PSA7_HUMAN
ID PSA7_HUMAN Reviewed; 248 AA.
AC O14818; B2R515; Q5JXJ2; Q9BR53; Q9H4K5; Q9UEU8;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 226.
DE RecName: Full=Proteasome subunit alpha type-7;
DE AltName: Full=Proteasome subunit RC6-1;
DE AltName: Full=Proteasome subunit XAPC7;
GN Name=PSMA7; Synonyms=HSPC;
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 INTERACTION WITH HBV PROTEIN
RP HBX (MICROBIAL INFECTION).
RX PubMed=8764072; DOI=10.1128/jvi.70.8.5582-5591.1996;
RA Huang J., Kwong J., Sun E.C.-Y., Liang T.J.;
RT "Proteasome complex as a potential cellular target of hepatitis B virus X
RT protein.";
RL J. Virol. 70:5582-5591(1996).
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 [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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Urinary bladder;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Leukocyte, and Lung;
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 96-109, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [9]
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 [10]
RP INTERACTION WITH HBV PROTEIN HBX (MICROBIAL INFECTION).
RX PubMed=10748218; DOI=10.1074/jbc.m910378199;
RA Zhang Z., Torii N., Furusaka A., Malayaman N., Hu Z., Liang T.J.;
RT "Structural and functional characterization of interaction between
RT hepatitis B virus X protein and the proteasome complex.";
RL J. Biol. Chem. 275:15157-15165(2000).
RN [11]
RP FUNCTION, AND INTERACTION WITH HIF1A.
RX PubMed=11389899; DOI=10.1016/s0014-5793(01)02499-1;
RA Cho S., Choi Y.J., Kim J.M., Jeong S.T., Kim J.H., Kim S.H., Ryu S.E.;
RT "Binding and regulation of HIF-1alpha by a subunit of the proteasome
RT complex, PSMA7.";
RL FEBS Lett. 498:62-66(2001).
RN [12]
RP FUNCTION.
RX PubMed=11713272; DOI=10.1128/mcb.21.24.8357-8364.2001;
RA Kruger M., Beger C., Welch P.J., Barber J.R., Manns M.P., Wong-Staal F.;
RT "Involvement of proteasome alpha-subunit PSMA7 in hepatitis C virus
RT internal ribosome entry site-mediated translation.";
RL Mol. Cell. Biol. 21:8357-8364(2001).
RN [13]
RP INDUCTION.
RX PubMed=11574696; DOI=10.1093/nar/29.19.e94;
RA Kruger M., Beger C., Welch P.J., Barber J.R., Wong-Staal F.;
RT "C-SPACE (cleavage-specific amplification of cDNA ends): a novel method of
RT ribozyme-mediated gene identification.";
RL Nucleic Acids Res. 29:E94-E94(2001).
RN [14]
RP FUNCTION.
RX PubMed=12119296; DOI=10.1074/jbc.m204751200;
RA Lin H.K., Altuwaijri S., Lin W.J., Kan P.Y., Collins L.L., Chang C.;
RT "Proteasome activity is required for androgen receptor transcriptional
RT activity via regulation of androgen receptor nuclear translocation and
RT interaction with coregulators in prostate cancer cells.";
RL J. Biol. Chem. 277:36570-36576(2002).
RN [15]
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 [16]
RP INTERACTION WITH HIV-1 TAT (MICROBIAL INFECTION).
RX PubMed=14550573; DOI=10.1016/s0014-5793(03)01025-1;
RA Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P.,
RA Mayer R.J., Krueger E.;
RT "Human immunodeficiency virus-1 Tat protein interacts with distinct
RT proteasomal alpha and beta subunits.";
RL FEBS Lett. 553:200-204(2003).
RN [17]
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 [18]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [19]
RP INTERACTION WITH RAB7A.
RX PubMed=14998988; DOI=10.1074/jbc.m401022200;
RA Dong J., Chen W., Welford A., Wandinger-Ness A.;
RT "The proteasome alpha-subunit XAPC7 interacts specifically with Rab7 and
RT late endosomes.";
RL J. Biol. Chem. 279:21334-21342(2004).
RN [20]
RP INTERACTION WITH PRKN.
RX PubMed=15987638; DOI=10.1016/j.febslet.2005.06.003;
RA Dachsel J.C., Lucking C.B., Deeg S., Schultz E., Lalowski M.,
RA Casademunt E., Corti O., Hampe C., Patenge N., Vaupel K., Yamamoto A.,
RA Dichgans M., Brice A., Wanker E.E., Kahle P.J., Gasser T.;
RT "Parkin interacts with the proteasome subunit alpha4.";
RL FEBS Lett. 579:3913-3919(2005).
RN [21]
RP INTERACTION WITH PSMG1 AND PSMG2.
RX PubMed=16251969; DOI=10.1038/nature04106;
RA Hirano Y., Hendil K.B., Yashiroda H., Iemura S., Nagane R., Hioki Y.,
RA Natsume T., Tanaka K., Murata S.;
RT "A heterodimeric complex that promotes the assembly of mammalian 20S
RT proteasomes.";
RL Nature 437:1381-1385(2005).
RN [22]
RP INTERACTION WITH ABL1 AND ABL2, PHOSPHORYLATION AT TYR-153 BY ABL1 AND
RP ABL2, AND MUTAGENESIS OF TYR-153.
RX PubMed=16678104; DOI=10.1016/j.molcel.2006.04.007;
RA Liu X., Huang W., Li C., Li P., Yuan J., Li X., Qiu X.B., Ma Q., Cao C.;
RT "Interaction between c-Abl and Arg tyrosine kinases and proteasome subunit
RT PSMA7 regulates proteasome degradation.";
RL Mol. Cell 22:317-327(2006).
RN [23]
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 [24]
RP INDUCTION.
RX PubMed=18202793;
RA Hu X.T., Chen W., Wang D., Shi Q.L., Zhang F.B., Liao Y.Q., Jin M., He C.;
RT "The proteasome subunit PSMA7 located on the 20q13 amplicon is
RT overexpressed and associated with liver metastasis in colorectal cancer.";
RL Oncol. Rep. 19:441-446(2008).
RN [25]
RP INTERACTION WITH EMAP2.
RX PubMed=19362550; DOI=10.1016/j.yexcr.2009.03.021;
RA Tandle A.T., Calvani M., Uranchimeg B., Zahavi D., Melillo G.,
RA Libutti S.K.;
RT "Endothelial monocyte activating polypeptide-II modulates endothelial cell
RT responses by degrading hypoxia-inducible factor-1alpha through interaction
RT with PSMA7, a component of the proteasome.";
RL Exp. Cell Res. 315:1850-1859(2009).
RN [26]
RP FUNCTION, AND INTERACTION WITH MAVS.
RX PubMed=19734229; DOI=10.4049/jimmunol.0901646;
RA Jia Y., Song T., Wei C., Ni C., Zheng Z., Xu Q., Ma H., Li L., Zhang Y.,
RA He X., Xu Y., Shi W., Zhong H.;
RT "Negative regulation of MAVS-mediated innate immune response by PSMA7.";
RL J. Immunol. 183:4241-4248(2009).
RN [27]
RP FUNCTION.
RX PubMed=19442227; DOI=10.2174/092986609788167824;
RA Du H., Huang X., Wang S., Wu Y., Xu W., Li M.;
RT "PSMA7, a potential biomarker of diseases.";
RL Protein Pept. Lett. 16:486-489(2009).
RN [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-227, 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 [29]
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 [30]
RP IDENTIFICATION BY 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 [31]
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 [32]
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 [33]
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 [34]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2-244, 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 [35]
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 [36]
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 [37]
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).
RN [38]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) IN COMPLEX WITH AKIRIN2,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=34711951; DOI=10.1038/s41586-021-04035-8;
RA de Almeida M., Hinterndorfer M., Brunner H., Grishkovskaya I., Singh K.,
RA Schleiffer A., Jude J., Deswal S., Kalis R., Vunjak M., Lendl T., Imre R.,
RA Roitinger E., Neumann T., Kandolf S., Schutzbier M., Mechtler K.,
RA Versteeg G.A., Haselbach D., Zuber J.;
RT "AKIRIN2 controls the nuclear import of proteasomes in vertebrates.";
RL Nature 599:491-496(2021).
RN [39]
RP VARIANT ASP-112.
RX PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
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). Inhibits the transactivation function of HIF-1A
CC under both normoxic and hypoxia-mimicking conditions. The interaction
CC with EMAP2 increases the proteasome-mediated HIF-1A degradation under
CC the hypoxic conditions. Plays a role in hepatitis C virus internal
CC ribosome entry site-mediated translation. Mediates nuclear
CC translocation of the androgen receptor (AR) and thereby enhances
CC androgen-mediated transactivation. Promotes MAVS degradation and
CC thereby negatively regulates MAVS-mediated innate immune response.
CC {ECO:0000269|PubMed:11389899, ECO:0000269|PubMed:11713272,
CC ECO:0000269|PubMed:12119296, ECO:0000269|PubMed:15244466,
CC ECO:0000269|PubMed:19442227, ECO:0000269|PubMed:19734229,
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 (PubMed:25599644, PubMed:26133119,
CC PubMed:27342858, PubMed:27428775, PubMed:27493187, PubMed:34711951).
CC The 20S proteasome core is a barrel-shaped complex made of 28 subunits
CC that are arranged in four stacked rings (PubMed:25599644,
CC PubMed:26133119, PubMed:27342858, PubMed:27428775, PubMed:27493187,
CC PubMed:34711951). The two outer rings are each formed by seven alpha
CC subunits, and the two inner rings are formed by seven beta subunits
CC (PubMed:25599644, PubMed:26133119, PubMed:27342858, PubMed:27428775,
CC PubMed:27493187, PubMed:34711951). The proteolytic activity is exerted
CC by three beta-subunits PSMB5, PSMB6 and PSMB7 (PubMed:25599644,
CC PubMed:26133119, PubMed:27342858, PubMed:27428775, PubMed:27493187,
CC PubMed:34711951). PSMA7 interacts directly with the PSMG1-PSMG2
CC heterodimer which promotes 20S proteasome assembly (PubMed:16251969).
CC Interacts with HIF1A (PubMed:11389899). Interacts with RAB7A
CC (PubMed:14998988). Interacts with PRKN (PubMed:15987638). Interacts
CC with ABL1 and ABL2 (PubMed:16678104). Interacts with EMAP2
CC (PubMed:19362550). Interacts with MAVS (PubMed:19734229).
CC {ECO:0000269|PubMed:11389899, ECO:0000269|PubMed:14998988,
CC ECO:0000269|PubMed:15987638, ECO:0000269|PubMed:16251969,
CC ECO:0000269|PubMed:16678104, ECO:0000269|PubMed:19362550,
CC ECO:0000269|PubMed:19734229, ECO:0000269|PubMed:25599644,
CC ECO:0000269|PubMed:26133119, ECO:0000269|PubMed:27342858,
CC ECO:0000269|PubMed:27428775, ECO:0000269|PubMed:27493187,
CC ECO:0000269|PubMed:34711951}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 TAT protein.
CC {ECO:0000269|PubMed:14550573}.
CC -!- SUBUNIT: (Microbial infection) Interacts with hepatitis B virus X
CC protein (HBX). {ECO:0000269|PubMed:10748218,
CC ECO:0000269|PubMed:8764072}.
CC -!- INTERACTION:
CC O14818; Q19T08: ECSCR; NbExp=3; IntAct=EBI-603272, EBI-15778214;
CC O14818; Q7L775: EPM2AIP1; NbExp=3; IntAct=EBI-603272, EBI-6255981;
CC O14818; P42858: HTT; NbExp=13; IntAct=EBI-603272, EBI-466029;
CC O14818; P25786: PSMA1; NbExp=14; IntAct=EBI-603272, EBI-359352;
CC O14818; P25787: PSMA2; NbExp=6; IntAct=EBI-603272, EBI-603262;
CC O14818; P25788: PSMA3; NbExp=6; IntAct=EBI-603272, EBI-348380;
CC O14818; P25789: PSMA4; NbExp=11; IntAct=EBI-603272, EBI-359310;
CC O14818; P28066: PSMA5; NbExp=2; IntAct=EBI-603272, EBI-355475;
CC O14818; P60900: PSMA6; NbExp=11; IntAct=EBI-603272, EBI-357793;
CC O14818; O14818: PSMA7; NbExp=3; IntAct=EBI-603272, EBI-603272;
CC O14818; P49720: PSMB3; NbExp=3; IntAct=EBI-603272, EBI-603340;
CC O14818; Q5VVQ6: YOD1; NbExp=5; IntAct=EBI-603272, EBI-2510804;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12181345,
CC ECO:0000269|PubMed:34711951}. Nucleus {ECO:0000269|PubMed:12181345,
CC ECO:0000269|PubMed:34711951}. Note=Translocated from the cytoplasm into
CC the nucleus following interaction with AKIRIN2, which bridges the
CC proteasome with the nuclear import receptor IPO9.
CC {ECO:0000269|PubMed:34711951}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1;
CC IsoId=O14818-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14818-2; Sequence=VSP_005281;
CC Name=3;
CC IsoId=O14818-4; Sequence=VSP_046556, VSP_046557;
CC -!- INDUCTION: Down-regulated by the ribozyme Rz3'X. Up-regulated in
CC colorectal cancer tissues. {ECO:0000269|PubMed:11574696,
CC ECO:0000269|PubMed:18202793}.
CC -!- PTM: Phosphorylation by ABL1 or ABL2 leads to an inhibition of
CC proteasomal activity and cell cycle transition blocks.
CC {ECO:0000269|PubMed:16678104}.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC ProRule:PRU00808}.
CC ---------------------------------------------------------------------------
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DR EMBL; AF022815; AAB81515.1; -; mRNA.
DR EMBL; AF054185; AAC99402.1; -; mRNA.
DR EMBL; BT007165; AAP35829.1; -; mRNA.
DR EMBL; AK312025; BAG34962.1; -; mRNA.
DR EMBL; AL078633; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75398.1; -; Genomic_DNA.
DR EMBL; BC004427; AAH04427.1; -; mRNA.
DR EMBL; BI906714; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS13489.1; -. [O14818-1]
DR PIR; PC2326; PC2326.
DR RefSeq; NP_002783.1; NM_002792.3. [O14818-1]
DR PDB; 4R3O; X-ray; 2.60 A; D/R=2-244.
DR PDB; 4R67; X-ray; 2.89 A; D/R/f/t=2-244.
DR PDB; 5A0Q; EM; 3.50 A; D/R=1-248.
DR PDB; 5GJQ; EM; 4.50 A; E/k=1-248.
DR PDB; 5GJR; EM; 3.50 A; E/k=1-248.
DR PDB; 5L4G; EM; 4.02 A; D/Q=1-248.
DR PDB; 5LE5; X-ray; 1.80 A; C/Q=1-248.
DR PDB; 5LEX; X-ray; 2.20 A; C/Q=1-248.
DR PDB; 5LEY; X-ray; 1.90 A; C/Q=1-248.
DR PDB; 5LEZ; X-ray; 2.19 A; C/Q=1-248.
DR PDB; 5LF0; X-ray; 2.41 A; C/Q=1-248.
DR PDB; 5LF1; X-ray; 2.00 A; C/Q=1-248.
DR PDB; 5LF3; X-ray; 2.10 A; C/Q=1-248.
DR PDB; 5LF4; X-ray; 1.99 A; C/Q=1-248.
DR PDB; 5LF6; X-ray; 2.07 A; C/Q=1-248.
DR PDB; 5LF7; X-ray; 2.00 A; C/Q=1-248.
DR PDB; 5LN3; EM; 6.80 A; D=1-248.
DR PDB; 5M32; EM; 3.80 A; C=2-235, Q=2-236.
DR PDB; 5T0C; EM; 3.80 A; AJ/BJ=2-248.
DR PDB; 5T0G; EM; 4.40 A; J=2-248.
DR PDB; 5T0H; EM; 6.80 A; J=2-248.
DR PDB; 5T0I; EM; 8.00 A; J=2-248.
DR PDB; 5T0J; EM; 8.00 A; J=2-248.
DR PDB; 5VFO; EM; 3.50 A; J/j=2-244.
DR PDB; 5VFP; EM; 4.20 A; J/j=2-244.
DR PDB; 5VFQ; EM; 4.20 A; J/j=2-244.
DR PDB; 5VFR; EM; 4.90 A; J/j=2-244.
DR PDB; 5VFS; EM; 3.60 A; J/j=2-244.
DR PDB; 5VFT; EM; 7.00 A; J/j=2-244.
DR PDB; 5VFU; EM; 5.80 A; J/j=2-244.
DR PDB; 6AVO; EM; 3.80 A; I/N=1-248.
DR PDB; 6E5B; X-ray; 2.77 A; C/Q=1-248.
DR PDB; 6KWY; EM; 2.72 A; C/Q=1-248.
DR PDB; 6MSB; EM; 3.00 A; J/j=2-248.
DR PDB; 6MSD; EM; 3.20 A; J/j=2-248.
DR PDB; 6MSE; EM; 3.30 A; J/j=2-248.
DR PDB; 6MSG; EM; 3.50 A; J/j=2-248.
DR PDB; 6MSH; EM; 3.60 A; J/j=2-248.
DR PDB; 6MSJ; EM; 3.30 A; J/j=2-248.
DR PDB; 6MSK; EM; 3.20 A; J/j=2-248.
DR PDB; 6R70; EM; 3.50 A; C/Q=2-238.
DR PDB; 6REY; EM; 3.00 A; D/R=1-248.
DR PDB; 6RGQ; EM; 2.60 A; D/R=1-248.
DR PDB; 6WJD; EM; 4.80 A; J/j=2-248.
DR PDB; 6WJN; EM; 5.70 A; J/j=2-244.
DR PDB; 6XMJ; EM; 3.00 A; D=2-244.
DR PDB; 7AWE; X-ray; 2.29 A; D/R=2-238.
DR PDB; 7B12; X-ray; 2.43 A; D/r=2-236.
DR PDB; 7LXV; EM; 3.40 A; C/Q=1-248.
DR PDB; 7NHT; EM; 2.80 A; C=1-248.
DR PDB; 7PG9; EM; 3.70 A; D/R=1-248.
DR PDB; 7V5G; EM; 4.47 A; R/Y=1-248.
DR PDB; 7V5M; EM; 3.88 A; D/R=1-248.
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 PDBsum; 7AWE; -.
DR PDBsum; 7B12; -.
DR PDBsum; 7LXV; -.
DR PDBsum; 7NHT; -.
DR PDBsum; 7PG9; -.
DR PDBsum; 7V5G; -.
DR PDBsum; 7V5M; -.
DR AlphaFoldDB; O14818; -.
DR SMR; O14818; -.
DR BioGRID; 111661; 198.
DR ComplexPortal; CPX-5993; 26S Proteasome complex.
DR CORUM; O14818; -.
DR DIP; DIP-29363N; -.
DR IntAct; O14818; 77.
DR MINT; O14818; -.
DR STRING; 9606.ENSP00000359910; -.
DR BindingDB; O14818; -.
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 DrugBank; DB07558; acetylleucyl-leucyl-norleucinal.
DR MEROPS; T01.974; -.
DR GlyGen; O14818; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; O14818; -.
DR MetOSite; O14818; -.
DR PhosphoSitePlus; O14818; -.
DR SwissPalm; O14818; -.
DR BioMuta; PSMA7; -.
DR REPRODUCTION-2DPAGE; IPI00024175; -.
DR UCD-2DPAGE; O14818; -.
DR EPD; O14818; -.
DR jPOST; O14818; -.
DR MassIVE; O14818; -.
DR MaxQB; O14818; -.
DR PaxDb; O14818; -.
DR PeptideAtlas; O14818; -.
DR PRIDE; O14818; -.
DR ProteomicsDB; 48256; -. [O14818-1]
DR ProteomicsDB; 48257; -. [O14818-2]
DR ProteomicsDB; 63458; -.
DR Antibodypedia; 29428; 492 antibodies from 33 providers.
DR DNASU; 5688; -.
DR Ensembl; ENST00000370858.3; ENSP00000359895.3; ENSG00000101182.15. [O14818-4]
DR Ensembl; ENST00000370861.1; ENSP00000359898.1; ENSG00000101182.15. [O14818-2]
DR Ensembl; ENST00000370873.9; ENSP00000359910.4; ENSG00000101182.15. [O14818-1]
DR GeneID; 5688; -.
DR KEGG; hsa:5688; -.
DR MANE-Select; ENST00000370873.9; ENSP00000359910.4; NM_002792.4; NP_002783.1.
DR UCSC; uc002ybx.3; human. [O14818-1]
DR CTD; 5688; -.
DR DisGeNET; 5688; -.
DR GeneCards; PSMA7; -.
DR HGNC; HGNC:9536; PSMA7.
DR HPA; ENSG00000101182; Tissue enhanced (skeletal).
DR MIM; 606607; gene.
DR neXtProt; NX_O14818; -.
DR OpenTargets; ENSG00000101182; -.
DR PharmGKB; PA33881; -.
DR VEuPathDB; HostDB:ENSG00000101182; -.
DR eggNOG; KOG0183; Eukaryota.
DR GeneTree; ENSGT00940000159695; -.
DR HOGENOM; CLU_035750_4_0_1; -.
DR InParanoid; O14818; -.
DR OMA; KICMLDH; -.
DR PhylomeDB; O14818; -.
DR TreeFam; TF106212; -.
DR PathwayCommons; O14818; -.
DR Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
DR Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
DR Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-HSA-202424; Downstream TCR signaling.
DR Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-HSA-4641257; Degradation of AXIN.
DR Reactome; R-HSA-4641258; Degradation of DVL.
DR Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD.
DR Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
DR Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
DR Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex.
DR Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-HSA-69481; G2/M Checkpoints.
DR Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-HSA-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-HSA-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; O14818; -.
DR SIGNOR; O14818; -.
DR BioGRID-ORCS; 5688; 821 hits in 1068 CRISPR screens.
DR ChiTaRS; PSMA7; human.
DR GeneWiki; PSMA7; -.
DR GenomeRNAi; 5688; -.
DR Pharos; O14818; Tbio.
DR PRO; PR:O14818; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; O14818; protein.
DR Bgee; ENSG00000101182; Expressed in gastrocnemius and 204 other tissues.
DR ExpressionAtlas; O14818; baseline and differential.
DR Genevisible; O14818; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0098794; C:postsynapse; IEA:Ensembl.
DR GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
DR GO; GO:0005839; C:proteasome core complex; IDA:UniProtKB.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IC:ComplexPortal.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR023332; Proteasome_alpha-type.
DR InterPro; IPR035190; Proteasome_alpha7.
DR InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR001353; Proteasome_sua/b.
DR PANTHER; PTHR11599:SF40; PTHR11599:SF40; 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; Glycoprotein; Host-virus interaction; Nucleus;
KW Phosphoprotein; Proteasome; Reference proteome.
FT CHAIN 1..248
FT /note="Proteasome subunit alpha type-7"
FT /id="PRO_0000124142"
FT MOD_RES 153
FT /note="Phosphotyrosine; by ABL1 and ABL2"
FT /evidence="ECO:0000269|PubMed:16678104"
FT MOD_RES 227
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CARBOHYD 130
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..70
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_005281"
FT VAR_SEQ 117..149
FT /note="RYTQSNGRRPFGISALIVGFDFDGTPRLYQTDP -> VGACPLACSPLAAGQ
FT SRLRHGGSCHVTSGESEN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046556"
FT VAR_SEQ 150..248
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046557"
FT VARIANT 112
FT /note="A -> D (found in patient with severe intellectual
FT disability; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:23033978"
FT /id="VAR_078692"
FT MUTAGEN 153
FT /note="Y->F: Displays impaired G1/S transition and S/G2
FT progression."
FT /evidence="ECO:0000269|PubMed:16678104"
FT CONFLICT 160
FT /note="A -> S (in Ref. 2; AAC99402)"
FT /evidence="ECO:0000305"
FT STRAND 7..9
FT /evidence="ECO:0007829|PDB:6XMJ"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:5LE5"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:4R3O"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:5LE5"
FT HELIX 77..98
FT /evidence="ECO:0007829|PDB:5LE5"
FT HELIX 104..117
FT /evidence="ECO:0007829|PDB:5LE5"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 129..136
FT /evidence="ECO:0007829|PDB:5LE5"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:5VFO"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 153..162
FT /evidence="ECO:0007829|PDB:5LE5"
FT HELIX 165..175
FT /evidence="ECO:0007829|PDB:5LE5"
FT TURN 178..181
FT /evidence="ECO:0007829|PDB:5LE5"
FT HELIX 184..196
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:4R67"
FT STRAND 202..212
FT /evidence="ECO:0007829|PDB:5LE5"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:5LF6"
FT HELIX 222..233
FT /evidence="ECO:0007829|PDB:5LE5"
FT TURN 234..237
FT /evidence="ECO:0007829|PDB:5LE5"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:4R3O"
SQ SEQUENCE 248 AA; 27887 MW; 5DD0276A1C2DEF91 CRC64;
MSYDRAITVF SPDGHLFQVE YAQEAVKKGS TAVGVRGRDI VVLGVEKKSV AKLQDERTVR
KICALDDNVC MAFAGLTADA RIVINRARVE CQSHRLTVED PVTVEYITRY IASLKQRYTQ
SNGRRPFGIS ALIVGFDFDG TPRLYQTDPS GTYHAWKANA IGRGAKSVRE FLEKNYTDEA
IETDDLTIKL VIKALLEVVQ SGGKNIELAV MRRDQSLKIL NPEEIEKYVA EIEKEKEENE
KKKQKKAS
