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P99026 (PSB4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Psmb4
Synonyms:Lmp3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length264 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.10

Catalytic activity

Cleavage of peptide bonds with very broad specificity.

Subunit structure

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. Ref.7 Ref.9 Ref.10

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Tissue specificity

Detected in liver (at protein level). Ref.10

Induction

Up-regulated in liver tumor tissues (at protein level). Ref.8

Sequence similarities

Belongs to the peptidase T1B family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 4545
PRO_0000026581
Chain46 – 264219Proteasome subunit beta type-4
PRO_0000026582

Sites

Active site461Nucleophile By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue1021Phosphotyrosine By similarity

Experimental info

Sequence conflict261A → S in BAE33781. Ref.2
Sequence conflict261A → S in AAH08241. Ref.3
Sequence conflict271T → A in BAE33781. Ref.2
Sequence conflict421P → H in BAE40213. Ref.2
Sequence conflict2151E → G in BAE23215. Ref.2
Sequence conflict2241R → K in BAC36805. Ref.2
Sequence conflict2341I → V in BAE33781. Ref.2

Secondary structure

....................................... 264
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P99026 [UniParc].

Last modified December 15, 1998. Version 1.
Checksum: 6B6B42B21DFA2B74

FASTA26429,116
        10         20         30         40         50         60 
MEAFWESRAG HWAGGPAPGQ FYRIPATPSG LMDPASAPCE GPITRTQNPM VTGTSVLGVK 

        70         80         90        100        110        120 
FDGGVVIAAD MLGSYGSLAR FRNISRIMRV NDSTMLGASG DYADFQYLKQ VLGQMVIDEE 

       130        140        150        160        170        180 
LLGDGHSYSP RAIHSWLTRA MYSRRSKMNP LWNTMVIGGY ADGESFLGYV DMLGVAYEAP 

       190        200        210        220        230        240 
SLATGYGAYL AQPLLREVLE KQPVLSQTEA RELVERCMRV LYYRDARSYN RFQIATVTEK 

       250        260 
GVEIEGPLSA QTNWDIAHMI SGFE 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Sanchez J.-C., Rouge V., Frutiger S., Hughes G., Yan J.X., Hoogland C., Appel R.D., Binz P.-A., Hochstrasser D.F., Cowthorne M.
Submitted (AUG-1998) to UniProtKB
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]"Mapping the murine cardiac 26S proteasome complexes."
Gomes A.V., Zong C., Edmondson R.D., Li X., Stefani E., Zhang J., Jones R.C., Thyparambil S., Wang G.W., Qiao X., Bardag-Gorce F., Ping P.
Circ. Res. 99:362-371(2006) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS17597.1.
RefSeqNP_032971.2. NM_008945.3.
UniGeneMm.368.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP99026.
SMRP99026. Positions 46-261.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202420. 4 interactions.
IntActP99026. 5 interactions.
MINTMINT-1850556.

Protein family/group databases

MEROPST01.987.

PTM databases

PhosphoSiteP99026.

2D gel databases

REPRODUCTION-2DPAGEP99026.
SWISS-2DPAGEP99026.

Proteomic databases

MaxQBP99026.
PaxDbP99026.
PRIDEP99026.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000005923; ENSMUSP00000005923; ENSMUSG00000005779.
GeneID19172.
KEGGmmu:19172.
UCSCuc008qhe.2. mouse.

Organism-specific databases

CTD5692.
MGIMGI:1098257. Psmb4.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00390000000698.
HOVERGENHBG018194.
InParanoidP99026.
KOK02736.
OMARIMRVND.
OrthoDBEOG74FF1D.
PhylomeDBP99026.
TreeFamTF106220.

Gene expression databases

BgeeP99026.
GenevestigatorP99026.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
InterProIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR016295. Proteasome_endopept_cplx_B.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
[Graphical view]
PIRSFPIRSF001213. Psome_endopept_beta. 1 hit.
SUPFAMSSF56235. SSF56235. 1 hit.
PROSITEPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPSMB4. mouse.
NextBio295846.
PROP99026.
SOURCESearch...

Entry information

Entry namePSB4_MOUSE
AccessionPrimary (citable) accession number: P99026
Secondary accession number(s): Q3THC0 expand/collapse secondary AC list , Q3THI3, Q3U0S0, Q3UVQ4, Q62008, Q8BK27, Q91VV7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: July 9, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot