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Database: UniProt
Entry: P62191
LinkDB: P62191
Original site: P62191 
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   02-JUN-2021, entry version 181.
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;
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   SMR; P62191; -.
DR   BioGRID; 111673; 234.
DR   ComplexPortal; CPX-5993; 26S Proteasome complex.
DR   CORUM; P62191; -.
DR   IntAct; P62191; 113.
DR   MINT; P62191; -.
DR   STRING; 9606.ENSP00000261303; -.
DR   ChEMBL; CHEMBL2364701; -.
DR   CarbonylDB; P62191; -.
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   PaxDb; P62191; -.
DR   PeptideAtlas; P62191; -.
DR   PRIDE; P62191; -.
DR   ProteomicsDB; 4926; -.
DR   ProteomicsDB; 57370; -. [P62191-1]
DR   Antibodypedia; 82; 172 antibodies.
DR   DNASU; 5700; -.
DR   Ensembl; ENST00000261303; ENSP00000261303; ENSG00000100764. [P62191-1]
DR   Ensembl; ENST00000543772; ENSP00000445147; ENSG00000100764. [P62191-2]
DR   GeneID; 5700; -.
DR   KEGG; hsa:5700; -.
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:ENSG00000100764.13; -.
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-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; P62191; -.
DR   BioGRID-ORCS; 5700; 712 hits in 998 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 120 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:ATPase activity; ISS:UniProtKB.
DR   GO; GO:0036402; F:proteasome-activating ATPase activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0017025; F:TBP-class protein binding; IBA:GO_Central.
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:1901215; P:negative regulation of neuron death; IEA:Ensembl.
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: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:0006457; P:protein folding; TAS:Reactome.
DR   GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
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   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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032501; Prot_ATP_ID_OB.
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   NP_BIND         226..233
FT                   /note="ATP"
FT                   /evidence="ECO:0000255"
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   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
//
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