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Proteasome subunit alpha type-7 (EC 3.4.25.1) (Proteasome subunit RC6-1) (Proteasome subunit XAPC7)

 PSA7_HUMAN              Reviewed;         248 AA.
O14818; B2R515; Q5JXJ2; Q9BR53; Q9H4K5; Q9UEU8;
08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
25-OCT-2017, entry version 191.
RecName: Full=Proteasome subunit alpha type-7;
EC=3.4.25.1 {ECO:0000269|PubMed:27176742};
AltName: Full=Proteasome subunit RC6-1;
AltName: Full=Proteasome subunit XAPC7;
Name=PSMA7; Synonyms=HSPC;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH HBX.
PubMed=8764072;
Huang J., Kwong J., Sun E.C.-Y., Liang T.J.;
"Proteasome complex as a potential cellular target of hepatitis B
virus X protein.";
J. Virol. 70:5582-5591(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Umbilical cord blood;
PubMed=11042152; DOI=10.1101/gr.140200;
Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
"Cloning and functional analysis of cDNAs with open reading frames for
300 previously undefined genes expressed in CD34+ hematopoietic
stem/progenitor cells.";
Genome Res. 10:1546-1560(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Urinary bladder;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Leukocyte, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 96-109, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[9]
FUNCTION IN ANTIGEN PRESENTATION.
PubMed=8610016; DOI=10.1038/381166a0;
Groettrup M., Soza A., Eggers M., Kuehn L., Dick T.P., Schild H.,
Rammensee H.G., Koszinowski U.H., Kloetzel P.M.;
"A role for the proteasome regulator PA28alpha in antigen
presentation.";
Nature 381:166-168(1996).
[10]
INTERACTION WITH HBX.
PubMed=10748218; DOI=10.1074/jbc.M910378199;
Zhang Z., Torii N., Furusaka A., Malayaman N., Hu Z., Liang T.J.;
"Structural and functional characterization of interaction between
hepatitis B virus X protein and the proteasome complex.";
J. Biol. Chem. 275:15157-15165(2000).
[11]
FUNCTION, AND INTERACTION WITH HIF1A.
PubMed=11389899; DOI=10.1016/S0014-5793(01)02499-1;
Cho S., Choi Y.J., Kim J.M., Jeong S.T., Kim J.H., Kim S.H., Ryu S.E.;
"Binding and regulation of HIF-1alpha by a subunit of the proteasome
complex, PSMA7.";
FEBS Lett. 498:62-66(2001).
[12]
FUNCTION.
PubMed=11713272; DOI=10.1128/MCB.21.24.8357-8364.2001;
Kruger M., Beger C., Welch P.J., Barber J.R., Manns M.P.,
Wong-Staal F.;
"Involvement of proteasome alpha-subunit PSMA7 in hepatitis C virus
internal ribosome entry site-mediated translation.";
Mol. Cell. Biol. 21:8357-8364(2001).
[13]
INDUCTION.
PubMed=11574696;
Kruger M., Beger C., Welch P.J., Barber J.R., Wong-Staal F.;
"C-SPACE (cleavage-specific amplification of cDNA ends): a novel
method of ribozyme-mediated gene identification.";
Nucleic Acids Res. 29:E94-E94(2001).
[14]
FUNCTION.
PubMed=12119296; DOI=10.1074/jbc.M204751200;
Lin H.K., Altuwaijri S., Lin W.J., Kan P.Y., Collins L.L., Chang C.;
"Proteasome activity is required for androgen receptor transcriptional
activity via regulation of androgen receptor nuclear translocation and
interaction with coregulators in prostate cancer cells.";
J. Biol. Chem. 277:36570-36576(2002).
[15]
SUBCELLULAR LOCATION.
PubMed=12181345; DOI=10.1091/mbc.E02-03-0122;
Lafarga M., Berciano M.T., Pena E., Mayo I., Castano J.G., Bohmann D.,
Rodrigues J.P., Tavanez J.P., Carmo-Fonseca M.;
"Clastosome: a subtype of nuclear body enriched in 19S and 20S
proteasomes, ubiquitin, and protein substrates of proteasome.";
Mol. Biol. Cell 13:2771-2782(2002).
[16]
INTERACTION WITH HIV-1 TAT.
PubMed=14550573; DOI=10.1016/S0014-5793(03)01025-1;
Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P.,
Mayer R.J., Krueger E.;
"Human immunodeficiency virus-1 Tat protein interacts with distinct
proteasomal alpha and beta subunits.";
FEBS Lett. 553:200-204(2003).
[17]
FUNCTION.
PubMed=15244466; DOI=10.1021/bm049957a;
Yano M., Koumoto Y., Kanesaki Y., Wu X., Kido H.;
"20S proteasome prevents aggregation of heat-denatured proteins
without PA700 regulatory subcomplex like a molecular chaperone.";
Biomacromolecules 5:1465-1469(2004).
[18]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:R8.1-R8.16(2004).
[19]
INTERACTION WITH RAB7A.
PubMed=14998988; DOI=10.1074/jbc.M401022200;
Dong J., Chen W., Welford A., Wandinger-Ness A.;
"The proteasome alpha-subunit XAPC7 interacts specifically with Rab7
and late endosomes.";
J. Biol. Chem. 279:21334-21342(2004).
[20]
INTERACTION WITH PRKN.
PubMed=15987638; DOI=10.1016/j.febslet.2005.06.003;
Dachsel J.C., Lucking C.B., Deeg S., Schultz E., Lalowski M.,
Casademunt E., Corti O., Hampe C., Patenge N., Vaupel K., Yamamoto A.,
Dichgans M., Brice A., Wanker E.E., Kahle P.J., Gasser T.;
"Parkin interacts with the proteasome subunit alpha4.";
FEBS Lett. 579:3913-3919(2005).
[21]
INTERACTION WITH PSMG1 AND PSMG2.
PubMed=16251969; DOI=10.1038/nature04106;
Hirano Y., Hendil K.B., Yashiroda H., Iemura S., Nagane R., Hioki Y.,
Natsume T., Tanaka K., Murata S.;
"A heterodimeric complex that promotes the assembly of mammalian 20S
proteasomes.";
Nature 437:1381-1385(2005).
[22]
INTERACTION WITH ABL1 AND ABL2, PHOSPHORYLATION AT TYR-153 BY ABL1 AND
ABL2, AND MUTAGENESIS OF TYR-153.
PubMed=16678104; DOI=10.1016/j.molcel.2006.04.007;
Liu X., Huang W., Li C., Li P., Yuan J., Li X., Qiu X.B., Ma Q.,
Cao C.;
"Interaction between c-Abl and Arg tyrosine kinases and proteasome
subunit PSMA7 regulates proteasome degradation.";
Mol. Cell 22:317-327(2006).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17323924; DOI=10.1021/bi061994u;
Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
"Mass spectrometric characterization of the affinity-purified human
26S proteasome complex.";
Biochemistry 46:3553-3565(2007).
[24]
INDUCTION.
PubMed=18202793;
Hu X.T., Chen W., Wang D., Shi Q.L., Zhang F.B., Liao Y.Q., Jin M.,
He C.;
"The proteasome subunit PSMA7 located on the 20q13 amplicon is
overexpressed and associated with liver metastasis in colorectal
cancer.";
Oncol. Rep. 19:441-446(2008).
[25]
INTERACTION WITH EMAP2.
PubMed=19362550; DOI=10.1016/j.yexcr.2009.03.021;
Tandle A.T., Calvani M., Uranchimeg B., Zahavi D., Melillo G.,
Libutti S.K.;
"Endothelial monocyte activating polypeptide-II modulates endothelial
cell responses by degrading hypoxia-inducible factor-1alpha through
interaction with PSMA7, a component of the proteasome.";
Exp. Cell Res. 315:1850-1859(2009).
[26]
FUNCTION, AND INTERACTION WITH MAVS.
PubMed=19734229; DOI=10.4049/jimmunol.0901646;
Jia Y., Song T., Wei C., Ni C., Zheng Z., Xu Q., Ma H., Li L.,
Zhang Y., He X., Xu Y., Shi W., Zhong H.;
"Negative regulation of MAVS-mediated innate immune response by
PSMA7.";
J. Immunol. 183:4241-4248(2009).
[27]
FUNCTION.
PubMed=19442227; DOI=10.2174/092986609788167824;
Du H., Huang X., Wang S., Wu Y., Xu W., Li M.;
"PSMA7, a potential biomarker of diseases.";
Protein Pept. Lett. 16:486-489(2009).
[28]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-227, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[30]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[32]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=27176742; DOI=10.1515/hsz-2016-0176;
Rut W., Drag M.;
"Human 20S proteasome activity towards fluorogenic peptides of various
chain lengths.";
Biol. Chem. 397:921-926(2016).
[33]
STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND SUBUNIT.
PubMed=26133119; DOI=10.1038/ncomms8573;
da Fonseca P.C., Morris E.P.;
"Cryo-EM reveals the conformation of a substrate analogue in the human
20S proteasome core.";
Nat. Commun. 6:7573-7573(2015).
[34]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2-244, AND SUBUNIT.
PubMed=25599644; DOI=10.1016/j.str.2014.11.017;
Harshbarger W., Miller C., Diedrich C., Sacchettini J.;
"Crystal structure of the human 20S proteasome in complex with
carfilzomib.";
Structure 23:418-424(2015).
[35]
STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND SUBUNIT.
PubMed=27428775; DOI=10.1038/nsmb.3273;
Huang X., Luan B., Wu J., Shi Y.;
"An atomic structure of the human 26S proteasome.";
Nat. Struct. Mol. Biol. 23:778-785(2016).
[36]
STRUCTURE BY ELECTRON MICROSCOPY (4.02 ANGSTROMS), AND SUBUNIT.
PubMed=27342858; DOI=10.1073/pnas.1608050113;
Schweitzer A., Aufderheide A., Rudack T., Beck F., Pfeifer G.,
Plitzko J.M., Sakata E., Schulten K., Foerster F., Baumeister W.;
"Structure of the human 26S proteasome at a resolution of 3.9 Aa.";
Proc. Natl. Acad. Sci. U.S.A. 113:7816-7821(2016).
[37]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), AND SUBUNIT.
PubMed=27493187; DOI=10.1126/science.aaf8993;
Schrader J., Henneberg F., Mata R.A., Tittmann K., Schneider T.R.,
Stark H., Bourenkov G., Chari A.;
"The inhibition mechanism of human 20S proteasomes enables next-
generation inhibitor design.";
Science 353:594-598(2016).
[38]
VARIANT ASP-112.
PubMed=23033978; DOI=10.1056/NEJMoa1206524;
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P.,
Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B.,
Brunner H.G., Veltman J.A., Vissers L.E.;
"Diagnostic exome sequencing in persons with severe intellectual
disability.";
N. Engl. J. Med. 367:1921-1929(2012).
-!- FUNCTION: Component of the 20S core proteasome complex involved in
the proteolytic degradation of most intracellular proteins. This
complex plays numerous essential roles within the cell by
associating with different regulatory particles. Associated with
two 19S regulatory particles, forms the 26S proteasome and thus
participates in the ATP-dependent degradation of ubiquitinated
proteins. The 26S proteasome plays a key role in the maintenance
of protein homeostasis by removing misfolded or damaged proteins
that could impair cellular functions, and by removing proteins
whose functions are no longer required. Associated with the PA200
or PA28, the 20S proteasome mediates ubiquitin-independent protein
degradation. This type of proteolysis is required in several
pathways including spermatogenesis (20S-PA200 complex) or
generation of a subset of MHC class I-presented antigenic peptides
(20S-PA28 complex). Inhibits the transactivation function of HIF-
1A under both normoxic and hypoxia-mimicking conditions. The
interaction with EMAP2 increases the proteasome-mediated HIF-1A
degradation under the hypoxic conditions. Plays a role in
hepatitis C virus internal ribosome entry site-mediated
translation. Mediates nuclear translocation of the androgen
receptor (AR) and thereby enhances androgen-mediated
transactivation. Promotes MAVS degradation and thereby negatively
regulates MAVS-mediated innate immune response.
{ECO:0000269|PubMed:11389899, ECO:0000269|PubMed:11713272,
ECO:0000269|PubMed:12119296, ECO:0000269|PubMed:15244466,
ECO:0000269|PubMed:19442227, ECO:0000269|PubMed:19734229,
ECO:0000269|PubMed:27176742, ECO:0000269|PubMed:8610016}.
-!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
specificity. {ECO:0000255|PROSITE-ProRule:PRU00808,
ECO:0000269|PubMed:27176742}.
-!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and
two 19S regulatory subunits. The 20S proteasome core is a barrel-
shaped complex made of 28 subunits that are arranged in four
stacked rings. The two outer rings are each formed by seven alpha
subunits, and the two inner rings are formed by seven beta
subunits. The proteolytic activity is exerted by three beta-
subunits PSMB5, PSMB6 and PSMB7. PSMA7 interacts directly with the
PSMG1-PSMG2 heterodimer which promotes 20S proteasome assembly
(PubMed:16251969). Interacts with HIV-1 TAT protein
(PubMed:14550573). Interacts with hepatitis B virus X protein
(HBX) (PubMed:8764072). Interacts with HIF1A. Interacts with RAB7A
(PubMed:14998988). Interacts with PRKN (PubMed:15987638).
Interacts with ABL1 and ABL2 (PubMed:16678104). Interacts with
EMAP2 (PubMed:19362550). Interacts with MAVS (PubMed:19734229).
{ECO:0000269|PubMed:10748218, ECO:0000269|PubMed:11389899,
ECO:0000269|PubMed:14550573, ECO:0000269|PubMed:14998988,
ECO:0000269|PubMed:15987638, ECO:0000269|PubMed:16251969,
ECO:0000269|PubMed:16678104, ECO:0000269|PubMed:19362550,
ECO:0000269|PubMed:19734229, ECO:0000269|PubMed:25599644,
ECO:0000269|PubMed:26133119, ECO:0000269|PubMed:27342858,
ECO:0000269|PubMed:27428775, ECO:0000269|PubMed:27493187,
ECO:0000269|PubMed:8764072}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-603272, EBI-603272;
Q19T08:ECSCR; NbExp=3; IntAct=EBI-603272, EBI-15778214;
P25786:PSMA1; NbExp=10; IntAct=EBI-603272, EBI-359352;
P25787:PSMA2; NbExp=5; IntAct=EBI-603272, EBI-603262;
P25788:PSMA3; NbExp=6; IntAct=EBI-603272, EBI-348380;
P25789:PSMA4; NbExp=8; IntAct=EBI-603272, EBI-359310;
P28066:PSMA5; NbExp=2; IntAct=EBI-603272, EBI-355475;
P60900:PSMA6; NbExp=11; IntAct=EBI-603272, EBI-357793;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12181345}.
Nucleus {ECO:0000269|PubMed:12181345}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Experimental confirmation may be lacking for some
isoforms.;
Name=1;
IsoId=O14818-1; Sequence=Displayed;
Name=2;
IsoId=O14818-2; Sequence=VSP_005281;
Name=3;
IsoId=O14818-4; Sequence=VSP_046556, VSP_046557;
-!- INDUCTION: Down-regulated by the ribozyme Rz3'X. Up-regulated in
colorectal cancer tissues. {ECO:0000269|PubMed:11574696,
ECO:0000269|PubMed:18202793}.
-!- PTM: Phosphorylation by ABL1 or ABL2 leads to an inhibition of
proteasomal activity and cell cycle transition blocks.
{ECO:0000269|PubMed:16678104}.
-!- SIMILARITY: Belongs to the peptidase T1A family.
{ECO:0000255|PROSITE-ProRule:PRU00808}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF022815; AAB81515.1; -; mRNA.
EMBL; AF054185; AAC99402.1; -; mRNA.
EMBL; BT007165; AAP35829.1; -; mRNA.
EMBL; AK312025; BAG34962.1; -; mRNA.
EMBL; AL078633; CAC04017.1; -; Genomic_DNA.
EMBL; AL078633; CAC04018.1; -; Genomic_DNA.
EMBL; CH471077; EAW75398.1; -; Genomic_DNA.
EMBL; BC004427; AAH04427.1; -; mRNA.
EMBL; BI906714; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS13489.1; -. [O14818-1]
PIR; PC2326; PC2326.
RefSeq; NP_002783.1; NM_002792.3. [O14818-1]
UniGene; Hs.233952; -.
PDB; 4R3O; X-ray; 2.60 A; D/R=2-244.
PDB; 4R67; X-ray; 2.89 A; D/R/f/t=2-244.
PDB; 5A0Q; EM; 3.50 A; D/R=1-248.
PDB; 5GJQ; EM; 4.50 A; E/k=1-248.
PDB; 5GJR; EM; 3.50 A; E/k=1-248.
PDB; 5L4G; EM; 4.02 A; D/Q=1-248.
PDB; 5LE5; X-ray; 1.80 A; C/Q=1-248.
PDB; 5LEX; X-ray; 2.20 A; C/Q=1-248.
PDB; 5LEY; X-ray; 1.90 A; C/Q=1-248.
PDB; 5LEZ; X-ray; 2.19 A; C/Q=1-248.
PDB; 5LF0; X-ray; 2.41 A; C/Q=1-248.
PDB; 5LF1; X-ray; 2.00 A; C/Q=1-248.
PDB; 5LF3; X-ray; 2.10 A; C/Q=1-248.
PDB; 5LF4; X-ray; 1.99 A; C/Q=1-248.
PDB; 5LF6; X-ray; 2.07 A; C/Q=1-248.
PDB; 5LF7; X-ray; 2.00 A; C/Q=1-248.
PDB; 5LN3; EM; 6.80 A; D=1-248.
PDB; 5M32; EM; 3.80 A; C=2-235, Q=2-236.
PDB; 5T0C; EM; 3.80 A; AJ/BJ=2-248.
PDB; 5T0G; EM; 4.40 A; J=2-248.
PDB; 5T0H; EM; 6.80 A; J=2-248.
PDB; 5T0I; EM; 8.00 A; J=2-248.
PDB; 5T0J; EM; 8.00 A; J=2-248.
PDBsum; 4R3O; -.
PDBsum; 4R67; -.
PDBsum; 5A0Q; -.
PDBsum; 5GJQ; -.
PDBsum; 5GJR; -.
PDBsum; 5L4G; -.
PDBsum; 5LE5; -.
PDBsum; 5LEX; -.
PDBsum; 5LEY; -.
PDBsum; 5LEZ; -.
PDBsum; 5LF0; -.
PDBsum; 5LF1; -.
PDBsum; 5LF3; -.
PDBsum; 5LF4; -.
PDBsum; 5LF6; -.
PDBsum; 5LF7; -.
PDBsum; 5LN3; -.
PDBsum; 5M32; -.
PDBsum; 5T0C; -.
PDBsum; 5T0G; -.
PDBsum; 5T0H; -.
PDBsum; 5T0I; -.
PDBsum; 5T0J; -.
ProteinModelPortal; O14818; -.
SMR; O14818; -.
BioGrid; 111661; 115.
CORUM; O14818; -.
DIP; DIP-29363N; -.
IntAct; O14818; 43.
MINT; MINT-5000782; -.
STRING; 9606.ENSP00000359910; -.
BindingDB; O14818; -.
ChEMBL; CHEMBL3831201; -.
DrugBank; DB07558; 2-ACETYLAMINO-4-METHYL-PENTANOIC ACID [1-(1-FORMYL-PENTYLCARBAMOYL)-3-METHYL-BUTYL]-AMIDE.
MEROPS; T01.979; -.
iPTMnet; O14818; -.
PhosphoSitePlus; O14818; -.
SwissPalm; O14818; -.
BioMuta; PSMA7; -.
REPRODUCTION-2DPAGE; IPI00024175; -.
UCD-2DPAGE; O14818; -.
EPD; O14818; -.
MaxQB; O14818; -.
PaxDb; O14818; -.
PeptideAtlas; O14818; -.
PRIDE; O14818; -.
DNASU; 5688; -.
Ensembl; ENST00000370858; ENSP00000359895; ENSG00000101182. [O14818-4]
Ensembl; ENST00000370861; ENSP00000359898; ENSG00000101182. [O14818-2]
Ensembl; ENST00000370873; ENSP00000359910; ENSG00000101182. [O14818-1]
GeneID; 5688; -.
KEGG; hsa:5688; -.
UCSC; uc002ybx.3; human. [O14818-1]
CTD; 5688; -.
DisGeNET; 5688; -.
EuPathDB; HostDB:ENSG00000101182.14; -.
GeneCards; PSMA7; -.
HGNC; HGNC:9536; PSMA7.
HPA; HPA047266; -.
MIM; 606607; gene.
neXtProt; NX_O14818; -.
OpenTargets; ENSG00000101182; -.
PharmGKB; PA33881; -.
eggNOG; KOG0183; Eukaryota.
eggNOG; ENOG410XP21; LUCA.
GeneTree; ENSGT00550000074753; -.
HOGENOM; HOG000091085; -.
HOVERGEN; HBG003005; -.
InParanoid; O14818; -.
KO; K02731; -.
OMA; PYTQKPA; -.
OrthoDB; EOG091G0GX6; -.
PhylomeDB; O14818; -.
TreeFam; TF106212; -.
Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
Reactome; R-HSA-446652; Interleukin-1 family signaling.
Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
Reactome; R-HSA-4641257; Degradation of AXIN.
Reactome; R-HSA-4641258; Degradation of DVL.
Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
Reactome; R-HSA-5362768; Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-HSA-5632684; Hedgehog 'on' state.
Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-68827; CDT1 association with the CDC6:ORC:origin complex.
Reactome; R-HSA-68949; Orc1 removal from chromatin.
Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-HSA-69229; Ubiquitin-dependent degradation of Cyclin D1.
Reactome; R-HSA-69481; G2/M Checkpoints.
Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SIGNOR; O14818; -.
ChiTaRS; PSMA7; human.
GeneWiki; PSMA7; -.
GenomeRNAi; 5688; -.
PRO; PR:O14818; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000101182; -.
CleanEx; HS_PSMA7; -.
ExpressionAtlas; O14818; baseline and differential.
Genevisible; O14818; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0098794; C:postsynapse; IEA:Ensembl.
GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB.
GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition; TAS:Reactome.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
Gene3D; 3.60.20.10; -; 1.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR023332; Proteasome_alpha-type.
InterPro; IPR035190; Proteasome_alpha7.
InterPro; IPR000426; Proteasome_asu_N.
InterPro; IPR001353; Proteasome_sua/b.
PANTHER; PTHR11599:SF40; PTHR11599:SF40; 1.
Pfam; PF00227; Proteasome; 1.
Pfam; PF10584; Proteasome_A_N; 1.
SMART; SM00948; Proteasome_A_N; 1.
SUPFAM; SSF56235; SSF56235; 1.
PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Glycoprotein;
Host-virus interaction; Hydrolase; Nucleus; Phosphoprotein;
Polymorphism; Protease; Proteasome; Reference proteome;
Threonine protease.
CHAIN 1 248 Proteasome subunit alpha type-7.
/FTId=PRO_0000124142.
MOD_RES 153 153 Phosphotyrosine; by ABL1 and ABL2.
{ECO:0000269|PubMed:16678104}.
MOD_RES 227 227 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
CARBOHYD 130 130 O-linked (GlcNAc) serine. {ECO:0000250}.
VAR_SEQ 1 70 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_005281.
VAR_SEQ 117 149 RYTQSNGRRPFGISALIVGFDFDGTPRLYQTDP -> VGAC
PLACSPLAAGQSRLRHGGSCHVTSGESEN (in isoform
3). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_046556.
VAR_SEQ 150 248 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_046557.
VARIANT 112 112 A -> D (found in patient with severe
intellectual disability; unknown
pathological significance).
{ECO:0000269|PubMed:23033978}.
/FTId=VAR_078692.
MUTAGEN 153 153 Y->F: Displays impaired G1/S transition
and S/G2 progression.
{ECO:0000269|PubMed:16678104}.
CONFLICT 160 160 A -> S (in Ref. 2; AAC99402).
{ECO:0000305}.
STRAND 6 8 {ECO:0000244|PDB:5A0Q}.
HELIX 12 14 {ECO:0000244|PDB:5LE5}.
HELIX 17 27 {ECO:0000244|PDB:5LE5}.
STRAND 32 36 {ECO:0000244|PDB:5LE5}.
STRAND 38 46 {ECO:0000244|PDB:5LE5}.
STRAND 52 54 {ECO:0000244|PDB:4R3O}.
HELIX 56 59 {ECO:0000244|PDB:5LE5}.
STRAND 61 66 {ECO:0000244|PDB:5LE5}.
STRAND 69 75 {ECO:0000244|PDB:5LE5}.
HELIX 77 98 {ECO:0000244|PDB:5LE5}.
HELIX 104 117 {ECO:0000244|PDB:5LE5}.
TURN 118 120 {ECO:0000244|PDB:5LE5}.
STRAND 129 136 {ECO:0000244|PDB:5LE5}.
STRAND 142 147 {ECO:0000244|PDB:5LE5}.
STRAND 153 162 {ECO:0000244|PDB:5LE5}.
HELIX 165 175 {ECO:0000244|PDB:5LE5}.
TURN 178 181 {ECO:0000244|PDB:5LE5}.
HELIX 184 196 {ECO:0000244|PDB:5LE5}.
STRAND 199 201 {ECO:0000244|PDB:4R67}.
STRAND 202 212 {ECO:0000244|PDB:5LE5}.
TURN 213 215 {ECO:0000244|PDB:5LE5}.
STRAND 216 219 {ECO:0000244|PDB:5LF6}.
HELIX 222 233 {ECO:0000244|PDB:5LE5}.
TURN 234 237 {ECO:0000244|PDB:5LE5}.
TURN 241 243 {ECO:0000244|PDB:4R3O}.
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


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