PRS4_HUMAN
ID PRS4_HUMAN Reviewed; 440 AA.
AC P62191; B4DR63; P49014; Q03527; Q6IAW0; Q6NW36; Q96AZ3;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=26S proteasome regulatory subunit 4;
DE Short=P26s4;
DE AltName: Full=26S proteasome AAA-ATPase subunit RPT2;
DE AltName: Full=Proteasome 26S subunit ATPase 1;
GN Name=PSMC1;
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), AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1429620; DOI=10.1016/s0021-9258(18)50002-8;
RA Dubiel W., Ferrell K., Pratt G., Rechsteiner M.C.;
RT "Subunit 4 of the 26 S protease is a member of a novel eukaryotic ATPase
RT family.";
RL J. Biol. Chem. 267:22699-22702(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow, Brain, Lung, and Prostate;
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 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 [7]
RP INTERACTION WITH SCA7.
RX PubMed=11734547; DOI=10.1093/hmg/10.24.2821;
RA Matilla A., Gorbea C., Einum D.D., Townsend J., Michalik A.,
RA van Broeckhoven C., Jensen C.C., Murphy K.J., Ptacek L.J., Fu Y.H.;
RT "Association of ataxin-7 with the proteasome subunit S4 of the 19S
RT regulatory complex.";
RL Hum. Mol. Genet. 10:2821-2831(2001).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-439, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [9]
RP INTERACTION WITH NGLY1.
RX PubMed=15358861; DOI=10.1073/pnas.0405663101;
RA Katiyar S., Li G., Lennarz W.J.;
RT "A complex between peptide:N-glycanase and two proteasome-linked proteins
RT suggests a mechanism for the degradation of misfolded glycoproteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13774-13779(2004).
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 UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-237, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Mammary cancer;
RX PubMed=17370265; DOI=10.1002/pmic.200600410;
RA Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
RT "Tryptic digestion of ubiquitin standards reveals an improved strategy for
RT identifying ubiquitinated proteins by mass spectrometry.";
RL Proteomics 7:868-874(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND IDENTIFICATION BY MASS
RP 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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-258, 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 [15]
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 [16]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-53 AND THR-434, AND
RP IDENTIFICATION BY 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-53, 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 [19]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25255805; DOI=10.1038/ncomms5919;
RA Thinon E., Serwa R.A., Broncel M., Brannigan J.A., Brassat U., Wright M.H.,
RA Heal W.P., Wilkinson A.J., Mann D.J., Tate E.W.;
RT "Global profiling of co- and post-translationally N-myristoylated proteomes
RT in human cells.";
RL Nat. Commun. 5:4919-4919(2014).
RN [20]
RP MYRISTOYLATION AT GLY-2, CLEAVAGE OF INITIATOR METHIONINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25807930; DOI=10.1002/anie.201500342;
RA Broncel M., Serwa R.A., Ciepla P., Krause E., Dallman M.J., Magee A.I.,
RA Tate E.W.;
RT "Multifunctional reagents for quantitative proteome-wide analysis of
RT protein modification in human cells and dynamic profiling of protein
RT lipidation during vertebrate development.";
RL Angew. Chem. Int. Ed. 54:5948-5951(2015).
RN [21]
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 [22]
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. PSMC1 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 PSMC1 and
CC few additional components (PubMed:27428775, PubMed:27342858). Interacts
CC with SCA7 (PubMed:11734547). Interacts with NGLY1 (PubMed:15358861).
CC Interacts with PAAF1 (PubMed:15831487). {ECO:0000269|PubMed:11734547,
CC ECO:0000269|PubMed:15358861, ECO:0000269|PubMed:15831487,
CC ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775}.
CC -!- INTERACTION:
CC P62191; O60341: KDM1A; NbExp=2; IntAct=EBI-357598, EBI-710124;
CC P62191; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-357598, EBI-739832;
CC P62191; P43356: MAGEA2B; NbExp=3; IntAct=EBI-357598, EBI-5650739;
CC P62191; P50222: MEOX2; NbExp=3; IntAct=EBI-357598, EBI-748397;
CC P62191; Q3KNR5: PAX4; NbExp=3; IntAct=EBI-357598, EBI-10240813;
CC P62191; P35998: PSMC2; NbExp=6; IntAct=EBI-357598, EBI-359710;
CC P62191; P43686: PSMC4; NbExp=2; IntAct=EBI-357598, EBI-743997;
CC P62191; P62333: PSMC6; NbExp=7; IntAct=EBI-357598, EBI-357669;
CC P62191; Q13200: PSMD2; NbExp=16; IntAct=EBI-357598, EBI-357648;
CC P62191; P55036: PSMD4; NbExp=2; IntAct=EBI-357598, EBI-359318;
CC P62191; Q16401: PSMD5; NbExp=12; IntAct=EBI-357598, EBI-752143;
CC P62191; P37840: SNCA; NbExp=3; IntAct=EBI-357598, EBI-985879;
CC P62191; P00441: SOD1; NbExp=5; IntAct=EBI-357598, EBI-990792;
CC P62191; O43463: SUV39H1; NbExp=2; IntAct=EBI-357598, EBI-349968;
CC P62191; P55072: VCP; NbExp=3; IntAct=EBI-357598, EBI-355164;
CC P62191; Q96BR9: ZBTB8A; NbExp=3; IntAct=EBI-357598, EBI-742740;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Membrane {ECO:0000305};
CC Lipid-anchor {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P62191-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P62191-2; Sequence=VSP_055768;
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; L02426; AAA35484.1; -; mRNA.
DR EMBL; AK299121; BAG61175.1; -; mRNA.
DR EMBL; CR457044; CAG33325.1; -; mRNA.
DR EMBL; AL161662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355074; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000512; AAH00512.1; -; mRNA.
DR EMBL; BC016368; AAH16368.1; -; mRNA.
DR EMBL; BC067741; AAH67741.1; -; mRNA.
DR EMBL; BC073818; AAH73818.1; -; mRNA.
DR CCDS; CCDS32139.1; -. [P62191-1]
DR CCDS; CCDS81837.1; -. [P62191-2]
DR PIR; A44468; A44468.
DR RefSeq; NP_001317141.1; NM_001330212.1. [P62191-2]
DR RefSeq; NP_002793.2; NM_002802.2. [P62191-1]
DR RefSeq; XP_016876959.1; XM_017021470.1. [P62191-2]
DR PDB; 5GJQ; EM; 4.50 A; I=1-440.
DR PDB; 5GJR; EM; 3.50 A; I/w=1-440.
DR PDB; 5L4G; EM; 4.02 A; I=1-440.
DR PDB; 5LN3; EM; 6.80 A; I=1-440.
DR PDB; 5M32; EM; 3.80 A; d=1-428.
DR PDB; 5T0C; EM; 3.80 A; AB/BB=1-440.
DR PDB; 5T0G; EM; 4.40 A; B=1-440.
DR PDB; 5T0H; EM; 6.80 A; B=1-440.
DR PDB; 5T0I; EM; 8.00 A; B=1-440.
DR PDB; 5T0J; EM; 8.00 A; B=1-440.
DR PDB; 5VFP; EM; 4.20 A; B=52-440.
DR PDB; 5VFQ; EM; 4.20 A; B=52-440.
DR PDB; 5VFR; EM; 4.90 A; B=52-440.
DR PDB; 5VFS; EM; 3.60 A; B=65-433.
DR PDB; 5VFT; EM; 7.00 A; B=93-433.
DR PDB; 5VFU; EM; 5.80 A; B=93-440.
DR PDB; 5VGZ; EM; 3.70 A; B=93-165.
DR PDB; 5VHF; EM; 5.70 A; B=93-432.
DR PDB; 5VHH; EM; 6.10 A; B=93-432.
DR PDB; 5VHI; EM; 6.80 A; B=93-433.
DR PDB; 5VHJ; EM; 8.50 A; B=167-432.
DR PDB; 5VHM; EM; 8.30 A; B=167-432.
DR PDB; 5VHN; EM; 7.30 A; B=167-432.
DR PDB; 5VHO; EM; 8.30 A; B=167-433.
DR PDB; 5VHP; EM; 7.90 A; B=167-432.
DR PDB; 5VHQ; EM; 8.90 A; B=167-433.
DR PDB; 5VHR; EM; 7.70 A; B=167-433.
DR PDB; 5VHS; EM; 8.80 A; B=93-433.
DR PDB; 6MSB; EM; 3.00 A; B=1-440.
DR PDB; 6MSD; EM; 3.20 A; B=1-440.
DR PDB; 6MSG; EM; 3.50 A; B=1-440.
DR PDB; 6MSH; EM; 3.60 A; B=1-440.
DR PDB; 6MSJ; EM; 3.30 A; B=1-440.
DR PDB; 6MSK; EM; 3.20 A; B=1-440.
DR PDB; 6WJD; EM; 4.80 A; B=1-440.
DR PDB; 6WJN; EM; 5.70 A; B=52-440.
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; P62191; -.
DR SMR; P62191; -.
DR BioGRID; 111673; 263.
DR ComplexPortal; CPX-5993; 26S Proteasome complex.
DR CORUM; P62191; -.
DR IntAct; P62191; 121.
DR MINT; P62191; -.
DR STRING; 9606.ENSP00000261303; -.
DR ChEMBL; CHEMBL2364701; -.
DR CarbonylDB; P62191; -.
DR GlyGen; P62191; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P62191; -.
DR MetOSite; P62191; -.
DR PhosphoSitePlus; P62191; -.
DR SwissPalm; P62191; -.
DR BioMuta; PSMC1; -.
DR DMDM; 49065817; -.
DR EPD; P62191; -.
DR jPOST; P62191; -.
DR MassIVE; P62191; -.
DR MaxQB; P62191; -.
DR PaxDb; P62191; -.
DR PeptideAtlas; P62191; -.
DR PRIDE; P62191; -.
DR ProteomicsDB; 4926; -.
DR ProteomicsDB; 57370; -. [P62191-1]
DR Antibodypedia; 82; 185 antibodies from 33 providers.
DR DNASU; 5700; -.
DR Ensembl; ENST00000261303.13; ENSP00000261303.8; ENSG00000100764.14. [P62191-1]
DR Ensembl; ENST00000543772.2; ENSP00000445147.2; ENSG00000100764.14. [P62191-2]
DR GeneID; 5700; -.
DR KEGG; hsa:5700; -.
DR MANE-Select; ENST00000261303.13; ENSP00000261303.8; NM_002802.3; NP_002793.2.
DR UCSC; uc001xyg.4; human. [P62191-1]
DR CTD; 5700; -.
DR DisGeNET; 5700; -.
DR GeneCards; PSMC1; -.
DR HGNC; HGNC:9547; PSMC1.
DR HPA; ENSG00000100764; Tissue enhanced (skeletal).
DR MIM; 602706; gene.
DR neXtProt; NX_P62191; -.
DR OpenTargets; ENSG00000100764; -.
DR PharmGKB; PA33892; -.
DR VEuPathDB; HostDB:ENSG00000100764; -.
DR eggNOG; KOG0726; Eukaryota.
DR GeneTree; ENSGT01020000230346; -.
DR HOGENOM; CLU_000688_2_3_1; -.
DR InParanoid; P62191; -.
DR OMA; ARCKLRY; -.
DR PhylomeDB; P62191; -.
DR TreeFam; TF106226; -.
DR PathwayCommons; P62191; -.
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-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
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; P62191; -.
DR SIGNOR; P62191; -.
DR BioGRID-ORCS; 5700; 724 hits in 1086 CRISPR screens.
DR ChiTaRS; PSMC1; human.
DR GeneWiki; PSMC1; -.
DR GenomeRNAi; 5700; -.
DR Pharos; P62191; Tbio.
DR PRO; PR:P62191; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P62191; protein.
DR Bgee; ENSG00000100764; Expressed in calcaneal tendon and 99 other tissues.
DR ExpressionAtlas; P62191; baseline and differential.
DR Genevisible; P62191; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
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: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; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0017025; F:TBP-class protein binding; IEA:Ensembl.
DR GO; GO:1901215; P:negative regulation of neuron death; IEA:Ensembl.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR005937; 26S_Psome_P45-like.
DR InterPro; IPR035244; 26S_subunit_4.
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 PANTHER; PTHR23073:SF77; PTHR23073:SF77; 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; Isopeptide bond; Lipoprotein; Membrane;
KW Myristate; Nucleotide-binding; Nucleus; Phosphoprotein; Proteasome;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:22223895,
FT ECO:0000269|PubMed:25255805, ECO:0000269|PubMed:25807930,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..440
FT /note="26S proteasome regulatory subunit 4"
FT /id="PRO_0000084677"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..33
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 226..233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 53
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 258
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 434
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 439
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15144186"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:22223895,
FT ECO:0000269|PubMed:25255805, ECO:0000269|PubMed:25807930"
FT CROSSLNK 237
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:17370265"
FT VAR_SEQ 1..73
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055768"
FT CONFLICT 19
FT /note="K -> E (in Ref. 1; AAA35484)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="D -> G (in Ref. 5; AAH67741)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="H -> R (in Ref. 5; AAH16368)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 440 AA; 49185 MW; ACA80782F4F96F49 CRC64;
MGQSQSGGHG PGGGKKDDKD KKKKYEPPVP TRVGKKKKKT KGPDAASKLP LVTPHTQCRL
KLLKLERIKD YLLMEEEFIR NQEQMKPLEE KQEEERSKVD DLRGTPMSVG TLEEIIDDNH
AIVSTSVGSE HYVSILSFVD KDLLEPGCSV LLNHKVHAVI GVLMDDTDPL VTVMKVEKAP
QETYADIGGL DNQIQEIKES VELPLTHPEY YEEMGIKPPK GVILYGPPGT GKTLLAKAVA
NQTSATFLRV VGSELIQKYL GDGPKLVREL FRVAEEHAPS IVFIDEIDAI GTKRYDSNSG
GEREIQRTML ELLNQLDGFD SRGDVKVIMA TNRIETLDPA LIRPGRIDRK IEFPLPDEKT
KKRIFQIHTS RMTLADDVTL DDLIMAKDDL SGADIKAICT EAGLMALRER RMKVTNEDFK
KSKENVLYKK QEGTPEGLYL
