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0036402; F:proteasome-activating activity; IBA:GO_Central.
DR GO; GO:0001824; P:blastocyst development; IEA:Ensembl.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; TAS:ProtInc.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR IDEAL; IID00236; -.
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; IPR035256; PSMC4.
DR PANTHER; PTHR23073:SF120; PTHR23073:SF120; 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; Alternative splicing; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Proteasome; Reference proteome.
FT CHAIN 1..418
FT /note="26S proteasome regulatory subunit 6B"
FT /id="PRO_0000084686"
FT BINDING 206..213
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 25
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17323924,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 397
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 401
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 46..76
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_000022"
FT CONFLICT 73
FT /note="L -> F (in Ref. 4; AAC32612)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="N -> S (in Ref. 4; AAC32612)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="T -> A (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="D -> G (in Ref. 4; AAC32612)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="L -> V (in Ref. 4; AAC32612)"
FT /evidence="ECO:0000305"
FT HELIX 338..348
FT /evidence="ECO:0007829|PDB:2DVW"
FT TURN 349..351
FT /evidence="ECO:0007829|PDB:2DVW"
FT HELIX 361..364
FT /evidence="ECO:0007829|PDB:2DVW"
FT HELIX 372..388
FT /evidence="ECO:0007829|PDB:2DVW"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:2DVW"
FT HELIX 396..406
FT /evidence="ECO:0007829|PDB:2DVW"
SQ SEQUENCE 418 AA; 47366 MW; 80F9523C61B88F0C CRC64;
MEEIGILVEK AQDEIPALSV SRPQTGLSFL GPEPEDLEDL YSRYKKLQQE LEFLEVQEEY
IKDEQKNLKK EFLHAQEEVK RIQSIPLVIG QFLEAVDQNT AIVGSTTGSN YYVRILSTID
RELLKPNASV ALHKHSNALV DVLPPEADSS IMMLTSDQKP DVMYADIGGM DIQKQEVREA
VELPLTHFEL YKQIGIDPPR GVLMYGPPGC GKTMLAKAVA HHTTAAFIRV VGSEFVQKYL
GEGPRMVRDV FRLAKENAPA IIFIDEIDAI ATKRFDAQTG ADREVQRILL ELLNQMDGFD
QNVNVKVIMA TNRADTLDPA LLRPGRLDRK IEFPLPDRRQ KRLIFSTITS KMNLSEEVDL
EDYVARPDKI SGADINSICQ ESGMLAVREN RYIVLAKDFE KAYKTVIKKD EQEHEFYK
