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Proteasome subunit beta type-2 (EC 3.4.25.1) (Macropain subunit C7-I) (Multicatalytic endopeptidase complex subunit C7-I) (Proteasome component C7-I)

 PSB2_HUMAN              Reviewed;         201 AA.
P49721; D3DPS0; P31145; Q9BWZ9;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
10-OCT-2018, entry version 194.
RecName: Full=Proteasome subunit beta type-2;
EC=3.4.25.1 {ECO:0000269|PubMed:27176742};
AltName: Full=Macropain subunit C7-I;
AltName: Full=Multicatalytic endopeptidase complex subunit C7-I;
AltName: Full=Proteasome component C7-I;
Name=PSMB2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7918633; DOI=10.1016/0167-4781(94)90060-4;
Nothwang H.G., Tamura T., Tanaka K., Ichihara A.;
"Sequence analyses and inter-species comparisons of three novel human
proteasomal subunits, HsN3, HsC7-I and HsC10-II, confine potential
proteolytic active-site residues.";
Biochim. Biophys. Acta 1219:361-368(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 71-85 AND 171-181, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[8]
PROTEIN SEQUENCE OF 172-177 AND 186-193.
TISSUE=Keratinocyte;
PubMed=1286667; DOI=10.1002/elps.11501301199;
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel
protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[9]
PROTEIN SEQUENCE OF 72-85.
TISSUE=Placenta;
PubMed=7811265; DOI=10.1006/bbrc.1994.2876;
Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B.;
"Human proteasome subunits from 2-dimensional gels identified by
partial sequencing.";
Biochem. Biophys. Res. Commun. 205:1785-1789(1994).
[10]
FUNCTION IN ANTIGEN PRESENTATION.
PubMed=8610016; DOI=10.1038/381166a0;
Groettrup M., Soza A., Eggers M., Kuehn L., Dick T.P., Schild H.,
Rammensee H.G., Koszinowski U.H., Kloetzel P.M.;
"A role for the proteasome regulator PA28alpha in antigen
presentation.";
Nature 381:166-168(1996).
[11]
SUBCELLULAR LOCATION.
PubMed=12181345; DOI=10.1091/mbc.E02-03-0122;
Lafarga M., Berciano M.T., Pena E., Mayo I., Castano J.G., Bohmann D.,
Rodrigues J.P., Tavanez J.P., Carmo-Fonseca M.;
"Clastosome: a subtype of nuclear body enriched in 19S and 20S
proteasomes, ubiquitin, and protein substrates of proteasome.";
Mol. Biol. Cell 13:2771-2782(2002).
[12]
INTERACTION WITH HIV-1 TAT (MICROBIAL INFECTION).
PubMed=14550573; DOI=10.1016/S0014-5793(03)01025-1;
Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P.,
Mayer R.J., Krueger E.;
"Human immunodeficiency virus-1 Tat protein interacts with distinct
proteasomal alpha and beta subunits.";
FEBS Lett. 553:200-204(2003).
[13]
FUNCTION.
PubMed=15244466; DOI=10.1021/bm049957a;
Yano M., Koumoto Y., Kanesaki Y., Wu X., Kido H.;
"20S proteasome prevents aggregation of heat-denatured proteins
without PA700 regulatory subcomplex like a molecular chaperone.";
Biomacromolecules 5:1465-1469(2004).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17323924; DOI=10.1021/bi061994u;
Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
"Mass spectrometric characterization of the affinity-purified human
26S proteasome complex.";
Biochemistry 46:3553-3565(2007).
[15]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[16]
INDUCTION.
PubMed=19787249;
Wada T., Yamashita Y., Saga Y., Takahashi K., Koinuma K., Choi Y.L.,
Kaneda R., Fujiwara S., Soda M., Watanabe H., Kurashina K.,
Hatanaka H., Enomoto M., Takada S., Mano H., Suzuki M.;
"Screening for genetic abnormalities involved in ovarian
carcinogenesis using retroviral expression libraries.";
Int. J. Oncol. 35:973-976(2009).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[21]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=27176742; DOI=10.1515/hsz-2016-0176;
Rut W., Drag M.;
"Human 20S proteasome activity towards fluorogenic peptides of various
chain lengths.";
Biol. Chem. 397:921-926(2016).
[22]
STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND SUBUNIT.
PubMed=26133119; DOI=10.1038/ncomms8573;
da Fonseca P.C., Morris E.P.;
"Cryo-EM reveals the conformation of a substrate analogue in the human
20S proteasome core.";
Nat. Commun. 6:7573-7573(2015).
[23]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS), AND SUBUNIT.
PubMed=25599644; DOI=10.1016/j.str.2014.11.017;
Harshbarger W., Miller C., Diedrich C., Sacchettini J.;
"Crystal structure of the human 20S proteasome in complex with
carfilzomib.";
Structure 23:418-424(2015).
[24]
STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND SUBUNIT.
PubMed=27428775; DOI=10.1038/nsmb.3273;
Huang X., Luan B., Wu J., Shi Y.;
"An atomic structure of the human 26S proteasome.";
Nat. Struct. Mol. Biol. 23:778-785(2016).
[25]
STRUCTURE BY ELECTRON MICROSCOPY (4.02 ANGSTROMS), AND SUBUNIT.
PubMed=27342858; DOI=10.1073/pnas.1608050113;
Schweitzer A., Aufderheide A., Rudack T., Beck F., Pfeifer G.,
Plitzko J.M., Sakata E., Schulten K., Foerster F., Baumeister W.;
"Structure of the human 26S proteasome at a resolution of 3.9 Aa.";
Proc. Natl. Acad. Sci. U.S.A. 113:7816-7821(2016).
[26]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), AND SUBUNIT.
PubMed=27493187; DOI=10.1126/science.aaf8993;
Schrader J., Henneberg F., Mata R.A., Tittmann K., Schneider T.R.,
Stark H., Bourenkov G., Chari A.;
"The inhibition mechanism of human 20S proteasomes enables next-
generation inhibitor design.";
Science 353:594-598(2016).
[27]
X-RAY CRYSTALLOGRAPHY (3.75 ANGSTROMS) OF 1-255, AND SUBUNIT.
PubMed=26657688; DOI=10.1038/srep18167;
Ishii K., Noda M., Yagi H., Thammaporn R., Seetaha S., Satoh T.,
Kato K., Uchiyama S.;
"Disassembly of the self-assembled, double-ring structure of
proteasome alpha7 homo-tetradecamer by alpha6.";
Sci. Rep. 5:18167-18167(2015).
-!- FUNCTION: Component of the 20S core proteasome complex involved in
the proteolytic degradation of most intracellular proteins. This
complex plays numerous essential roles within the cell by
associating with different regulatory particles. Associated with
two 19S regulatory particles, forms the 26S proteasome and thus
participates in the ATP-dependent degradation of ubiquitinated
proteins. The 26S proteasome plays a key role in the maintenance
of protein homeostasis by removing misfolded or damaged proteins
that could impair cellular functions, and by removing proteins
whose functions are no longer required. Associated with the PA200
or PA28, the 20S proteasome mediates ubiquitin-independent protein
degradation. This type of proteolysis is required in several
pathways including spermatogenesis (20S-PA200 complex) or
generation of a subset of MHC class I-presented antigenic peptides
(20S-PA28 complex). {ECO:0000269|PubMed:15244466,
ECO:0000269|PubMed:27176742, ECO:0000269|PubMed:8610016}.
-!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
specificity. {ECO:0000269|PubMed:27176742}.
-!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and
two 19S regulatory subunits. The 20S proteasome core is a barrel-
shaped complex made of 28 subunits that are arranged in four
stacked rings. The two outer rings are each formed by seven alpha
subunits, and the two inner rings are formed by seven beta
subunits. The proteolytic activity is exerted by three beta-
subunits PSMB5, PSMB6 and PSMB7. {ECO:0000269|PubMed:25599644,
ECO:0000269|PubMed:26133119, ECO:0000269|PubMed:26657688,
ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775,
ECO:0000269|PubMed:27493187}.
-!- SUBUNIT: (Microbial infection) Interacts with HIV-1 protein Tat.
{ECO:0000269|PubMed:14550573}.
-!- INTERACTION:
Q7L273:KCTD9; NbExp=3; IntAct=EBI-359335, EBI-4397613;
A1A4E9:KRT13; NbExp=3; IntAct=EBI-359335, EBI-10171552;
P25786:PSMA1; NbExp=7; IntAct=EBI-359335, EBI-359352;
P49720:PSMB3; NbExp=4; IntAct=EBI-359335, EBI-603340;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12181345}.
Nucleus {ECO:0000269|PubMed:12181345}.
-!- INDUCTION: Up-regulated in ovarian cancer cell lines.
{ECO:0000269|PubMed:19787249}.
-!- SIMILARITY: Belongs to the peptidase T1B family.
{ECO:0000255|PROSITE-ProRule:PRU00809}.
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EMBL; D26599; BAA05646.1; -; mRNA.
EMBL; CR456862; CAG33143.1; -; mRNA.
EMBL; BT007137; AAP35801.1; -; mRNA.
EMBL; AL354864; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL357035; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL157951; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471059; EAX07406.1; -; Genomic_DNA.
EMBL; CH471059; EAX07407.1; -; Genomic_DNA.
EMBL; BC101836; AAI01837.1; -; mRNA.
EMBL; BC105126; AAI05127.1; -; mRNA.
EMBL; BC107901; AAI07902.1; -; mRNA.
CCDS; CCDS394.1; -.
PIR; S55040; S55040.
RefSeq; NP_002785.1; NM_002794.4.
UniGene; Hs.471441; -.
PDB; 4R3O; X-ray; 2.60 A; K/Y=1-199.
PDB; 4R67; X-ray; 2.89 A; 0/K/Y/m=1-199.
PDB; 5A0Q; EM; 3.50 A; K/Y=1-201.
PDB; 5GJQ; EM; 4.50 A; d/r=1-201.
PDB; 5GJR; EM; 3.50 A; d/r=1-201.
PDB; 5L4G; EM; 4.02 A; 2/V=1-201.
PDB; 5LE5; X-ray; 1.80 A; J/X=1-201.
PDB; 5LEX; X-ray; 2.20 A; J/X=1-201.
PDB; 5LEY; X-ray; 1.90 A; J/X=1-201.
PDB; 5LEZ; X-ray; 2.19 A; J/X=1-201.
PDB; 5LF0; X-ray; 2.41 A; J/X=1-201.
PDB; 5LF1; X-ray; 2.00 A; J/X=1-201.
PDB; 5LF3; X-ray; 2.10 A; J/X=1-201.
PDB; 5LF4; X-ray; 1.99 A; J/X=1-201.
PDB; 5LF6; X-ray; 2.07 A; J/X=1-201.
PDB; 5LF7; X-ray; 2.00 A; J/X=1-201.
PDB; 5LN3; EM; 6.80 A; 4=1-201.
PDB; 5M32; EM; 3.80 A; J/X=1-196.
PDB; 5T0C; EM; 3.80 A; AQ/BQ=1-201.
PDB; 5T0G; EM; 4.40 A; Q=1-201.
PDB; 5T0H; EM; 6.80 A; Q=1-201.
PDB; 5T0I; EM; 8.00 A; Q=1-201.
PDB; 5T0J; EM; 8.00 A; Q=1-201.
PDB; 5VFO; EM; 3.50 A; Q/q=1-199.
PDB; 5VFP; EM; 4.20 A; Q/q=1-199.
PDB; 5VFQ; EM; 4.20 A; Q/q=1-199.
PDB; 5VFR; EM; 4.90 A; Q/q=1-199.
PDB; 5VFS; EM; 3.60 A; Q/q=1-199.
PDB; 5VFT; EM; 7.00 A; Q/q=1-199.
PDB; 5VFU; EM; 5.80 A; Q/q=1-199.
PDB; 6AVO; EM; 3.80 A; T/V=1-201.
PDBsum; 4R3O; -.
PDBsum; 4R67; -.
PDBsum; 5A0Q; -.
PDBsum; 5GJQ; -.
PDBsum; 5GJR; -.
PDBsum; 5L4G; -.
PDBsum; 5LE5; -.
PDBsum; 5LEX; -.
PDBsum; 5LEY; -.
PDBsum; 5LEZ; -.
PDBsum; 5LF0; -.
PDBsum; 5LF1; -.
PDBsum; 5LF3; -.
PDBsum; 5LF4; -.
PDBsum; 5LF6; -.
PDBsum; 5LF7; -.
PDBsum; 5LN3; -.
PDBsum; 5M32; -.
PDBsum; 5T0C; -.
PDBsum; 5T0G; -.
PDBsum; 5T0H; -.
PDBsum; 5T0I; -.
PDBsum; 5T0J; -.
PDBsum; 5VFO; -.
PDBsum; 5VFP; -.
PDBsum; 5VFQ; -.
PDBsum; 5VFR; -.
PDBsum; 5VFS; -.
PDBsum; 5VFT; -.
PDBsum; 5VFU; -.
PDBsum; 6AVO; -.
ProteinModelPortal; P49721; -.
SMR; P49721; -.
BioGrid; 111663; 100.
CORUM; P49721; -.
DIP; DIP-33848N; -.
IntAct; P49721; 39.
MINT; P49721; -.
STRING; 9606.ENSP00000362334; -.
BindingDB; P49721; -.
ChEMBL; CHEMBL3492; -.
DrugBank; DB08889; Carfilzomib.
MEROPS; T01.984; -.
iPTMnet; P49721; -.
PhosphoSitePlus; P49721; -.
SwissPalm; P49721; -.
BioMuta; PSMB2; -.
DMDM; 1709762; -.
OGP; P49721; -.
REPRODUCTION-2DPAGE; IPI00028006; -.
REPRODUCTION-2DPAGE; P49721; -.
EPD; P49721; -.
MaxQB; P49721; -.
PaxDb; P49721; -.
PeptideAtlas; P49721; -.
PRIDE; P49721; -.
ProteomicsDB; 56057; -.
TopDownProteomics; P49721; -.
DNASU; 5690; -.
Ensembl; ENST00000373237; ENSP00000362334; ENSG00000126067.
GeneID; 5690; -.
KEGG; hsa:5690; -.
UCSC; uc001bzf.4; human.
CTD; 5690; -.
DisGeNET; 5690; -.
EuPathDB; HostDB:ENSG00000126067.11; -.
GeneCards; PSMB2; -.
HGNC; HGNC:9539; PSMB2.
HPA; HPA026322; -.
HPA; HPA026324; -.
MIM; 602175; gene.
neXtProt; NX_P49721; -.
OpenTargets; ENSG00000126067; -.
PharmGKB; PA33884; -.
eggNOG; KOG0177; Eukaryota.
eggNOG; COG0638; LUCA.
GeneTree; ENSGT00640000091536; -.
HOGENOM; HOG000188743; -.
HOVERGEN; HBG000815; -.
InParanoid; P49721; -.
KO; K02734; -.
OMA; QLYSMRN; -.
OrthoDB; EOG091G0K9M; -.
PhylomeDB; P49721; -.
TreeFam; TF106219; -.
Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
Reactome; R-HSA-4641257; Degradation of AXIN.
Reactome; R-HSA-4641258; Degradation of DVL.
Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
Reactome; R-HSA-5362768; Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-HSA-5632684; Hedgehog 'on' state.
Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-68827; CDT1 association with the CDC6:ORC:origin complex.
Reactome; R-HSA-68949; Orc1 removal from chromatin.
Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-HSA-69229; Ubiquitin-dependent degradation of Cyclin D1.
Reactome; R-HSA-69481; G2/M Checkpoints.
Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
Reactome; R-HSA-9020702; Interleukin-1 signaling.
Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
ChiTaRS; PSMB2; human.
GeneWiki; PSMB2; -.
GenomeRNAi; 5690; -.
PRO; PR:P49721; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000126067; Expressed in 238 organ(s), highest expression level in deltoid.
CleanEx; HS_PSMB2; -.
ExpressionAtlas; P49721; baseline and differential.
Genevisible; P49721; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; HDA:UniProtKB.
GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
GO; GO:0005839; C:proteasome core complex; ISS:UniProtKB.
GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IEA:InterPro.
GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
GO; GO:0010243; P:response to organonitrogen compound; IEA:Ensembl.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd03758; proteasome_beta_type_2; 1.
Gene3D; 3.60.20.10; -; 1.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR035206; Proteasome_beta2.
InterPro; IPR016050; Proteasome_bsu_CS.
InterPro; IPR001353; Proteasome_sua/b.
InterPro; IPR023333; Proteasome_suB-type.
PANTHER; PTHR11599:SF6; PTHR11599:SF6; 1.
Pfam; PF00227; Proteasome; 1.
SUPFAM; SSF56235; SSF56235; 1.
PROSITE; PS00854; PROTEASOME_BETA_1; 1.
PROSITE; PS51476; PROTEASOME_BETA_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Host-virus interaction; Hydrolase; Nucleus;
Protease; Proteasome; Reference proteome; Threonine protease.
CHAIN 1 201 Proteasome subunit beta type-2.
/FTId=PRO_0000148043.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378}.
STRAND 4 8 {ECO:0000244|PDB:5LE5}.
STRAND 13 18 {ECO:0000244|PDB:5LE5}.
STRAND 21 23 {ECO:0000244|PDB:5LE5}.
STRAND 26 31 {ECO:0000244|PDB:5LE5}.
STRAND 35 39 {ECO:0000244|PDB:5LE5}.
STRAND 42 49 {ECO:0000244|PDB:5LE5}.
HELIX 52 71 {ECO:0000244|PDB:5LE5}.
HELIX 77 89 {ECO:0000244|PDB:5LE5}.
TURN 91 93 {ECO:0000244|PDB:4R67}.
STRAND 94 96 {ECO:0000244|PDB:5LE5}.
STRAND 100 108 {ECO:0000244|PDB:5LE5}.
TURN 109 111 {ECO:0000244|PDB:5LE5}.
STRAND 112 118 {ECO:0000244|PDB:5LE5}.
STRAND 124 126 {ECO:0000244|PDB:5LE5}.
STRAND 128 133 {ECO:0000244|PDB:5LE5}.
HELIX 136 146 {ECO:0000244|PDB:5LE5}.
HELIX 153 170 {ECO:0000244|PDB:5LE5}.
STRAND 171 173 {ECO:0000244|PDB:5LE5}.
STRAND 177 184 {ECO:0000244|PDB:5LE5}.
STRAND 187 190 {ECO:0000244|PDB:5LE5}.
SEQUENCE 201 AA; 22836 MW; 04D085D7BAA76130 CRC64;
MEYLIGIQGP DYVLVASDRV AASNIVQMKD DHDKMFKMSE KILLLCVGEA GDTVQFAEYI
QKNVQLYKMR NGYELSPTAA ANFTRRNLAD CLRSRTPYHV NLLLAGYDEH EGPALYYMDY
LAALAKAPFA AHGYGAFLTL SILDRYYTPT ISRERAVELL RKCLEELQKR FILNLPTFSV
RIIDKNGIHD LDNISFPKQG S


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