ID   Q2TNB3_HUMAN            Unreviewed;       239 AA.
AC   Q2TNB3;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   18-JUN-2025, entry version 76.
DE   RecName: Full=Proteasome activator complex subunit 2 {ECO:0000256|ARBA:ARBA00039312};
DE   AltName: Full=11S regulator complex subunit beta {ECO:0000256|ARBA:ARBA00077786};
DE   AltName: Full=Activator of multicatalytic protease subunit 2 {ECO:0000256|ARBA:ARBA00081734};
DE   AltName: Full=Proteasome activator 28 subunit beta {ECO:0000256|ARBA:ARBA00041908};
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 {ECO:0000313|EMBL:AAX11425.1};
RN   [1] {ECO:0000313|EMBL:AAX11425.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Kim J.W.;
RT   "Identification of a cell migration-inducing gene.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Implicated in immunoproteasome assembly and required for
CC       efficient antigen processing. The PA28 activator complex enhances the
CC       generation of class I binding peptides by altering the cleavage pattern
CC       of the proteasome. {ECO:0000256|ARBA:ARBA00037467}.
CC   -!- SUBUNIT: Heterodimer of PSME1 and PSME2, which forms a hexameric ring.
CC       {ECO:0000256|ARBA:ARBA00038631}.
CC   -!- SIMILARITY: Belongs to the PA28 family.
CC       {ECO:0000256|ARBA:ARBA00005883}.
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DR   EMBL; AY771595; AAX11425.1; -; mRNA.
DR   AlphaFoldDB; Q2TNB3; -.
DR   SMR; Q2TNB3; -.
DR   PeptideAtlas; Q2TNB3; -.
DR   GO; GO:0008537; C:proteasome activator complex; IEA:InterPro.
DR   FunFam; 1.20.120.180:FF:000002; Proteasome activator complex subunit 1; 1.
DR   FunFam; 1.20.5.120:FF:000002; proteasome activator complex subunit 2; 1.
DR   Gene3D; 1.20.120.180; Proteasome activator pa28, C-terminal domain; 1.
DR   Gene3D; 1.20.5.120; Proteasome activator pa28, N-terminal domain; 1.
DR   InterPro; IPR003186; PA28_C.
DR   InterPro; IPR036997; PA28_C_sf.
DR   InterPro; IPR036996; PA28_N_sf.
DR   InterPro; IPR009077; Proteasome_activ_PA28.
DR   InterPro; IPR003185; Proteasome_activ_PA28_N.
DR   InterPro; IPR036252; Proteasome_activ_sf.
DR   PANTHER; PTHR10660:SF6; PROTEASOME ACTIVATOR COMPLEX SUBUNIT 2; 1.
DR   PANTHER; PTHR10660; PROTEASOME REGULATOR PA28; 1.
DR   Pfam; PF02252; PA28_C; 1.
DR   Pfam; PF02251; PA28_N; 1.
DR   SUPFAM; SSF47216; Proteasome activator; 1.
PE   2: Evidence at transcript level;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942}.
FT   DOMAIN          12..71
FT                   /note="Proteasome activator PA28 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02251"
FT   DOMAIN          94..235
FT                   /note="Proteasome activator PA28 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02252"
FT   REGION          65..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..86
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   239 AA;  27349 MW;  97A28971AA78A87C CRC64;
     MAKPCGVRLS GEARKQVEVF RQNLFQEAEE FLYRFLPQKI IYLNQLLQED SLNVADLTSL
     RAPLDIPIPD PPPKDDEMET DKQEKKEVPK CGFLPGNEKV LSLLALVKPE VWTLKEKCIL
     VITWIQHLIP KIEDGNDFGV AIQEKVLERV NAVKTKVEAF QTTISKYFSE RGDAVAKASK
     ETHVMDYRAL VHERDEAAYG ELRAMVLDLR AFYAELYHII SSNLEKIVTP KGEEKPSMY
//