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Protein

Proteasome subunit beta type-3

Gene

Psmb3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.1 Publication

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

GO - Molecular functioni

  1. endopeptidase activity Source: MGI
  2. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. protein catabolic process Source: MGI
  2. proteolysis involved in cellular protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

ReactomeiREACT_274287. Degradation of beta-catenin by the destruction complex.
REACT_275686. Activation of NF-kappaB in B cells.
REACT_275732. degradation of AXIN.
REACT_278878. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_289441. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_294625. Ubiquitin-dependent degradation of Cyclin D1.
REACT_297888. degradation of DVL.
REACT_299120. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_301078. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_308964. ER-Phagosome pathway.
REACT_310780. Degradation of GLI2 by the proteasome.
REACT_315933. Orc1 removal from chromatin.
REACT_321346. Separation of Sister Chromatids.
REACT_324511. Degradation of GLI1 by the proteasome.
REACT_326233. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_329431. APC/C:Cdc20 mediated degradation of Securin.
REACT_331452. Hh ligand biogenesis disease.
REACT_334737. Regulation of ornithine decarboxylase (ODC).
REACT_336463. CDK-mediated phosphorylation and removal of Cdc6.
REACT_336745. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_337766. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_341044. SCF-beta-TrCP mediated degradation of Emi1.
REACT_341075. ER-Phagosome pathway.
REACT_342086. SCF(Skp2)-mediated degradation of p27/p21.
REACT_342636. Asymmetric localization of PCP proteins.
REACT_343561. CDT1 association with the CDC6:ORC:origin complex.
REACT_343568. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_345193. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_347264. Hedgehog ligand biogenesis.
REACT_351311. Hedgehog 'on' state.
REACT_353777. GLI3 is processed to GLI3R by the proteasome.

Protein family/group databases

MEROPSiT01.983.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-3 (EC:3.4.25.1)
Alternative name(s):
Proteasome chain 13
Proteasome component C10-II
Proteasome theta chain
Gene namesi
Name:Psmb3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1347014. Psmb3.

Subcellular locationi

GO - Cellular componenti

  1. actin cytoskeleton Source: MGI
  2. cytoplasm Source: MGI
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: MGI
  5. Golgi apparatus Source: MGI
  6. mitochondrion Source: MGI
  7. nucleus Source: MGI
  8. proteasome complex Source: MGI
  9. proteasome core complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 205204Proteasome subunit beta type-3PRO_0000148058Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei77 – 771N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9R1P1.
PaxDbiQ9R1P1.
PRIDEiQ9R1P1.

2D gel databases

REPRODUCTION-2DPAGEQ9R1P1.
UCD-2DPAGEQ9R1P1.

PTM databases

PhosphoSiteiQ9R1P1.

Expressioni

Tissue specificityi

Detected in liver (at protein level).1 Publication

Gene expression databases

BgeeiQ9R1P1.
ExpressionAtlasiQ9R1P1. baseline and differential.
GenevestigatoriQ9R1P1.

Interactioni

Subunit structurei

The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel.2 Publications

Protein-protein interaction databases

BioGridi204997. 3 interactions.
IntActiQ9R1P1. 2 interactions.

Structurei

Secondary structure

1
205
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni4 – 74Combined sources
Beta strandi10 – 156Combined sources
Beta strandi20 – 256Combined sources
Beta strandi28 – 303Combined sources
Beta strandi33 – 375Combined sources
Beta strandi42 – 5514Combined sources
Helixi57 – 7721Combined sources
Beta strandi78 – 803Combined sources
Helixi84 – 9613Combined sources
Turni97 – 1004Combined sources
Beta strandi104 – 1129Combined sources
Turni114 – 1163Combined sources
Beta strandi119 – 1235Combined sources
Beta strandi130 – 1323Combined sources
Beta strandi134 – 1407Combined sources
Helixi143 – 15311Combined sources
Helixi160 – 17516Combined sources
Beta strandi178 – 1814Combined sources
Beta strandi185 – 1906Combined sources
Beta strandi192 – 2009Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.90I/W/k/y1-205[»]
3UNEX-ray3.20I/W/k/y1-205[»]
3UNFX-ray2.90I/W1-205[»]
3UNHX-ray3.20I/W1-205[»]
ProteinModelPortaliQ9R1P1.
SMRiQ9R1P1. Positions 2-205.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074820.
HOGENOMiHOG000090523.
HOVERGENiHBG004446.
InParanoidiQ9R1P1.
KOiK02735.
OMAiGCLNFAK.
OrthoDBiEOG783MWB.
PhylomeDBiQ9R1P1.
TreeFamiTF106216.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9R1P1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIMSYNGGA VMAMKGKNCV AIAADRRFGI QAQMVTTDFQ KIFPMGDRLY
60 70 80 90 100
IGLAGLATDV QTVAQRLKFR LNLYELKEGR QIKPYTLMSM VANLLYEKRF
110 120 130 140 150
GPYYTEPVIA GLDPKTFKPF ICSLDLIGCP MVTDDFVVSG TCSEQMYGMC
160 170 180 190 200
ESLWEPNMDP EHLFETISQA MLNAVDRDAV SGMGVIVHVI EKDKITTRTL

KARMD
Length:205
Mass (Da):22,965
Last modified:May 1, 2000 - v1
Checksum:i743DDA584D5045FA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF060092 mRNA. Translation: AAD50537.1.
AK002331 mRNA. Translation: BAB22017.1.
BC014783 mRNA. Translation: AAH14783.1.
CCDSiCCDS25328.1.
RefSeqiNP_036101.1. NM_011971.4.
UniGeneiMm.21874.

Genome annotation databases

EnsembliENSMUST00000103147; ENSMUSP00000099436; ENSMUSG00000069744.
GeneIDi26446.
KEGGimmu:26446.
UCSCiuc007lep.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF060092 mRNA. Translation: AAD50537.1.
AK002331 mRNA. Translation: BAB22017.1.
BC014783 mRNA. Translation: AAH14783.1.
CCDSiCCDS25328.1.
RefSeqiNP_036101.1. NM_011971.4.
UniGeneiMm.21874.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.90I/W/k/y1-205[»]
3UNEX-ray3.20I/W/k/y1-205[»]
3UNFX-ray2.90I/W1-205[»]
3UNHX-ray3.20I/W1-205[»]
ProteinModelPortaliQ9R1P1.
SMRiQ9R1P1. Positions 2-205.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204997. 3 interactions.
IntActiQ9R1P1. 2 interactions.

Protein family/group databases

MEROPSiT01.983.

PTM databases

PhosphoSiteiQ9R1P1.

2D gel databases

REPRODUCTION-2DPAGEQ9R1P1.
UCD-2DPAGEQ9R1P1.

Proteomic databases

MaxQBiQ9R1P1.
PaxDbiQ9R1P1.
PRIDEiQ9R1P1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000103147; ENSMUSP00000099436; ENSMUSG00000069744.
GeneIDi26446.
KEGGimmu:26446.
UCSCiuc007lep.1. mouse.

Organism-specific databases

CTDi5691.
MGIiMGI:1347014. Psmb3.

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074820.
HOGENOMiHOG000090523.
HOVERGENiHBG004446.
InParanoidiQ9R1P1.
KOiK02735.
OMAiGCLNFAK.
OrthoDBiEOG783MWB.
PhylomeDBiQ9R1P1.
TreeFamiTF106216.

Enzyme and pathway databases

ReactomeiREACT_274287. Degradation of beta-catenin by the destruction complex.
REACT_275686. Activation of NF-kappaB in B cells.
REACT_275732. degradation of AXIN.
REACT_278878. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_289441. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_294625. Ubiquitin-dependent degradation of Cyclin D1.
REACT_297888. degradation of DVL.
REACT_299120. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_301078. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_308964. ER-Phagosome pathway.
REACT_310780. Degradation of GLI2 by the proteasome.
REACT_315933. Orc1 removal from chromatin.
REACT_321346. Separation of Sister Chromatids.
REACT_324511. Degradation of GLI1 by the proteasome.
REACT_326233. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_329431. APC/C:Cdc20 mediated degradation of Securin.
REACT_331452. Hh ligand biogenesis disease.
REACT_334737. Regulation of ornithine decarboxylase (ODC).
REACT_336463. CDK-mediated phosphorylation and removal of Cdc6.
REACT_336745. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_337766. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_341044. SCF-beta-TrCP mediated degradation of Emi1.
REACT_341075. ER-Phagosome pathway.
REACT_342086. SCF(Skp2)-mediated degradation of p27/p21.
REACT_342636. Asymmetric localization of PCP proteins.
REACT_343561. CDT1 association with the CDC6:ORC:origin complex.
REACT_343568. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_345193. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_347264. Hedgehog ligand biogenesis.
REACT_351311. Hedgehog 'on' state.
REACT_353777. GLI3 is processed to GLI3R by the proteasome.

Miscellaneous databases

NextBioi304541.
PROiQ9R1P1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9R1P1.
ExpressionAtlasiQ9R1P1. baseline and differential.
GenevestigatoriQ9R1P1.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: B10.BR.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary gland.
  4. Lubec G., Klug S., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 6-14; 49-66; 71-77; 100-115 AND 394-403, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain and Hippocampus.
  5. Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX, ACETYLATION AT SER-2.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-77, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  7. "Immuno- and constitutive proteasome crystal structures reveal differences in substrate and inhibitor specificity."
    Huber E.M., Basler M., Schwab R., Heinemeyer W., Kirk C.J., Groettrup M., Groll M.
    Cell 148:727-738(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 20S IMMUNOPROTEASOME, SUBUNIT, FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiPSB3_MOUSE
AccessioniPrimary (citable) accession number: Q9R1P1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: April 1, 2015
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.