PSB2_CAEEL
ID PSB2_CAEEL Reviewed; 199 AA.
AC P91477;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Proteasome subunit beta type-2;
DE AltName: Full=Proteasome subunit beta 4;
GN Name=pbs-4; ORFNames=T20F5.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Non-catalytic component of the proteasome, a multicatalytic
CC proteinase complex which is characterized by its ability to cleave
CC peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group
CC at neutral or slightly basic pH. The proteasome has an ATP-dependent
CC proteolytic activity (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and two
CC 19S regulatory subunits. The 20S proteasome core is composed of 28
CC subunits that are arranged in four stacked rings, resulting in a
CC barrel-shaped structure. The two end rings are each formed by seven
CC alpha subunits, and the two central rings are each formed by seven beta
CC subunits. The catalytic chamber with the active sites is on the inside
CC of the barrel (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}.
CC Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCD67779.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; FO080916; CCD67779.1; ALT_INIT; Genomic_DNA.
DR PIR; T29206; T29206.
DR RefSeq; NP_491261.1; NM_058860.6.
DR AlphaFoldDB; P91477; -.
DR SMR; P91477; -.
DR BioGRID; 37448; 34.
DR IntAct; P91477; 1.
DR STRING; 6239.T20F5.2; -.
DR MEROPS; T01.984; -.
DR EPD; P91477; -.
DR PaxDb; P91477; -.
DR PeptideAtlas; P91477; -.
DR EnsemblMetazoa; T20F5.2.1; T20F5.2.1; WBGene00003950.
DR GeneID; 171975; -.
DR KEGG; cel:CELE_T20F5.2; -.
DR UCSC; T20F5.2; c. elegans.
DR CTD; 171975; -.
DR WormBase; T20F5.2; CE13818; WBGene00003950; pbs-4.
DR eggNOG; KOG0177; Eukaryota.
DR GeneTree; ENSGT00640000091536; -.
DR HOGENOM; CLU_035750_12_1_1; -.
DR InParanoid; P91477; -.
DR OrthoDB; 1392180at2759; -.
DR PhylomeDB; P91477; -.
DR Reactome; R-CEL-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-CEL-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-CEL-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-CEL-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-CEL-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-CEL-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-CEL-382556; ABC-family proteins mediated transport.
DR Reactome; R-CEL-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-CEL-4641258; Degradation of DVL.
DR Reactome; R-CEL-5632684; Hedgehog 'on' state.
DR Reactome; R-CEL-5689603; UCH proteinases.
DR Reactome; R-CEL-5689880; Ub-specific processing proteases.
DR Reactome; R-CEL-68949; Orc1 removal from chromatin.
DR Reactome; R-CEL-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-CEL-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-CEL-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-CEL-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-CEL-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-CEL-8951664; Neddylation.
DR Reactome; R-CEL-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-CEL-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:P91477; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00003950; Expressed in adult organism and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005839; C:proteasome core complex; IBA:GO_Central.
DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR CDD; cd03758; proteasome_beta_type_2; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR035206; Proteasome_beta2.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR11599:SF6; PTHR11599:SF6; 1.
DR Pfam; PF00227; Proteasome; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Nucleus; Proteasome; Reference proteome.
FT CHAIN 1..199
FT /note="Proteasome subunit beta type-2"
FT /id="PRO_0000148046"
SQ SEQUENCE 199 AA; 22549 MW; 27510AF7CBA8DEBF CRC64;
MHFLVGISTE NYVILAADKA TFAYGAILAD SENDKEYRLG KKLTMMCIGE EGDVAQFGDW
TKRNLQLYSV RNGYEVSPSC AHHFVRRSIA EGLRSQDHYT VDVLIGGYDD KEDKAFLGSV
DYLANGLGQQ PYLFRGFCGR FCYAIMDREY KKDMTEAEGL ALMNKCIGEA KRRFVANIPG
YKVVIIDKKG YRKLDDVLF
