ID PSB1_BOVIN Reviewed; 241 AA. AC Q2TBX6; DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 24-JAN-2024, entry version 103. DE RecName: Full=Proteasome subunit beta type-1; DE Flags: Precursor; GN Name=PSMB1; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Crossbred X Angus; TISSUE=Liver; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases. RN [2] RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 29-241 OF COMPLEX WITH 20S RP PROTEASOME. RX PubMed=12015144; DOI=10.1016/s0969-2126(02)00748-7; RA Unno M., Mizushima T., Morimoto Y., Tomisugi Y., Tanaka K., Yasuoka N., RA Tsukihara T.; RT "The structure of the mammalian 20S proteasome at 2.75 A resolution."; RL Structure 10:609-618(2002). CC -!- FUNCTION: Non-catalytic component of the 20S core proteasome complex CC involved in the proteolytic degradation of most intracellular proteins. CC This complex plays numerous essential roles within the cell by CC associating with different regulatory particles. Associated with two CC 19S regulatory particles, forms the 26S proteasome and thus CC participates in the ATP-dependent degradation of ubiquitinated CC proteins. The 26S proteasome plays a key role in the maintenance of CC protein homeostasis by removing misfolded or damaged proteins that CC could impair cellular functions, and by removing proteins whose CC functions are no longer required. Associated with the PA200 or PA28, CC the 20S proteasome mediates ubiquitin-independent protein degradation. CC This type of proteolysis is required in several pathways including CC spermatogenesis (20S-PA200 complex) or generation of a subset of MHC CC class I-presented antigenic peptides (20S-PA28 complex). CC {ECO:0000250|UniProtKB:P20618}. 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 (PubMed:12015144). Interacts with SERPINB2. Interacts with RFPL4A (By CC similarity). {ECO:0000250|UniProtKB:O09061, CC ECO:0000250|UniProtKB:P20618, ECO:0000269|PubMed:12015144}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P20618}. Nucleus CC {ECO:0000250|UniProtKB:P20618}. Note=Translocated from the cytoplasm CC into the nucleus following interaction with AKIRIN2, which bridges the CC proteasome with the nuclear import receptor IPO9. CC {ECO:0000250|UniProtKB:P20618}. CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE- CC ProRule:PRU00809}. 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; BC109494; AAI09495.1; -; mRNA. DR RefSeq; NP_001033628.1; NM_001038539.2. DR PDB; 1IRU; X-ray; 2.75 A; 1/M=29-241. DR PDB; 7DR6; EM; 4.10 A; J/U=1-241. DR PDB; 7DR7; EM; 3.30 A; J/U=1-241. DR PDB; 7DRW; EM; 4.20 A; U/m=1-241. DR PDB; 8FZ5; EM; 2.23 A; M/a=1-241. DR PDB; 8FZ6; EM; 2.54 A; M/a=1-241. DR PDBsum; 1IRU; -. DR PDBsum; 7DR6; -. DR PDBsum; 7DR7; -. DR PDBsum; 7DRW; -. DR PDBsum; 8FZ5; -. DR PDBsum; 8FZ6; -. DR AlphaFoldDB; Q2TBX6; -. DR EMDB; EMD-29603; -. DR EMDB; EMD-29604; -. DR SMR; Q2TBX6; -. DR IntAct; Q2TBX6; 1. DR STRING; 9913.ENSBTAP00000010108; -. DR MEROPS; T01.990; -. DR GlyCosmos; Q2TBX6; 2 sites, No reported glycans. DR PaxDb; 9913-ENSBTAP00000010108; -. DR PeptideAtlas; Q2TBX6; -. DR GeneID; 514237; -. DR KEGG; bta:514237; -. DR CTD; 5689; -. DR eggNOG; KOG0179; Eukaryota. DR InParanoid; Q2TBX6; -. DR OrthoDB; 158278at2759; -. DR EvolutionaryTrace; Q2TBX6; -. DR Proteomes; UP000009136; Unplaced. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB. DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB. DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro. DR CDD; cd03757; proteasome_beta_type_1; 1. DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR016050; Proteasome_bsu_CS. DR InterPro; IPR001353; Proteasome_sua/b. DR InterPro; IPR023333; Proteasome_suB-type. DR PANTHER; PTHR32194; METALLOPROTEASE TLDD; 1. DR PANTHER; PTHR32194:SF2; PROTEASOME SUBUNIT BETA TYPE-1; 1. DR Pfam; PF00227; Proteasome; 1. DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1. DR PROSITE; PS00854; PROTEASOME_BETA_1; 1. DR PROSITE; PS51476; PROTEASOME_BETA_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cytoplasm; Glycoprotein; Nucleus; KW Phosphoprotein; Proteasome; Reference proteome. FT PROPEP 1..28 FT /evidence="ECO:0000250" FT /id="PRO_0000259622" FT CHAIN 29..241 FT /note="Proteasome subunit beta type-1" FT /id="PRO_0000239853" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:P20618" FT MOD_RES 62 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P20618" FT MOD_RES 68 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P20618" FT MOD_RES 150 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:O09061" FT MOD_RES 162 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P20618" FT MOD_RES 204 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P20618" FT CARBOHYD 58 FT /note="O-linked (GlcNAc) serine" FT /evidence="ECO:0000250" FT CARBOHYD 209 FT /note="O-linked (GlcNAc) serine" FT /evidence="ECO:0000250" FT STRAND 39..45 FT /evidence="ECO:0007829|PDB:1IRU" FT STRAND 48..54 FT /evidence="ECO:0007829|PDB:1IRU" FT STRAND 57..59 FT /evidence="ECO:0007829|PDB:1IRU" FT STRAND 62..66 FT /evidence="ECO:0007829|PDB:1IRU" FT STRAND 71..75 FT /evidence="ECO:0007829|PDB:1IRU" FT STRAND 78..84 FT /evidence="ECO:0007829|PDB:1IRU" FT HELIX 86..107 FT /evidence="ECO:0007829|PDB:1IRU" FT HELIX 113..125 FT /evidence="ECO:0007829|PDB:1IRU" FT TURN 126..129 FT /evidence="ECO:0007829|PDB:1IRU" FT STRAND 134..141 FT /evidence="ECO:0007829|PDB:1IRU" FT STRAND 147..152 FT /evidence="ECO:0007829|PDB:1IRU" FT STRAND 158..167 FT /evidence="ECO:0007829|PDB:1IRU" FT HELIX 170..180 FT /evidence="ECO:0007829|PDB:1IRU" FT HELIX 196..213 FT /evidence="ECO:0007829|PDB:1IRU" FT STRAND 219..227 FT /evidence="ECO:0007829|PDB:1IRU" FT STRAND 230..237 FT /evidence="ECO:0007829|PDB:1IRU" SQ SEQUENCE 241 AA; 26246 MW; 8682655C19CF2ACD CRC64; MLSSVAAYSG AGRDLAMEPH SSVGPLQLRF SPYAFNGGTV LAIAGEDFSI VASDTRLSEG FSIHTRDSPK CYKLTDKTVI GCSGFHGDCL TLTKIIEARL KMYKHSNNKA MTTGAIAAML STILYSRRFF PYYVYNIIGG LDEEGKGAVY SFDPVGSYQR DSFKAGGSAS AMLQPLLDNQ VGFKNMQNVE HVPLSLDRAM RLVKDVFISA AERDVYTGDA LKVCIVTKEG IRGETVPLRK D //