ID Q6FHK9_HUMAN Unreviewed; 239 AA. AC Q6FHK9; DT 19-JUL-2004, integrated into UniProtKB/TrEMBL. DT 19-JUL-2004, sequence version 1. DT 27-NOV-2024, entry version 80. DE RecName: Full=Proteasome activator complex subunit 2 {ECO:0000256|ARBA:ARBA00039312}; DE AltName: Full=Proteasome activator 28 subunit beta {ECO:0000256|ARBA:ARBA00041908}; GN Name=PSME2 {ECO:0000313|EMBL:CAG46543.1}; 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:CAG46543.1}; RN [1] {ECO:0000313|EMBL:CAG46543.1} RP NUCLEOTIDE SEQUENCE. RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., RA LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CR541743; CAG46543.1; -; mRNA. DR AlphaFoldDB; Q6FHK9; -. DR SMR; Q6FHK9; -. DR PeptideAtlas; Q6FHK9; -. DR ChiTaRS; PSME2; human. 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 70..86 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 239 AA; 27432 MW; 7E86145518EC739A CRC64; MAKPCGVRLS GEVRKQVEVF RQNLFQEAEE FLYRFLPQKI IYLNQLLQED SLNVADLTSL RAPLDIPIPD PPPKDDEMET DKQEKKEVPK CGFLPGNEKV LSLLALVKPE VWTLKEKCIL VITWIQHLIP KIEDGNDFGV AIQEKVLERV NAVKTKVEAF QTTISKYFSE RGDAVAKASK ETHVMDYRAL VHERDEAAYV ELRAMVLDLR AFYAELYHII SSNLEKIVNP KGEEKPSMY //