GenomeNet

Database: UniProt
Entry: P25786
LinkDB: P25786
Original site: P25786 
ID   PSA1_HUMAN              Reviewed;         263 AA.
AC   P25786; A8K400; Q53YE8; Q9BRV9;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   02-JUN-2021, entry version 236.
DE   RecName: Full=Proteasome subunit alpha type-1;
DE   AltName: Full=30 kDa prosomal protein;
DE            Short=PROS-30;
DE   AltName: Full=Macropain subunit C2;
DE   AltName: Full=Multicatalytic endopeptidase complex subunit C2;
DE   AltName: Full=Proteasome component C2;
DE   AltName: Full=Proteasome nu chain;
GN   Name=PSMA1; Synonyms=HC2, NU, PROS30, PSC2;
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 SHORT).
RX   PubMed=1888762; DOI=10.1016/0167-4838(91)90020-z;
RA   DeMartino G.N., Orth K., McCullough M.L., Lee L.W., Munn T.Z., Moomaw C.R.,
RA   Dawson P.A., Slaughter C.A.;
RT   "The primary structures of four subunits of the human, high-molecular-
RT   weight proteinase, macropain (proteasome), are distinct but homologous.";
RL   Biochim. Biophys. Acta 1079:29-38(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RX   PubMed=2025653; DOI=10.1016/0167-4781(91)90090-9;
RA   Tamura T., Lee D.H., Osaka F., Fujiwara T., Shin S., Chung C.H., Tanaka K.,
RA   Ichihara A.;
RT   "Molecular cloning and sequence analysis of cDNAs for five major subunits
RT   of human proteasomes (multi-catalytic proteinase complexes).";
RL   Biochim. Biophys. Acta 1089:95-102(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RX   PubMed=1398136; DOI=10.1016/0378-1119(92)90098-a;
RA   Silva-Pereira I., Bey F., Coux O., Scherrer K.;
RT   "Two mRNAs exist for the Hs PROS-30 gene encoding a component of human
RT   prosomes.";
RL   Gene 120:235-242(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-37.
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
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   [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] (ISOFORM SHORT), AND VARIANT VAL-37.
RC   TISSUE=Bone marrow, Brain, Ovary, Placenta, and Prostate;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   PROTEIN SEQUENCE OF 4-18; 63-82; 97-107 AND 244-256, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA   Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [9]
RP   PROTEIN SEQUENCE OF 63-82.
RX   PubMed=7811265; DOI=10.1006/bbrc.1994.2876;
RA   Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B.;
RT   "Human proteasome subunits from 2-dimensional gels identified by partial
RT   sequencing.";
RL   Biochem. Biophys. Res. Commun. 205:1785-1789(1994).
RN   [10]
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   [11]
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   [12]
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   [13]
RP   INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=17127214; DOI=10.1016/s1672-0229(06)60029-6;
RA   Deng S., Xing T., Zhou H., Xiong R., Lu Y., Wen B., Liu S., Yang J.;
RT   "Comparative proteome analysis of breast cancer and adjacent normal breast
RT   tissues in human.";
RL   Genomics Proteomics Bioinformatics 4:165-172(2006).
RN   [14]
RP   INDUCTION.
RX   PubMed=16317774; DOI=10.1002/pmic.200500218;
RA   Cui F., Wang Y., Wang J., Wei K., Hu J., Liu F., Wang H., Zhao X.,
RA   Zhang X., Yang X.;
RT   "The up-regulation of proteasome subunits and lysosomal proteases in
RT   hepatocellular carcinomas of the HBx gene knockin transgenic mice.";
RL   Proteomics 6:498-504(2006).
RN   [15]
RP   INTERACTION WITH NOTCH3.
RX   PubMed=17292860; DOI=10.1016/j.bbrc.2007.01.151;
RA   Zhang Y., Jia L., Lee S.J., Wang M.M.;
RT   "Conserved signal peptide of Notch3 inhibits interaction with proteasome.";
RL   Biochem. Biophys. Res. Commun. 355:245-251(2007).
RN   [16]
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   [17]
RP   INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=17004105; DOI=10.1007/s10549-006-9393-7;
RA   Deng S., Zhou H., Xiong R., Lu Y., Yan D., Xing T., Dong L., Tang E.,
RA   Yang H.;
RT   "Over-expression of genes and proteins of ubiquitin specific peptidases
RT   (USPs) and proteasome subunits (PSs) in breast cancer tissue observed by
RT   the methods of RFDD-PCR and proteomics.";
RL   Breast Cancer Res. Treat. 104:21-30(2007).
RN   [18]
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   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110 AND SER-177, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [20]
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   [21]
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   [22]
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   [23]
RP   INTERACTION WITH ZFAND1.
RX   PubMed=29804830; DOI=10.1016/j.molcel.2018.04.021;
RA   Turakhiya A., Meyer S.R., Marincola G., Boehm S., Vanselow J.T.,
RA   Schlosser A., Hofmann K., Buchberger A.;
RT   "ZFAND1 recruits p97 and the 26S proteasome to promote the clearance of
RT   arsenite-induced stress granules.";
RL   Mol. Cell 70:906-919(2018).
RN   [24]
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   [25]
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 4-241, 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   [26]
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   [27]
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   [28]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), AND SUBUNIT.
RX   PubMed=27493187; DOI=10.1126/science.aaf8993;
RA   Schrader J., Henneberg F., Mata R.A., Tittmann K., Schneider T.R.,
RA   Stark H., Bourenkov G., Chari A.;
RT   "The inhibition mechanism of human 20S proteasomes enables next-generation
RT   inhibitor design.";
RL   Science 353:594-598(2016).
CC   -!- FUNCTION: Component of the 20S core proteasome complex involved in the
CC       proteolytic degradation of most intracellular proteins. This complex
CC       plays numerous essential roles within the cell by associating with
CC       different regulatory particles. Associated with two 19S regulatory
CC       particles, forms the 26S proteasome and thus participates in the ATP-
CC       dependent degradation of ubiquitinated proteins. The 26S proteasome
CC       plays a key role in the maintenance of protein homeostasis by removing
CC       misfolded or damaged proteins that could impair cellular functions, and
CC       by removing proteins whose functions are no longer required. Associated
CC       with the PA200 or PA28, the 20S proteasome mediates ubiquitin-
CC       independent protein degradation. This type of proteolysis is required
CC       in several pathways including spermatogenesis (20S-PA200 complex) or
CC       generation of a subset of MHC class I-presented antigenic peptides
CC       (20S-PA28 complex). {ECO:0000269|PubMed:15244466,
CC       ECO:0000269|PubMed:27176742, ECO:0000269|PubMed:8610016}.
CC   -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC       19S regulatory subunits. The 20S proteasome core is a barrel-shaped
CC       complex made of 28 subunits that are arranged in four stacked rings.
CC       The two outer rings are each formed by seven alpha subunits, and the
CC       two inner rings are formed by seven beta subunits. The proteolytic
CC       activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7.
CC       Interacts with NOTCH3. Interacts with ZFAND1 (PubMed:29804830).
CC       {ECO:0000269|PubMed:17292860, 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:29804830}.
CC   -!- INTERACTION:
CC       P25786; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-359352, EBI-11096309;
CC       P25786; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-359352, EBI-742038;
CC       P25786; P35609: ACTN2; NbExp=3; IntAct=EBI-359352, EBI-77797;
CC       P25786; O95994: AGR2; NbExp=3; IntAct=EBI-359352, EBI-712648;
CC       P25786; Q96GX9: APIP; NbExp=3; IntAct=EBI-359352, EBI-359248;
CC       P25786; P54253: ATXN1; NbExp=3; IntAct=EBI-359352, EBI-930964;
CC       P25786; Q9H503-2: BANF2; NbExp=6; IntAct=EBI-359352, EBI-11977289;
CC       P25786; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-359352, EBI-2548012;
CC       P25786; Q6P5X5: C22orf39; NbExp=3; IntAct=EBI-359352, EBI-7317823;
CC       P25786; Q9NP86: CABP5; NbExp=3; IntAct=EBI-359352, EBI-10311131;
CC       P25786; Q13137: CALCOCO2; NbExp=4; IntAct=EBI-359352, EBI-739580;
CC       P25786; P35520: CBS; NbExp=4; IntAct=EBI-359352, EBI-740135;
CC       P25786; Q68D86: CCDC102B; NbExp=6; IntAct=EBI-359352, EBI-10171570;
CC       P25786; Q494R4-2: CCDC153; NbExp=3; IntAct=EBI-359352, EBI-11974185;
CC       P25786; P51946: CCNH; NbExp=9; IntAct=EBI-359352, EBI-741406;
CC       P25786; P32320: CDA; NbExp=3; IntAct=EBI-359352, EBI-9250559;
CC       P25786; P55273: CDKN2D; NbExp=3; IntAct=EBI-359352, EBI-745859;
CC       P25786; Q01850: CDR2; NbExp=3; IntAct=EBI-359352, EBI-1181367;
CC       P25786; Q8NHQ1: CEP70; NbExp=6; IntAct=EBI-359352, EBI-739624;
CC       P25786; Q9P209: CEP72; NbExp=5; IntAct=EBI-359352, EBI-739498;
CC       P25786; Q8IYR0: CFAP206; NbExp=3; IntAct=EBI-359352, EBI-749051;
CC       P25786; Q9HD42: CHMP1A; NbExp=3; IntAct=EBI-359352, EBI-1057156;
CC       P25786; Q9BW66: CINP; NbExp=3; IntAct=EBI-359352, EBI-739784;
CC       P25786; Q9H9E3: COG4; NbExp=3; IntAct=EBI-359352, EBI-368382;
CC       P25786; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-359352, EBI-3866319;
CC       P25786; O43186: CRX; NbExp=3; IntAct=EBI-359352, EBI-748171;
CC       P25786; P32321: DCTD; NbExp=3; IntAct=EBI-359352, EBI-739870;
CC       P25786; Q9H773: DCTPP1; NbExp=3; IntAct=EBI-359352, EBI-723569;
CC       P25786; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-359352, EBI-742054;
CC       P25786; Q9H4E7: DEF6; NbExp=3; IntAct=EBI-359352, EBI-745369;
CC       P25786; Q8WWB3: DYDC1; NbExp=3; IntAct=EBI-359352, EBI-740680;
CC       P25786; P63172: DYNLT1; NbExp=3; IntAct=EBI-359352, EBI-1176455;
CC       P25786; A2ABF9: EHMT2; NbExp=3; IntAct=EBI-359352, EBI-10174566;
CC       P25786; P38919: EIF4A3; NbExp=3; IntAct=EBI-359352, EBI-299104;
CC       P25786; Q7Z589-5: EMSY; NbExp=3; IntAct=EBI-359352, EBI-11989522;
CC       P25786; Q9BVV2: FNDC11; NbExp=5; IntAct=EBI-359352, EBI-744935;
CC       P25786; Q3T906: GNPTAB; NbExp=3; IntAct=EBI-359352, EBI-1104907;
CC       P25786; Q08379: GOLGA2; NbExp=6; IntAct=EBI-359352, EBI-618309;
CC       P25786; Q9NYA3: GOLGA6A; NbExp=3; IntAct=EBI-359352, EBI-11163335;
CC       P25786; Q9NQX3-2: GPHN; NbExp=3; IntAct=EBI-359352, EBI-11043087;
CC       P25786; P57764: GSDMD; NbExp=3; IntAct=EBI-359352, EBI-2798865;
CC       P25786; Q96NT3-2: GUCD1; NbExp=3; IntAct=EBI-359352, EBI-11978177;
CC       P25786; V9HW80: HEL-S-70; NbExp=3; IntAct=EBI-359352, EBI-10175326;
CC       P25786; Q96MH2: HEXIM2; NbExp=3; IntAct=EBI-359352, EBI-5460660;
CC       P25786; Q9NSC5: HOMER3; NbExp=11; IntAct=EBI-359352, EBI-748420;
CC       P25786; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-359352, EBI-10961706;
CC       P25786; O43248: HOXC11; NbExp=3; IntAct=EBI-359352, EBI-2652631;
CC       P25786; Q9BPX1: HSD17B14; NbExp=3; IntAct=EBI-359352, EBI-742664;
CC       P25786; O75031: HSF2BP; NbExp=3; IntAct=EBI-359352, EBI-7116203;
CC       P25786; P42858: HTT; NbExp=3; IntAct=EBI-359352, EBI-466029;
CC       P25786; Q8IY31: IFT20; NbExp=3; IntAct=EBI-359352, EBI-744203;
CC       P25786; Q13422: IKZF1; NbExp=3; IntAct=EBI-359352, EBI-745305;
CC       P25786; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-359352, EBI-747204;
CC       P25786; Q8NBZ0: INO80E; NbExp=3; IntAct=EBI-359352, EBI-769401;
CC       P25786; O94829: IPO13; NbExp=3; IntAct=EBI-359352, EBI-747310;
CC       P25786; Q674X7-2: KAZN; NbExp=6; IntAct=EBI-359352, EBI-12024294;
CC       P25786; Q719H9: KCTD1; NbExp=3; IntAct=EBI-359352, EBI-9027502;
CC       P25786; Q8WZ19: KCTD13; NbExp=3; IntAct=EBI-359352, EBI-742916;
CC       P25786; Q8NC69: KCTD6; NbExp=6; IntAct=EBI-359352, EBI-2511344;
CC       P25786; Q96MP8-2: KCTD7; NbExp=3; IntAct=EBI-359352, EBI-11954971;
CC       P25786; Q7L273: KCTD9; NbExp=6; IntAct=EBI-359352, EBI-4397613;
CC       P25786; O75525: KHDRBS3; NbExp=3; IntAct=EBI-359352, EBI-722504;
CC       P25786; P13646: KRT13; NbExp=3; IntAct=EBI-359352, EBI-1223876;
CC       P25786; P19012: KRT15; NbExp=4; IntAct=EBI-359352, EBI-739566;
CC       P25786; P08727: KRT19; NbExp=3; IntAct=EBI-359352, EBI-742756;
CC       P25786; Q15323: KRT31; NbExp=3; IntAct=EBI-359352, EBI-948001;
CC       P25786; O76011: KRT34; NbExp=3; IntAct=EBI-359352, EBI-1047093;
CC       P25786; O76014: KRT37; NbExp=3; IntAct=EBI-359352, EBI-1045716;
CC       P25786; O76015: KRT38; NbExp=6; IntAct=EBI-359352, EBI-1047263;
CC       P25786; Q6A162: KRT40; NbExp=3; IntAct=EBI-359352, EBI-10171697;
CC       P25786; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-359352, EBI-11959885;
CC       P25786; A0A087WY89: KRTAP4-1; NbExp=3; IntAct=EBI-359352, EBI-11957260;
CC       P25786; P26371: KRTAP5-9; NbExp=6; IntAct=EBI-359352, EBI-3958099;
CC       P25786; O95751: LDOC1; NbExp=8; IntAct=EBI-359352, EBI-740738;
CC       P25786; P25791-3: LMO2; NbExp=3; IntAct=EBI-359352, EBI-11959475;
CC       P25786; Q17RB8: LONRF1; NbExp=3; IntAct=EBI-359352, EBI-2341787;
CC       P25786; Q9NQ48: LZTFL1; NbExp=3; IntAct=EBI-359352, EBI-2824799;
CC       P25786; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-359352, EBI-1216080;
CC       P25786; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-359352, EBI-741037;
CC       P25786; Q9Y6D9: MAD1L1; NbExp=3; IntAct=EBI-359352, EBI-742610;
CC       P25786; P28482: MAPK1; NbExp=3; IntAct=EBI-359352, EBI-959949;
CC       P25786; Q15691: MAPRE1; NbExp=6; IntAct=EBI-359352, EBI-1004115;
CC       P25786; Q9UPY8: MAPRE3; NbExp=4; IntAct=EBI-359352, EBI-726739;
CC       P25786; Q9UJV3-2: MID2; NbExp=6; IntAct=EBI-359352, EBI-10172526;
CC       P25786; Q9NQG6: MIEF1; NbExp=3; IntAct=EBI-359352, EBI-740987;
CC       P25786; Q9HBH9-2: MKNK2; NbExp=3; IntAct=EBI-359352, EBI-14141314;
CC       P25786; Q13064: MKRN3; NbExp=6; IntAct=EBI-359352, EBI-2340269;
CC       P25786; P40692: MLH1; NbExp=5; IntAct=EBI-359352, EBI-744248;
CC       P25786; Q96HT8: MRFAP1L1; NbExp=4; IntAct=EBI-359352, EBI-748896;
CC       P25786; Q8NCY6: MSANTD4; NbExp=3; IntAct=EBI-359352, EBI-7850168;
CC       P25786; Q5JR59: MTUS2; NbExp=6; IntAct=EBI-359352, EBI-742948;
CC       P25786; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-359352, EBI-11522433;
CC       P25786; Q15742: NAB2; NbExp=3; IntAct=EBI-359352, EBI-8641936;
CC       P25786; Q9Y5B8: NME7; NbExp=3; IntAct=EBI-359352, EBI-744782;
CC       P25786; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-359352, EBI-945833;
CC       P25786; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-359352, EBI-22310682;
CC       P25786; P61457: PCBD1; NbExp=3; IntAct=EBI-359352, EBI-740475;
CC       P25786; Q99447: PCYT2; NbExp=3; IntAct=EBI-359352, EBI-750317;
CC       P25786; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-359352, EBI-79165;
CC       P25786; Q8IYS1: PM20D2; NbExp=3; IntAct=EBI-359352, EBI-11339910;
CC       P25786; Q8ND90: PNMA1; NbExp=6; IntAct=EBI-359352, EBI-302345;
CC       P25786; Q9UL42: PNMA2; NbExp=4; IntAct=EBI-359352, EBI-302355;
CC       P25786; Q96PV4: PNMA5; NbExp=3; IntAct=EBI-359352, EBI-10171633;
CC       P25786; O15160: POLR1C; NbExp=3; IntAct=EBI-359352, EBI-1055079;
CC       P25786; Q9GZV8: PRDM14; NbExp=3; IntAct=EBI-359352, EBI-3957793;
CC       P25786; Q96LW4: PRIMPOL; NbExp=3; IntAct=EBI-359352, EBI-10044038;
CC       P25786; O60260-5: PRKN; NbExp=6; IntAct=EBI-359352, EBI-21251460;
CC       P25786; P41219: PRPH; NbExp=3; IntAct=EBI-359352, EBI-752074;
CC       P25786; P25787: PSMA2; NbExp=12; IntAct=EBI-359352, EBI-603262;
CC       P25786; P25788: PSMA3; NbExp=15; IntAct=EBI-359352, EBI-348380;
CC       P25786; P25789: PSMA4; NbExp=8; IntAct=EBI-359352, EBI-359310;
CC       P25786; O14818: PSMA7; NbExp=15; IntAct=EBI-359352, EBI-603272;
CC       P25786; P20618: PSMB1; NbExp=9; IntAct=EBI-359352, EBI-372273;
CC       P25786; P49721: PSMB2; NbExp=8; IntAct=EBI-359352, EBI-359335;
CC       P25786; Q9BYM8: RBCK1; NbExp=3; IntAct=EBI-359352, EBI-2340624;
CC       P25786; Q04864: REL; NbExp=3; IntAct=EBI-359352, EBI-307352;
CC       P25786; P35250-2: RFC2; NbExp=3; IntAct=EBI-359352, EBI-12936957;
CC       P25786; P49795: RGS19; NbExp=3; IntAct=EBI-359352, EBI-874907;
CC       P25786; Q9HAT0: ROPN1; NbExp=6; IntAct=EBI-359352, EBI-1378139;
CC       P25786; P21673: SAT1; NbExp=3; IntAct=EBI-359352, EBI-711613;
CC       P25786; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-359352, EBI-2623095;
CC       P25786; Q8IX21: SLF2; NbExp=3; IntAct=EBI-359352, EBI-2682240;
CC       P25786; O95238: SPDEF; NbExp=3; IntAct=EBI-359352, EBI-12811275;
CC       P25786; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-359352, EBI-2212028;
CC       P25786; Q99081: TCF12; NbExp=4; IntAct=EBI-359352, EBI-722877;
CC       P25786; P15884: TCF4; NbExp=3; IntAct=EBI-359352, EBI-533224;
CC       P25786; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-359352, EBI-750487;
CC       P25786; Q13829: TNFAIP1; NbExp=3; IntAct=EBI-359352, EBI-2505861;
CC       P25786; A1L306: TNR; NbExp=3; IntAct=EBI-359352, EBI-10182881;
CC       P25786; Q13077: TRAF1; NbExp=3; IntAct=EBI-359352, EBI-359224;
CC       P25786; O00463: TRAF5; NbExp=3; IntAct=EBI-359352, EBI-523498;
CC       P25786; Q9UDY6: TRIM10; NbExp=4; IntAct=EBI-359352, EBI-6427325;
CC       P25786; P36406: TRIM23; NbExp=5; IntAct=EBI-359352, EBI-740098;
CC       P25786; P14373: TRIM27; NbExp=6; IntAct=EBI-359352, EBI-719493;
CC       P25786; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-359352, EBI-5235829;
CC       P25786; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-359352, EBI-2130429;
CC       P25786; Q5T124: UBXN11; NbExp=3; IntAct=EBI-359352, EBI-746004;
CC       P25786; Q5T124-6: UBXN11; NbExp=3; IntAct=EBI-359352, EBI-11524408;
CC       P25786; P55072: VCP; NbExp=3; IntAct=EBI-359352, EBI-355164;
CC       P25786; Q2NL98: VMAC; NbExp=3; IntAct=EBI-359352, EBI-2803134;
CC       P25786; Q15007: WTAP; NbExp=3; IntAct=EBI-359352, EBI-751647;
CC       P25786; P62699: YPEL5; NbExp=3; IntAct=EBI-359352, EBI-11721624;
CC       P25786; Q96E35: ZMYND19; NbExp=3; IntAct=EBI-359352, EBI-746595;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12181345}. Nucleus
CC       {ECO:0000269|PubMed:12181345}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Short;
CC         IsoId=P25786-1; Sequence=Displayed;
CC       Name=Long;
CC         IsoId=P25786-2; Sequence=VSP_005279;
CC   -!- INDUCTION: Induced in breast cancer tissue (at protein level). Up-
CC       regulated in liver tumor tissues. {ECO:0000269|PubMed:16317774,
CC       ECO:0000269|PubMed:17004105, ECO:0000269|PubMed:17127214}.
CC   -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00808}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X61969; CAA43961.1; -; mRNA.
DR   EMBL; D00759; BAA00656.1; -; mRNA.
DR   EMBL; M64992; AAA92734.1; -; mRNA.
DR   EMBL; BT006647; AAP35293.1; -; mRNA.
DR   EMBL; AK290765; BAF83454.1; -; mRNA.
DR   EMBL; CH471064; EAW68479.1; -; Genomic_DNA.
DR   EMBL; BC002577; AAH02577.1; -; mRNA.
DR   EMBL; BC005932; AAH05932.1; -; mRNA.
DR   EMBL; BC008472; AAH08472.1; -; mRNA.
DR   EMBL; BC009576; AAH09576.1; -; mRNA.
DR   EMBL; BC015105; AAH15105.1; -; mRNA.
DR   EMBL; BC015356; AAH15356.1; -; mRNA.
DR   EMBL; BC022372; AAH22372.1; -; mRNA.
DR   CCDS; CCDS31431.1; -. [P25786-2]
DR   CCDS; CCDS7816.1; -. [P25786-1]
DR   PIR; JC1445; JC1445.
DR   RefSeq; NP_002777.1; NM_002786.3. [P25786-1]
DR   RefSeq; NP_683877.1; NM_148976.2. [P25786-2]
DR   PDB; 4R3O; X-ray; 2.60 A; F/T=4-241.
DR   PDB; 4R67; X-ray; 2.89 A; F/T/h/v=4-241.
DR   PDB; 5A0Q; EM; 3.50 A; F/T=1-263.
DR   PDB; 5GJQ; EM; 4.50 A; G/m=1-263.
DR   PDB; 5GJR; EM; 3.50 A; G/m=1-263.
DR   PDB; 5L4G; EM; 4.02 A; F/S=1-263.
DR   PDB; 5LE5; X-ray; 1.80 A; E/S=1-263.
DR   PDB; 5LEX; X-ray; 2.20 A; E/S=1-263.
DR   PDB; 5LEY; X-ray; 1.90 A; E/S=1-263.
DR   PDB; 5LEZ; X-ray; 2.19 A; E/S=1-263.
DR   PDB; 5LF0; X-ray; 2.41 A; E/S=1-263.
DR   PDB; 5LF1; X-ray; 2.00 A; E/S=1-263.
DR   PDB; 5LF3; X-ray; 2.10 A; E/S=1-263.
DR   PDB; 5LF4; X-ray; 1.99 A; E/S=1-263.
DR   PDB; 5LF6; X-ray; 2.07 A; E/S=1-263.
DR   PDB; 5LF7; X-ray; 2.00 A; E/S=1-263.
DR   PDB; 5LN3; EM; 6.80 A; F=1-263.
DR   PDB; 5M32; EM; 3.80 A; E/S=2-239.
DR   PDB; 5T0C; EM; 3.80 A; AL/BL=2-263.
DR   PDB; 5T0G; EM; 4.40 A; L=2-263.
DR   PDB; 5T0H; EM; 6.80 A; L=2-263.
DR   PDB; 5T0I; EM; 8.00 A; L=2-263.
DR   PDB; 5T0J; EM; 8.00 A; L=2-263.
DR   PDB; 5VFO; EM; 3.50 A; L/l=4-241.
DR   PDB; 5VFP; EM; 4.20 A; L/l=4-241.
DR   PDB; 5VFQ; EM; 4.20 A; L/l=4-241.
DR   PDB; 5VFR; EM; 4.90 A; L/l=4-241.
DR   PDB; 5VFS; EM; 3.60 A; L/l=4-241.
DR   PDB; 5VFT; EM; 7.00 A; L/l=4-241.
DR   PDB; 5VFU; EM; 5.80 A; L/l=4-241.
DR   PDB; 6AVO; EM; 3.80 A; G/L=1-263.
DR   PDB; 6E5B; X-ray; 2.77 A; E/S=1-263.
DR   PDB; 6KWY; EM; 2.72 A; E/S=1-263.
DR   PDB; 6MSB; EM; 3.00 A; L/l=2-263.
DR   PDB; 6MSD; EM; 3.20 A; L/l=2-263.
DR   PDB; 6MSE; EM; 3.30 A; Z=56-234.
DR   PDB; 6MSG; EM; 3.50 A; L/l=2-263.
DR   PDB; 6MSH; EM; 3.60 A; L/l=2-263.
DR   PDB; 6MSJ; EM; 3.30 A; L/l=2-263.
DR   PDB; 6MSK; EM; 3.20 A; L/l=2-263.
DR   PDB; 6R70; EM; 3.50 A; E/S=2-239.
DR   PDB; 6REY; EM; 3.00 A; F/T=1-263.
DR   PDB; 6RGQ; EM; 2.60 A; F/T=1-263.
DR   PDB; 6WJD; EM; 4.80 A; L/l=2-263.
DR   PDB; 6WJN; EM; 5.70 A; L/l=4-241.
DR   PDB; 6XMJ; EM; 3.00 A; F=4-241.
DR   PDBsum; 4R3O; -.
DR   PDBsum; 4R67; -.
DR   PDBsum; 5A0Q; -.
DR   PDBsum; 5GJQ; -.
DR   PDBsum; 5GJR; -.
DR   PDBsum; 5L4G; -.
DR   PDBsum; 5LE5; -.
DR   PDBsum; 5LEX; -.
DR   PDBsum; 5LEY; -.
DR   PDBsum; 5LEZ; -.
DR   PDBsum; 5LF0; -.
DR   PDBsum; 5LF1; -.
DR   PDBsum; 5LF3; -.
DR   PDBsum; 5LF4; -.
DR   PDBsum; 5LF6; -.
DR   PDBsum; 5LF7; -.
DR   PDBsum; 5LN3; -.
DR   PDBsum; 5M32; -.
DR   PDBsum; 5T0C; -.
DR   PDBsum; 5T0G; -.
DR   PDBsum; 5T0H; -.
DR   PDBsum; 5T0I; -.
DR   PDBsum; 5T0J; -.
DR   PDBsum; 5VFO; -.
DR   PDBsum; 5VFP; -.
DR   PDBsum; 5VFQ; -.
DR   PDBsum; 5VFR; -.
DR   PDBsum; 5VFS; -.
DR   PDBsum; 5VFT; -.
DR   PDBsum; 5VFU; -.
DR   PDBsum; 6AVO; -.
DR   PDBsum; 6E5B; -.
DR   PDBsum; 6KWY; -.
DR   PDBsum; 6MSB; -.
DR   PDBsum; 6MSD; -.
DR   PDBsum; 6MSE; -.
DR   PDBsum; 6MSG; -.
DR   PDBsum; 6MSH; -.
DR   PDBsum; 6MSJ; -.
DR   PDBsum; 6MSK; -.
DR   PDBsum; 6R70; -.
DR   PDBsum; 6REY; -.
DR   PDBsum; 6RGQ; -.
DR   PDBsum; 6WJD; -.
DR   PDBsum; 6WJN; -.
DR   PDBsum; 6XMJ; -.
DR   SMR; P25786; -.
DR   BioGRID; 111655; 365.
DR   ComplexPortal; CPX-5993; 26S Proteasome complex.
DR   CORUM; P25786; -.
DR   DIP; DIP-29369N; -.
DR   IntAct; P25786; 237.
DR   MINT; P25786; -.
DR   STRING; 9606.ENSP00000414359; -.
DR   BindingDB; P25786; -.
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   DrugCentral; P25786; -.
DR   MEROPS; T01.976; -.
DR   GlyGen; P25786; 1 site.
DR   iPTMnet; P25786; -.
DR   MetOSite; P25786; -.
DR   PhosphoSitePlus; P25786; -.
DR   SwissPalm; P25786; -.
DR   BioMuta; PSMA1; -.
DR   DMDM; 130848; -.
DR   OGP; P25786; -.
DR   REPRODUCTION-2DPAGE; IPI00016832; -.
DR   EPD; P25786; -.
DR   jPOST; P25786; -.
DR   MassIVE; P25786; -.
DR   MaxQB; P25786; -.
DR   PaxDb; P25786; -.
DR   PeptideAtlas; P25786; -.
DR   PRIDE; P25786; -.
DR   ProteomicsDB; 54287; -. [P25786-1]
DR   ProteomicsDB; 54288; -. [P25786-2]
DR   TopDownProteomics; P25786-1; -. [P25786-1]
DR   Antibodypedia; 11977; 353 antibodies.
DR   CPTC; P25786; 1 antibody.
DR   DNASU; 5682; -.
DR   Ensembl; ENST00000396394; ENSP00000379676; ENSG00000129084. [P25786-1]
DR   Ensembl; ENST00000418988; ENSP00000414359; ENSG00000129084. [P25786-2]
DR   GeneID; 5682; -.
DR   KEGG; hsa:5682; -.
DR   UCSC; uc001mlk.4; human. [P25786-1]
DR   CTD; 5682; -.
DR   DisGeNET; 5682; -.
DR   GeneCards; PSMA1; -.
DR   HGNC; HGNC:9530; PSMA1.
DR   HPA; ENSG00000129084; Low tissue specificity.
DR   MIM; 602854; gene.
DR   neXtProt; NX_P25786; -.
DR   OpenTargets; ENSG00000129084; -.
DR   PharmGKB; PA33875; -.
DR   VEuPathDB; HostDB:ENSG00000129084.17; -.
DR   eggNOG; KOG0863; Eukaryota.
DR   GeneTree; ENSGT00550000074855; -.
DR   HOGENOM; CLU_035750_8_0_1; -.
DR   InParanoid; P25786; -.
DR   OMA; TQEMVAC; -.
DR   OrthoDB; 1222564at2759; -.
DR   PhylomeDB; P25786; -.
DR   TreeFam; TF106206; -.
DR   PathwayCommons; P25786; -.
DR   Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
DR   Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR   Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR   Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR   Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR   Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR   Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR   Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
DR   Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
DR   Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR   Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR   Reactome; R-HSA-202424; Downstream TCR signaling.
DR   Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
DR   Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR   Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR   Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR   Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
DR   Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR   Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR   Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR   Reactome; R-HSA-4641257; Degradation of AXIN.
DR   Reactome; R-HSA-4641258; Degradation of DVL.
DR   Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
DR   Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD.
DR   Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR   Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR   Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
DR   Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
DR   Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR   Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR   Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
DR   Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR   Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
DR   Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR   Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR   Reactome; R-HSA-5689603; UCH proteinases.
DR   Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR   Reactome; R-HSA-68827; CDT1 association with the CDC6:ORC:origin complex.
DR   Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR   Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-HSA-69481; G2/M Checkpoints.
DR   Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR   Reactome; R-HSA-75815; Ubiquitin-dependent degradation of Cyclin D.
DR   Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR   Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR   Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR   Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR   Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
DR   Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
DR   Reactome; R-HSA-8951664; Neddylation.
DR   Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR   Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR   Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SIGNOR; P25786; -.
DR   BioGRID-ORCS; 5682; 778 hits in 993 CRISPR screens.
DR   ChiTaRS; PSMA1; human.
DR   GeneWiki; Proteasome_(prosome,_macropain)_subunit,_alpha_1; -.
DR   GenomeRNAi; 5682; -.
DR   Pharos; P25786; Tclin.
DR   PRO; PR:P25786; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; P25786; protein.
DR   Bgee; ENSG00000129084; Expressed in left adrenal gland and 127 other tissues.
DR   ExpressionAtlas; P25786; baseline and differential.
DR   Genevisible; P25786; HS.
DR   GO; GO:0005813; C:centrosome; IDA:HPA.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR   GO; GO:0005844; C:polysome; TAS:ProtInc.
DR   GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
DR   GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB.
DR   GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB.
DR   GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0001530; F:lipopolysaccharide binding; IEA:Ensembl.
DR   GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
DR   GO; GO:0002479; P:antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent; TAS:Reactome.
DR   GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0070498; P:interleukin-1-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
DR   GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
DR   GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IEA:Ensembl.
DR   GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; TAS:Reactome.
DR   GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
DR   GO; GO:0036388; P:pre-replicative complex assembly; TAS:Reactome.
DR   GO; GO:0010499; P:proteasomal ubiquitin-independent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
DR   GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
DR   GO; GO:0006521; P:regulation of cellular amino acid metabolic process; TAS:Reactome.
DR   GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
DR   GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; TAS:Reactome.
DR   GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
DR   GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
DR   GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
DR   GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
DR   GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
DR   CDD; cd03749; proteasome_alpha_type_1; 1.
DR   Gene3D; 3.60.20.10; -; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR023332; Proteasome_alpha-type.
DR   InterPro; IPR035144; Proteasome_alpha1.
DR   InterPro; IPR000426; Proteasome_asu_N.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   PANTHER; PTHR11599:SF12; PTHR11599:SF12; 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; Immunity; Isopeptide bond;
KW   Nucleus; Phosphoprotein; Proteasome; Reference proteome; Ubl conjugation.
FT   CHAIN           1..263
FT                   /note="Proteasome subunit alpha type-1"
FT                   /id="PRO_0000124060"
FT   REGION          232..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P18420"
FT   MOD_RES         110
FT                   /note="Phosphoserine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         177
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   CARBOHYD        110
FT                   /note="O-linked (GlcNAc) serine; alternate"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        115
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT   CROSSLNK        208
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT   VAR_SEQ         1
FT                   /note="M -> MQLSKVK (in isoform Long)"
FT                   /evidence="ECO:0000303|PubMed:1398136"
FT                   /id="VSP_005279"
FT   VARIANT         37
FT                   /note="G -> V (in dbSNP:rs17850016)"
FT                   /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4"
FT                   /id="VAR_067454"
FT   CONFLICT        14..15
FT                   /note="SP -> TA (in Ref. 3; AAA92734)"
FT                   /evidence="ECO:0000305"
FT   STRAND          6..8
FT                   /evidence="ECO:0007829|PDB:4R3O"
FT   STRAND          9..11
FT                   /evidence="ECO:0007829|PDB:5A0Q"
FT   STRAND          15..18
FT                   /evidence="ECO:0007829|PDB:5A0Q"
FT   HELIX           20..31
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          35..39
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          41..49
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          53..57
FT                   /evidence="ECO:0007829|PDB:5LF6"
FT   STRAND          63..67
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          70..76
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           78..99
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           105..117
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           118..121
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          122..124
FT                   /evidence="ECO:0007829|PDB:6REY"
FT   STRAND          130..138
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          141..147
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          149..151
FT                   /evidence="ECO:0007829|PDB:6RGQ"
FT   STRAND          154..162
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           165..175
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           176..181
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           184..196
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   TURN            207..209
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          210..216
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   STRAND          219..224
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           226..229
FT                   /evidence="ECO:0007829|PDB:5LE5"
FT   HELIX           230..233
FT                   /evidence="ECO:0007829|PDB:5LE5"
SQ   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
//
DBGET integrated database retrieval system