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P28076 (PSB9_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. 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-9

EC=3.4.25.1
Alternative name(s):
LMP-2d
Low molecular mass protein 2
Macropain chain 7
Multicatalytic endopeptidase complex chain 7
Proteasome chain 7
Proteasome subunit beta-1i
Really interesting new gene 12 protein
Gene names
Name:Psmb9
Synonyms:Lmp2, Ring12
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length219 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. This subunit is involved in antigen processing to generate class I binding peptides. Contributes to NFKBIA degradation and subsequently NFKB1 generation. Ref.12 Ref.17

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. Component of the immunoproteasome, where it displaces the equivalent houskeeping subunit PSMB6. Component of the spermatoproteasome, a form of the proteasome specifically found in testis. Interacts with NCOA1, NCOA2 and NCOA3. Ref.15 Ref.16 Ref.17

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Tissue specificity

Detected in liver (at protein level). Expressed at high levels in the thymus, spleen, lung, heart and liver. Expressed at moderate levels in the kidney. Ref.4 Ref.17

Induction

Up-regulated by interferon gamma (at protein level). Up-regulated by IRF1. Up-regulated by heat shock treatment. Down-regulated by EGR1 in neuronal cells. Ref.11 Ref.13 Ref.14

Post-translational modification

Autocleaved. The resulting N-terminal Thr residue of the mature subunit is responsible for the nucleophile proteolytic activity By similarity.

Disruption phenotype

Depletion of LMP2 by RNAi suppresses expression and activities of the matrix metalloproteinase MMP2 and MMP9 by blocking the transfer of active NF-kappa-B heterodimers into the nucleus. Ref.12

Sequence similarities

Belongs to the peptidase T1B family.

Sequence caution

The sequence AAA39439.1 differs from that shown. Reason: Frameshift at positions 10 and 130.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 2020Removed in mature form By similarity
PRO_0000026621
Chain21 – 219199Proteasome subunit beta type-9
PRO_0000026622

Sites

Active site211Nucleophile By similarity
Site20 – 212Cleavage; by autocatalysis By similarity

Amino acid modifications

Modified residue531N6-acetyllysine By similarity
Modified residue1091N6-acetyllysine By similarity

Natural variations

Natural variant601R → H in LMP-2b.
Natural variant1261R → C in LMP-2b.
Natural variant1771N → D in LMP-2b and LMP-2q.

Secondary structure

.................................... 219
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P28076 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 036BC558E770BD3E

FASTA21923,397
        10         20         30         40         50         60 
MLRAGAPTAG SFRTEEVHTG TTIMAVEFDG GVVVGSDSRV SAGTAVVNRV FDKLSPLHQR 

        70         80         90        100        110        120 
IFCALSGSAA DAQAIADMAA YQLELHGLEL EEPPLVLAAA NVVKNISYKY REDLLAHLIV 

       130        140        150        160        170        180 
AGWDQREGGQ VYGTMGGMLI RQPFTIGGSG SSYIYGYVDA AYKPGMTPEE CRRFTTNAIT 

       190        200        210 
LAMNRDGSSG GVIYLVTITA AGVDHRVILG DELPKFYDE 

« Hide

References

« Hide 'large scale' references
[1]"Homology of proteasome subunits to a major histocompatibility complex-linked LMP gene."
Martinez C.K., Monaco J.J.
Nature 353:664-667(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Various strains.
[2]"Genomic organization of the mouse Lmp-2 gene and characteristic structure of its promoter."
Kishi F., Suminami Y., Monaco J.J.
Gene 133:243-248(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NOD.
[3]"Molecular basis of genetic polymorphism in major histocompatibility complex-linked proteasome gene (Lmp-2)."
Zhou P., Cao H., Smart M., David C.
Proc. Natl. Acad. Sci. U.S.A. 90:2681-2684(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LMP-2B AND LMP-2Q.
[4]"Genomic organization and tissue expression of mouse proteasome gene Lmp-2."
Zhou P., Zanelli E., Smart M., David C.
Genomics 16:664-668(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
Strain: BALB/c.
[5]"Molecular and serological analysis of polymorphisms in the murine major histocompatibility complex-encoded proteasome subunits, LMP-2 and LMP-7."
Nandi D., Iyer M.N., Monaco J.J.
Exp. Clin. Immunogenet. 13:20-29(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: B10.RIII, C57BL/6 and R37.
[6]"Genomic organization of a mouse MHC class II region including the H2-M and Lmp2 loci."
Peleraux A., Karlsson L., Chambers J., Peterson P.A.
Immunogenetics 43:204-214(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BALB/c.
[7]Mizuno K., Saitou N., Tsutiya K., Sagai T., Moriwaki K., Shiroishi T.
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Various strains.
Tissue: Spleen.
[8]"Molecular analysis of a recombinational hotspot adjacent to Lmp2 gene in the mouse MHC: fine location and chromatin structure."
Mizuno K., Koide T., Sagai T., Moriwaki K., Shiroishi T.
Mamm. Genome 7:490-496(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: B10.MOL-SGR.
[9]"Sequence of the mouse major histocomaptibility locus class II region."
Rowen L., Qin S., Madan A., Loretz C., James R., Dors M., Mix L., Hall J., Lasky S., Hood L.
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 129/SvJ.
[10]"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: C57BL/6J.
Tissue: Small intestine.
[11]"IRF-1 mediates upregulation of LMP7 by IFN-gamma and concerted expression of immunosubunits of the proteasome."
Namiki S., Nakamura T., Oshima S., Yamazaki M., Sekine Y., Tsuchiya K., Okamoto R., Kanai T., Watanabe M.
FEBS Lett. 579:2781-2787(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY INTERFERON GAMMA AND IRF1.
[12]"Proteasome subunit LMP2 is required for matrix metalloproteinase-2 and -9 expression and activities in human invasive extravillous trophoblast cell line."
Wang H.X., Wang H.M., Lin H.Y., Yang Q., Zhang H., Tsang B.K., Zhu C.
J. Cell. Physiol. 206:616-623(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[13]"Heat shock up-regulates lmp2 and lmp7 and enhances presentation of immunoproteasome-dependent epitopes."
Callahan M.K., Wohlfert E.A., Menoret A., Srivastava P.K.
J. Immunol. 177:8393-8399(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY HEAT SHOCK.
[14]"Regulation of the neuronal proteasome by Zif268 (Egr1)."
James A.B., Conway A.M., Morris B.J.
J. Neurosci. 26:1624-1634(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY EGR1.
[15]"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.
[16]"Acetylation-mediated proteasomal degradation of core histones during DNA repair and spermatogenesis."
Qian M.X., Pang Y., Liu C.H., Haratake K., Du B.Y., Ji D.Y., Wang G.F., Zhu Q.Q., Song W., Yu Y., Zhang X.X., Huang H.T., Miao S., Chen L.B., Zhang Z.H., Liang Y.N., Liu S., Cha H. expand/collapse author list , Yang D., Zhai Y., Komatsu T., Tsuruta F., Li H., Cao C., Li W., Li G.H., Cheng Y., Chiba T., Wang L., Goldberg A.L., Shen Y., Qiu X.B.
Cell 153:1012-1024(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE SPERMATOPROTEASOME.
[17]"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
S59862 mRNA. Translation: AAB20105.1.
U22448 mRNA. Translation: AAA75305.1.
U22447 mRNA. Translation: AAA75304.1.
S58203 mRNA. Translation: AAP13903.1.
L11613 Genomic DNA. Translation: AAA39439.1. Frameshift.
U22919 mRNA. Translation: AAA75306.1.
U22920 mRNA. Translation: AAA75307.1.
U35323 Genomic DNA. Translation: AAA98932.1.
D14566 Genomic DNA. Translation: BAA40680.1.
D44454 mRNA. Translation: BAA22575.1.
D44457 mRNA. Translation: BAA22578.1.
D44458 mRNA. Translation: BAA22579.1.
D44460 mRNA. Translation: BAA22581.1.
D44461 mRNA. Translation: BAA22582.1.
D44462 mRNA. Translation: BAA22583.1.
D43620 Genomic DNA. Translation: BAA19855.1.
AF027865 Genomic DNA. Translation: AAB81528.1.
AF100956 Genomic DNA. Translation: AAC69911.1.
AK008429 mRNA. Translation: BAB25664.1.
CCDSCCDS28642.1.
PIRJC2019.
RefSeqNP_038613.1. NM_013585.2.
UniGeneMm.390983.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3UNFX-ray2.90N/b21-219[»]
3UNHX-ray3.20N/b21-219[»]
ProteinModelPortalP28076.
SMRP28076. Positions 21-219.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP28076. 7 interactions.
MINTMINT-4108888.

Chemistry

ChEMBLCHEMBL1944491.

Protein family/group databases

MEROPST01.013.

PTM databases

PhosphoSiteP28076.

Proteomic databases

PaxDbP28076.
PRIDEP28076.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000174576; ENSMUSP00000133499; ENSMUSG00000096727.
GeneID16912.
KEGGmmu:16912.

Organism-specific databases

CTD5698.
MGIMGI:1346526. Psmb9.

Phylogenomic databases

eggNOGNOG291022.
GeneTreeENSGT00510000046484.
HOGENOMHOG000091079.
HOVERGENHBG000123.
InParanoidP28076.
KOK02741.
OrthoDBEOG79GT80.
PhylomeDBP28076.
TreeFamTF106221.

Gene expression databases

ArrayExpressP28076.
BgeeP28076.
GenevestigatorP28076.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
InterProIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSPR00141. PROTEASOME.
SUPFAMSSF56235. SSF56235. 1 hit.
PROSITEPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio290956.
PROP28076.
SOURCESearch...

Entry information

Entry namePSB9_MOUSE
AccessionPrimary (citable) accession number: P28076
Secondary accession number(s): O09085 expand/collapse secondary AC list , O09151, Q07704, Q60827, Q64278
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: July 9, 2014
This is version 139 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