ID   Q6IAT9_HUMAN            Unreviewed;       239 AA.
AC   Q6IAT9;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 156.
DE   RecName: Full=Proteasome subunit beta {ECO:0000256|RuleBase:RU004203};
GN   Name=PSMB6 {ECO:0000313|EMBL:CAG33346.1};
GN   ORFNames=hCG_32695 {ECO:0000313|EMBL:EAW90407.1};
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:CAG33346.1};
RN   [1] {ECO:0000313|EMBL:EAW90407.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=11181995; DOI=10.1126/science.1058040;
RA   Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G.,
RA   Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P.,
RA   Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H.,
RA   Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J.,
RA   Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J.,
RA   McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C.,
RA   Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M.,
RA   Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C.,
RA   Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K.,
RA   Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R.,
RA   Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K.,
RA   Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P.,
RA   Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y.,
RA   Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N.,
RA   Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B.,
RA   Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J.,
RA   Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W.,
RA   Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S.,
RA   Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T.,
RA   Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I.,
RA   Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L.,
RA   Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L.,
RA   Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C.,
RA   Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C.,
RA   Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D.,
RA   McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B.,
RA   Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M.,
RA   Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C.,
RA   Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S.,
RA   Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S.,
RA   Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R.,
RA   Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B.,
RA   Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S.,
RA   Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S.,
RA   Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J.,
RA   Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M.,
RA   Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S.,
RA   Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M.,
RA   Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J.,
RA   Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J.,
RA   Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N.,
RA   Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J.,
RA   Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E.,
RA   Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.;
RT   "The sequence of the human genome.";
RL   Science 291:1304-1351(2001).
RN   [2] {ECO:0000313|EMBL:AAP88811.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:CAG33346.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
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.
RN   [4] {ECO:0000313|EMBL:EAW90407.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:BAG34711.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Tongue {ECO:0000313|EMBL:BAG34711.1};
RA   Wakamatsu A., Yamamoto J., Kimura K., Kaida T., Tsuchiya K., Iida Y.,
RA   Takayama Y., Murakawa K., Kanehori K., Andoh T., Kagawa N., Sato R.,
RA   Kawamura Y., Tanaka S., Kisu Y., Sugano S., Goshima N., Nomura N.,
RA   Isogai T.;
RT   "NEDO functional analysis of protein and research application project.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the proteasome, a multicatalytic proteinase
CC       complex which is characterized by its ability to cleave peptides with
CC       Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or
CC       slightly basic pH. The proteasome has an ATP-dependent proteolytic
CC       activity. {ECO:0000256|RuleBase:RU004203}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of peptide bonds with very broad specificity.;
CC         EC=3.4.25.1; Evidence={ECO:0000256|ARBA:ARBA00001198};
CC   -!- SUBUNIT: Component of the proteasome complex.
CC       {ECO:0000256|RuleBase:RU004203}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU004203}.
CC       Nucleus {ECO:0000256|RuleBase:RU004203}.
CC   -!- SIMILARITY: Belongs to the peptidase T1B family.
CC       {ECO:0000256|RuleBase:RU004203}.
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DR   EMBL; BT009809; AAP88811.1; -; mRNA.
DR   EMBL; AK311768; BAG34711.1; -; mRNA.
DR   EMBL; CR457065; CAG33346.1; -; mRNA.
DR   EMBL; CH471108; EAW90407.1; -; Genomic_DNA.
DR   RefSeq; NP_002789.1; NM_002798.2.
DR   AlphaFoldDB; Q6IAT9; -.
DR   SMR; Q6IAT9; -.
DR   IntAct; Q6IAT9; 2.
DR   MEROPS; T01.010; -.
DR   MaxQB; Q6IAT9; -.
DR   Antibodypedia; 11325; 179 antibodies from 28 providers.
DR   DNASU; 5694; -.
DR   GeneID; 5694; -.
DR   KEGG; hsa:5694; -.
DR   UCSC; uc002fzb.4; human.
DR   CTD; 5694; -.
DR   PharmGKB; PA33888; -.
DR   VEuPathDB; HostDB:ENSG00000142507; -.
DR   HOGENOM; CLU_035750_5_2_1; -.
DR   OMA; TFIYGYC; -.
DR   OrthoDB; 754468at2759; -.
DR   BioGRID-ORCS; 5694; 787 hits in 1169 CRISPR screens.
DR   ChiTaRS; PSMB6; human.
DR   GenomeRNAi; 5694; -.
DR   ExpressionAtlas; Q6IAT9; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005839; C:proteasome core complex; IEA:Ensembl.
DR   GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro.
DR   CDD; cd03762; proteasome_beta_type_6; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR000243; Pept_T1A_subB.
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:SF8; PROTEASOME SUBUNIT BETA; 1.
DR   Pfam; PF00227; Proteasome; 1.
DR   PRINTS; PR00141; PROTEASOME.
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   2: Evidence at transcript level;
KW   Cytoplasm {ECO:0000256|RuleBase:RU004203};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU004203};
KW   Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|RuleBase:RU004203}.
FT   ACT_SITE        35
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600243-1"
SQ   SEQUENCE   239 AA;  25358 MW;  7DF4081DC735930C CRC64;
     MAATLLAARG AGPAPAWGPE AFTPDWESRE VSTGTTIMAV QFDGGVVLGA DSRTTTGSYI
     ANRVTDKLTP IHDRIFCCRS GSAADTQAVA DAVTYQLGFH SIELNEPPLV HTAASLFKEM
     CYRYREDLMA GIIIAGWDPQ EGGQVYSVPM GGMMVRQSFA IGGSGSSYIY GYVDATYREG
     MTKEECLQFT ANALALAMER DGSSGGVIRL AAIAESGVER QVLLGDQIPK FAVATLPPA
//