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Proteasome subunit beta type-9 (EC 3.4.25.1) (LMP-2d) (Low molecular mass protein 2) (Macropain chain 7) (Multicatalytic endopeptidase complex chain 7) (Proteasome chain 7) (Proteasome subunit beta-1i) (Really interesting new gene 12 protein)

 PSB9_MOUSE              Reviewed;         219 AA.
P28076; O09085; O09151; Q07704; Q60827; Q64278;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 1.
22-NOV-2017, entry version 165.
RecName: Full=Proteasome subunit beta type-9;
EC=3.4.25.1;
AltName: Full=LMP-2d;
AltName: Full=Low molecular mass protein 2;
AltName: Full=Macropain chain 7;
AltName: Full=Multicatalytic endopeptidase complex chain 7;
AltName: Full=Proteasome chain 7;
AltName: Full=Proteasome subunit beta-1i;
AltName: Full=Really interesting new gene 12 protein;
Flags: Precursor;
Name=Psmb9; Synonyms=Lmp2, Ring12;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Various strains;
PubMed=1681432; DOI=10.1038/353664a0;
Martinez C.K., Monaco J.J.;
"Homology of proteasome subunits to a major histocompatibility
complex-linked LMP gene.";
Nature 353:664-667(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=NOD;
PubMed=7901128; DOI=10.1016/0378-1119(93)90646-K;
Kishi F., Suminami Y., Monaco J.J.;
"Genomic organization of the mouse Lmp-2 gene and characteristic
structure of its promoter.";
Gene 133:243-248(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS LMP-2B AND LMP-2Q.
PubMed=7681985; DOI=10.1073/pnas.90.7.2681;
Zhou P., Cao H., Smart M., David C.;
"Molecular basis of genetic polymorphism in major histocompatibility
complex-linked proteasome gene (Lmp-2).";
Proc. Natl. Acad. Sci. U.S.A. 90:2681-2684(1993).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
STRAIN=BALB/cJ;
PubMed=8325639; DOI=10.1006/geno.1993.1245;
Zhou P., Zanelli E., Smart M., David C.;
"Genomic organization and tissue expression of mouse proteasome gene
Lmp-2.";
Genomics 16:664-668(1993).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=B10.RIII, C57BL/6J, and R37;
PubMed=8854085;
Nandi D., Iyer M.N., Monaco J.J.;
"Molecular and serological analysis of polymorphisms in the murine
major histocompatibility complex-encoded proteasome subunits, LMP-2
and LMP-7.";
Exp. Clin. Immunogenet. 13:20-29(1996).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=BALB/cJ;
PubMed=8575819; DOI=10.1007/BF00587301;
Peleraux A., Karlsson L., Chambers J., Peterson P.A.;
"Genomic organization of a mouse MHC class II region including the H2-
M and Lmp2 loci.";
Immunogenetics 43:204-214(1996).
[7]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Various strains; TISSUE=Spleen;
Mizuno K., Saitou N., Tsutiya K., Sagai T., Moriwaki K., Shiroishi T.;
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=B10.MOL-SGR;
PubMed=8672125; DOI=10.1007/s003359900149;
Mizuno K., Koide T., Sagai T., Moriwaki K., Shiroishi T.;
"Molecular analysis of a recombinational hotspot adjacent to Lmp2 gene
in the mouse MHC: fine location and chromatin structure.";
Mamm. Genome 7:490-496(1996).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=129/SvJ;
Rowen L., Qin S., Madan A., Loretz C., James R., Dors M., Mix L.,
Hall J., Lasky S., Hood L.;
"Sequence of the mouse major histocomaptibility locus class II
region.";
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Small intestine;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[11]
INDUCTION BY INTERFERON GAMMA AND IRF1.
PubMed=15907481; DOI=10.1016/j.febslet.2005.04.012;
Namiki S., Nakamura T., Oshima S., Yamazaki M., Sekine Y.,
Tsuchiya K., Okamoto R., Kanai T., Watanabe M.;
"IRF-1 mediates upregulation of LMP7 by IFN-gamma and concerted
expression of immunosubunits of the proteasome.";
FEBS Lett. 579:2781-2787(2005).
[12]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16222703; DOI=10.1002/jcp.20508;
Wang H.X., Wang H.M., Lin H.Y., Yang Q., Zhang H., Tsang B.K., Zhu C.;
"Proteasome subunit LMP2 is required for matrix metalloproteinase-2
and -9 expression and activities in human invasive extravillous
trophoblast cell line.";
J. Cell. Physiol. 206:616-623(2006).
[13]
INDUCTION BY HEAT SHOCK.
PubMed=17142736; DOI=10.4049/jimmunol.177.12.8393;
Callahan M.K., Wohlfert E.A., Menoret A., Srivastava P.K.;
"Heat shock up-regulates lmp2 and lmp7 and enhances presentation of
immunoproteasome-dependent epitopes.";
J. Immunol. 177:8393-8399(2006).
[14]
INDUCTION BY EGR1.
PubMed=16452686; DOI=10.1523/JNEUROSCI.4199-05.2006;
James A.B., Conway A.M., Morris B.J.;
"Regulation of the neuronal proteasome by Zif268 (Egr1).";
J. Neurosci. 26:1624-1634(2006).
[15]
IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.
PubMed=16857966; DOI=10.1161/01.RES.0000237386.98506.f7;
Gomes A.V., Zong C., Edmondson R.D., Li X., Stefani E., Zhang J.,
Jones R.C., Thyparambil S., Wang G.W., Qiao X., Bardag-Gorce F.,
Ping P.;
"Mapping the murine cardiac 26S proteasome complexes.";
Circ. Res. 99:362-371(2006).
[16]
IDENTIFICATION IN THE SPERMATOPROTEASOME.
PubMed=23706739; DOI=10.1016/j.cell.2013.04.032;
Qian M.X., Pang Y., Liu C.H., Haratake K., Du B.Y., Ji D.Y.,
Wang G.F., Zhu Q.Q., Song W., Yu Y., Zhang X.X., Huang H.T., Miao S.,
Chen L.B., Zhang Z.H., Liang Y.N., Liu S., Cha H., Yang D., Zhai Y.,
Komatsu T., Tsuruta F., Li H., Cao C., Li W., Li G.H., Cheng Y.,
Chiba T., Wang L., Goldberg A.L., Shen Y., Qiu X.B.;
"Acetylation-mediated proteasomal degradation of core histones during
DNA repair and spermatogenesis.";
Cell 153:1012-1024(2013).
[17]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 20S IMMUNOPROTEASOME,
SUBUNIT, FUNCTION, AND TISSUE SPECIFICITY.
PubMed=22341445; DOI=10.1016/j.cell.2011.12.030;
Huber E.M., Basler M., Schwab R., Heinemeyer W., Kirk C.J.,
Groettrup M., Groll M.;
"Immuno- and constitutive proteasome crystal structures reveal
differences in substrate and inhibitor specificity.";
Cell 148:727-738(2012).
[18]
VARIANT [LARGE SCALE ANALYSIS] ASP-177, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Kidney, Liver, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: The proteasome is a multicatalytic proteinase complex
which is characterized by its ability to cleave peptides with Arg,
Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or
slightly basic pH. The proteasome has an ATP-dependent proteolytic
activity. This subunit is involved in antigen processing to
generate class I binding peptides. Contributes to NFKBIA
degradation and subsequently NFKB1 generation.
{ECO:0000269|PubMed:16222703, ECO:0000269|PubMed:22341445}.
-!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
specificity.
-!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and
two 19S regulatory subunits. The 20S proteasome core is composed
of 28 subunits that are arranged in four stacked rings, resulting
in a barrel-shaped structure. The two end rings are each formed by
seven alpha subunits, and the two central rings are each formed by
seven beta subunits. The catalytic chamber with the active sites
is on the inside of the barrel. Component of the immunoproteasome,
where it displaces the equivalent houskeeping subunit PSMB6.
Component of the spermatoproteasome, a form of the proteasome
specifically found in testis. Interacts with NCOA1, NCOA2 and
NCOA3. {ECO:0000269|PubMed:16857966, ECO:0000269|PubMed:22341445,
ECO:0000269|PubMed:23706739}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-
ProRule:PRU00809}. Nucleus {ECO:0000250}.
-!- TISSUE SPECIFICITY: Detected in liver (at protein level).
Expressed at high levels in the thymus, spleen, lung, heart and
liver. Expressed at moderate levels in the kidney.
{ECO:0000269|PubMed:22341445, ECO:0000269|PubMed:8325639}.
-!- INDUCTION: Up-regulated by interferon gamma (at protein level).
Up-regulated by IRF1. Up-regulated by heat shock treatment. Down-
regulated by EGR1 in neuronal cells. {ECO:0000269|PubMed:15907481,
ECO:0000269|PubMed:16452686, ECO:0000269|PubMed:17142736}.
-!- PTM: Autocleaved. The resulting N-terminal Thr residue of the
mature subunit is responsible for the nucleophile proteolytic
activity. {ECO:0000250|UniProtKB:O35955}.
-!- DISRUPTION PHENOTYPE: Depletion of LMP2 by RNAi suppresses
expression and activities of the matrix metalloproteinase MMP2 and
MMP9 by blocking the transfer of active NF-kappa-B heterodimers
into the nucleus. {ECO:0000269|PubMed:16222703}.
-!- SIMILARITY: Belongs to the peptidase T1B family.
{ECO:0000255|PROSITE-ProRule:PRU00809}.
-!- SEQUENCE CAUTION:
Sequence=AAA39439.1; Type=Frameshift; Positions=10, 130; Evidence={ECO:0000305};
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EMBL; S59862; AAB20105.1; -; mRNA.
EMBL; U22448; AAA75305.1; -; mRNA.
EMBL; U22447; AAA75304.1; -; mRNA.
EMBL; S58203; AAP13903.1; -; mRNA.
EMBL; L11613; AAA39439.1; ALT_FRAME; Genomic_DNA.
EMBL; U22919; AAA75306.1; -; mRNA.
EMBL; U22920; AAA75307.1; -; mRNA.
EMBL; U35323; AAA98932.1; -; Genomic_DNA.
EMBL; D14566; BAA40680.1; -; Genomic_DNA.
EMBL; D44454; BAA22575.1; -; mRNA.
EMBL; D44457; BAA22578.1; -; mRNA.
EMBL; D44458; BAA22579.1; -; mRNA.
EMBL; D44460; BAA22581.1; -; mRNA.
EMBL; D44461; BAA22582.1; -; mRNA.
EMBL; D44462; BAA22583.1; -; mRNA.
EMBL; D43620; BAA19855.1; -; Genomic_DNA.
EMBL; AF027865; AAB81528.1; -; Genomic_DNA.
EMBL; AF100956; AAC69911.1; -; Genomic_DNA.
EMBL; AK008429; BAB25664.1; -; mRNA.
CCDS; CCDS28642.1; -.
PIR; JC2019; JC2019.
RefSeq; NP_038613.1; NM_013585.2.
UniGene; Mm.390983; -.
PDB; 3UNF; X-ray; 2.90 A; N/b=21-219.
PDB; 3UNH; X-ray; 3.20 A; N/b=21-219.
PDBsum; 3UNF; -.
PDBsum; 3UNH; -.
ProteinModelPortal; P28076; -.
SMR; P28076; -.
CORUM; P28076; -.
IntAct; P28076; 7.
MINT; MINT-4108888; -.
STRING; 10090.ENSMUSP00000133499; -.
ChEMBL; CHEMBL1944491; -.
MEROPS; T01.013; -.
iPTMnet; P28076; -.
PhosphoSitePlus; P28076; -.
EPD; P28076; -.
MaxQB; P28076; -.
PaxDb; P28076; -.
PeptideAtlas; P28076; -.
PRIDE; P28076; -.
GeneID; 16912; -.
KEGG; mmu:16912; -.
CTD; 5698; -.
MGI; MGI:1346526; Psmb9.
eggNOG; KOG0174; Eukaryota.
eggNOG; ENOG410XS23; LUCA.
HOGENOM; HOG000091079; -.
HOVERGEN; HBG000123; -.
InParanoid; P28076; -.
KO; K02741; -.
PhylomeDB; P28076; -.
TreeFam; TF106221; -.
PRO; PR:P28076; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005839; C:proteasome core complex; IDA:UniProtKB.
GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
GO; GO:1990111; C:spermatoproteasome complex; IDA:UniProtKB.
GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0019882; P:antigen processing and presentation; IDA:MGI.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IEA:InterPro.
GO; GO:2000116; P:regulation of cysteine-type endopeptidase activity; ISO:MGI.
Gene3D; 3.60.20.10; -; 1.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR000243; Pept_T1A_subB.
InterPro; IPR034383; Proteasome_beta9.
InterPro; IPR016050; Proteasome_bsu_CS.
InterPro; IPR001353; Proteasome_sua/b.
InterPro; IPR023333; Proteasome_suB-type.
PANTHER; PTHR11599:SF50; PTHR11599:SF50; 1.
Pfam; PF00227; Proteasome; 1.
PRINTS; PR00141; PROTEASOME.
SUPFAM; SSF56235; SSF56235; 1.
PROSITE; PS00854; PROTEASOME_BETA_1; 1.
PROSITE; PS51476; PROTEASOME_BETA_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm; Hydrolase;
Immunity; Nucleus; Polymorphism; Protease; Proteasome;
Reference proteome; Threonine protease; Zymogen.
PROPEP 1 20 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000026621.
CHAIN 21 219 Proteasome subunit beta type-9.
/FTId=PRO_0000026622.
ACT_SITE 21 21 Nucleophile. {ECO:0000250}.
SITE 20 21 Cleavage; by autolysis.
{ECO:0000250|UniProtKB:O35955}.
MOD_RES 53 53 N6-acetyllysine.
{ECO:0000250|UniProtKB:P28065}.
MOD_RES 109 109 N6-acetyllysine.
{ECO:0000250|UniProtKB:P28065}.
VARIANT 60 60 R -> H (in LMP-2b).
VARIANT 126 126 R -> C (in LMP-2b).
VARIANT 177 177 N -> D (in LMP-2b and LMP-2q).
{ECO:0000244|PubMed:21183079}.
STRAND 22 27 {ECO:0000244|PDB:3UNF}.
STRAND 32 36 {ECO:0000244|PDB:3UNF}.
STRAND 40 42 {ECO:0000244|PDB:3UNF}.
STRAND 45 50 {ECO:0000244|PDB:3UNF}.
STRAND 54 58 {ECO:0000244|PDB:3UNF}.
STRAND 61 65 {ECO:0000244|PDB:3UNF}.
HELIX 69 89 {ECO:0000244|PDB:3UNF}.
HELIX 96 109 {ECO:0000244|PDB:3UNF}.
TURN 110 113 {ECO:0000244|PDB:3UNF}.
STRAND 118 124 {ECO:0000244|PDB:3UNF}.
TURN 125 127 {ECO:0000244|PDB:3UNF}.
STRAND 128 133 {ECO:0000244|PDB:3UNF}.
HELIX 135 137 {ECO:0000244|PDB:3UNF}.
STRAND 143 148 {ECO:0000244|PDB:3UNF}.
HELIX 149 154 {ECO:0000244|PDB:3UNF}.
HELIX 155 161 {ECO:0000244|PDB:3UNF}.
HELIX 168 185 {ECO:0000244|PDB:3UNF}.
STRAND 193 198 {ECO:0000244|PDB:3UNF}.
STRAND 203 208 {ECO:0000244|PDB:3UNF}.
HELIX 210 212 {ECO:0000244|PDB:3UNF}.
SEQUENCE 219 AA; 23397 MW; 036BC558E770BD3E CRC64;
MLRAGAPTAG SFRTEEVHTG TTIMAVEFDG GVVVGSDSRV SAGTAVVNRV FDKLSPLHQR
IFCALSGSAA DAQAIADMAA YQLELHGLEL EEPPLVLAAA NVVKNISYKY REDLLAHLIV
AGWDQREGGQ VYGTMGGMLI RQPFTIGGSG SSYIYGYVDA AYKPGMTPEE CRRFTTNAIT
LAMNRDGSSG GVIYLVTITA AGVDHRVILG DELPKFYDE


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EIAAB32755 Macropain beta chain,Multicatalytic endopeptidase complex beta chain,Pig,Proteasome beta chain,Proteasome chain 3,Proteasome subunit beta type-4,PSMB4,Sus scrofa
EIAAB32761 Homo sapiens,Human,LMPX,Macropain epsilon chain,MB1,Multicatalytic endopeptidase complex epsilon chain,Proteasome chain 6,Proteasome epsilon chain,Proteasome subunit beta type-5,Proteasome subunit MB1
EIAAB32766 Macropain delta chain,Multicatalytic endopeptidase complex delta chain,Proteasome chain 5,Proteasome delta chain,Proteasome subunit beta type-6,Proteasome subunit Y,Psmb6,Psmb6l,Rat,Rattus norvegicus
EIAAB32772 Lmp7,Low molecular mass protein 7,Macropain subunit C13,Mc13,Mouse,Multicatalytic endopeptidase complex subunit C13,Mus musculus,Proteasome component C13,Proteasome subunit beta type-8,Proteasome subu
EIAAB32758 Macropain epsilon chain,Mouse,Multicatalytic endopeptidase complex epsilon chain,Mus musculus,Proteasome chain 6,Proteasome epsilon chain,Proteasome subunit beta type-5,Proteasome subunit X,Psmb5
EIAAB32762 Macropain epsilon chain,Multicatalytic endopeptidase complex epsilon chain,Proteasome chain 6,Proteasome epsilon chain,Proteasome subunit beta type-5,Proteasome subunit X,Psmb5,Rat,Rattus norvegicus
EIAAB32754 26 kDa prosomal protein,Homo sapiens,HsBPROS26,HsN3,Human,Macropain beta chain,Multicatalytic endopeptidase complex beta chain,PROS26,PROS-26,Proteasome beta chain,Proteasome chain 3,Proteasome subuni
EIAAB32760 Chicken,Gallus gallus,Macropain chain 1,Multicatalytic endopeptidase complex chain 1,Proteasome chain 1,Proteasome subunit beta type-5,Proteasome subunit C1,PSMB5


 

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