PSA6_HUMAN
ID PSA6_HUMAN Reviewed; 246 AA.
AC P60900; B2R7J9; B4DQR4; B4DXJ9; P34062; Q6IB60;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Proteasome subunit alpha type-6;
DE AltName: Full=27 kDa prosomal protein;
DE Short=PROS-27;
DE Short=p27K;
DE AltName: Full=Macropain iota chain;
DE AltName: Full=Multicatalytic endopeptidase complex iota chain;
DE AltName: Full=Proteasome iota chain;
GN Name=PSMA6; Synonyms=PROS27;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7681138; DOI=10.1007/bf00282801;
RA Bey F., Pereira I.S., Coux O., Viegas-Pequignot E., Targa F.R.,
RA Nothwang H.G., Dutrillaux B., Scherrer K.;
RT "The prosomal RNA-binding protein p27K is a member of the alpha-type human
RT prosomal gene family.";
RL Mol. Gen. Genet. 237:193-205(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Cerebellum, and Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Lymph, Skeletal muscle, and Skin;
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 [7]
RP PROTEIN SEQUENCE OF 12-43; 60-88; 105-116; 154-164; 172-181 AND 229-246,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-246 (ISOFORM 1), AND PARTIAL PROTEIN
RP SEQUENCE.
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 [9]
RP PARTIAL PROTEIN SEQUENCE.
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 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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-102 AND LYS-104, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [15]
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 [16]
RP INTERACTION WITH ALKBH4.
RX PubMed=23145062; DOI=10.1371/journal.pone.0049045;
RA Bjornstad L.G., Meza T.J., Otterlei M., Olafsrud S.M., Meza-Zepeda L.A.,
RA Falnes P.O.;
RT "Human ALKBH4 interacts with proteins associated with transcription.";
RL PLoS ONE 7:E49045-E49045(2012).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-63 AND SER-64, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [18]
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 [19]
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 [20]
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 [21]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2-245, 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 [22]
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 [23]
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 [24]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), AND SUBUNIT.
RX PubMed=27493187; DOI=10.1126/science.aaf8993;
RA Schrader J., Henneberg F., Mata R.A., Tittmann K., Schneider T.R.,
RA Stark H., Bourenkov G., Chari A.;
RT "The inhibition mechanism of human 20S proteasomes enables next-generation
RT inhibitor design.";
RL Science 353:594-598(2016).
RN [25]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) IN COMPLEX WITH AKIRIN2,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=34711951; DOI=10.1038/s41586-021-04035-8;
RA de Almeida M., Hinterndorfer M., Brunner H., Grishkovskaya I., Singh K.,
RA Schleiffer A., Jude J., Deswal S., Kalis R., Vunjak M., Lendl T., Imre R.,
RA Roitinger E., Neumann T., Kandolf S., Schutzbier M., Mechtler K.,
RA Versteeg G.A., Haselbach D., Zuber J.;
RT "AKIRIN2 controls the nuclear import of proteasomes in vertebrates.";
RL Nature 599:491-496(2021).
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 (PubMed:25599644, PubMed:26133119,
CC PubMed:27342858, PubMed:27428775, PubMed:27493187, PubMed:34711951).
CC The 20S proteasome core is a barrel-shaped complex made of 28 subunits
CC that are arranged in four stacked rings (PubMed:25599644,
CC PubMed:26133119, PubMed:27342858, PubMed:27428775, PubMed:27493187,
CC PubMed:34711951). The two outer rings are each formed by seven alpha
CC subunits, and the two inner rings are formed by seven beta subunits
CC (PubMed:25599644, PubMed:26133119, PubMed:27342858, PubMed:27428775,
CC PubMed:27493187, PubMed:34711951). The proteolytic activity is exerted
CC by three beta-subunits PSMB5, PSMB6 and PSMB7 (PubMed:25599644,
CC PubMed:26133119, PubMed:27342858, PubMed:27428775, PubMed:27493187,
CC PubMed:34711951). Interacts with ALKBH4 (PubMed:23145062).
CC {ECO:0000269|PubMed:23145062, ECO:0000269|PubMed:25599644,
CC ECO:0000269|PubMed:26133119, ECO:0000269|PubMed:27342858,
CC ECO:0000269|PubMed:27428775, ECO:0000269|PubMed:27493187,
CC ECO:0000269|PubMed:34711951}.
CC -!- INTERACTION:
CC P60900; Q0VDD7: BRME1; NbExp=3; IntAct=EBI-357793, EBI-741210;
CC P60900; Q8N9M1-2: C19orf47; NbExp=3; IntAct=EBI-357793, EBI-10979594;
CC P60900; Q9BY67: CADM1; NbExp=3; IntAct=EBI-357793, EBI-5652260;
CC P60900; P84090: ERH; NbExp=3; IntAct=EBI-357793, EBI-711389;
CC P60900; P42858: HTT; NbExp=4; IntAct=EBI-357793, EBI-466029;
CC P60900; Q9BYR5: KRTAP4-2; NbExp=3; IntAct=EBI-357793, EBI-10172511;
CC P60900; Q9BT23: LIMD2; NbExp=3; IntAct=EBI-357793, EBI-2805292;
CC P60900; P62875: POLR2L; NbExp=3; IntAct=EBI-357793, EBI-359527;
CC P60900; P25787: PSMA2; NbExp=6; IntAct=EBI-357793, EBI-603262;
CC P60900; P25788: PSMA3; NbExp=10; IntAct=EBI-357793, EBI-348380;
CC P60900; P25789: PSMA4; NbExp=5; IntAct=EBI-357793, EBI-359310;
CC P60900; O14818: PSMA7; NbExp=11; IntAct=EBI-357793, EBI-603272;
CC P60900; O43242: PSMD3; NbExp=3; IntAct=EBI-357793, EBI-357622;
CC P60900; Q96K19: RNF170; NbExp=3; IntAct=EBI-357793, EBI-2130336;
CC P60900; Q14D33: RTP5; NbExp=3; IntAct=EBI-357793, EBI-10217913;
CC P60900; A2RU48: SMCO3; NbExp=3; IntAct=EBI-357793, EBI-10173195;
CC P60900; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-357793, EBI-11139477;
CC P60900; Q9HCM9: TRIM39; NbExp=3; IntAct=EBI-357793, EBI-739510;
CC P60900; Q9HCM9-2: TRIM39; NbExp=5; IntAct=EBI-357793, EBI-11523450;
CC P60900; Q6FI91: TSPYL; NbExp=3; IntAct=EBI-357793, EBI-723389;
CC P60900; Q9Y5K5: UCHL5; NbExp=4; IntAct=EBI-357793, EBI-1051183;
CC P60900; Q8NCP5: ZBTB44; NbExp=3; IntAct=EBI-357793, EBI-5658292;
CC P60900; Q969J2: ZKSCAN4; NbExp=3; IntAct=EBI-357793, EBI-2818641;
CC P60900; Q8TC21: ZNF596; NbExp=3; IntAct=EBI-357793, EBI-3923453;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9QUM9,
CC ECO:0000269|PubMed:12181345}. Nucleus {ECO:0000269|PubMed:12181345,
CC ECO:0000269|PubMed:34711951}. Note=Translocated from the cytoplasm into
CC the nucleus following interaction with AKIRIN2, which bridges the
CC proteasome with the nuclear import receptor IPO9 (PubMed:34711951).
CC Colocalizes with TRIM5 in cytoplasmic bodies (By similarity).
CC {ECO:0000250|UniProtKB:Q9QUM9, ECO:0000269|PubMed:34711951}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P60900-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P60900-2; Sequence=VSP_054587;
CC Name=3;
CC IsoId=P60900-3; Sequence=VSP_054586;
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC ProRule:PRU00808}.
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DR EMBL; X59417; CAA42052.1; -; mRNA.
DR EMBL; CR456944; CAG33225.1; -; mRNA.
DR EMBL; AK298920; BAG61026.1; -; mRNA.
DR EMBL; AK302008; BAG63411.1; -; mRNA.
DR EMBL; AK313011; BAG35846.1; -; mRNA.
DR EMBL; AK316223; BAH14594.1; -; mRNA.
DR EMBL; AL121594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133163; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW65876.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW65877.1; -; Genomic_DNA.
DR EMBL; BC002979; AAH02979.1; -; mRNA.
DR EMBL; BC017882; AAH17882.1; -; mRNA.
DR EMBL; BC022354; AAH22354.1; -; mRNA.
DR EMBL; BC023659; AAH23659.1; -; mRNA.
DR EMBL; BC070137; AAH70137.1; -; mRNA.
DR EMBL; X61972; CAA43964.1; -; mRNA.
DR CCDS; CCDS61437.1; -. [P60900-2]
DR CCDS; CCDS61438.1; -. [P60900-3]
DR CCDS; CCDS9655.1; -. [P60900-1]
DR PIR; S30274; S30274.
DR RefSeq; NP_001269161.1; NM_001282232.1. [P60900-3]
DR RefSeq; NP_001269162.1; NM_001282233.1. [P60900-3]
DR RefSeq; NP_001269163.1; NM_001282234.1. [P60900-2]
DR RefSeq; NP_002782.1; NM_002791.2. [P60900-1]
DR RefSeq; XP_016876957.1; XM_017021468.1. [P60900-3]
DR PDB; 4R3O; X-ray; 2.60 A; A/O=2-245.
DR PDB; 4R67; X-ray; 2.89 A; A/O/c/q=2-245.
DR PDB; 5A0Q; EM; 3.50 A; A/O=1-246.
DR PDB; 5GJQ; EM; 4.50 A; B/h=1-246.
DR PDB; 5GJR; EM; 3.50 A; B/h=1-246.
DR PDB; 5L4G; EM; 4.02 A; A/N=1-246.
DR PDB; 5LE5; X-ray; 1.80 A; G/U=1-246.
DR PDB; 5LEX; X-ray; 2.20 A; G/U=1-246.
DR PDB; 5LEY; X-ray; 1.90 A; G/U=1-246.
DR PDB; 5LEZ; X-ray; 2.19 A; G/U=1-246.
DR PDB; 5LF0; X-ray; 2.41 A; G/U=1-246.
DR PDB; 5LF1; X-ray; 2.00 A; G/U=1-246.
DR PDB; 5LF3; X-ray; 2.10 A; G/U=1-246.
DR PDB; 5LF4; X-ray; 1.99 A; G/U=1-246.
DR PDB; 5LF6; X-ray; 2.07 A; G/U=1-246.
DR PDB; 5LF7; X-ray; 2.00 A; G/U=1-246.
DR PDB; 5LN3; EM; 6.80 A; A=1-246.
DR PDB; 5M32; EM; 3.80 A; G/U=1-246.
DR PDB; 5T0C; EM; 3.80 A; AG/BG=2-246.
DR PDB; 5T0G; EM; 4.40 A; G=2-246.
DR PDB; 5T0H; EM; 6.80 A; G=2-246.
DR PDB; 5T0I; EM; 8.00 A; G=2-246.
DR PDB; 5T0J; EM; 8.00 A; G=2-246.
DR PDB; 5VFO; EM; 3.50 A; G/g=5-244.
DR PDB; 5VFP; EM; 4.20 A; G/g=5-244.
DR PDB; 5VFQ; EM; 4.20 A; G/g=5-244.
DR PDB; 5VFR; EM; 4.90 A; G/g=5-244.
DR PDB; 5VFS; EM; 3.60 A; G/g=5-244.
DR PDB; 5VFT; EM; 7.00 A; G/g=5-244.
DR PDB; 5VFU; EM; 5.80 A; G/g=5-244.
DR PDB; 6AVO; EM; 3.80 A; K/R=1-246.
DR PDB; 6E5B; X-ray; 2.77 A; G/U=1-246.
DR PDB; 6KWY; EM; 2.72 A; G/U=1-246.
DR PDB; 6MSB; EM; 3.00 A; G/g=2-246.
DR PDB; 6MSD; EM; 3.20 A; G/g=2-246.
DR PDB; 6MSG; EM; 3.50 A; G/g=2-246.
DR PDB; 6MSH; EM; 3.60 A; G/g=2-246.
DR PDB; 6MSK; EM; 3.20 A; G/g=2-246.
DR PDB; 6R70; EM; 3.50 A; G/U=2-245.
DR PDB; 6REY; EM; 3.00 A; A/O=1-246.
DR PDB; 6RGQ; EM; 2.60 A; A/O=1-246.
DR PDB; 6WJD; EM; 4.80 A; G/g=2-246.
DR PDB; 6WJN; EM; 5.70 A; G/g=5-244.
DR PDB; 6XMJ; EM; 3.00 A; A=2-245.
DR PDB; 7AWE; X-ray; 2.29 A; A/O=4-245.
DR PDB; 7B12; X-ray; 2.43 A; A/O=4-245.
DR PDB; 7LXV; EM; 3.40 A; G/U=1-246.
DR PDB; 7NHT; EM; 2.80 A; G=1-246.
DR PDB; 7PG9; EM; 3.70 A; A/O=1-246.
DR PDB; 7V5G; EM; 4.47 A; O/V=1-246.
DR PDB; 7V5M; EM; 3.88 A; A/O=1-246.
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; 6MSG; -.
DR PDBsum; 6MSH; -.
DR PDBsum; 6MSK; -.
DR PDBsum; 6R70; -.
DR PDBsum; 6REY; -.
DR PDBsum; 6RGQ; -.
DR PDBsum; 6WJD; -.
DR PDBsum; 6WJN; -.
DR PDBsum; 6XMJ; -.
DR PDBsum; 7AWE; -.
DR PDBsum; 7B12; -.
DR PDBsum; 7LXV; -.
DR PDBsum; 7NHT; -.
DR PDBsum; 7PG9; -.
DR PDBsum; 7V5G; -.
DR PDBsum; 7V5M; -.
DR AlphaFoldDB; P60900; -.
DR SMR; P60900; -.
DR BioGRID; 111660; 220.
DR ComplexPortal; CPX-5993; 26S Proteasome complex.
DR CORUM; P60900; -.
DR DIP; DIP-29367N; -.
DR IntAct; P60900; 82.
DR MINT; P60900; -.
DR STRING; 9606.ENSP00000261479; -.
DR BindingDB; P60900; -.
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 MEROPS; T01.971; -.
DR GlyGen; P60900; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P60900; -.
DR MetOSite; P60900; -.
DR PhosphoSitePlus; P60900; -.
DR SwissPalm; P60900; -.
DR BioMuta; PSMA6; -.
DR DMDM; 46397659; -.
DR REPRODUCTION-2DPAGE; IPI00029623; -.
DR SWISS-2DPAGE; P60900; -.
DR UCD-2DPAGE; P60900; -.
DR EPD; P60900; -.
DR jPOST; P60900; -.
DR MassIVE; P60900; -.
DR MaxQB; P60900; -.
DR PaxDb; P60900; -.
DR PeptideAtlas; P60900; -.
DR PRIDE; P60900; -.
DR ProteomicsDB; 4898; -.
DR ProteomicsDB; 5443; -.
DR ProteomicsDB; 57236; -. [P60900-1]
DR TopDownProteomics; P60900-1; -. [P60900-1]
DR Antibodypedia; 155; 503 antibodies from 34 providers.
DR DNASU; 5687; -.
DR Ensembl; ENST00000261479.9; ENSP00000261479.4; ENSG00000100902.11. [P60900-1]
DR Ensembl; ENST00000540871.5; ENSP00000444844.1; ENSG00000100902.11. [P60900-2]
DR Ensembl; ENST00000555764.5; ENSP00000452566.1; ENSG00000100902.11. [P60900-3]
DR Ensembl; ENST00000622405.4; ENSP00000479620.1; ENSG00000100902.11. [P60900-3]
DR GeneID; 5687; -.
DR KEGG; hsa:5687; -.
DR MANE-Select; ENST00000261479.9; ENSP00000261479.4; NM_002791.3; NP_002782.1.
DR UCSC; uc001wtd.5; human. [P60900-1]
DR CTD; 5687; -.
DR DisGeNET; 5687; -.
DR GeneCards; PSMA6; -.
DR HGNC; HGNC:9535; PSMA6.
DR HPA; ENSG00000100902; Low tissue specificity.
DR MalaCards; PSMA6; -.
DR MIM; 602855; gene.
DR neXtProt; NX_P60900; -.
DR OpenTargets; ENSG00000100902; -.
DR PharmGKB; PA33880; -.
DR VEuPathDB; HostDB:ENSG00000100902; -.
DR eggNOG; KOG0182; Eukaryota.
DR GeneTree; ENSGT00550000074807; -.
DR HOGENOM; CLU_035750_6_0_1; -.
DR InParanoid; P60900; -.
DR PhylomeDB; P60900; -.
DR TreeFam; TF106210; -.
DR PathwayCommons; P60900; -.
DR Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
DR Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
DR Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-HSA-202424; Downstream TCR signaling.
DR Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-HSA-4641257; Degradation of AXIN.
DR Reactome; R-HSA-4641258; Degradation of DVL.
DR Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD.
DR Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
DR Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
DR Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex.
DR Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-HSA-69481; G2/M Checkpoints.
DR Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-HSA-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-HSA-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; P60900; -.
DR SIGNOR; P60900; -.
DR BioGRID-ORCS; 5687; 793 hits in 1055 CRISPR screens.
DR ChiTaRS; PSMA6; human.
DR GeneWiki; PSMA6; -.
DR GenomeRNAi; 5687; -.
DR Pharos; P60900; Tbio.
DR PRO; PR:P60900; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P60900; protein.
DR Bgee; ENSG00000100902; Expressed in left testis and 101 other tissues.
DR ExpressionAtlas; P60900; baseline and differential.
DR Genevisible; P60900; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0030016; C:myofibril; ISS:BHF-UCL.
DR GO; GO:0016363; C:nuclear matrix; ISS:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000932; C:P-body; ISS:UniProtKB.
DR GO; GO:0005844; C:polysome; IDA:BHF-UCL.
DR GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
DR GO; GO:0005839; C:proteasome core complex; IDA:UniProtKB.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IDA:UniProtKB.
DR GO; GO:0030017; C:sarcomere; ISS:BHF-UCL.
DR GO; GO:0004175; F:endopeptidase activity; NAS:UniProtKB.
DR GO; GO:0051059; F:NF-kappaB binding; IPI:BHF-UCL.
DR GO; GO:0035639; F:purine ribonucleoside triphosphate binding; NAS:BHF-UCL.
DR GO; GO:0003723; F:RNA binding; IDA:BHF-UCL.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:BHF-UCL.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IC:ComplexPortal.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IMP:BHF-UCL.
DR GO; GO:0050727; P:regulation of inflammatory response; IC:BHF-UCL.
DR CDD; cd03754; proteasome_alpha_type_6; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR023332; Proteasome_alpha-type.
DR InterPro; IPR000426; Proteasome_asu_N.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR034642; Proteasome_subunit_alpha6.
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; Nucleus; Phosphoprotein;
KW Proteasome; Reference proteome.
FT CHAIN 1..246
FT /note="Proteasome subunit alpha type-6"
FT /id="PRO_0000124130"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 102
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 104
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 159
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9QUM9"
FT CARBOHYD 5
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..79
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054586"
FT VAR_SEQ 1..25
FT /note="MSRGSSAGFDRHITIFSPEGRLYQV -> MAGLRR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054587"
FT CONFLICT 59
FT /note="K -> C (in Ref. 8; CAA43964)"
FT /evidence="ECO:0000305"
FT TURN 8..12
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:7AWE"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:5VFO"
FT HELIX 23..34
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:5LF0"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:5LE5"
FT HELIX 84..105
FT /evidence="ECO:0007829|PDB:5LE5"
FT HELIX 111..125
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:4R3O"
FT STRAND 135..144
FT /evidence="ECO:0007829|PDB:5LE5"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:4R3O"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:5A0Q"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:5LE5"
FT HELIX 172..185
FT /evidence="ECO:0007829|PDB:5LE5"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:5LE5"
FT HELIX 194..206
FT /evidence="ECO:0007829|PDB:5LE5"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:6E5B"
FT HELIX 232..243
FT /evidence="ECO:0007829|PDB:5LE5"
SQ SEQUENCE 246 AA; 27399 MW; 94D1FD3C0A7CC72A CRC64;
MSRGSSAGFD RHITIFSPEG RLYQVEYAFK AINQGGLTSV AVRGKDCAVI VTQKKVPDKL
LDSSTVTHLF KITENIGCVM TGMTADSRSQ VQRARYEAAN WKYKYGYEIP VDMLCKRIAD
ISQVYTQNAE MRPLGCCMIL IGIDEEQGPQ VYKCDPAGYY CGFKATAAGV KQTESTSFLE
KKVKKKFDWT FEQTVETAIT CLSTVLSIDF KPSEIEVGVV TVENPKFRIL TEAEIDAHLV
ALAERD
