PSA2_MOUSE
ID PSA2_MOUSE Reviewed; 234 AA.
AC P49722; E9Q3A4; Q6ZWV8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 3.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Proteasome subunit alpha type-2;
DE AltName: Full=Macropain subunit C3;
DE AltName: Full=Multicatalytic endopeptidase complex subunit C3;
DE AltName: Full=Proteasome component C3;
GN Name=Psma2; Synonyms=Lmpc3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7697131; DOI=10.1159/000468691;
RA Seelig A., Boes B., Kloetzel P.-M.;
RT "Characterization of mouse proteasome subunit MC3 and identification of
RT proteasome subtypes with different cleavage characteristics. Proteasome
RT subunits, proteasome subpopulations.";
RL Enzyme Protein 47:330-342(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10436176; DOI=10.1007/s002510050562;
RA Elenich L.A., Nandi D., Kent E.A., McCluskey T.S., Cruz M., Iyer M.N.,
RA Woodward E.C., Conn C.W., Ochoa A.L., Ginsburg D.B., Monaco J.J.;
RT "The complete primary structure of mouse 20S proteasomes.";
RL Immunogenetics 49:835-842(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, C57BL/6J, and NOD;
RC TISSUE=Bone marrow, Thymus, and Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 5-39; 71-84; 93-113 AND 178-196, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.;
RL Submitted (JUL-2007) to UniProtKB.
RN [8]
RP IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX, AND ACETYLATION AT
RP ALA-2.
RX PubMed=16857966; DOI=10.1161/01.res.0000237386.98506.f7;
RA Gomes A.V., Zong C., Edmondson R.D., Li X., Stefani E., Zhang J.,
RA Jones R.C., Thyparambil S., Wang G.W., Qiao X., Bardag-Gorce F., Ping P.;
RT "Mapping the murine cardiac 26S proteasome complexes.";
RL Circ. Res. 99:362-371(2006).
RN [9]
RP FUNCTION.
RX PubMed=16581775; DOI=10.1128/mcb.26.8.2999-3007.2006;
RA Khor B., Bredemeyer A.L., Huang C.-Y., Turnbull I.R., Evans R.,
RA Maggi L.B. Jr., White J.M., Walker L.M., Carnes K., Hess R.A.,
RA Sleckman B.P.;
RT "Proteasome activator PA200 is required for normal spermatogenesis.";
RL Mol. Cell. Biol. 26:2999-3007(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-76, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-6, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=22078707; DOI=10.1186/1742-4690-8-93;
RA Lukic Z., Hausmann S., Sebastian S., Rucci J., Sastri J., Robia S.L.,
RA Luban J., Campbell E.M.;
RT "TRIM5alpha associates with proteasomal subunits in cells while in complex
RT with HIV-1 virions.";
RL Retrovirology 8:93-93(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-171, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 20S IMMUNOPROTEASOME, SUBUNIT,
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22341445; DOI=10.1016/j.cell.2011.12.030;
RA Huber E.M., Basler M., Schwab R., Heinemeyer W., Kirk C.J., Groettrup M.,
RA Groll M.;
RT "Immuno- and constitutive proteasome crystal structures reveal differences
RT in substrate and inhibitor specificity.";
RL Cell 148:727-738(2012).
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:16581775,
CC ECO:0000269|PubMed:22341445}.
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC 19S regulatory subunits. The 20S proteasome core is a barrel-shaped
CC complex made of 28 subunits that are arranged in four stacked rings.
CC The two outer rings are each formed by seven alpha subunits, and the
CC two inner rings are formed by seven beta subunits. The proteolytic
CC activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7.
CC {ECO:0000269|PubMed:16857966, ECO:0000269|PubMed:22341445}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22078707}. Nucleus
CC {ECO:0000269|PubMed:22078707}. Note=Translocated from the cytoplasm
CC into the nucleus following interaction with AKIRIN2, which bridges the
CC proteasome with the nuclear import receptor IPO9 (By similarity).
CC Colocalizes with TRIM5 in cytoplasmic bodies (PubMed:22078707).
CC {ECO:0000250|UniProtKB:P25787, ECO:0000269|PubMed:22078707}.
CC -!- TISSUE SPECIFICITY: Detected in liver (at protein level).
CC {ECO:0000269|PubMed:22341445}.
CC -!- PTM: Phosphorylated on tyrosine residues; which may be important for
CC nuclear import. {ECO:0000250|UniProtKB:P17220}.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000255|PROSITE-
CC ProRule:PRU00808}.
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DR EMBL; X70303; CAA49782.1; -; mRNA.
DR EMBL; AF099733; AAD50623.1; -; mRNA.
DR EMBL; AK012119; BAB28045.1; -; mRNA.
DR EMBL; AK035578; BAC29110.1; -; mRNA.
DR EMBL; AK151883; BAE30769.1; -; mRNA.
DR EMBL; AK152862; BAE31553.1; -; mRNA.
DR EMBL; AK154011; BAE32314.1; -; mRNA.
DR EMBL; AK167752; BAE39787.1; -; mRNA.
DR EMBL; AC092710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466561; EDL32738.1; -; Genomic_DNA.
DR EMBL; BC026768; AAH26768.1; -; mRNA.
DR CCDS; CCDS36602.1; -.
DR RefSeq; NP_032970.2; NM_008944.2.
DR PDB; 3UNB; X-ray; 2.90 A; A/O/c/q=1-234.
DR PDB; 3UNE; X-ray; 3.20 A; A/O/c/q=1-234.
DR PDB; 3UNF; X-ray; 2.90 A; A/O=1-234.
DR PDB; 3UNH; X-ray; 3.20 A; A/O=1-234.
DR PDBsum; 3UNB; -.
DR PDBsum; 3UNE; -.
DR PDBsum; 3UNF; -.
DR PDBsum; 3UNH; -.
DR AlphaFoldDB; P49722; -.
DR SMR; P49722; -.
DR BioGRID; 202416; 62.
DR CORUM; P49722; -.
DR IntAct; P49722; 8.
DR STRING; 10090.ENSMUSP00000129767; -.
DR MEROPS; T01.972; -.
DR iPTMnet; P49722; -.
DR PhosphoSitePlus; P49722; -.
DR SwissPalm; P49722; -.
DR COMPLUYEAST-2DPAGE; P49722; -.
DR REPRODUCTION-2DPAGE; P49722; -.
DR SWISS-2DPAGE; P49722; -.
DR CPTAC; non-CPTAC-3940; -.
DR EPD; P49722; -.
DR jPOST; P49722; -.
DR PaxDb; P49722; -.
DR PeptideAtlas; P49722; -.
DR PRIDE; P49722; -.
DR ProteomicsDB; 291828; -.
DR TopDownProteomics; P49722; -.
DR Antibodypedia; 2176; 406 antibodies from 35 providers.
DR DNASU; 19166; -.
DR Ensembl; ENSMUST00000170836; ENSMUSP00000129767; ENSMUSG00000015671.
DR GeneID; 19166; -.
DR KEGG; mmu:19166; -.
DR UCSC; uc007pnl.1; mouse.
DR CTD; 5683; -.
DR MGI; MGI:104885; Psma2.
DR VEuPathDB; HostDB:ENSMUSG00000015671; -.
DR eggNOG; KOG0181; Eukaryota.
DR GeneTree; ENSGT00550000074870; -.
DR HOGENOM; CLU_035750_4_1_1; -.
DR InParanoid; P49722; -.
DR OMA; YQEQIPT; -.
DR OrthoDB; 1222564at2759; -.
DR PhylomeDB; P49722; -.
DR TreeFam; TF106207; -.
DR Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-MMU-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-MMU-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-MMU-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-MMU-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-MMU-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-MMU-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-MMU-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-MMU-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-MMU-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-MMU-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-MMU-382556; ABC-family proteins mediated transport.
DR Reactome; R-MMU-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-MMU-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-MMU-4641257; Degradation of AXIN.
DR Reactome; R-MMU-4641258; Degradation of DVL.
DR Reactome; R-MMU-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-MMU-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-MMU-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-MMU-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-MMU-5632684; Hedgehog 'on' state.
DR Reactome; R-MMU-5658442; Regulation of RAS by GAPs.
DR Reactome; R-MMU-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-MMU-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-68867; Assembly of the pre-replicative complex.
DR Reactome; R-MMU-68949; Orc1 removal from chromatin.
DR Reactome; R-MMU-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-MMU-69481; G2/M Checkpoints.
DR Reactome; R-MMU-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-MMU-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-MMU-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-MMU-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-MMU-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-MMU-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-9020702; Interleukin-1 signaling.
DR Reactome; R-MMU-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-MMU-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 19166; 30 hits in 70 CRISPR screens.
DR ChiTaRS; Psma2; mouse.
DR PRO; PR:P49722; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; P49722; protein.
DR Bgee; ENSMUSG00000015671; Expressed in somite and 255 other tissues.
DR ExpressionAtlas; P49722; baseline and differential.
DR Genevisible; P49722; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0000502; C:proteasome complex; ISO:MGI.
DR GO; GO:0005839; C:proteasome core complex; IDA:UniProtKB.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; ISS:UniProtKB.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0009615; P:response to virus; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
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; IPR034644; Proteasome_subunit_alpha2.
DR PANTHER; PTHR11599:SF16; PTHR11599:SF16; 1.
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; Cytoplasm; Direct protein sequencing; Nucleus;
KW Phosphoprotein; Proteasome; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:16857966"
FT CHAIN 2..234
FT /note="Proteasome subunit alpha type-2"
FT /id="PRO_0000124078"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:16857966"
FT MOD_RES 6
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25787"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25787"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P25787"
FT MOD_RES 24
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P25787"
FT MOD_RES 70
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P25787"
FT MOD_RES 76
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 121
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P17220"
FT MOD_RES 171
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 3
FT /note="E -> K (in Ref. 1; CAA49782)"
FT /evidence="ECO:0000305"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:3UNF"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:3UNE"
FT HELIX 20..30
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 80..101
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 107..120
FT /evidence="ECO:0007829|PDB:3UNB"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 131..140
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 143..149
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 155..164
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 167..177
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 184..196
FT /evidence="ECO:0007829|PDB:3UNB"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:3UNB"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:3UNB"
FT HELIX 223..229
FT /evidence="ECO:0007829|PDB:3UNB"
SQ SEQUENCE 234 AA; 25927 MW; 4ECB56A233583821 CRC64;
MAERGYSFSL TTFSPSGKLV QIEYALAAVA GGAPSVGIKA ANGVVLATEK KQKSILYDER
SVHKVEPITK HIGLVYSGMG PDYRVLVHRA RKLAQQYYLV YQEPIPTAQL VQRVASVMQE
YTQSGGVRPF GVSLLICGWN EGRPYLFQSD PSGAYFAWKA TAMGKNYVNG KTFLEKRYNE
DLELEDAIHT AILTLKESFE GQMTEDNIEV GICNEAGFRR LTPTEVRDYL AAIA
