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Proteasome subunit beta type-1 (EC 3.4.25.1) (Macropain subunit C5) (Multicatalytic endopeptidase complex subunit C5) (Proteasome component C5) (Proteasome gamma chain)

 PSB1_MOUSE              Reviewed;         240 AA.
O09061; Q62038; Q62039;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
20-JUN-2018, entry version 161.
RecName: Full=Proteasome subunit beta type-1;
EC=3.4.25.1 {ECO:0000250|UniProtKB:P20618};
AltName: Full=Macropain subunit C5;
AltName: Full=Multicatalytic endopeptidase complex subunit C5;
AltName: Full=Proteasome component C5;
AltName: Full=Proteasome gamma chain;
Flags: Precursor;
Name=Psmb1;
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=C57BL/10J; TISSUE=Brain, and Testis;
PubMed=7579585; DOI=10.3109/10425179509030985;
Savioz A., Houghton I., Davies R.W.;
"Cloning and sequencing of a murine cDNA encoding the proteasome
component C5.";
DNA Seq. 5:307-309(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary gland;
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).
[4]
PROTEIN SEQUENCE OF 77-93; 109-126; 146-159; 164-197 AND 204-212, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[5]
INTERACTION WITH RFPL4A.
PubMed=12525704; DOI=10.1073/pnas.0234474100;
Suzumori N., Burns K.H., Yan W., Matzuk M.M.;
"RFPL4 interacts with oocyte proteins of the ubiquitin-proteasome
degradation pathway.";
Proc. Natl. Acad. Sci. U.S.A. 100:550-555(2003).
[6]
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).
[7]
FUNCTION.
PubMed=16581775; DOI=10.1128/MCB.26.8.2999-3007.2006;
Khor B., Bredemeyer A.L., Huang C.-Y., Turnbull I.R., Evans R.,
Maggi L.B. Jr., White J.M., Walker L.M., Carnes K., Hess R.A.,
Sleckman B.P.;
"Proteasome activator PA200 is required for normal spermatogenesis.";
Mol. Cell. Biol. 26:2999-3007(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-149, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
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).
[10]
GLYCOSYLATION AT SER-57 AND SER-208.
TISSUE=Brain, and Spleen;
PubMed=22556278; DOI=10.1074/mcp.M111.015966;
Overath T., Kuckelkorn U., Henklein P., Strehl B., Bonar D., Kloss A.,
Siele D., Kloetzel P.M., Janek K.;
"Mapping of O-GlcNAc sites of 20 S proteasome subunits and Hsp90 by a
novel biotin-cystamine tag.";
Mol. Cell. Proteomics 11:467-477(2012).
[11]
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).
-!- 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:16581775,
ECO:0000269|PubMed:22341445}.
-!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
specificity. {ECO:0000250|UniProtKB:P20618}.
-!- 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 (PubMed:16857966,
PubMed:22341445). Interacts with SERPINB2 (By similarity).
Interacts with RFPL4A (PubMed:12525704).
{ECO:0000250|UniProtKB:P20618, ECO:0000269|PubMed:12525704,
ECO:0000269|PubMed:16857966, ECO:0000269|PubMed:22341445}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P20618}.
Nucleus {ECO:0000250|UniProtKB:P20618}.
-!- TISSUE SPECIFICITY: Detected in liver (at protein level).
{ECO:0000269|PubMed:22341445}.
-!- SIMILARITY: Belongs to the peptidase T1B family.
{ECO:0000255|PROSITE-ProRule:PRU00809}.
-!- SEQUENCE CAUTION:
Sequence=CAA56702.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; U60824; AAB37251.1; -; mRNA.
EMBL; X80686; CAA56701.1; -; mRNA.
EMBL; X80686; CAA56702.1; ALT_INIT; mRNA.
EMBL; AK077520; BAC36841.1; -; mRNA.
EMBL; BC018351; AAH18351.1; -; mRNA.
CCDS; CCDS28411.1; -.
RefSeq; NP_035315.1; NM_011185.3.
UniGene; Mm.32912; -.
PDB; 3UNB; X-ray; 2.90 A; 2/L/Z/n=28-240.
PDB; 3UNE; X-ray; 3.20 A; 2/L/Z/n=28-240.
PDB; 3UNF; X-ray; 2.90 A; L/Z=28-240.
PDB; 3UNH; X-ray; 3.20 A; L/Z=28-240.
PDB; 5L65; X-ray; 2.90 A; L/Z=123-137, L/Z=144-159.
PDB; 5L66; X-ray; 2.80 A; L/Z=123-137, L/Z=144-159.
PDB; 5L67; X-ray; 2.60 A; L/Z=123-137, L/Z=144-159.
PDB; 5L68; X-ray; 2.80 A; L/Z=123-137, L/Z=144-159.
PDB; 5L69; X-ray; 2.70 A; L/Z=123-137, L/Z=144-159.
PDB; 5L6A; X-ray; 2.80 A; L/Z=123-137, L/Z=144-159.
PDB; 5L6B; X-ray; 2.60 A; L/Z=123-137, L/Z=144-159.
PDB; 5L6C; X-ray; 2.60 A; L/Z=123-137, L/Z=144-159.
PDBsum; 3UNB; -.
PDBsum; 3UNE; -.
PDBsum; 3UNF; -.
PDBsum; 3UNH; -.
PDBsum; 5L65; -.
PDBsum; 5L66; -.
PDBsum; 5L67; -.
PDBsum; 5L68; -.
PDBsum; 5L69; -.
PDBsum; 5L6A; -.
PDBsum; 5L6B; -.
PDBsum; 5L6C; -.
ProteinModelPortal; O09061; -.
SMR; O09061; -.
BioGrid; 202418; 4.
CORUM; O09061; -.
IntAct; O09061; 6.
MINT; O09061; -.
STRING; 10090.ENSMUSP00000014913; -.
iPTMnet; O09061; -.
PhosphoSitePlus; O09061; -.
SwissPalm; O09061; -.
EPD; O09061; -.
PaxDb; O09061; -.
PeptideAtlas; O09061; -.
PRIDE; O09061; -.
Ensembl; ENSMUST00000014913; ENSMUSP00000014913; ENSMUSG00000014769.
GeneID; 19170; -.
KEGG; mmu:19170; -.
UCSC; uc008aol.1; mouse.
CTD; 5689; -.
MGI; MGI:104884; Psmb1.
eggNOG; KOG0179; Eukaryota.
eggNOG; COG0638; LUCA.
GeneTree; ENSGT00550000075035; -.
HOGENOM; HOG000091081; -.
HOVERGEN; HBG000961; -.
InParanoid; O09061; -.
KO; K02732; -.
OMA; EHRFNPY; -.
OrthoDB; EOG091G0FUK; -.
PhylomeDB; O09061; -.
TreeFam; TF106218; -.
Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
Reactome; R-MMU-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-MMU-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
Reactome; R-MMU-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
Reactome; R-MMU-174113; SCF-beta-TrCP mediated degradation of Emi1.
Reactome; R-MMU-174154; APC/C:Cdc20 mediated degradation of Securin.
Reactome; R-MMU-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-MMU-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-MMU-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-MMU-202424; Downstream TCR signaling.
Reactome; R-MMU-2467813; Separation of Sister Chromatids.
Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
Reactome; R-MMU-349425; Autodegradation of the E3 ubiquitin ligase COP1.
Reactome; R-MMU-350562; Regulation of ornithine decarboxylase (ODC).
Reactome; R-MMU-382556; ABC-family proteins mediated transport.
Reactome; R-MMU-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-MMU-4608870; Asymmetric localization of PCP proteins.
Reactome; R-MMU-4641257; Degradation of AXIN.
Reactome; R-MMU-4641258; Degradation of DVL.
Reactome; R-MMU-5358346; Hedgehog ligand biogenesis.
Reactome; R-MMU-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-MMU-5610780; Degradation of GLI1 by the proteasome.
Reactome; R-MMU-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-MMU-5632684; Hedgehog 'on' state.
Reactome; R-MMU-5658442; Regulation of RAS by GAPs.
Reactome; R-MMU-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-MMU-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
Reactome; R-MMU-5689603; UCH proteinases.
Reactome; R-MMU-5689880; Ub-specific processing proteases.
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-68827; CDT1 association with the CDC6:ORC:origin complex.
Reactome; R-MMU-68949; Orc1 removal from chromatin.
Reactome; R-MMU-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-MMU-69229; Ubiquitin-dependent degradation of Cyclin D1.
Reactome; R-MMU-69481; G2/M Checkpoints.
Reactome; R-MMU-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-MMU-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
Reactome; R-MMU-8939902; Regulation of RUNX2 expression and activity.
Reactome; R-MMU-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-MMU-8948751; Regulation of PTEN stability and activity.
Reactome; R-MMU-9020702; Interleukin-1 signaling.
Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
PRO; PR:O09061; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000014769; -.
ExpressionAtlas; O09061; baseline and differential.
Genevisible; O09061; MM.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0000502; C:proteasome complex; ISO:MGI.
GO; GO:0005839; C:proteasome core complex; IDA:UniProtKB.
GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IEA:InterPro.
Gene3D; 3.60.20.10; -; 1.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR035202; Proteasome_beta1.
InterPro; IPR016050; Proteasome_bsu_CS.
InterPro; IPR001353; Proteasome_sua/b.
InterPro; IPR023333; Proteasome_suB-type.
PANTHER; PTHR11599:SF59; PTHR11599:SF59; 1.
Pfam; PF00227; Proteasome; 1.
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;
Direct protein sequencing; Glycoprotein; Hydrolase; Nucleus;
Phosphoprotein; Protease; Proteasome; Reference proteome;
Threonine protease.
PROPEP 1 27 {ECO:0000250}.
/FTId=PRO_0000259624.
CHAIN 28 240 Proteasome subunit beta type-1.
/FTId=PRO_0000148031.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P20618}.
MOD_RES 61 61 Phosphoserine.
{ECO:0000250|UniProtKB:P20618}.
MOD_RES 67 67 Phosphoserine.
{ECO:0000250|UniProtKB:P20618}.
MOD_RES 149 149 Phosphotyrosine.
{ECO:0000244|PubMed:18034455}.
MOD_RES 161 161 Phosphoserine.
{ECO:0000250|UniProtKB:P20618}.
MOD_RES 203 203 N6-acetyllysine.
{ECO:0000250|UniProtKB:P20618}.
CARBOHYD 57 57 O-linked (GlcNAc) serine.
{ECO:0000269|PubMed:22556278}.
CARBOHYD 208 208 O-linked (GlcNAc) serine.
{ECO:0000269|PubMed:22556278}.
STRAND 38 43 {ECO:0000244|PDB:3UNB}.
STRAND 48 53 {ECO:0000244|PDB:3UNB}.
STRAND 56 58 {ECO:0000244|PDB:3UNB}.
STRAND 61 65 {ECO:0000244|PDB:3UNB}.
STRAND 70 72 {ECO:0000244|PDB:3UNB}.
STRAND 74 83 {ECO:0000244|PDB:3UNB}.
HELIX 85 106 {ECO:0000244|PDB:3UNB}.
HELIX 112 124 {ECO:0000244|PDB:3UNB}.
TURN 125 128 {ECO:0000244|PDB:5L67}.
STRAND 133 137 {ECO:0000244|PDB:5L67}.
STRAND 142 144 {ECO:0000244|PDB:3UNE}.
STRAND 146 151 {ECO:0000244|PDB:3UNB}.
STRAND 157 166 {ECO:0000244|PDB:3UNB}.
HELIX 169 179 {ECO:0000244|PDB:3UNB}.
HELIX 195 212 {ECO:0000244|PDB:3UNB}.
STRAND 213 215 {ECO:0000244|PDB:3UNB}.
STRAND 218 226 {ECO:0000244|PDB:3UNB}.
STRAND 229 236 {ECO:0000244|PDB:3UNB}.
SEQUENCE 240 AA; 26372 MW; 22ADBC6ACB3A8D31 CRC64;
MLSTAAYRDV ERELGMGPHG SAGPVQLRFS PYAFNGGTVL AIAGEDFSIV ASDTRLSEGF
SIHTRDSPKC YKLTDKTVIG CSGFHGDCLT LTKIIEARLK MYKHSNNKAM TTGAIAAMLS
TILYSRRFFP YYVYNIIGGL DEEGKGAVYS FDPVGSYQRD SFKAGGSASA MLQPLLDNQV
GFKNMQNVEH VPLTLDRAMR LVKDVFISAA ERDVYTGDAL RICIVTKEGI REETVPLRKD


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EIAAB32777 Macropain subunit C13,Multicatalytic endopeptidase complex subunit C13,Proteasome component C13,Proteasome subunit beta type-8,Proteasome subunit beta-5i,Psmb8,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
EIAAB32773 Macropain subunit C13,Multicatalytic endopeptidase complex subunit C13,Pig,Proteasome component C13,Proteasome subunit beta type-8,Proteasome subunit beta-5i,PSMB8,Sus scrofa
EIAAB32718 HC9,Homo sapiens,Human,Macropain subunit C9,Multicatalytic endopeptidase complex subunit C9,Proteasome component C9,Proteasome subunit alpha type-4,Proteasome subunit L,PSC9,PSMA4
EIAAB32711 Macropain subunit C8,Multicatalytic endopeptidase complex subunit C8,Proteasome component C8,Proteasome subunit alpha type-3,Proteasome subunit K,Psma3,Rat,Rattus norvegicus
EIAAB32716 Macropain subunit C9,Multicatalytic endopeptidase complex subunit C9,Proteasome component C9,Proteasome subunit alpha type-4,Proteasome subunit L,Psma4,Rat,Rattus norvegicus
EIAAB32715 Macropain subunit C9,Mouse,Multicatalytic endopeptidase complex subunit C9,Mus musculus,Proteasome component C9,Proteasome subunit alpha type-4,Proteasome subunit L,Psma4
EIAAB32714 Macropain subunit C8,Mouse,Multicatalytic endopeptidase complex subunit C8,Mus musculus,Proteasome component C8,Proteasome subunit alpha type-3,Proteasome subunit K,Psma3
EIAAB32703 30 kDa prosomal protein,HC2,Homo sapiens,Human,Macropain subunit C2,Multicatalytic endopeptidase complex subunit C2,NU,PROS30,PROS-30,Proteasome component C2,Proteasome nu chain,Proteasome subunit alp
EIAAB32748 Macropain subunit C7-I,Multicatalytic endopeptidase complex subunit C7-I,Proteasome component C7-I,Proteasome subunit beta type-2,Psmb2,Rat,Rattus norvegicus
EIAAB32745 Macropain subunit C7-I,Mouse,Multicatalytic endopeptidase complex subunit C7-I,Mus musculus,Proteasome component C7-I,Proteasome subunit beta type-2,Psmb2
EIAAB32746 Homo sapiens,Human,Macropain subunit C7-I,Multicatalytic endopeptidase complex subunit C7-I,Proteasome component C7-I,Proteasome subunit beta type-2,PSMB2
E1177m ELISA Lmp2,LMP-2d,Low molecular mass protein 2,Macropain chain 7,Mouse,Multicatalytic endopeptidase complex chain 7,Mus musculus,Proteasome chain 7,Proteasome subunit beta type-9,Proteasome subunit be 96T


 

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