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P99026

- PSB4_MOUSE

UniProt

P99026 - PSB4_MOUSE

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Protein

Proteasome subunit beta type-4

Gene

Psmb4

Organism
Mus musculus (Mouse)
Status
Reviewed - 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. Mediates the lipopolysaccharide-induced signal macrophage proteasome. SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1 (By similarity).By similarity

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei46 – 461NucleophileBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. negative regulation of inflammatory response to antigenic stimulus Source: UniProtKB
  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_197102. ER-Phagosome pathway.
REACT_198693. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_199105. ER-Phagosome pathway.
REACT_199114. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_199121. Activation of NF-kappaB in B cells.
REACT_203517. SCF-beta-TrCP mediated degradation of Emi1.
REACT_203973. Asymmetric localization of PCP proteins.
REACT_207679. Separation of Sister Chromatids.
REACT_212633. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_218318. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_219129. degradation of AXIN.
REACT_219897. APC/C:Cdc20 mediated degradation of Securin.
REACT_220647. SCF(Skp2)-mediated degradation of p27/p21.
REACT_225686. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_227429. degradation of DVL.

Protein family/group databases

MEROPSiT01.987.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-4 (EC:3.4.25.1)
Alternative name(s):
Low molecular mass protein 3
Macropain beta chain
Multicatalytic endopeptidase complex beta chain
Proteasome beta chain
Proteasome chain 3
Gene namesi
Name:Psmb4
Synonyms:Lmp3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:1098257. Psmb4.

Subcellular locationi

Cytoplasm PROSITE-ProRule annotation. Nucleus By similarity

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: Ensembl
  3. nucleus Source: UniProtKB-KW
  4. proteasome core complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 45452 PublicationsPRO_0000026581Add
BLAST
Chaini46 – 264219Proteasome subunit beta type-4PRO_0000026582Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei102 – 1021PhosphotyrosineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Zymogen

Proteomic databases

MaxQBiP99026.
PaxDbiP99026.
PRIDEiP99026.

2D gel databases

REPRODUCTION-2DPAGEP99026.
SWISS-2DPAGEP99026.

PTM databases

PhosphoSiteiP99026.

Expressioni

Tissue specificityi

Detected in liver (at protein level).1 Publication

Inductioni

Up-regulated in liver tumor tissues (at protein level).1 Publication

Gene expression databases

BgeeiP99026.
GenevestigatoriP99026.

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. Interacts with bacterial lipopolysaccharide (LPS). Forms a ternary complex with SMAD1 and OAZ1 before PSMB4 is incorporated into the 20S proteasome. Interacts with PRPF19.3 Publications

Protein-protein interaction databases

BioGridi202420. 4 interactions.
IntActiP99026. 5 interactions.
MINTiMINT-1850556.

Structurei

Secondary structure

1
264
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi51 – 533
Beta strandi56 – 616
Beta strandi64 – 707
Beta strandi73 – 753
Beta strandi78 – 836
Beta strandi87 – 893
Beta strandi91 – 10111
Helixi102 – 12221
Helixi130 – 14617
Beta strandi153 – 1619
Beta strandi164 – 1707
Beta strandi172 – 1743
Beta strandi176 – 1783
Beta strandi180 – 1834
Helixi187 – 20115
Helixi207 – 22418
Beta strandi232 – 2376
Beta strandi242 – 2487
Helixi255 – 2573
Turni258 – 2603

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.903/M/a/o46-264[»]
3UNEX-ray3.203/M/a/o46-264[»]
3UNFX-ray2.90M/a46-264[»]
3UNHX-ray3.20M/a46-264[»]
ProteinModelPortaliP99026.
SMRiP99026. Positions 46-261.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00390000000698.
HOVERGENiHBG018194.
InParanoidiP99026.
KOiK02736.
OMAiRIMRVND.
OrthoDBiEOG74FF1D.
PhylomeDBiP99026.
TreeFamiTF106220.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR016295. Proteasome_endopept_cplx_B.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PIRSFiPIRSF001213. Psome_endopept_beta. 1 hit.
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.

P99026-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEAFWESRAG HWAGGPAPGQ FYRIPATPSG LMDPASAPCE GPITRTQNPM
60 70 80 90 100
VTGTSVLGVK FDGGVVIAAD MLGSYGSLAR FRNISRIMRV NDSTMLGASG
110 120 130 140 150
DYADFQYLKQ VLGQMVIDEE LLGDGHSYSP RAIHSWLTRA MYSRRSKMNP
160 170 180 190 200
LWNTMVIGGY ADGESFLGYV DMLGVAYEAP SLATGYGAYL AQPLLREVLE
210 220 230 240 250
KQPVLSQTEA RELVERCMRV LYYRDARSYN RFQIATVTEK GVEIEGPLSA
260
QTNWDIAHMI SGFE
Length:264
Mass (Da):29,116
Last modified:December 15, 1998 - v1
Checksum:i6B6B42B21DFA2B74
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261A → S in BAE33781. (PubMed:16141072)Curated
Sequence conflicti26 – 261A → S in AAH08241. (PubMed:15489334)Curated
Sequence conflicti27 – 271T → A in BAE33781. (PubMed:16141072)Curated
Sequence conflicti42 – 421P → H in BAE40213. (PubMed:16141072)Curated
Sequence conflicti215 – 2151E → G in BAE23215. (PubMed:16141072)Curated
Sequence conflicti224 – 2241R → K in BAC36805. (PubMed:16141072)Curated
Sequence conflicti234 – 2341I → V in BAE33781. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U65636 mRNA. Translation: AAC53263.1.
AK077448 mRNA. Translation: BAC36805.1.
AK137044 mRNA. Translation: BAE23215.1.
AK156624 mRNA. Translation: BAE33781.1.
AK168265 mRNA. Translation: BAE40213.1.
AK168340 mRNA. Translation: BAE40277.1.
BC008241 mRNA. Translation: AAH08241.1.
M74556 mRNA. Translation: AAA39863.1.
CCDSiCCDS17597.1.
RefSeqiNP_032971.2. NM_008945.3.
UniGeneiMm.368.

Genome annotation databases

EnsembliENSMUST00000005923; ENSMUSP00000005923; ENSMUSG00000005779.
GeneIDi19172.
KEGGimmu:19172.
UCSCiuc008qhe.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U65636 mRNA. Translation: AAC53263.1 .
AK077448 mRNA. Translation: BAC36805.1 .
AK137044 mRNA. Translation: BAE23215.1 .
AK156624 mRNA. Translation: BAE33781.1 .
AK168265 mRNA. Translation: BAE40213.1 .
AK168340 mRNA. Translation: BAE40277.1 .
BC008241 mRNA. Translation: AAH08241.1 .
M74556 mRNA. Translation: AAA39863.1 .
CCDSi CCDS17597.1.
RefSeqi NP_032971.2. NM_008945.3.
UniGenei Mm.368.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3UNB X-ray 2.90 3/M/a/o 46-264 [» ]
3UNE X-ray 3.20 3/M/a/o 46-264 [» ]
3UNF X-ray 2.90 M/a 46-264 [» ]
3UNH X-ray 3.20 M/a 46-264 [» ]
ProteinModelPortali P99026.
SMRi P99026. Positions 46-261.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202420. 4 interactions.
IntActi P99026. 5 interactions.
MINTi MINT-1850556.

Protein family/group databases

MEROPSi T01.987.

PTM databases

PhosphoSitei P99026.

2D gel databases

REPRODUCTION-2DPAGE P99026.
SWISS-2DPAGE P99026.

Proteomic databases

MaxQBi P99026.
PaxDbi P99026.
PRIDEi P99026.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000005923 ; ENSMUSP00000005923 ; ENSMUSG00000005779 .
GeneIDi 19172.
KEGGi mmu:19172.
UCSCi uc008qhe.2. mouse.

Organism-specific databases

CTDi 5692.
MGIi MGI:1098257. Psmb4.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00390000000698.
HOVERGENi HBG018194.
InParanoidi P99026.
KOi K02736.
OMAi RIMRVND.
OrthoDBi EOG74FF1D.
PhylomeDBi P99026.
TreeFami TF106220.

Enzyme and pathway databases

Reactomei REACT_197102. ER-Phagosome pathway.
REACT_198693. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_199105. ER-Phagosome pathway.
REACT_199114. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_199121. Activation of NF-kappaB in B cells.
REACT_203517. SCF-beta-TrCP mediated degradation of Emi1.
REACT_203973. Asymmetric localization of PCP proteins.
REACT_207679. Separation of Sister Chromatids.
REACT_212633. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_218318. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_219129. degradation of AXIN.
REACT_219897. APC/C:Cdc20 mediated degradation of Securin.
REACT_220647. SCF(Skp2)-mediated degradation of p27/p21.
REACT_225686. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_227429. degradation of DVL.

Miscellaneous databases

ChiTaRSi PSMB4. mouse.
NextBioi 295846.
PROi P99026.
SOURCEi Search...

Gene expression databases

Bgeei P99026.
Genevestigatori P99026.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR016295. Proteasome_endopept_cplx_B.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
[Graphical view ]
PIRSFi PIRSF001213. Psome_endopept_beta. 1 hit.
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of mouse Lmp3 cDNA, encoding a proteasome beta subunit."
    Cruz M., Nandi D., Hendil K.B., Monaco J.J.
    Gene 190:251-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: B10.A.
    Tissue: Macrophage.
  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: BALB/c, C57BL/6J and NOD.
    Tissue: Spleen.
  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: NMRI.
    Tissue: Mammary tumor.
  4. Lubec G., Klug S., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 46-80; 110-131 AND 232-240, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain and Hippocampus.
  5. Cited for: PROTEIN SEQUENCE OF 46-51.
    Tissue: Liver.
  6. Wang B., Hunsperger J., Laib J., Fan D.
    Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 95-112.
    Strain: C57BL/6.
  7. "The proteasome as a lipopolysaccharide-binding protein in macrophages: differential effects of proteasome inhibition on lipopolysaccharide-induced signaling events."
    Qureshi N., Perera P.-Y., Shen J., Zhang G., Lenschat A., Splitter G., Morrison D.C., Vogel S.N.
    J. Immunol. 171:1515-1525(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH LPS.
  8. "The up-regulation of proteasome subunits and lysosomal proteases in hepatocellular carcinomas of the HBx gene knockin transgenic mice."
    Cui F., Wang Y., Wang J., Wei K., Hu J., Liu F., Wang H., Zhao X., Zhang X., Yang X.
    Proteomics 6:498-504(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
  9. Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.
  10. "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 nameiPSB4_MOUSE
AccessioniPrimary (citable) accession number: P99026
Secondary accession number(s): Q3THC0
, Q3THI3, Q3U0S0, Q3UVQ4, Q62008, Q8BK27, Q91VV7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: October 29, 2014
This is version 127 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