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Proteasome subunit alpha type-1 (EC 3.4.25.1) (30 kDa prosomal protein) (PROS-30) (Macropain subunit C2) (Multicatalytic endopeptidase complex subunit C2) (Proteasome component C2) (Proteasome nu chain)

 PSA1_HUMAN              Reviewed;         263 AA.
P25786; A8K400; Q53YE8; Q9BRV9;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
01-MAY-1992, sequence version 1.
25-OCT-2017, entry version 204.
RecName: Full=Proteasome subunit alpha type-1;
EC=3.4.25.1 {ECO:0000269|PubMed:27176742};
AltName: Full=30 kDa prosomal protein;
Short=PROS-30;
AltName: Full=Macropain subunit C2;
AltName: Full=Multicatalytic endopeptidase complex subunit C2;
AltName: Full=Proteasome component C2;
AltName: Full=Proteasome nu chain;
Name=PSMA1; Synonyms=HC2, NU, PROS30, PSC2;
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 SHORT).
PubMed=1888762; DOI=10.1016/0167-4838(91)90020-Z;
DeMartino G.N., Orth K., McCullough M.L., Lee L.W., Munn T.Z.,
Moomaw C.R., Dawson P.A., Slaughter C.A.;
"The primary structures of four subunits of the human, high-molecular-
weight proteinase, macropain (proteasome), are distinct but
homologous.";
Biochim. Biophys. Acta 1079:29-38(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
PubMed=2025653; DOI=10.1016/0167-4781(91)90090-9;
Tamura T., Lee D.H., Osaka F., Fujiwara T., Shin S., Chung C.H.,
Tanaka K., Ichihara A.;
"Molecular cloning and sequence analysis of cDNAs for five major
subunits of human proteasomes (multi-catalytic proteinase
complexes).";
Biochim. Biophys. Acta 1089:95-102(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
PubMed=1398136; DOI=10.1016/0378-1119(92)90098-A;
Silva-Pereira I., Bey F., Coux O., Scherrer K.;
"Two mRNAs exist for the Hs PROS-30 gene encoding a component of human
prosomes.";
Gene 120:235-242(1992).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-37.
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
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).
[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] (ISOFORM SHORT), AND VARIANT
VAL-37.
TISSUE=Bone marrow, Brain, Ovary, Placenta, and Prostate;
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 4-18; 63-82; 97-107 AND 244-256, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[9]
PROTEIN SEQUENCE OF 63-82.
PubMed=7811265; DOI=10.1006/bbrc.1994.2876;
Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B.;
"Human proteasome subunits from 2-dimensional gels identified by
partial sequencing.";
Biochem. Biophys. Res. Commun. 205:1785-1789(1994).
[10]
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).
[11]
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).
[12]
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).
[13]
INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17127214; DOI=10.1016/S1672-0229(06)60029-6;
Deng S., Xing T., Zhou H., Xiong R., Lu Y., Wen B., Liu S., Yang J.;
"Comparative proteome analysis of breast cancer and adjacent normal
breast tissues in human.";
Genomics Proteomics Bioinformatics 4:165-172(2006).
[14]
INDUCTION.
PubMed=16317774; DOI=10.1002/pmic.200500218;
Cui F., Wang Y., Wang J., Wei K., Hu J., Liu F., Wang H., Zhao X.,
Zhang X., Yang X.;
"The up-regulation of proteasome subunits and lysosomal proteases in
hepatocellular carcinomas of the HBx gene knockin transgenic mice.";
Proteomics 6:498-504(2006).
[15]
INTERACTION WITH NOTCH3.
PubMed=17292860; DOI=10.1016/j.bbrc.2007.01.151;
Zhang Y., Jia L., Lee S.J., Wang M.M.;
"Conserved signal peptide of Notch3 inhibits interaction with
proteasome.";
Biochem. Biophys. Res. Commun. 355:245-251(2007).
[16]
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).
[17]
INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17004105; DOI=10.1007/s10549-006-9393-7;
Deng S., Zhou H., Xiong R., Lu Y., Yan D., Xing T., Dong L., Tang E.,
Yang H.;
"Over-expression of genes and proteins of ubiquitin specific
peptidases (USPs) and proteasome subunits (PSs) in breast cancer
tissue observed by the methods of RFDD-PCR and proteomics.";
Breast Cancer Res. Treat. 104:21-30(2007).
[18]
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).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110 AND SER-177, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
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).
[21]
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).
[22]
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).
[23]
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).
[24]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 4-241, 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).
[25]
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).
[26]
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).
[27]
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).
-!- 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). {ECO:0000269|PubMed:15244466,
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. Interacts with NOTCH3.
{ECO:0000269|PubMed:17292860, ECO:0000269|PubMed:25599644,
ECO:0000269|PubMed:26133119, ECO:0000269|PubMed:27342858,
ECO:0000269|PubMed:27428775, ECO:0000269|PubMed:27493187}.
-!- INTERACTION:
Q9P2A4:ABI3; NbExp=3; IntAct=EBI-359352, EBI-742038;
Q96GX9:APIP; NbExp=3; IntAct=EBI-359352, EBI-359248;
Q9H2G9:BLZF1; NbExp=3; IntAct=EBI-359352, EBI-2548012;
Q13137:CALCOCO2; NbExp=3; IntAct=EBI-359352, EBI-739580;
P35520:CBS; NbExp=3; IntAct=EBI-359352, EBI-740135;
Q68D86:CCDC102B; NbExp=3; IntAct=EBI-359352, EBI-10171570;
P51946:CCNH; NbExp=8; IntAct=EBI-359352, EBI-741406;
P32320:CDA; NbExp=3; IntAct=EBI-359352, EBI-9250559;
Q8NHQ1:CEP70; NbExp=5; IntAct=EBI-359352, EBI-739624;
Q9P209:CEP72; NbExp=5; IntAct=EBI-359352, EBI-739498;
Q9Y2V7:COG6; NbExp=4; IntAct=EBI-359352, EBI-3866319;
A2ABF9:EHMT2; NbExp=3; IntAct=EBI-359352, EBI-10174566;
Q3T906:GNPTAB; NbExp=3; IntAct=EBI-359352, EBI-1104907;
Q08379:GOLGA2; NbExp=5; IntAct=EBI-359352, EBI-618309;
V9HW80:HEL-S-70; NbExp=3; IntAct=EBI-359352, EBI-10175326;
Q9NSC5:HOMER3; NbExp=7; IntAct=EBI-359352, EBI-748420;
Q8IY31:IFT20; NbExp=3; IntAct=EBI-359352, EBI-744203;
Q13422:IKZF1; NbExp=3; IntAct=EBI-359352, EBI-745305;
Q9UKT9:IKZF3; NbExp=3; IntAct=EBI-359352, EBI-747204;
Q8NBZ0:INO80E; NbExp=3; IntAct=EBI-359352, EBI-769401;
Q719H9:KCTD1; NbExp=3; IntAct=EBI-359352, EBI-9027502;
Q7L273:KCTD9; NbExp=3; IntAct=EBI-359352, EBI-4397613;
P19012:KRT15; NbExp=4; IntAct=EBI-359352, EBI-739566;
Q15323:KRT31; NbExp=3; IntAct=EBI-359352, EBI-948001;
O76015:KRT38; NbExp=5; IntAct=EBI-359352, EBI-1047263;
Q6A162:KRT40; NbExp=3; IntAct=EBI-359352, EBI-10171697;
P26371:KRTAP5-9; NbExp=5; IntAct=EBI-359352, EBI-3958099;
O95751:LDOC1; NbExp=7; IntAct=EBI-359352, EBI-740738;
Q9BRK4:LZTS2; NbExp=3; IntAct=EBI-359352, EBI-741037;
Q9Y6D9:MAD1L1; NbExp=3; IntAct=EBI-359352, EBI-742610;
Q15691:MAPRE1; NbExp=3; IntAct=EBI-359352, EBI-1004115;
Q9UPY8:MAPRE3; NbExp=4; IntAct=EBI-359352, EBI-726739;
Q9UJV3-2:MID2; NbExp=3; IntAct=EBI-359352, EBI-10172526;
Q13064:MKRN3; NbExp=5; IntAct=EBI-359352, EBI-2340269;
P40692:MLH1; NbExp=3; IntAct=EBI-359352, EBI-744248;
Q96HT8:MRFAP1L1; NbExp=4; IntAct=EBI-359352, EBI-748896;
Q5JR59:MTUS2; NbExp=6; IntAct=EBI-359352, EBI-742948;
Q7Z3S9:NOTCH2NL; NbExp=5; IntAct=EBI-359352, EBI-945833;
Q9NRD5:PICK1; NbExp=4; IntAct=EBI-359352, EBI-79165;
Q8ND90:PNMA1; NbExp=5; IntAct=EBI-359352, EBI-302345;
Q9UL42:PNMA2; NbExp=3; IntAct=EBI-359352, EBI-302355;
Q96PV4:PNMA5; NbExp=3; IntAct=EBI-359352, EBI-10171633;
Q9GZV8:PRDM14; NbExp=3; IntAct=EBI-359352, EBI-3957793;
P25787:PSMA2; NbExp=6; IntAct=EBI-359352, EBI-603262;
P25788:PSMA3; NbExp=9; IntAct=EBI-359352, EBI-348380;
P25789:PSMA4; NbExp=4; IntAct=EBI-359352, EBI-359310;
O14818:PSMA7; NbExp=10; IntAct=EBI-359352, EBI-603272;
P49721:PSMB2; NbExp=3; IntAct=EBI-359352, EBI-359335;
Q04864:REL; NbExp=3; IntAct=EBI-359352, EBI-307352;
Q9HAT0:ROPN1; NbExp=5; IntAct=EBI-359352, EBI-1378139;
Q9Y371:SH3GLB1; NbExp=3; IntAct=EBI-359352, EBI-2623095;
Q9Y2D8:SSX2IP; NbExp=3; IntAct=EBI-359352, EBI-2212028;
Q99081:TCF12; NbExp=3; IntAct=EBI-359352, EBI-722877;
P15884:TCF4; NbExp=3; IntAct=EBI-359352, EBI-533224;
Q13829:TNFAIP1; NbExp=3; IntAct=EBI-359352, EBI-2505861;
A1L306:TNR; NbExp=3; IntAct=EBI-359352, EBI-10182881;
Q13077:TRAF1; NbExp=3; IntAct=EBI-359352, EBI-359224;
Q9UDY6:TRIM10; NbExp=3; IntAct=EBI-359352, EBI-6427325;
P36406:TRIM23; NbExp=5; IntAct=EBI-359352, EBI-740098;
P14373:TRIM27; NbExp=5; IntAct=EBI-359352, EBI-719493;
Q8IWZ5:TRIM42; NbExp=3; IntAct=EBI-359352, EBI-5235829;
Q5T124:UBXN11; NbExp=3; IntAct=EBI-359352, EBI-746004;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12181345}.
Nucleus {ECO:0000269|PubMed:12181345}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Short;
IsoId=P25786-1; Sequence=Displayed;
Name=Long;
IsoId=P25786-2; Sequence=VSP_005279;
-!- INDUCTION: Induced in breast cancer tissue (at protein level). Up-
regulated in liver tumor tissues. {ECO:0000269|PubMed:16317774,
ECO:0000269|PubMed:17004105, ECO:0000269|PubMed:17127214}.
-!- SIMILARITY: Belongs to the peptidase T1A family.
{ECO:0000255|PROSITE-ProRule:PRU00808}.
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EMBL; X61969; CAA43961.1; -; mRNA.
EMBL; D00759; BAA00656.1; -; mRNA.
EMBL; M64992; AAA92734.1; -; mRNA.
EMBL; BT006647; AAP35293.1; -; mRNA.
EMBL; AK290765; BAF83454.1; -; mRNA.
EMBL; CH471064; EAW68479.1; -; Genomic_DNA.
EMBL; BC002577; AAH02577.1; -; mRNA.
EMBL; BC005932; AAH05932.1; -; mRNA.
EMBL; BC008472; AAH08472.1; -; mRNA.
EMBL; BC009576; AAH09576.1; -; mRNA.
EMBL; BC015105; AAH15105.1; -; mRNA.
EMBL; BC015356; AAH15356.1; -; mRNA.
EMBL; BC022372; AAH22372.1; -; mRNA.
CCDS; CCDS31431.1; -. [P25786-2]
CCDS; CCDS7816.1; -. [P25786-1]
PIR; JC1445; JC1445.
RefSeq; NP_002777.1; NM_002786.3. [P25786-1]
RefSeq; NP_683877.1; NM_148976.2. [P25786-2]
UniGene; Hs.102798; -.
PDB; 4R3O; X-ray; 2.60 A; F/T=4-241.
PDB; 4R67; X-ray; 2.89 A; F/T/h/v=4-241.
PDB; 5A0Q; EM; 3.50 A; F/T=1-263.
PDB; 5GJQ; EM; 4.50 A; G/m=1-263.
PDB; 5GJR; EM; 3.50 A; G/m=1-263.
PDB; 5L4G; EM; 4.02 A; F/S=1-263.
PDB; 5LE5; X-ray; 1.80 A; E/S=1-263.
PDB; 5LEX; X-ray; 2.20 A; E/S=1-263.
PDB; 5LEY; X-ray; 1.90 A; E/S=1-263.
PDB; 5LEZ; X-ray; 2.19 A; E/S=1-263.
PDB; 5LF0; X-ray; 2.41 A; E/S=1-263.
PDB; 5LF1; X-ray; 2.00 A; E/S=1-263.
PDB; 5LF3; X-ray; 2.10 A; E/S=1-263.
PDB; 5LF4; X-ray; 1.99 A; E/S=1-263.
PDB; 5LF6; X-ray; 2.07 A; E/S=1-263.
PDB; 5LF7; X-ray; 2.00 A; E/S=1-263.
PDB; 5LN3; EM; 6.80 A; F=1-263.
PDB; 5T0C; EM; 3.80 A; AL/BL=2-263.
PDB; 5T0G; EM; 4.40 A; L=2-263.
PDB; 5T0H; EM; 6.80 A; L=2-263.
PDB; 5T0I; EM; 8.00 A; L=2-263.
PDB; 5T0J; EM; 8.00 A; L=2-263.
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; 5T0C; -.
PDBsum; 5T0G; -.
PDBsum; 5T0H; -.
PDBsum; 5T0I; -.
PDBsum; 5T0J; -.
ProteinModelPortal; P25786; -.
SMR; P25786; -.
BioGrid; 111655; 196.
CORUM; P25786; -.
DIP; DIP-29369N; -.
IntAct; P25786; 166.
MINT; MINT-1155600; -.
STRING; 9606.ENSP00000414359; -.
BindingDB; P25786; -.
ChEMBL; CHEMBL3831201; -.
MEROPS; T01.976; -.
iPTMnet; P25786; -.
PhosphoSitePlus; P25786; -.
SwissPalm; P25786; -.
BioMuta; PSMA1; -.
DMDM; 130848; -.
OGP; P25786; -.
REPRODUCTION-2DPAGE; IPI00016832; -.
EPD; P25786; -.
MaxQB; P25786; -.
PaxDb; P25786; -.
PeptideAtlas; P25786; -.
PRIDE; P25786; -.
TopDownProteomics; P25786-1; -. [P25786-1]
DNASU; 5682; -.
Ensembl; ENST00000396394; ENSP00000379676; ENSG00000129084. [P25786-1]
Ensembl; ENST00000418988; ENSP00000414359; ENSG00000129084. [P25786-2]
GeneID; 5682; -.
KEGG; hsa:5682; -.
UCSC; uc001mlk.4; human. [P25786-1]
CTD; 5682; -.
DisGeNET; 5682; -.
EuPathDB; HostDB:ENSG00000129084.17; -.
GeneCards; PSMA1; -.
HGNC; HGNC:9530; PSMA1.
HPA; CAB033765; -.
HPA; HPA037646; -.
HPA; HPA043891; -.
MIM; 602854; gene.
neXtProt; NX_P25786; -.
OpenTargets; ENSG00000129084; -.
PharmGKB; PA33875; -.
eggNOG; KOG0863; Eukaryota.
eggNOG; COG0638; LUCA.
GeneTree; ENSGT00550000074855; -.
HOGENOM; HOG000091080; -.
HOVERGEN; HBG105373; -.
InParanoid; P25786; -.
KO; K02725; -.
OMA; FMKQQCL; -.
OrthoDB; EOG091G0DNK; -.
PhylomeDB; P25786; -.
TreeFam; TF106206; -.
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.
ChiTaRS; PSMA1; human.
GeneWiki; Proteasome_(prosome,_macropain)_subunit,_alpha_1; -.
GenomeRNAi; 5682; -.
PRO; PR:P25786; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000129084; -.
CleanEx; HS_PSMA1; -.
ExpressionAtlas; P25786; baseline and differential.
Genevisible; P25786; HS.
GO; GO:0005813; C:centrosome; IDA:HPA.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005844; C:polysome; TAS:ProtInc.
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:0003723; F:RNA binding; TAS:ProtInc.
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:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
CDD; cd03749; proteasome_alpha_type_1; 1.
Gene3D; 3.60.20.10; -; 1.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR023332; Proteasome_alpha-type.
InterPro; IPR035144; Proteasome_alpha1.
InterPro; IPR000426; Proteasome_asu_N.
InterPro; IPR001353; Proteasome_sua/b.
PANTHER; PTHR11599:SF12; PTHR11599:SF12; 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; Hydrolase;
Immunity; Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism;
Protease; Proteasome; Reference proteome; Threonine protease;
Ubl conjugation.
CHAIN 1 263 Proteasome subunit alpha type-1.
/FTId=PRO_0000124060.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P18420}.
MOD_RES 110 110 Phosphoserine; alternate.
{ECO:0000244|PubMed:23186163}.
MOD_RES 177 177 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CARBOHYD 110 110 O-linked (GlcNAc) serine; alternate.
{ECO:0000250}.
CROSSLNK 115 115 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
CROSSLNK 208 208 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
VAR_SEQ 1 1 M -> MQLSKVK (in isoform Long).
{ECO:0000303|PubMed:1398136}.
/FTId=VSP_005279.
VARIANT 37 37 G -> V (in dbSNP:rs17850016).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.4}.
/FTId=VAR_067454.
CONFLICT 14 15 SP -> TA (in Ref. 3; AAA92734).
{ECO:0000305}.
STRAND 6 8 {ECO:0000244|PDB:4R3O}.
STRAND 9 11 {ECO:0000244|PDB:5A0Q}.
STRAND 15 18 {ECO:0000244|PDB:5A0Q}.
HELIX 20 31 {ECO:0000244|PDB:5LE5}.
STRAND 35 39 {ECO:0000244|PDB:5LE5}.
STRAND 41 49 {ECO:0000244|PDB:5LE5}.
STRAND 53 57 {ECO:0000244|PDB:5LF6}.
STRAND 63 67 {ECO:0000244|PDB:5LE5}.
STRAND 70 76 {ECO:0000244|PDB:5LE5}.
HELIX 78 99 {ECO:0000244|PDB:5LE5}.
HELIX 105 117 {ECO:0000244|PDB:5LE5}.
HELIX 118 121 {ECO:0000244|PDB:5LE5}.
STRAND 122 124 {ECO:0000244|PDB:5A0Q}.
STRAND 130 138 {ECO:0000244|PDB:5LE5}.
STRAND 141 147 {ECO:0000244|PDB:5LE5}.
STRAND 149 151 {ECO:0000244|PDB:5A0Q}.
STRAND 154 162 {ECO:0000244|PDB:5LE5}.
HELIX 165 175 {ECO:0000244|PDB:5LE5}.
HELIX 176 181 {ECO:0000244|PDB:5LE5}.
HELIX 184 196 {ECO:0000244|PDB:5LE5}.
TURN 207 209 {ECO:0000244|PDB:5LE5}.
STRAND 210 216 {ECO:0000244|PDB:5LE5}.
STRAND 219 224 {ECO:0000244|PDB:5LE5}.
HELIX 226 229 {ECO:0000244|PDB:5LE5}.
HELIX 230 233 {ECO:0000244|PDB:5LE5}.
SEQUENCE 263 AA; 29556 MW; 3F159C5BCEFE8DED CRC64;
MFRNQYDNDV TVWSPQGRIH QIEYAMEAVK QGSATVGLKS KTHAVLVALK RAQSELAAHQ
KKILHVDNHI GISIAGLTAD ARLLCNFMRQ ECLDSRFVFD RPLPVSRLVS LIGSKTQIPT
QRYGRRPYGV GLLIAGYDDM GPHIFQTCPS ANYFDCRAMS IGARSQSART YLERHMSEFM
ECNLNELVKH GLRALRETLP AEQDLTTKNV SIGIVGKDLE FTIYDDDDVS PFLEGLEERP
QRKAQPAQPA DEPAEKADEP MEH


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