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Proteasome subunit alpha type-6 (EC 3.4.25.1) (27 kDa prosomal protein) (PROS-27) (p27K) (Macropain iota chain) (Multicatalytic endopeptidase complex iota chain) (Proteasome iota chain)

 PSA6_HUMAN              Reviewed;         246 AA.
P60900; B2R7J9; B4DQR4; B4DXJ9; P34062; Q6IB60;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
13-APR-2004, sequence version 1.
18-JUL-2018, entry version 168.
RecName: Full=Proteasome subunit alpha type-6;
EC=3.4.25.1 {ECO:0000269|PubMed:27176742};
AltName: Full=27 kDa prosomal protein;
Short=PROS-27;
Short=p27K;
AltName: Full=Macropain iota chain;
AltName: Full=Multicatalytic endopeptidase complex iota chain;
AltName: Full=Proteasome iota chain;
Name=PSMA6; Synonyms=PROS27;
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=7681138; DOI=10.1007/BF00282801;
Bey F., Pereira I.S., Coux O., Viegas-Pequignot E., Targa F.R.,
Nothwang H.G., Dutrillaux B., Scherrer K.;
"The prosomal RNA-binding protein p27K is a member of the alpha-type
human prosomal gene family.";
Mol. Gen. Genet. 237:193-205(1993).
[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; 2 AND 3).
TISSUE=Cerebellum, and Testis;
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=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, Lymph, Skeletal muscle, and Skin;
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 12-43; 60-88; 105-116; 154-164; 172-181 AND
229-246, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 26-246 (ISOFORM 1), AND PARTIAL PROTEIN
SEQUENCE.
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).
[9]
PARTIAL PROTEIN SEQUENCE.
PubMed=7811265; DOI=10.1006/bbrc.1994.2876;
Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B.;
"Human proteasome subunits from 2-dimensional gels identified by
partial sequencing.";
Biochem. Biophys. Res. Commun. 205:1785-1789(1994).
[10]
FUNCTION IN ANTIGEN PRESENTATION.
PubMed=8610016; DOI=10.1038/381166a0;
Groettrup M., Soza A., Eggers M., Kuehn L., Dick T.P., Schild H.,
Rammensee H.G., Koszinowski U.H., Kloetzel P.M.;
"A role for the proteasome regulator PA28alpha in antigen
presentation.";
Nature 381:166-168(1996).
[11]
SUBCELLULAR LOCATION.
PubMed=12181345; DOI=10.1091/mbc.E02-03-0122;
Lafarga M., Berciano M.T., Pena E., Mayo I., Castano J.G., Bohmann D.,
Rodrigues J.P., Tavanez J.P., Carmo-Fonseca M.;
"Clastosome: a subtype of nuclear body enriched in 19S and 20S
proteasomes, ubiquitin, and protein substrates of proteasome.";
Mol. Biol. Cell 13:2771-2782(2002).
[12]
FUNCTION.
PubMed=15244466; DOI=10.1021/bm049957a;
Yano M., Koumoto Y., Kanesaki Y., Wu X., Kido H.;
"20S proteasome prevents aggregation of heat-denatured proteins
without PA700 regulatory subcomplex like a molecular chaperone.";
Biomacromolecules 5:1465-1469(2004).
[13]
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).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-102 AND LYS-104, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[15]
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).
[16]
INTERACTION WITH ALKBH4.
PubMed=23145062; DOI=10.1371/journal.pone.0049045;
Bjornstad L.G., Meza T.J., Otterlei M., Olafsrud S.M.,
Meza-Zepeda L.A., Falnes P.O.;
"Human ALKBH4 interacts with proteins associated with transcription.";
PLoS ONE 7:E49045-E49045(2012).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-63 AND SER-64,
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).
[18]
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).
[19]
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).
[20]
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).
[21]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2-245, 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).
[22]
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).
[23]
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).
[24]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), AND SUBUNIT.
PubMed=27493187; DOI=10.1126/science.aaf8993;
Schrader J., Henneberg F., Mata R.A., Tittmann K., Schneider T.R.,
Stark H., Bourenkov G., Chari A.;
"The inhibition mechanism of human 20S proteasomes enables next-
generation inhibitor design.";
Science 353:594-598(2016).
-!- FUNCTION: Component of the 20S core proteasome complex involved in
the proteolytic degradation of most intracellular proteins. This
complex plays numerous essential roles within the cell by
associating with different regulatory particles. Associated with
two 19S regulatory particles, forms the 26S proteasome and thus
participates in the ATP-dependent degradation of ubiquitinated
proteins. The 26S proteasome plays a key role in the maintenance
of protein homeostasis by removing misfolded or damaged proteins
that could impair cellular functions, and by removing proteins
whose functions are no longer required. Associated with the PA200
or PA28, the 20S proteasome mediates ubiquitin-independent protein
degradation. This type of proteolysis is required in several
pathways including spermatogenesis (20S-PA200 complex) or
generation of a subset of MHC class I-presented antigenic peptides
(20S-PA28 complex). {ECO:0000269|PubMed:15244466,
ECO:0000269|PubMed:27176742, ECO:0000269|PubMed:8610016}.
-!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
specificity. {ECO:0000255|PROSITE-ProRule:PRU00808,
ECO:0000269|PubMed:27176742}.
-!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and
two 19S regulatory subunits. The 20S proteasome core is a barrel-
shaped complex made of 28 subunits that are arranged in four
stacked rings. The two outer rings are each formed by seven alpha
subunits, and the two inner rings are formed by seven beta
subunits. The proteolytic activity is exerted by three beta-
subunits PSMB5, PSMB6 and PSMB7. Interacts with ALKBH4
(PubMed:23145062). {ECO:0000269|PubMed:23145062,
ECO:0000269|PubMed:25599644, ECO:0000269|PubMed:26133119,
ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775,
ECO:0000269|PubMed:27493187}.
-!- INTERACTION:
Q0VDD7:C19orf57; NbExp=3; IntAct=EBI-357793, EBI-741210;
Q9BY67:CADM1; NbExp=3; IntAct=EBI-357793, EBI-5652260;
Q9BYR5:KRTAP4-2; NbExp=3; IntAct=EBI-357793, EBI-10172511;
Q9BT23:LIMD2; NbExp=3; IntAct=EBI-357793, EBI-2805292;
P25787:PSMA2; NbExp=5; IntAct=EBI-357793, EBI-603262;
P25788:PSMA3; NbExp=9; IntAct=EBI-357793, EBI-348380;
P25789:PSMA4; NbExp=5; IntAct=EBI-357793, EBI-359310;
O14818:PSMA7; NbExp=11; IntAct=EBI-357793, EBI-603272;
Q96K19:RNF170; NbExp=3; IntAct=EBI-357793, EBI-2130336;
Q14D33:RTP5; NbExp=3; IntAct=EBI-357793, EBI-10217913;
Q9HCM9:TRIM39; NbExp=3; IntAct=EBI-357793, EBI-739510;
Q9Y5K5:UCHL5; NbExp=4; IntAct=EBI-357793, EBI-1051183;
Q8NCP5:ZBTB44; NbExp=3; IntAct=EBI-357793, EBI-5658292;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12181345}.
Nucleus {ECO:0000269|PubMed:12181345}. Note=Colocalizes with TRIM5
in cytoplasmic bodies. {ECO:0000250|UniProtKB:P60900}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P60900-1; Sequence=Displayed;
Name=2;
IsoId=P60900-2; Sequence=VSP_054587;
Note=No experimental confirmation available.;
Name=3;
IsoId=P60900-3; Sequence=VSP_054586;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the peptidase T1A family.
{ECO:0000255|PROSITE-ProRule:PRU00808}.
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EMBL; X59417; CAA42052.1; -; mRNA.
EMBL; CR456944; CAG33225.1; -; mRNA.
EMBL; AK298920; BAG61026.1; -; mRNA.
EMBL; AK302008; BAG63411.1; -; mRNA.
EMBL; AK313011; BAG35846.1; -; mRNA.
EMBL; AK316223; BAH14594.1; -; mRNA.
EMBL; AL121594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL133163; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471078; EAW65876.1; -; Genomic_DNA.
EMBL; CH471078; EAW65877.1; -; Genomic_DNA.
EMBL; BC002979; AAH02979.1; -; mRNA.
EMBL; BC017882; AAH17882.1; -; mRNA.
EMBL; BC022354; AAH22354.1; -; mRNA.
EMBL; BC023659; AAH23659.1; -; mRNA.
EMBL; BC070137; AAH70137.1; -; mRNA.
EMBL; X61972; CAA43964.1; -; mRNA.
CCDS; CCDS61437.1; -. [P60900-2]
CCDS; CCDS61438.1; -. [P60900-3]
CCDS; CCDS9655.1; -. [P60900-1]
PIR; S30274; S30274.
RefSeq; NP_001269161.1; NM_001282232.1. [P60900-3]
RefSeq; NP_001269162.1; NM_001282233.1. [P60900-3]
RefSeq; NP_001269163.1; NM_001282234.1. [P60900-2]
RefSeq; NP_002782.1; NM_002791.2. [P60900-1]
RefSeq; XP_016876957.1; XM_017021468.1. [P60900-3]
UniGene; Hs.446260; -.
PDB; 4R3O; X-ray; 2.60 A; A/O=2-245.
PDB; 4R67; X-ray; 2.89 A; A/O/c/q=2-245.
PDB; 5A0Q; EM; 3.50 A; A/O=1-246.
PDB; 5GJQ; EM; 4.50 A; B/h=1-246.
PDB; 5GJR; EM; 3.50 A; B/h=1-246.
PDB; 5L4G; EM; 4.02 A; A/N=1-246.
PDB; 5LE5; X-ray; 1.80 A; G/U=1-246.
PDB; 5LEX; X-ray; 2.20 A; G/U=1-246.
PDB; 5LEY; X-ray; 1.90 A; G/U=1-246.
PDB; 5LEZ; X-ray; 2.19 A; G/U=1-246.
PDB; 5LF0; X-ray; 2.41 A; G/U=1-246.
PDB; 5LF1; X-ray; 2.00 A; G/U=1-246.
PDB; 5LF3; X-ray; 2.10 A; G/U=1-246.
PDB; 5LF4; X-ray; 1.99 A; G/U=1-246.
PDB; 5LF6; X-ray; 2.07 A; G/U=1-246.
PDB; 5LF7; X-ray; 2.00 A; G/U=1-246.
PDB; 5LN3; EM; 6.80 A; A=1-246.
PDB; 5M32; EM; 3.80 A; G/U=1-246.
PDB; 5T0C; EM; 3.80 A; AG/BG=2-246.
PDB; 5T0G; EM; 4.40 A; G=2-246.
PDB; 5T0H; EM; 6.80 A; G=2-246.
PDB; 5T0I; EM; 8.00 A; G=2-246.
PDB; 5T0J; EM; 8.00 A; G=2-246.
PDB; 6AVO; EM; 3.80 A; K/R=1-246.
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; 6AVO; -.
ProteinModelPortal; P60900; -.
SMR; P60900; -.
BioGrid; 111660; 148.
CORUM; P60900; -.
DIP; DIP-29367N; -.
IntAct; P60900; 82.
MINT; P60900; -.
STRING; 9606.ENSP00000261479; -.
BindingDB; P60900; -.
ChEMBL; CHEMBL3831201; -.
MEROPS; T01.971; -.
iPTMnet; P60900; -.
PhosphoSitePlus; P60900; -.
SwissPalm; P60900; -.
DMDM; 46397659; -.
REPRODUCTION-2DPAGE; IPI00029623; -.
SWISS-2DPAGE; P60900; -.
UCD-2DPAGE; P60900; -.
EPD; P60900; -.
MaxQB; P60900; -.
PaxDb; P60900; -.
PeptideAtlas; P60900; -.
PRIDE; P60900; -.
ProteomicsDB; 57236; -.
TopDownProteomics; P60900-1; -. [P60900-1]
DNASU; 5687; -.
Ensembl; ENST00000261479; ENSP00000261479; ENSG00000100902. [P60900-1]
Ensembl; ENST00000540871; ENSP00000444844; ENSG00000100902. [P60900-2]
Ensembl; ENST00000555764; ENSP00000452566; ENSG00000100902. [P60900-3]
Ensembl; ENST00000622405; ENSP00000479620; ENSG00000100902. [P60900-3]
GeneID; 5687; -.
KEGG; hsa:5687; -.
UCSC; uc001wtd.5; human. [P60900-1]
CTD; 5687; -.
DisGeNET; 5687; -.
EuPathDB; HostDB:ENSG00000100902.10; -.
GeneCards; PSMA6; -.
HGNC; HGNC:9535; PSMA6.
HPA; HPA003049; -.
MalaCards; PSMA6; -.
MIM; 602855; gene.
neXtProt; NX_P60900; -.
OpenTargets; ENSG00000100902; -.
PharmGKB; PA33880; -.
eggNOG; KOG0182; Eukaryota.
eggNOG; ENOG410XR7X; LUCA.
GeneTree; ENSGT00550000074807; -.
HOGENOM; HOG000091084; -.
HOVERGEN; HBG107363; -.
InParanoid; P60900; -.
KO; K02730; -.
PhylomeDB; P60900; -.
TreeFam; TF106210; -.
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-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-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SIGNOR; P60900; -.
GeneWiki; PSMA6; -.
GenomeRNAi; 5687; -.
PRO; PR:P60900; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000100902; -.
CleanEx; HS_PSMA6; -.
ExpressionAtlas; P60900; baseline and differential.
Genevisible; P60900; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0030016; C:myofibril; ISS:BHF-UCL.
GO; GO:0016363; C:nuclear matrix; ISS:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0000932; C:P-body; ISS:UniProtKB.
GO; GO:0005844; C:polysome; IDA:BHF-UCL.
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; IDA:BHF-UCL.
GO; GO:0030017; C:sarcomere; ISS:BHF-UCL.
GO; GO:0004175; F:endopeptidase activity; NAS:UniProtKB.
GO; GO:0051059; F:NF-kappaB binding; IPI:BHF-UCL.
GO; GO:0035639; F:purine ribonucleoside triphosphate binding; NAS:BHF-UCL.
GO; GO:0003723; F:RNA binding; IDA:BHF-UCL.
GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:BHF-UCL.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IMP:BHF-UCL.
GO; GO:0050727; P:regulation of inflammatory response; IC:BHF-UCL.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
CDD; cd03754; proteasome_alpha_type_6; 1.
Gene3D; 3.60.20.10; -; 1.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR023332; Proteasome_alpha-type.
InterPro; IPR000426; Proteasome_asu_N.
InterPro; IPR001353; Proteasome_sua/b.
InterPro; IPR034642; Proteasome_subunit_alpha6.
PANTHER; PTHR11599:SF11; PTHR11599:SF11; 1.
Pfam; PF00227; Proteasome; 1.
Pfam; PF10584; Proteasome_A_N; 1.
SMART; SM00948; Proteasome_A_N; 1.
SUPFAM; SSF56235; SSF56235; 1.
PROSITE; PS00388; PROTEASOME_ALPHA_1; 1.
PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Direct protein sequencing; Glycoprotein; Hydrolase;
Nucleus; Phosphoprotein; Protease; Proteasome; Reference proteome;
Threonine protease.
CHAIN 1 246 Proteasome subunit alpha type-6.
/FTId=PRO_0000124130.
MOD_RES 17 17 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 63 63 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 64 64 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 102 102 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 104 104 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 159 159 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9QUM9}.
CARBOHYD 5 5 O-linked (GlcNAc) serine. {ECO:0000250}.
VAR_SEQ 1 79 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054586.
VAR_SEQ 1 25 MSRGSSAGFDRHITIFSPEGRLYQV -> MAGLRR (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054587.
CONFLICT 59 59 K -> C (in Ref. 8; CAA43964).
{ECO:0000305}.
TURN 8 12 {ECO:0000244|PDB:5LE5}.
HELIX 23 34 {ECO:0000244|PDB:5LE5}.
STRAND 38 42 {ECO:0000244|PDB:5LE5}.
STRAND 49 53 {ECO:0000244|PDB:5LE5}.
STRAND 59 61 {ECO:0000244|PDB:5LF0}.
HELIX 63 65 {ECO:0000244|PDB:5LE5}.
STRAND 68 73 {ECO:0000244|PDB:5LE5}.
STRAND 76 82 {ECO:0000244|PDB:5LE5}.
HELIX 84 105 {ECO:0000244|PDB:5LE5}.
HELIX 111 125 {ECO:0000244|PDB:5LE5}.
STRAND 128 131 {ECO:0000244|PDB:4R3O}.
STRAND 135 144 {ECO:0000244|PDB:5LE5}.
TURN 145 147 {ECO:0000244|PDB:5LE5}.
STRAND 148 154 {ECO:0000244|PDB:5LE5}.
STRAND 156 158 {ECO:0000244|PDB:4R3O}.
STRAND 160 162 {ECO:0000244|PDB:5A0Q}.
STRAND 163 169 {ECO:0000244|PDB:5LE5}.
HELIX 172 185 {ECO:0000244|PDB:5LE5}.
HELIX 187 189 {ECO:0000244|PDB:5LE5}.
STRAND 191 193 {ECO:0000244|PDB:5LE5}.
HELIX 194 206 {ECO:0000244|PDB:5LE5}.
HELIX 212 214 {ECO:0000244|PDB:5LE5}.
STRAND 215 219 {ECO:0000244|PDB:5LE5}.
HELIX 232 243 {ECO:0000244|PDB:5LE5}.
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


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