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Proteasome subunit alpha type-5 (EC 3.4.25.1) (Macropain zeta chain) (Multicatalytic endopeptidase complex zeta chain) (Proteasome zeta chain)

 PSA5_HUMAN              Reviewed;         241 AA.
P28066; B2R8F6; B4E2V4; Q3T1C1; Q6IBF7;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
31-OCT-2003, sequence version 3.
10-OCT-2018, entry version 208.
RecName: Full=Proteasome subunit alpha type-5;
EC=3.4.25.1 {ECO:0000269|PubMed:27176742};
AltName: Full=Macropain zeta chain;
AltName: Full=Multicatalytic endopeptidase complex zeta chain;
AltName: Full=Proteasome zeta chain;
Name=PSMA5;
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).
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 [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Testis, and Trachea;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[7]
PROTEIN SEQUENCE OF 54-58; 67-73; 94-99 AND 120-128.
TISSUE=Keratinocyte;
PubMed=1286667; DOI=10.1002/elps.11501301199;
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel
protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[8]
PROTEIN SEQUENCE OF 169-187.
Bienvenut W.V., Vuadens F., Crettaz D., Tissot J.-D., Quadroni M.;
Submitted (OCT-2003) 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]
INDUCTION, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=11771738;
Engidawork E., Juranville J.F., Fountoulakis M., Dierssen M.,
Lubec G.;
"Selective upregulation of the ubiquitin-proteasome proteolytic
pathway proteins, proteasome zeta chain and isopeptidase T in fetal
Down syndrome.";
J. Neural Transm. 61:117-130(2001).
[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]
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).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[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]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND THR-55, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[20]
INDUCTION.
PubMed=19734940; DOI=10.1038/onc.2009.264;
Arlt A., Bauer I., Schafmayer C., Tepel J., Mueerkoester S.S.,
Brosch M., Roeder C., Kalthoff H., Hampe J., Moyer M.P., Foelsch U.R.,
Schaefer H.;
"Increased proteasome subunit protein expression and proteasome
activity in colon cancer relate to an enhanced activation of nuclear
factor E2-related factor 2 (Nrf2).";
Oncogene 28:3983-3996(2009).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-56, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[23]
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).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-56 AND SER-63,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[26]
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).
[27]
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).
[28]
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).
[29]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS), 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).
[30]
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).
[31]
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).
[32]
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. PSMA5 interacts directly with the
PSMG1-PSMG2 heterodimer which promotes 20S proteasome assembly.
{ECO:0000269|PubMed:16251969, ECO:0000269|PubMed:25599644,
ECO:0000269|PubMed:26133119, ECO:0000269|PubMed:27342858,
ECO:0000269|PubMed:27428775, ECO:0000269|PubMed:27493187}.
-!- INTERACTION:
O14818:PSMA7; NbExp=2; IntAct=EBI-355475, EBI-603272;
P55036:PSMD4; NbExp=2; IntAct=EBI-355475, EBI-359318;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12181345}.
Nucleus {ECO:0000269|PubMed:12181345}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P28066-1; Sequence=Displayed;
Name=2;
IsoId=P28066-2; Sequence=VSP_046241;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in fetal brain (at protein level).
{ECO:0000269|PubMed:11771738}.
-!- INDUCTION: Up-regulated in colon cancer cell lines. Up-regulated
in fetal Down syndrome (DS) brain (at protein level). May be the
target of the transcriptional activator NFE2L2.
{ECO:0000269|PubMed:11771738, ECO:0000269|PubMed:19734940}.
-!- SIMILARITY: Belongs to the peptidase T1A family.
{ECO:0000255|PROSITE-ProRule:PRU00808}.
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EMBL; X61970; CAA43962.1; -; mRNA.
EMBL; CR456847; CAG33128.1; -; mRNA.
EMBL; AK304448; BAG65266.1; -; mRNA.
EMBL; AK313351; BAG36153.1; -; mRNA.
EMBL; AL356735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL390252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471122; EAW56381.1; -; Genomic_DNA.
EMBL; CH471122; EAW56383.1; -; Genomic_DNA.
EMBL; BC102018; AAI02019.1; -; mRNA.
EMBL; BC102019; AAI02020.1; -; mRNA.
EMBL; BC102020; AAI02021.1; -; mRNA.
EMBL; BC103751; AAI03752.1; -; mRNA.
CCDS; CCDS55619.1; -. [P28066-2]
CCDS; CCDS799.1; -. [P28066-1]
PIR; S17521; S17521.
RefSeq; NP_001186701.1; NM_001199772.1. [P28066-2]
RefSeq; NP_001186702.1; NM_001199773.1. [P28066-2]
RefSeq; NP_001186703.1; NM_001199774.1. [P28066-2]
RefSeq; NP_002781.2; NM_002790.3. [P28066-1]
UniGene; Hs.485246; -.
PDB; 4R3O; X-ray; 2.60 A; E/S=8-241.
PDB; 4R67; X-ray; 2.89 A; E/S/g/u=8-241.
PDB; 5A0Q; EM; 3.50 A; E/S=1-241.
PDB; 5GJQ; EM; 4.50 A; F/l=1-241.
PDB; 5GJR; EM; 3.50 A; F/l=1-241.
PDB; 5L4G; EM; 4.02 A; E/R=1-241.
PDB; 5LE5; X-ray; 1.80 A; D/R=1-241.
PDB; 5LEX; X-ray; 2.20 A; D/R=1-241.
PDB; 5LEY; X-ray; 1.90 A; D/R=1-241.
PDB; 5LEZ; X-ray; 2.19 A; D/R=1-241.
PDB; 5LF0; X-ray; 2.41 A; D/R=1-241.
PDB; 5LF1; X-ray; 2.00 A; D/R=1-241.
PDB; 5LF3; X-ray; 2.10 A; D/R=1-241.
PDB; 5LF4; X-ray; 1.99 A; D/R=1-241.
PDB; 5LF6; X-ray; 2.07 A; D/R=1-241.
PDB; 5LF7; X-ray; 2.00 A; D/R=1-241.
PDB; 5LN3; EM; 6.80 A; E=1-241.
PDB; 5M32; EM; 3.80 A; D/R=1-241.
PDB; 5T0C; EM; 3.80 A; AK/BK=2-241.
PDB; 5T0G; EM; 4.40 A; K=2-241.
PDB; 5T0H; EM; 6.80 A; K=2-241.
PDB; 5T0I; EM; 8.00 A; K=2-241.
PDB; 5T0J; EM; 8.00 A; K=2-241.
PDB; 5VFO; EM; 3.50 A; K/k=8-241.
PDB; 5VFP; EM; 4.20 A; K/k=8-241.
PDB; 5VFQ; EM; 4.20 A; K/k=8-241.
PDB; 5VFR; EM; 4.90 A; K/k=8-241.
PDB; 5VFS; EM; 3.60 A; K/k=8-241.
PDB; 5VFT; EM; 7.00 A; K/k=8-241.
PDB; 5VFU; EM; 5.80 A; K/k=8-241.
PDB; 6AVO; EM; 3.80 A; H/M=1-241.
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; -.
PDBsum; 5VFO; -.
PDBsum; 5VFP; -.
PDBsum; 5VFQ; -.
PDBsum; 5VFR; -.
PDBsum; 5VFS; -.
PDBsum; 5VFT; -.
PDBsum; 5VFU; -.
PDBsum; 6AVO; -.
ProteinModelPortal; P28066; -.
SMR; P28066; -.
BioGrid; 111659; 146.
CORUM; P28066; -.
DIP; DIP-29368N; -.
IntAct; P28066; 34.
MINT; P28066; -.
STRING; 9606.ENSP00000271308; -.
BindingDB; P28066; -.
ChEMBL; CHEMBL3831201; -.
MEROPS; T01.975; -.
iPTMnet; P28066; -.
PhosphoSitePlus; P28066; -.
SwissPalm; P28066; -.
BioMuta; PSMA5; -.
DMDM; 38258905; -.
DOSAC-COBS-2DPAGE; P28066; -.
REPRODUCTION-2DPAGE; IPI00291922; -.
SWISS-2DPAGE; P28066; -.
EPD; P28066; -.
MaxQB; P28066; -.
PaxDb; P28066; -.
PeptideAtlas; P28066; -.
PRIDE; P28066; -.
ProteomicsDB; 54441; -.
TopDownProteomics; P28066-1; -. [P28066-1]
DNASU; 5686; -.
Ensembl; ENST00000271308; ENSP00000271308; ENSG00000143106. [P28066-1]
Ensembl; ENST00000538610; ENSP00000440618; ENSG00000143106. [P28066-2]
GeneID; 5686; -.
KEGG; hsa:5686; -.
UCSC; uc001dxn.4; human. [P28066-1]
CTD; 5686; -.
DisGeNET; 5686; -.
EuPathDB; HostDB:ENSG00000143106.12; -.
GeneCards; PSMA5; -.
HGNC; HGNC:9534; PSMA5.
HPA; HPA028392; -.
HPA; HPA028398; -.
HPA; HPA028441; -.
MIM; 176844; gene.
neXtProt; NX_P28066; -.
OpenTargets; ENSG00000143106; -.
PharmGKB; PA33879; -.
eggNOG; KOG0176; Eukaryota.
eggNOG; COG0638; LUCA.
GeneTree; ENSGT00550000074958; -.
HOGENOM; HOG000091085; -.
HOVERGEN; HBG003005; -.
InParanoid; P28066; -.
KO; K02729; -.
OMA; FQVEYAR; -.
OrthoDB; EOG091G0GX6; -.
PhylomeDB; P28066; -.
TreeFam; TF106211; -.
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-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-6798695; Neutrophil degranulation.
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-8939902; Regulation of RUNX2 expression and activity.
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-9010553; Regulation of expression of SLITs and ROBOs.
Reactome; R-HSA-9020702; Interleukin-1 signaling.
Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SIGNOR; P28066; -.
ChiTaRS; PSMA5; human.
GeneWiki; PSMA5; -.
GenomeRNAi; 5686; -.
PRO; PR:P28066; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000143106; Expressed in 225 organ(s), highest expression level in oocyte.
CleanEx; HS_PSMA5; -.
ExpressionAtlas; P28066; baseline and differential.
Genevisible; P28066; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; HDA:UniProtKB.
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:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
CDD; cd03753; proteasome_alpha_type_5; 1.
Gene3D; 3.60.20.10; -; 1.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR023332; Proteasome_alpha-type.
InterPro; IPR033812; Proteasome_alpha_type_5.
InterPro; IPR000426; Proteasome_asu_N.
InterPro; IPR001353; Proteasome_sua/b.
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;
Nucleus; Phosphoprotein; Protease; Proteasome; Reference proteome;
Threonine protease.
CHAIN 1 241 Proteasome subunit alpha type-5.
/FTId=PRO_0000124117.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q9Z2U1}.
MOD_RES 16 16 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 55 55 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 56 56 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 63 63 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CARBOHYD 198 198 O-linked (GlcNAc) serine. {ECO:0000250}.
VAR_SEQ 1 58 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046241.
CONFLICT 27 27 A -> D (in Ref. 1; CAA43962).
{ECO:0000305}.
CONFLICT 184 184 V -> L (in Ref. 1; CAA43962).
{ECO:0000305}.
STRAND 19 21 {ECO:0000244|PDB:5A0Q}.
HELIX 22 31 {ECO:0000244|PDB:5LE5}.
STRAND 37 42 {ECO:0000244|PDB:5LE5}.
STRAND 45 51 {ECO:0000244|PDB:5LE5}.
STRAND 57 59 {ECO:0000244|PDB:5A0Q}.
HELIX 61 63 {ECO:0000244|PDB:5LE5}.
STRAND 67 71 {ECO:0000244|PDB:5LE5}.
STRAND 74 80 {ECO:0000244|PDB:5LE5}.
HELIX 82 84 {ECO:0000244|PDB:5LE5}.
HELIX 85 103 {ECO:0000244|PDB:5LE5}.
HELIX 109 117 {ECO:0000244|PDB:5LE5}.
TURN 118 121 {ECO:0000244|PDB:5LE5}.
STRAND 125 128 {ECO:0000244|PDB:5LE5}.
STRAND 133 135 {ECO:0000244|PDB:5LF6}.
STRAND 139 147 {ECO:0000244|PDB:5LE5}.
STRAND 150 156 {ECO:0000244|PDB:5LE5}.
STRAND 162 171 {ECO:0000244|PDB:5LE5}.
HELIX 174 184 {ECO:0000244|PDB:5LE5}.
HELIX 191 205 {ECO:0000244|PDB:5LE5}.
STRAND 206 208 {ECO:0000244|PDB:5A0Q}.
STRAND 214 220 {ECO:0000244|PDB:5LE5}.
STRAND 222 224 {ECO:0000244|PDB:5LE5}.
HELIX 231 238 {ECO:0000244|PDB:5LE5}.
SEQUENCE 241 AA; 26411 MW; 5610CDA00469120A CRC64;
MFLTRSEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGI QTSEGVCLAV EKRITSPLME
PSSIEKIVEI DAHIGCAMSG LIADAKTLID KARVETQNHW FTYNETMTVE SVTQAVSNLA
LQFGEEDADP GAMSRPFGVA LLFGGVDEKG PQLFHMDPSG TFVQCDARAI GSASEGAQSS
LQEVYHKSMT LKEAIKSSLI ILKQVMEEKL NATNIELATV QPGQNFHMFT KEELEEVIKD
I


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