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Database: UniProt
Entry: P25789
LinkDB: P25789
Original site: P25789 
ID   PSA4_HUMAN              Reviewed;         261 AA.
AC   P25789; D3DW86; Q53XP2; Q567Q5; Q8TBD1;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   02-JUN-2021, entry version 223.
DE   RecName: Full=Proteasome subunit alpha type-4;
DE   AltName: Full=Macropain subunit C9;
DE   AltName: Full=Multicatalytic endopeptidase complex subunit C9;
DE   AltName: Full=Proteasome component C9;
DE   AltName: Full=Proteasome subunit L;
GN   Name=PSMA4; Synonyms=HC9, PSC9;
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=2025653; DOI=10.1016/0167-4781(91)90090-9;
RA   Tamura T., Lee D.H., Osaka F., Fujiwara T., Shin S., Chung C.H., Tanaka K.,
RA   Ichihara A.;
RT   "Molecular cloning and sequence analysis of cDNAs for five major subunits
RT   of human proteasomes (multi-catalytic proteinase complexes).";
RL   Biochim. Biophys. Acta 1089:95-102(1991).
RN   [2]
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 (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16572171; DOI=10.1038/nature04601;
RA   Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA   Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA   Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA   Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA   DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA   Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA   Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA   Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA   O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA   Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA   Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human chromosome
RT   15.";
RL   Nature 440:671-675(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Blood, Brain, Lung, Pancreas, and Urinary bladder;
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   PROTEIN SEQUENCE OF 18-39.
RX   PubMed=7811265; DOI=10.1006/bbrc.1994.2876;
RA   Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B.;
RT   "Human proteasome subunits from 2-dimensional gels identified by partial
RT   sequencing.";
RL   Biochem. Biophys. Res. Commun. 205:1785-1789(1994).
RN   [7]
RP   FUNCTION IN ANTIGEN PRESENTATION.
RX   PubMed=8610016; DOI=10.1038/381166a0;
RA   Groettrup M., Soza A., Eggers M., Kuehn L., Dick T.P., Schild H.,
RA   Rammensee H.G., Koszinowski U.H., Kloetzel P.M.;
RT   "A role for the proteasome regulator PA28alpha in antigen presentation.";
RL   Nature 381:166-168(1996).
RN   [8]
RP   INTERACTION WITH HTLV-1 TAX (MICROBIAL INFECTION).
RX   PubMed=8692272; DOI=10.1038/381328a0;
RA   Rousset R., Desbois C., Bantignies F., Jalinot P.;
RT   "Effects on NF-kappa B1/p105 processing of the interaction between the
RT   HTLV-1 transactivator Tax and the proteasome.";
RL   Nature 381:328-331(1996).
RN   [9]
RP   INDUCTION BY BO-653 AND PROBUCOL.
RX   PubMed=11521686; DOI=10.5551/jat1994.7.223;
RA   Takabe W., Mataki C., Wada Y., Ishii M., Izumi A., Aburatani H.,
RA   Hamakubo T., Niki E., Kodama T., Noguchi N.;
RT   "Gene expression induced by BO-653, probucol and BHQ in human endothelial
RT   cells.";
RL   J. Atheroscler. Thromb. 7:223-230(2000).
RN   [10]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12181345; DOI=10.1091/mbc.e02-03-0122;
RA   Lafarga M., Berciano M.T., Pena E., Mayo I., Castano J.G., Bohmann D.,
RA   Rodrigues J.P., Tavanez J.P., Carmo-Fonseca M.;
RT   "Clastosome: a subtype of nuclear body enriched in 19S and 20S proteasomes,
RT   ubiquitin, and protein substrates of proteasome.";
RL   Mol. Biol. Cell 13:2771-2782(2002).
RN   [11]
RP   FUNCTION.
RX   PubMed=15244466; DOI=10.1021/bm049957a;
RA   Yano M., Koumoto Y., Kanesaki Y., Wu X., Kido H.;
RT   "20S proteasome prevents aggregation of heat-denatured proteins without
RT   PA700 regulatory subcomplex like a molecular chaperone.";
RL   Biomacromolecules 5:1465-1469(2004).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, 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-13, 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   [14]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-127 AND LYS-176, 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   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, 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   [16]
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   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and 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 SER-173, 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   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=27176742; DOI=10.1515/hsz-2016-0176;
RA   Rut W., Drag M.;
RT   "Human 20S proteasome activity towards fluorogenic peptides of various
RT   chain lengths.";
RL   Biol. Chem. 397:921-926(2016).
RN   [20]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND SUBUNIT.
RX   PubMed=26133119; DOI=10.1038/ncomms8573;
RA   da Fonseca P.C., Morris E.P.;
RT   "Cryo-EM reveals the conformation of a substrate analogue in the human 20S
RT   proteasome core.";
RL   Nat. Commun. 6:7573-7573(2015).
RN   [21]
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2-251, AND SUBUNIT.
RX   PubMed=25599644; DOI=10.1016/j.str.2014.11.017;
RA   Harshbarger W., Miller C., Diedrich C., Sacchettini J.;
RT   "Crystal structure of the human 20S proteasome in complex with
RT   carfilzomib.";
RL   Structure 23:418-424(2015).
RN   [22]
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), 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   [23]
RP   STRUCTURE BY ELECTRON MICROSCOPY (4.02 ANGSTROMS), 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).
RN   [24]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), AND SUBUNIT.
RX   PubMed=27493187; DOI=10.1126/science.aaf8993;
RA   Schrader J., Henneberg F., Mata R.A., Tittmann K., Schneider T.R.,
RA   Stark H., Bourenkov G., Chari A.;
RT   "The inhibition mechanism of human 20S proteasomes enables next-generation
RT   inhibitor design.";
RL   Science 353:594-598(2016).
CC   -!- FUNCTION: Component of the 20S core proteasome complex involved in the
CC       proteolytic degradation of most intracellular proteins. This complex
CC       plays numerous essential roles within the cell by associating with
CC       different regulatory particles. Associated with two 19S regulatory
CC       particles, forms the 26S proteasome and thus participates in the ATP-
CC       dependent degradation of ubiquitinated proteins. The 26S proteasome
CC       plays a key role in the maintenance of protein homeostasis by removing
CC       misfolded or damaged proteins that could impair cellular functions, and
CC       by removing proteins whose functions are no longer required. Associated
CC       with the PA200 or PA28, the 20S proteasome mediates ubiquitin-
CC       independent protein degradation. This type of proteolysis is required
CC       in several pathways including spermatogenesis (20S-PA200 complex) or
CC       generation of a subset of MHC class I-presented antigenic peptides
CC       (20S-PA28 complex). {ECO:0000269|PubMed:15244466,
CC       ECO:0000269|PubMed:27176742, ECO:0000269|PubMed:8610016}.
CC   -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC       19S regulatory subunits. The 20S proteasome core is a barrel-shaped
CC       complex made of 28 subunits that are arranged in four stacked rings.
CC       The two outer rings are each formed by seven alpha subunits, and the
CC       two inner rings are formed by seven beta subunits. The proteolytic
CC       activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7.
CC       {ECO:0000269|PubMed:25599644, ECO:0000269|PubMed:26133119,
CC       ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775,
CC       ECO:0000269|PubMed:27493187}.
CC   -!- SUBUNIT: (Microbial infection) Interaction with HTLV-1 TAX protein
CC       favors NFKB1 activation. {ECO:0000269|PubMed:8692272}.
CC   -!- INTERACTION:
CC       P25789; P54253: ATXN1; NbExp=7; IntAct=EBI-359310, EBI-930964;
CC       P25789; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-359310, EBI-11530605;
CC       P25789; Q08379: GOLGA2; NbExp=3; IntAct=EBI-359310, EBI-618309;
CC       P25789; Q16665: HIF1A; NbExp=4; IntAct=EBI-359310, EBI-447269;
CC       P25789; P42858: HTT; NbExp=4; IntAct=EBI-359310, EBI-466029;
CC       P25789; Q13422: IKZF1; NbExp=3; IntAct=EBI-359310, EBI-745305;
CC       P25789; Q13422-7: IKZF1; NbExp=3; IntAct=EBI-359310, EBI-11522367;
CC       P25789; P25786: PSMA1; NbExp=8; IntAct=EBI-359310, EBI-359352;
CC       P25789; P25787: PSMA2; NbExp=7; IntAct=EBI-359310, EBI-603262;
CC       P25789; P25788: PSMA3; NbExp=4; IntAct=EBI-359310, EBI-348380;
CC       P25789; P60900: PSMA6; NbExp=5; IntAct=EBI-359310, EBI-357793;
CC       P25789; O14818: PSMA7; NbExp=11; IntAct=EBI-359310, EBI-603272;
CC       P25789; Q04864-2: REL; NbExp=3; IntAct=EBI-359310, EBI-10829018;
CC       P25789; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-359310, EBI-1105213;
CC       P25789; O00635: TRIM38; NbExp=3; IntAct=EBI-359310, EBI-2130415;
CC       P25789; Q99PV5: Bhlhe41; Xeno; NbExp=2; IntAct=EBI-359310, EBI-6143801;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12181345}. Nucleus
CC       {ECO:0000269|PubMed:12181345}. Note=Colocalizes with TRIM5 in the
CC       cytoplasmic bodies. {ECO:0000250|UniProtKB:Q9R1P0}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P25789-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P25789-2; Sequence=VSP_043102;
CC   -!- INDUCTION: Down-regulated by antioxidants BO-653 and probucol.
CC       {ECO:0000269|PubMed:11521686}.
CC   -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00808}.
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DR   EMBL; D00763; BAA00660.1; -; mRNA.
DR   EMBL; BT009784; AAP88786.1; -; mRNA.
DR   EMBL; AC027228; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471136; EAW99163.1; -; Genomic_DNA.
DR   EMBL; CH471136; EAW99164.1; -; Genomic_DNA.
DR   EMBL; BC005361; AAH05361.1; -; mRNA.
DR   EMBL; BC022445; AAH22445.1; -; mRNA.
DR   EMBL; BC022817; AAH22817.2; -; mRNA.
DR   EMBL; BC047667; AAH47667.1; -; mRNA.
DR   EMBL; BC093069; AAH93069.1; -; mRNA.
DR   CCDS; CCDS10303.1; -. [P25789-1]
DR   CCDS; CCDS45319.1; -. [P25789-2]
DR   PIR; S15972; SNHUC9.
DR   RefSeq; NP_001096137.1; NM_001102667.2. [P25789-1]
DR   RefSeq; NP_001096138.1; NM_001102668.2. [P25789-2]
DR   RefSeq; NP_001317605.1; NM_001330676.1. [P25789-1]
DR   RefSeq; NP_002780.1; NM_002789.5. [P25789-1]
DR   PDB; 4R3O; X-ray; 2.60 A; C/Q=2-251.
DR   PDB; 4R67; X-ray; 2.89 A; C/Q/e/s=2-251.
DR   PDB; 5A0Q; EM; 3.50 A; C/Q=1-261.
DR   PDB; 5GJQ; EM; 4.50 A; D/j=1-261.
DR   PDB; 5GJR; EM; 3.50 A; D/j=1-261.
DR   PDB; 5L4G; EM; 4.02 A; C/P=1-261.
DR   PDB; 5LE5; X-ray; 1.80 A; B/P=1-261.
DR   PDB; 5LEX; X-ray; 2.20 A; B/P=1-261.
DR   PDB; 5LEY; X-ray; 1.90 A; B/P=1-261.
DR   PDB; 5LEZ; X-ray; 2.19 A; B/P=1-261.
DR   PDB; 5LF0; X-ray; 2.41 A; B/P=1-261.
DR   PDB; 5LF1; X-ray; 2.00 A; B/P=1-261.
DR   PDB; 5LF3; X-ray; 2.10 A; B/P=1-261.
DR   PDB; 5LF4; X-ray; 1.99 A; B/P=1-261.
DR   PDB; 5LF6; X-ray; 2.07 A; B/P=1-261.
DR   PDB; 5LF7; X-ray; 2.00 A; B/P=1-261.
DR   PDB; 5LN3; EM; 6.80 A; C=1-261.
DR   PDB; 5M32; EM; 3.80 A; B/P=1-261.
DR   PDB; 5T0C; EM; 3.80 A; AI/BI=2-261.
DR   PDB; 5T0G; EM; 4.40 A; I=2-261.
DR   PDB; 5T0H; EM; 6.80 A; I=2-261.
DR   PDB; 5T0I; EM; 8.00 A; I=2-261.
DR   PDB; 5T0J; EM; 8.00 A; I=2-261.
DR   PDB; 5VFO; EM; 3.50 A; I/i=2-251.
DR   PDB; 5VFP; EM; 4.20 A; I/i=2-251.
DR   PDB; 5VFQ; EM; 4.20 A; I/i=2-251.
DR   PDB; 5VFR; EM; 4.90 A; I/i=2-251.
DR   PDB; 5VFS; EM; 3.60 A; I/i=2-251.
DR   PDB; 5VFT; EM; 7.00 A; I/i=2-251.
DR   PDB; 5VFU; EM; 5.80 A; I/i=2-251.
DR   PDB; 6AVO; EM; 3.80 A; O/Z=1-261.
DR   PDB; 6E5B; X-ray; 2.77 A; B/P=1-261.
DR   PDB; 6KWY; EM; 2.72 A; B/P=1-261.
DR   PDB; 6MSB; EM; 3.00 A; I/i=2-261.
DR   PDB; 6MSD; EM; 3.20 A; I/i=2-261.
DR   PDB; 6MSE; EM; 3.30 A; I/i=2-261.
DR   PDB; 6MSG; EM; 3.50 A; I/i=2-261.
DR   PDB; 6MSH; EM; 3.60 A; I/i=2-261.
DR   PDB; 6MSJ; EM; 3.30 A; I/i=2-261.
DR   PDB; 6MSK; EM; 3.20 A; I/i=2-261.
DR   PDB; 6R70; EM; 3.50 A; B/P=2-249.
DR   PDB; 6REY; EM; 3.00 A; C/Q=1-261.
DR   PDB; 6RGQ; EM; 2.60 A; C/Q=1-261.
DR   PDB; 6WJD; EM; 4.80 A; I/i=2-261.
DR   PDB; 6WJN; EM; 5.70 A; I/i=2-251.
DR   PDB; 6XMJ; EM; 3.00 A; C=2-251.
DR   PDBsum; 4R3O; -.
DR   PDBsum; 4R67; -.
DR   PDBsum; 5A0Q; -.
DR   PDBsum; 5GJQ; -.
DR   PDBsum; 5GJR; -.
DR   PDBsum; 5L4G; -.
DR   PDBsum; 5LE5; -.
DR   PDBsum; 5LEX; -.
DR   PDBsum; 5LEY; -.
DR   PDBsum; 5LEZ; -.
DR   PDBsum; 5LF0; -.
DR   PDBsum; 5LF1; -.
DR   PDBsum; 5LF3; -.
DR   PDBsum; 5LF4; -.
DR   PDBsum; 5LF6; -.
DR   PDBsum; 5LF7; -.
DR   PDBsum; 5LN3; -.
DR   PDBsum; 5M32; -.
DR   PDBsum; 5T0C; -.
DR   PDBsum; 5T0G; -.
DR   PDBsum; 5T0H; -.
DR   PDBsum; 5T0I; -.
DR   PDBsum; 5T0J; -.
DR   PDBsum; 5VFO; -.
DR   PDBsum; 5VFP; -.
DR   PDBsum; 5VFQ; -.
DR   PDBsum; 5VFR; -.
DR   PDBsum; 5VFS; -.
DR   PDBsum; 5VFT; -.
DR   PDBsum; 5VFU; -.
DR   PDBsum; 6AVO; -.
DR   PDBsum; 6E5B; -.
DR   PDBsum; 6KWY; -.
DR   PDBsum; 6MSB; -.
DR   PDBsum; 6MSD; -.
DR   PDBsum; 6MSE; -.
DR   PDBsum; 6MSG; -.
DR   PDBsum; 6MSH; -.
DR   PDBsum; 6MSJ; -.
DR   PDBsum; 6MSK; -.
DR   PDBsum; 6R70; -.
DR   PDBsum; 6REY; -.
DR   PDBsum; 6RGQ; -.
DR   PDBsum; 6WJD; -.
DR   PDBsum; 6WJN; -.
DR   PDBsum; 6XMJ; -.
DR   SMR; P25789; -.
DR   BioGRID; 111658; 164.
DR   ComplexPortal; CPX-5993; 26S Proteasome complex.
DR   CORUM; P25789; -.
DR   DIP; DIP-29365N; -.
DR   IntAct; P25789; 58.
DR   MINT; P25789; -.
DR   STRING; 9606.ENSP00000044462; -.
DR   BindingDB; P25789; -.
DR   ChEMBL; CHEMBL2364701; -.
DR   ChEMBL; CHEMBL3831201; -.
DR   DrugBank; DB08515; (3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDE.
DR   MEROPS; T01.973; -.
DR   iPTMnet; P25789; -.
DR   MetOSite; P25789; -.
DR   PhosphoSitePlus; P25789; -.
DR   SwissPalm; P25789; -.
DR   BioMuta; PSMA4; -.
DR   DMDM; 130861; -.
DR   UCD-2DPAGE; P25789; -.
DR   EPD; P25789; -.
DR   jPOST; P25789; -.
DR   MassIVE; P25789; -.
DR   MaxQB; P25789; -.
DR   PaxDb; P25789; -.
DR   PeptideAtlas; P25789; -.
DR   PRIDE; P25789; -.
DR   ProteomicsDB; 54292; -. [P25789-1]
DR   ProteomicsDB; 54293; -. [P25789-2]
DR   TopDownProteomics; P25789-1; -. [P25789-1]
DR   Antibodypedia; 27657; 324 antibodies.
DR   DNASU; 5685; -.
DR   Ensembl; ENST00000044462; ENSP00000044462; ENSG00000041357. [P25789-1]
DR   Ensembl; ENST00000413382; ENSP00000402118; ENSG00000041357. [P25789-2]
DR   Ensembl; ENST00000559082; ENSP00000453887; ENSG00000041357. [P25789-1]
DR   GeneID; 5685; -.
DR   KEGG; hsa:5685; -.
DR   UCSC; uc002bdu.5; human. [P25789-1]
DR   CTD; 5685; -.
DR   DisGeNET; 5685; -.
DR   GeneCards; PSMA4; -.
DR   HGNC; HGNC:9533; PSMA4.
DR   HPA; ENSG00000041357; Low tissue specificity.
DR   MIM; 176846; gene.
DR   neXtProt; NX_P25789; -.
DR   OpenTargets; ENSG00000041357; -.
DR   PharmGKB; PA33878; -.
DR   VEuPathDB; HostDB:ENSG00000041357.15; -.
DR   eggNOG; KOG0178; Eukaryota.
DR   GeneTree; ENSGT00550000074827; -.
DR   InParanoid; P25789; -.
DR   OMA; CNEKQRY; -.
DR   OrthoDB; 1222564at2759; -.
DR   PhylomeDB; P25789; -.
DR   TreeFam; TF106209; -.
DR   BRENDA; 3.4.25.1; 2681.
DR   PathwayCommons; P25789; -.
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; P25789; -.
DR   BioGRID-ORCS; 5685; 762 hits in 962 CRISPR screens.
DR   ChiTaRS; PSMA4; human.
DR   GeneWiki; PSMA4; -.
DR   GenomeRNAi; 5685; -.
DR   Pharos; P25789; Tbio.
DR   PRO; PR:P25789; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; P25789; protein.
DR   Bgee; ENSG00000041357; Expressed in monocyte and 242 other tissues.
DR   ExpressionAtlas; P25789; baseline and differential.
DR   Genevisible; P25789; HS.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR   GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR   GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
DR   GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB.
DR   GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IDA:UniProtKB.
DR   GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0004298; F:threonine-type endopeptidase 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:0043687; P:post-translational protein modification; TAS:Reactome.
DR   GO; GO:0036388; P:pre-replicative complex assembly; TAS:Reactome.
DR   GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0016579; P:protein deubiquitination; 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:0016032; P:viral process; IEA:UniProtKB-KW.
DR   GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR023332; Proteasome_alpha-type.
DR   InterPro; IPR000426; Proteasome_asu_N.
DR   InterPro; IPR016050; Proteasome_bsu_CS.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   InterPro; IPR034647; Proteasome_subunit_alpha4.
DR   PANTHER; PTHR11599:SF13; PTHR11599:SF13; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   Pfam; PF10584; Proteasome_A_N; 1.
DR   SMART; SM00948; Proteasome_A_N; 1.
DR   SUPFAM; SSF56235; SSF56235; 1.
DR   PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
DR   PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW   Direct protein sequencing; Host-virus interaction; Nucleus; Phosphoprotein;
KW   Proteasome; Reference proteome.
FT   CHAIN           1..261
FT                   /note="Proteasome subunit alpha type-4"
FT                   /id="PRO_0000124103"
FT   REGION          240..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         13
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         75
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17323924"
FT   MOD_RES         127
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         173
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         176
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   VAR_SEQ         1..71
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_043102"
FT   TURN            3..5
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          7..11
FT                   /evidence="ECO:0007829|PDB:5VFO"
FT   TURN            14..16
FT                   /evidence="ECO:0007829|PDB:6E5B"
FT   HELIX           19..29
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          34..39
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          42..48
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   TURN            59..61
FT                   /evidence="ECO:0007829|PDB:6KWY"
FT   STRAND          63..69
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          72..78
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           80..101
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           107..123
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          124..126
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          132..140
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   TURN            141..143
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          144..150
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   TURN            152..154
FT                   /evidence="ECO:0007829|PDB:6E5B"
FT   STRAND          156..165
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           168..178
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   TURN            181..183
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           186..200
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          203..205
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           208..210
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          211..219
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          222..227
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           230..246
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           248..250
FT                   /evidence="ECO:0007829|PDB:5VFO"
SQ   SEQUENCE   261 AA;  29484 MW;  7867422B1B31F3B9 CRC64;
     MSRRYDSRTT IFSPEGRLYQ VEYAMEAIGH AGTCLGILAN DGVLLAAERR NIHKLLDEVF
     FSEKIYKLNE DMACSVAGIT SDANVLTNEL RLIAQRYLLQ YQEPIPCEQL VTALCDIKQA
     YTQFGGKRPF GVSLLYIGWD KHYGFQLYQS DPSGNYGGWK ATCIGNNSAA AVSMLKQDYK
     EGEMTLKSAL ALAIKVLNKT MDVSKLSAEK VEIATLTREN GKTVIRVLKQ KEVEQLIKKH
     EEEEAKAERE KKEKEQKEKD K
//
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