PSB7_HUMAN
ID PSB7_HUMAN Reviewed; 277 AA.
AC Q99436; B4E0P1; Q5TBG6; Q96AG8; Q9BWA7;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Proteasome subunit beta type-7;
DE EC=3.4.25.1 {ECO:0000269|PubMed:27176742};
DE AltName: Full=Macropain chain Z;
DE AltName: Full=Multicatalytic endopeptidase complex chain Z;
DE AltName: Full=Proteasome subunit Z;
DE Flags: Precursor;
GN Name=PSMB7; Synonyms=Z;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8666937; DOI=10.1084/jem.183.4.1807;
RA Hisamatsu H., Shimbara N., Saito Y., Kristensen P., Hendil K.B.,
RA Fujiwara T., Takahashi E., Tanahashi N., Tamura T., Ichihara A., Tanaka K.;
RT "Newly identified pair of proteasomal subunits regulated reciprocally by
RT interferon gamma.";
RL J. Exp. Med. 183:1807-1816(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-39.
RC TISSUE=Lung, Urinary bladder, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 165-184 AND 259-277, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
RP FUNCTION IN ANTIGEN PRESENTATION.
RX PubMed=8610016; DOI=10.1038/381166a0;
RA Groettrup M., Soza A., Eggers M., Kuehn L., Dick T.P., Schild H.,
RA Rammensee H.G., Koszinowski U.H., Kloetzel P.M.;
RT "A role for the proteasome regulator PA28alpha in antigen presentation.";
RL Nature 381:166-168(1996).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=12181345; DOI=10.1091/mbc.e02-03-0122;
RA Lafarga M., Berciano M.T., Pena E., Mayo I., Castano J.G., Bohmann D.,
RA Rodrigues J.P., Tavanez J.P., Carmo-Fonseca M.;
RT "Clastosome: a subtype of nuclear body enriched in 19S and 20S proteasomes,
RT ubiquitin, and protein substrates of proteasome.";
RL Mol. Biol. Cell 13:2771-2782(2002).
RN [9]
RP INTERACTION WITH HIV-1 TAT (MICROBIAL INFECTION).
RX PubMed=14550573; DOI=10.1016/s0014-5793(03)01025-1;
RA Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P.,
RA Mayer R.J., Krueger E.;
RT "Human immunodeficiency virus-1 Tat protein interacts with distinct
RT proteasomal alpha and beta subunits.";
RL FEBS Lett. 553:200-204(2003).
RN [10]
RP FUNCTION.
RX PubMed=15244466; DOI=10.1021/bm049957a;
RA Yano M., Koumoto Y., Kanesaki Y., Wu X., Kido H.;
RT "20S proteasome prevents aggregation of heat-denatured proteins without
RT PA700 regulatory subcomplex like a molecular chaperone.";
RL Biomacromolecules 5:1465-1469(2004).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17323924; DOI=10.1021/bi061994u;
RA Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
RT "Mass spectrometric characterization of the affinity-purified human 26S
RT proteasome complex.";
RL Biochemistry 46:3553-3565(2007).
RN [12]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=18549262; DOI=10.1021/pr8000892;
RA Rho J.H., Qin S., Wang J.Y., Roehrl M.H.;
RT "Proteomic expression analysis of surgical human colorectal cancer tissues:
RT up-regulation of PSB7, PRDX1, and SRP9 and hypoxic adaptation in cancer.";
RL J. Proteome Res. 7:2959-2972(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=27176742; DOI=10.1515/hsz-2016-0176;
RA Rut W., Drag M.;
RT "Human 20S proteasome activity towards fluorogenic peptides of various
RT chain lengths.";
RL Biol. Chem. 397:921-926(2016).
RN [17]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND SUBUNIT.
RX PubMed=26133119; DOI=10.1038/ncomms8573;
RA da Fonseca P.C., Morris E.P.;
RT "Cryo-EM reveals the conformation of a substrate analogue in the human 20S
RT proteasome core.";
RL Nat. Commun. 6:7573-7573(2015).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS), SUBUNIT, AND ACTIVE SITE.
RX PubMed=25599644; DOI=10.1016/j.str.2014.11.017;
RA Harshbarger W., Miller C., Diedrich C., Sacchettini J.;
RT "Crystal structure of the human 20S proteasome in complex with
RT carfilzomib.";
RL Structure 23:418-424(2015).
RN [19]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND SUBUNIT.
RX PubMed=27428775; DOI=10.1038/nsmb.3273;
RA Huang X., Luan B., Wu J., Shi Y.;
RT "An atomic structure of the human 26S proteasome.";
RL Nat. Struct. Mol. Biol. 23:778-785(2016).
RN [20]
RP STRUCTURE BY ELECTRON MICROSCOPY (4.02 ANGSTROMS), AND SUBUNIT.
RX PubMed=27342858; DOI=10.1073/pnas.1608050113;
RA Schweitzer A., Aufderheide A., Rudack T., Beck F., Pfeifer G.,
RA Plitzko J.M., Sakata E., Schulten K., Foerster F., Baumeister W.;
RT "Structure of the human 26S proteasome at a resolution of 3.9 Aa.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:7816-7821(2016).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), SUBUNIT, AND ACTIVE SITE.
RX PubMed=27493187; DOI=10.1126/science.aaf8993;
RA Schrader J., Henneberg F., Mata R.A., Tittmann K., Schneider T.R.,
RA Stark H., Bourenkov G., Chari A.;
RT "The inhibition mechanism of human 20S proteasomes enables next-generation
RT inhibitor design.";
RL Science 353:594-598(2016).
RN [22]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) IN COMPLEX WITH AKIRIN2,
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=34711951; DOI=10.1038/s41586-021-04035-8;
RA de Almeida M., Hinterndorfer M., Brunner H., Grishkovskaya I., Singh K.,
RA Schleiffer A., Jude J., Deswal S., Kalis R., Vunjak M., Lendl T., Imre R.,
RA Roitinger E., Neumann T., Kandolf S., Schutzbier M., Mechtler K.,
RA Versteeg G.A., Haselbach D., Zuber J.;
RT "AKIRIN2 controls the nuclear import of proteasomes in vertebrates.";
RL Nature 599:491-496(2021).
CC -!- FUNCTION: Component of the 20S core proteasome complex involved in the
CC proteolytic degradation of most intracellular proteins. This complex
CC plays numerous essential roles within the cell by associating with
CC different regulatory particles. Associated with two 19S regulatory
CC particles, forms the 26S proteasome and thus participates in the ATP-
CC dependent degradation of ubiquitinated proteins. The 26S proteasome
CC plays a key role in the maintenance of protein homeostasis by removing
CC misfolded or damaged proteins that could impair cellular functions, and
CC by removing proteins whose functions are no longer required. Associated
CC with the PA200 or PA28, the 20S proteasome mediates ubiquitin-
CC independent protein degradation. This type of proteolysis is required
CC in several pathways including spermatogenesis (20S-PA200 complex) or
CC generation of a subset of MHC class I-presented antigenic peptides
CC (20S-PA28 complex). Within the 20S core complex, PSMB7 displays a
CC trypsin-like activity. {ECO:0000269|PubMed:15244466,
CC ECO:0000269|PubMed:27176742, ECO:0000269|PubMed:8610016}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of peptide bonds with very broad specificity.;
CC EC=3.4.25.1; Evidence={ECO:0000269|PubMed:27176742};
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 {ECO:0000269|PubMed:25599644, ECO:0000269|PubMed:26133119,
CC ECO:0000269|PubMed:27342858, ECO:0000269|PubMed:27428775,
CC ECO:0000269|PubMed:27493187, ECO:0000269|PubMed:34711951}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Tat protein.
CC {ECO:0000269|PubMed:14550573}.
CC -!- INTERACTION:
CC Q99436; Q9Y244: POMP; NbExp=3; IntAct=EBI-603319, EBI-696895;
CC Q99436; P20618: PSMB1; NbExp=9; IntAct=EBI-603319, EBI-372273;
CC Q99436; P28074: PSMB5; NbExp=8; IntAct=EBI-603319, EBI-357828;
CC Q99436; P28072: PSMB6; NbExp=3; IntAct=EBI-603319, EBI-359288;
CC Q99436; P28065: PSMB9; NbExp=7; IntAct=EBI-603319, EBI-603300;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12181345,
CC ECO:0000269|PubMed:18549262, ECO:0000269|PubMed:34711951}. Nucleus
CC {ECO:0000269|PubMed:12181345, ECO:0000269|PubMed:18549262,
CC ECO:0000269|PubMed:34711951}. Note=Translocated from the cytoplasm into
CC the nucleus following interaction with AKIRIN2, which bridges the
CC proteasome with the nuclear import receptor IPO9.
CC {ECO:0000269|PubMed:34711951}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99436-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99436-2; Sequence=VSP_056573, VSP_056574;
CC -!- TISSUE SPECIFICITY: Expressed at a low level in colonic mucosa. Up-
CC regulated in colorectal cancer tissues. {ECO:0000269|PubMed:18549262}.
CC -!- SIMILARITY: Belongs to the peptidase T1B family. {ECO:0000255|PROSITE-
CC ProRule:PRU00809}.
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DR EMBL; D38048; BAA07238.1; -; mRNA.
DR EMBL; AK303460; BAG64503.1; -; mRNA.
DR EMBL; AL137846; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87582.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87583.1; -; Genomic_DNA.
DR EMBL; BC000509; AAH00509.1; -; mRNA.
DR EMBL; BC008414; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC017116; AAH17116.2; -; mRNA.
DR CCDS; CCDS6855.1; -. [Q99436-1]
DR RefSeq; NP_002790.1; NM_002799.3. [Q99436-1]
DR PDB; 4R3O; X-ray; 2.60 A; I/W=44-263.
DR PDB; 4R67; X-ray; 2.89 A; I/W/k/y=44-263.
DR PDB; 5A0Q; EM; 3.50 A; I/W=44-277.
DR PDB; 5GJQ; EM; 4.50 A; b/p=1-277.
DR PDB; 5GJR; EM; 3.50 A; b/p=1-277.
DR PDB; 5L4G; EM; 4.02 A; 7/8=1-277.
DR PDB; 5LE5; X-ray; 1.80 A; H/V=44-277.
DR PDB; 5LEX; X-ray; 2.20 A; H/V=44-277.
DR PDB; 5LEY; X-ray; 1.90 A; H/V=44-277.
DR PDB; 5LEZ; X-ray; 2.19 A; H/V=44-277.
DR PDB; 5LF0; X-ray; 2.41 A; H/V=44-277.
DR PDB; 5LF1; X-ray; 2.00 A; H/V=44-277.
DR PDB; 5LF3; X-ray; 2.10 A; H/V=44-277.
DR PDB; 5LF4; X-ray; 1.99 A; H/V=44-277.
DR PDB; 5LF6; X-ray; 2.07 A; H/V=44-277.
DR PDB; 5LF7; X-ray; 2.00 A; H/V=44-277.
DR PDB; 5LN3; EM; 6.80 A; 2=1-277.
DR PDB; 5M32; EM; 3.80 A; H/V=1-277.
DR PDB; 5T0C; EM; 3.80 A; AO/BO=2-277.
DR PDB; 5T0G; EM; 4.40 A; O=2-277.
DR PDB; 5T0H; EM; 6.80 A; O=2-277.
DR PDB; 5T0I; EM; 8.00 A; O=2-277.
DR PDB; 5T0J; EM; 8.00 A; O=2-277.
DR PDB; 5VFO; EM; 3.50 A; O/o=44-263.
DR PDB; 5VFP; EM; 4.20 A; O/o=44-263.
DR PDB; 5VFQ; EM; 4.20 A; O/o=44-263.
DR PDB; 5VFR; EM; 4.90 A; O/o=44-263.
DR PDB; 5VFS; EM; 3.60 A; O/o=44-263.
DR PDB; 5VFT; EM; 7.00 A; O/o=44-263.
DR PDB; 5VFU; EM; 5.80 A; O/o=44-263.
DR PDB; 6HTB; X-ray; 2.70 A; H/V=44-277.
DR PDB; 6HTC; X-ray; 2.80 A; H/V=44-277.
DR PDB; 6HTD; X-ray; 3.00 A; H/V=44-277.
DR PDB; 6HTP; X-ray; 3.00 A; H/V=44-277.
DR PDB; 6HTR; X-ray; 2.60 A; H/V=44-277.
DR PDB; 6HUB; X-ray; 2.90 A; H/V=44-277.
DR PDB; 6HUC; X-ray; 3.00 A; H/V=44-277.
DR PDB; 6HUQ; X-ray; 3.00 A; H/V=44-277.
DR PDB; 6HUU; X-ray; 2.80 A; H/V=44-277.
DR PDB; 6HUV; X-ray; 3.10 A; H/V=44-277.
DR PDB; 6KWY; EM; 2.72 A; H/V=1-277.
DR PDB; 6MSB; EM; 3.00 A; O/o=2-277.
DR PDB; 6MSD; EM; 3.20 A; O/o=2-277.
DR PDB; 6MSE; EM; 3.30 A; O/o=2-277.
DR PDB; 6MSG; EM; 3.50 A; O/o=2-277.
DR PDB; 6MSH; EM; 3.60 A; O/o=2-277.
DR PDB; 6MSJ; EM; 3.30 A; O/o=2-277.
DR PDB; 6MSK; EM; 3.20 A; O/o=2-277.
DR PDB; 6R70; EM; 3.50 A; H/V=44-263.
DR PDB; 6REY; EM; 3.00 A; I/W=44-277.
DR PDB; 6RGQ; EM; 2.60 A; I/W=44-277.
DR PDB; 6WJD; EM; 4.80 A; O/o=2-277.
DR PDB; 6WJN; EM; 5.70 A; O/o=44-263.
DR PDB; 6XMJ; EM; 3.00 A; I=44-263.
DR PDB; 7LXV; EM; 3.40 A; H/V=44-277.
DR PDB; 7NHT; EM; 2.80 A; H=1-277.
DR PDB; 7PG9; EM; 3.70 A; I/W=44-277.
DR PDB; 7V5G; EM; 4.47 A; B/I=44-277.
DR PDB; 7V5M; EM; 3.88 A; I/W=44-277.
DR PDBsum; 4R3O; -.
DR PDBsum; 4R67; -.
DR PDBsum; 5A0Q; -.
DR PDBsum; 5GJQ; -.
DR PDBsum; 5GJR; -.
DR PDBsum; 5L4G; -.
DR PDBsum; 5LE5; -.
DR PDBsum; 5LEX; -.
DR PDBsum; 5LEY; -.
DR PDBsum; 5LEZ; -.
DR PDBsum; 5LF0; -.
DR PDBsum; 5LF1; -.
DR PDBsum; 5LF3; -.
DR PDBsum; 5LF4; -.
DR PDBsum; 5LF6; -.
DR PDBsum; 5LF7; -.
DR PDBsum; 5LN3; -.
DR PDBsum; 5M32; -.
DR PDBsum; 5T0C; -.
DR PDBsum; 5T0G; -.
DR PDBsum; 5T0H; -.
DR PDBsum; 5T0I; -.
DR PDBsum; 5T0J; -.
DR PDBsum; 5VFO; -.
DR PDBsum; 5VFP; -.
DR PDBsum; 5VFQ; -.
DR PDBsum; 5VFR; -.
DR PDBsum; 5VFS; -.
DR PDBsum; 5VFT; -.
DR PDBsum; 5VFU; -.
DR PDBsum; 6HTB; -.
DR PDBsum; 6HTC; -.
DR PDBsum; 6HTD; -.
DR PDBsum; 6HTP; -.
DR PDBsum; 6HTR; -.
DR PDBsum; 6HUB; -.
DR PDBsum; 6HUC; -.
DR PDBsum; 6HUQ; -.
DR PDBsum; 6HUU; -.
DR PDBsum; 6HUV; -.
DR PDBsum; 6KWY; -.
DR PDBsum; 6MSB; -.
DR PDBsum; 6MSD; -.
DR PDBsum; 6MSE; -.
DR PDBsum; 6MSG; -.
DR PDBsum; 6MSH; -.
DR PDBsum; 6MSJ; -.
DR PDBsum; 6MSK; -.
DR PDBsum; 6R70; -.
DR PDBsum; 6REY; -.
DR PDBsum; 6RGQ; -.
DR PDBsum; 6WJD; -.
DR PDBsum; 6WJN; -.
DR PDBsum; 6XMJ; -.
DR PDBsum; 7LXV; -.
DR PDBsum; 7NHT; -.
DR PDBsum; 7PG9; -.
DR PDBsum; 7V5G; -.
DR PDBsum; 7V5M; -.
DR AlphaFoldDB; Q99436; -.
DR SMR; Q99436; -.
DR BioGRID; 111668; 126.
DR ComplexPortal; CPX-5993; 26S Proteasome complex.
DR CORUM; Q99436; -.
DR DIP; DIP-33843N; -.
DR IntAct; Q99436; 56.
DR MINT; Q99436; -.
DR STRING; 9606.ENSP00000259457; -.
DR BindingDB; Q99436; -.
DR ChEMBL; CHEMBL3347256; -.
DR DrugBank; DB08515; (3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDE.
DR MEROPS; T01.011; -.
DR MEROPS; T01.017; -.
DR GlyGen; Q99436; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q99436; -.
DR MetOSite; Q99436; -.
DR PhosphoSitePlus; Q99436; -.
DR SwissPalm; Q99436; -.
DR BioMuta; PSMB7; -.
DR DMDM; 17380263; -.
DR EPD; Q99436; -.
DR jPOST; Q99436; -.
DR MassIVE; Q99436; -.
DR MaxQB; Q99436; -.
DR PaxDb; Q99436; -.
DR PeptideAtlas; Q99436; -.
DR PRIDE; Q99436; -.
DR ProteomicsDB; 5686; -.
DR ProteomicsDB; 78266; -. [Q99436-1]
DR Antibodypedia; 30460; 330 antibodies from 33 providers.
DR DNASU; 5695; -.
DR Ensembl; ENST00000259457.8; ENSP00000259457.3; ENSG00000136930.13. [Q99436-1]
DR GeneID; 5695; -.
DR KEGG; hsa:5695; -.
DR MANE-Select; ENST00000259457.8; ENSP00000259457.3; NM_002799.4; NP_002790.1.
DR UCSC; uc004boj.5; human. [Q99436-1]
DR CTD; 5695; -.
DR DisGeNET; 5695; -.
DR GeneCards; PSMB7; -.
DR HGNC; HGNC:9544; PSMB7.
DR HPA; ENSG00000136930; Low tissue specificity.
DR MIM; 604030; gene.
DR neXtProt; NX_Q99436; -.
DR OpenTargets; ENSG00000136930; -.
DR PharmGKB; PA33889; -.
DR VEuPathDB; HostDB:ENSG00000136930; -.
DR eggNOG; KOG0173; Eukaryota.
DR GeneTree; ENSGT00940000157419; -.
DR HOGENOM; CLU_035750_3_0_1; -.
DR InParanoid; Q99436; -.
DR OMA; VDKTGPH; -.
DR PhylomeDB; Q99436; -.
DR TreeFam; TF106222; -.
DR PathwayCommons; Q99436; -.
DR Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
DR Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
DR Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
DR Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-HSA-202424; Downstream TCR signaling.
DR Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-HSA-350562; Regulation of ornithine decarboxylase (ODC).
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-HSA-4641257; Degradation of AXIN.
DR Reactome; R-HSA-4641258; Degradation of DVL.
DR Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD.
DR Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
DR Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
DR Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex.
DR Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-HSA-69481; G2/M Checkpoints.
DR Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-HSA-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-HSA-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q99436; -.
DR SIGNOR; Q99436; -.
DR BioGRID-ORCS; 5695; 782 hits in 1049 CRISPR screens.
DR ChiTaRS; PSMB7; human.
DR GeneWiki; PSMB7; -.
DR GenomeRNAi; 5695; -.
DR Pharos; Q99436; Tbio.
DR PRO; PR:Q99436; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q99436; protein.
DR Bgee; ENSG00000136930; Expressed in ganglionic eminence and 204 other tissues.
DR ExpressionAtlas; Q99436; baseline and differential.
DR Genevisible; Q99436; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000502; C:proteasome complex; IDA:UniProtKB.
DR GO; GO:0005839; C:proteasome core complex; IDA:UniProtKB.
DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; ISS:UniProtKB.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IC:ComplexPortal.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000243; Pept_T1A_subB.
DR InterPro; IPR035216; Proteasome_beta7.
DR InterPro; IPR024689; Proteasome_bsu_C.
DR InterPro; IPR016050; Proteasome_bsu_CS.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR023333; Proteasome_suB-type.
DR PANTHER; PTHR11599:SF42; PTHR11599:SF42; 1.
DR Pfam; PF12465; Pr_beta_C; 1.
DR Pfam; PF00227; Proteasome; 1.
DR PRINTS; PR00141; PROTEASOME.
DR SUPFAM; SSF56235; SSF56235; 1.
DR PROSITE; PS00854; PROTEASOME_BETA_1; 1.
DR PROSITE; PS51476; PROTEASOME_BETA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Host-virus interaction; Hydrolase; Nucleus; Protease; Proteasome;
KW Reference proteome; Threonine protease; Zymogen.
FT PROPEP 1..43
FT /note="Removed in mature form"
FT /id="PRO_0000026645"
FT CHAIN 44..277
FT /note="Proteasome subunit beta type-7"
FT /id="PRO_0000026646"
FT ACT_SITE 44
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:25599644,
FT ECO:0000269|PubMed:27493187"
FT VAR_SEQ 133..142
FT /note="YQGYIGAALV -> FWLLGSNGCI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056573"
FT VAR_SEQ 143..277
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056574"
FT VARIANT 39
FT /note="V -> A (in dbSNP:rs4574)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_013292"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:5LE5"
FT HELIX 92..113
FT /evidence="ECO:0007829|PDB:5LE5"
FT HELIX 119..133
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:5A0Q"
FT STRAND 139..147
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:5LE5"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:5A0Q"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:5LE5"
FT HELIX 174..184
FT /evidence="ECO:0007829|PDB:5LE5"
FT HELIX 191..208
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:6HUB"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 225..233
FT /evidence="ECO:0007829|PDB:5LE5"
FT STRAND 254..261
FT /evidence="ECO:0007829|PDB:5LE5"
SQ SEQUENCE 277 AA; 29965 MW; A610C949A0ACF1CE CRC64;
MAAVSVYAPP VGGFSFDNCR RNAVLEADFA KRGYKLPKVR KTGTTIAGVV YKDGIVLGAD
TRATEGMVVA DKNCSKIHFI SPNIYCCGAG TAADTDMTTQ LISSNLELHS LSTGRLPRVV
TANRMLKQML FRYQGYIGAA LVLGGVDVTG PHLYSIYPHG STDKLPYVTM GSGSLAAMAV
FEDKFRPDME EEEAKNLVSE AIAAGIFNDL GSGSNIDLCV ISKNKLDFLR PYTVPNKKGT
RLGRYRCEKG TTAVLTEKIT PLEIEVLEET VQTMDTS
