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Proteasome subunit beta type-7 (EC 3.4.25.1) (Macropain chain Z) (Multicatalytic endopeptidase complex chain Z) (Proteasome subunit Z)

 PSB7_HUMAN              Reviewed;         277 AA.
Q99436; B4E0P1; Q5TBG6; Q96AG8; Q9BWA7;
18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
12-SEP-2018, entry version 190.
RecName: Full=Proteasome subunit beta type-7;
EC=3.4.25.1 {ECO:0000269|PubMed:27176742};
AltName: Full=Macropain chain Z;
AltName: Full=Multicatalytic endopeptidase complex chain Z;
AltName: Full=Proteasome subunit Z;
Flags: Precursor;
Name=PSMB7; Synonyms=Z;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8666937; DOI=10.1084/jem.183.4.1807;
Hisamatsu H., Shimbara N., Saito Y., Kristensen P., Hendil K.B.,
Fujiwara T., Takahashi E., Tanahashi N., Tamura T., Ichihara A.,
Tanaka K.;
"Newly identified pair of proteasomal subunits regulated reciprocally
by interferon gamma.";
J. Exp. Med. 183:1807-1816(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ALA-39.
TISSUE=Lung, Urinary bladder, and Uterus;
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).
[6]
PROTEIN SEQUENCE OF 165-184 AND 259-277, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[7]
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).
[8]
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).
[9]
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).
[10]
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).
[11]
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).
[12]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=18549262; DOI=10.1021/pr8000892;
Rho J.H., Qin S., Wang J.Y., Roehrl M.H.;
"Proteomic expression analysis of surgical human colorectal cancer
tissues: up-regulation of PSB7, PRDX1, and SRP9 and hypoxic adaptation
in cancer.";
J. Proteome Res. 7:2959-2972(2008).
[13]
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).
[14]
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).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
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).
[17]
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).
[18]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS), SUBUNIT, AND ACTIVE SITE.
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).
[19]
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).
[20]
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).
[21]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), SUBUNIT, AND ACTIVE SITE.
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).
-!- 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). Within the 20S core complex, PSMB7 displays a
trypsin-like activity. {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:27342858,
ECO:0000269|PubMed:27428775, ECO:0000269|PubMed:27493187}.
-!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Tat protein.
{ECO:0000269|PubMed:14550573}.
-!- INTERACTION:
P20618:PSMB1; NbExp=8; IntAct=EBI-603319, EBI-372273;
P28074:PSMB5; NbExp=7; IntAct=EBI-603319, EBI-357828;
P28065:PSMB9; NbExp=5; IntAct=EBI-603319, EBI-603300;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12181345,
ECO:0000269|PubMed:18549262}. Nucleus
{ECO:0000269|PubMed:12181345, ECO:0000269|PubMed:18549262}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q99436-1; Sequence=Displayed;
Name=2;
IsoId=Q99436-2; Sequence=VSP_056573, VSP_056574;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed at a low level in colonic mucosa.
Up-regulated in colorectal cancer tissues.
{ECO:0000269|PubMed:18549262}.
-!- SIMILARITY: Belongs to the peptidase T1B family.
{ECO:0000255|PROSITE-ProRule:PRU00809}.
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EMBL; D38048; BAA07238.1; -; mRNA.
EMBL; AK303460; BAG64503.1; -; mRNA.
EMBL; AL137846; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471090; EAW87582.1; -; Genomic_DNA.
EMBL; CH471090; EAW87583.1; -; Genomic_DNA.
EMBL; BC000509; AAH00509.1; -; mRNA.
EMBL; BC008414; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC017116; AAH17116.2; -; mRNA.
CCDS; CCDS6855.1; -. [Q99436-1]
RefSeq; NP_002790.1; NM_002799.3. [Q99436-1]
UniGene; Hs.213470; -.
PDB; 4R3O; X-ray; 2.60 A; I/W=44-263.
PDB; 4R67; X-ray; 2.89 A; I/W/k/y=44-263.
PDB; 5A0Q; EM; 3.50 A; I/W=44-277.
PDB; 5GJQ; EM; 4.50 A; b/p=1-277.
PDB; 5GJR; EM; 3.50 A; b/p=1-277.
PDB; 5L4G; EM; 4.02 A; 7/8=1-277.
PDB; 5LE5; X-ray; 1.80 A; H/V=44-277.
PDB; 5LEX; X-ray; 2.20 A; H/V=44-277.
PDB; 5LEY; X-ray; 1.90 A; H/V=44-277.
PDB; 5LEZ; X-ray; 2.19 A; H/V=44-277.
PDB; 5LF0; X-ray; 2.41 A; H/V=44-277.
PDB; 5LF1; X-ray; 2.00 A; H/V=44-277.
PDB; 5LF3; X-ray; 2.10 A; H/V=44-277.
PDB; 5LF4; X-ray; 1.99 A; H/V=44-277.
PDB; 5LF6; X-ray; 2.07 A; H/V=44-277.
PDB; 5LF7; X-ray; 2.00 A; H/V=44-277.
PDB; 5LN3; EM; 6.80 A; 2=1-277.
PDB; 5M32; EM; 3.80 A; H/V=1-277.
PDB; 5T0C; EM; 3.80 A; AO/BO=2-277.
PDB; 5T0G; EM; 4.40 A; O=2-277.
PDB; 5T0H; EM; 6.80 A; O=2-277.
PDB; 5T0I; EM; 8.00 A; O=2-277.
PDB; 5T0J; EM; 8.00 A; O=2-277.
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; -.
ProteinModelPortal; Q99436; -.
SMR; Q99436; -.
BioGrid; 111668; 86.
CORUM; Q99436; -.
DIP; DIP-33843N; -.
IntAct; Q99436; 31.
MINT; Q99436; -.
STRING; 9606.ENSP00000259457; -.
BindingDB; Q99436; -.
ChEMBL; CHEMBL3347256; -.
MEROPS; T01.011; -.
iPTMnet; Q99436; -.
PhosphoSitePlus; Q99436; -.
BioMuta; PSMB7; -.
DMDM; 17380263; -.
EPD; Q99436; -.
MaxQB; Q99436; -.
PaxDb; Q99436; -.
PeptideAtlas; Q99436; -.
PRIDE; Q99436; -.
ProteomicsDB; 78266; -.
DNASU; 5695; -.
Ensembl; ENST00000259457; ENSP00000259457; ENSG00000136930. [Q99436-1]
GeneID; 5695; -.
KEGG; hsa:5695; -.
UCSC; uc004boj.5; human. [Q99436-1]
CTD; 5695; -.
DisGeNET; 5695; -.
EuPathDB; HostDB:ENSG00000136930.12; -.
GeneCards; PSMB7; -.
HGNC; HGNC:9544; PSMB7.
HPA; HPA052408; -.
HPA; HPA054902; -.
MIM; 604030; gene.
neXtProt; NX_Q99436; -.
OpenTargets; ENSG00000136930; -.
PharmGKB; PA33889; -.
eggNOG; KOG0173; Eukaryota.
eggNOG; COG0638; LUCA.
GeneTree; ENSGT00510000046533; -.
HOGENOM; HOG000182856; -.
HOVERGEN; HBG093416; -.
InParanoid; Q99436; -.
KO; K02739; -.
OMA; DLCVIRK; -.
OrthoDB; EOG091G0E5S; -.
PhylomeDB; Q99436; -.
TreeFam; TF106222; -.
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-6798695; Neutrophil degranulation.
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; PSMB7; human.
GeneWiki; PSMB7; -.
GenomeRNAi; 5695; -.
PRO; PR:Q99436; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000136930; Expressed in 232 organ(s), highest expression level in female gonad.
CleanEx; HS_PSMB7; -.
ExpressionAtlas; Q99436; baseline and differential.
Genevisible; Q99436; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
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:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
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:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 3.60.20.10; -; 1.
InterPro; IPR029055; Ntn_hydrolases_N.
InterPro; IPR000243; Pept_T1A_subB.
InterPro; IPR035216; Proteasome_beta7.
InterPro; IPR024689; Proteasome_bsu_C.
InterPro; IPR016050; Proteasome_bsu_CS.
InterPro; IPR001353; Proteasome_sua/b.
InterPro; IPR023333; Proteasome_suB-type.
PANTHER; PTHR11599:SF42; PTHR11599:SF42; 1.
Pfam; PF12465; Pr_beta_C; 1.
Pfam; PF00227; Proteasome; 1.
PRINTS; PR00141; PROTEASOME.
SUPFAM; SSF56235; SSF56235; 1.
PROSITE; PS00854; PROTEASOME_BETA_1; 1.
PROSITE; PS51476; PROTEASOME_BETA_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Host-virus interaction; Hydrolase; Nucleus;
Polymorphism; Protease; Proteasome; Reference proteome;
Threonine protease; Zymogen.
PROPEP 1 43 Removed in mature form.
/FTId=PRO_0000026645.
CHAIN 44 277 Proteasome subunit beta type-7.
/FTId=PRO_0000026646.
ACT_SITE 44 44 Nucleophile.
{ECO:0000269|PubMed:25599644,
ECO:0000269|PubMed:27493187}.
VAR_SEQ 133 142 YQGYIGAALV -> FWLLGSNGCI (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056573.
VAR_SEQ 143 277 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056574.
VARIANT 39 39 V -> A (in dbSNP:rs4574).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_013292.
STRAND 46 51 {ECO:0000244|PDB:5LE5}.
STRAND 54 60 {ECO:0000244|PDB:5LE5}.
STRAND 63 65 {ECO:0000244|PDB:5LE5}.
STRAND 68 73 {ECO:0000244|PDB:5LE5}.
STRAND 77 81 {ECO:0000244|PDB:5LE5}.
STRAND 84 91 {ECO:0000244|PDB:5LE5}.
HELIX 92 113 {ECO:0000244|PDB:5LE5}.
HELIX 119 133 {ECO:0000244|PDB:5LE5}.
STRAND 135 137 {ECO:0000244|PDB:5A0Q}.
STRAND 139 147 {ECO:0000244|PDB:5LE5}.
STRAND 150 156 {ECO:0000244|PDB:5LE5}.
TURN 158 160 {ECO:0000244|PDB:5A0Q}.
STRAND 162 164 {ECO:0000244|PDB:5LE5}.
STRAND 166 171 {ECO:0000244|PDB:5LE5}.
HELIX 174 184 {ECO:0000244|PDB:5LE5}.
HELIX 191 208 {ECO:0000244|PDB:5LE5}.
STRAND 216 222 {ECO:0000244|PDB:5LE5}.
STRAND 225 233 {ECO:0000244|PDB:5LE5}.
STRAND 254 261 {ECO:0000244|PDB:5LE5}.
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


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