GenomeNet

Database: UniProt
Entry: P43686
LinkDB: P43686
Original site: P43686 
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   02-JUN-2021, entry version 215.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   SMR; P43686; -.
DR   BioGRID; 111677; 209.
DR   ComplexPortal; CPX-5993; 26S Proteasome complex.
DR   CORUM; P43686; -.
DR   DIP; DIP-29274N; -.
DR   IntAct; P43686; 92.
DR   MINT; P43686; -.
DR   STRING; 9606.ENSP00000157812; -.
DR   ChEMBL; CHEMBL3831205; -.
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; 231 antibodies.
DR   DNASU; 5704; -.
DR   Ensembl; ENST00000157812; ENSP00000157812; ENSG00000013275. [P43686-1]
DR   Ensembl; ENST00000455878; ENSP00000413869; ENSG00000013275. [P43686-2]
DR   Ensembl; ENST00000629691; ENSP00000487367; ENSG00000281221. [P43686-1]
DR   Ensembl; ENST00000630857; ENSP00000485851; ENSG00000281221. [P43686-2]
DR   GeneID; 5704; -.
DR   KEGG; hsa:5704; -.
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:ENSG00000013275.7; -.
DR   eggNOG; KOG0727; Eukaryota.
DR   GeneTree; ENSGT01020000230346; -.
DR   HOGENOM; CLU_000688_2_0_1; -.
DR   InParanoid; P43686; -.
DR   OMA; QDIGGMD; -.
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-68827; CDT1 association with the CDC6:ORC:origin 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-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SIGNOR; P43686; -.
DR   BioGRID-ORCS; 5704; 730 hits in 1003 CRISPR screens.
DR   ChiTaRS; PSMC4; human.
DR   EvolutionaryTrace; P43686; -.
DR   GeneWiki; PSMC4; -.
DR   GenomeRNAi; 5704; -.
DR   Pharos; P43686; Tbio.
DR   PRO; PR:P43686; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; P43686; protein.
DR   Bgee; ENSG00000013275; Expressed in gastrocnemius and 242 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; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; TAS:ProtInc.
DR   GO; GO:0036402; F:proteasome-activating ATPase activity; IEA:InterPro.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
DR   GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR   GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0070498; P:interleukin-1-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
DR   GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; TAS:Reactome.
DR   GO; GO:0045899; P:positive regulation of RNA polymerase II transcription preinitiation complex assembly; IBA:GO_Central.
DR   GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR   GO; GO:0036388; P:pre-replicative complex assembly; TAS:Reactome.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR   GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
DR   GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR   GO; GO:0006508; P:proteolysis; TAS:ProtInc.
DR   GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR   GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
DR   GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; TAS:Reactome.
DR   GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
DR   GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR   GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
DR   GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032501; Prot_ATP_ID_OB.
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   NP_BIND         206..213
FT                   /note="ATP"
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
//
DBGET integrated database retrieval system