Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Proteasome subunit beta type-9

Gene

Psmb9

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. This subunit is involved in antigen processing to generate class I binding peptides. Contributes to NFKBIA degradation and subsequently NFKB1 generation.2 Publications

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei20 – 212Cleavage; by autolysisBy similarity
Active sitei21 – 211NucleophileBy similarity

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Keywords - Biological processi

Immunity

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

MEROPSiT01.013.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Psmb9
Synonyms:Lmp2, Ring12
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1346526. Psmb9.

Subcellular locationi

Cytoplasm PROSITE-ProRule annotation. Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: MGI
  4. nucleus Source: UniProtKB-SubCell
  5. proteasome core complex Source: UniProtKB
  6. spermatoproteasome complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 2020Removed in mature formBy similarityPRO_0000026621Add
BLAST
Chaini21 – 219199Proteasome subunit beta type-9PRO_0000026622Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 531N6-acetyllysineBy similarity
Modified residuei109 – 1091N6-acetyllysineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Zymogen

Proteomic databases

MaxQBiP28076.
PaxDbiP28076.
PRIDEiP28076.

PTM databases

PhosphoSiteiP28076.

Expressioni

Tissue specificityi

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.2 Publications

Inductioni

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.3 Publications

Gene expression databases

BgeeiP28076.
ExpressionAtlasiP28076. baseline and differential.
GenevestigatoriP28076.

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. 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 NCOA3.3 Publications

Protein-protein interaction databases

IntActiP28076. 7 interactions.
MINTiMINT-4108888.

Structurei

Secondary structure

1
219
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 276Combined sources
Beta strandi32 – 365Combined sources
Beta strandi40 – 423Combined sources
Beta strandi45 – 506Combined sources
Beta strandi54 – 585Combined sources
Beta strandi61 – 655Combined sources
Helixi69 – 8921Combined sources
Helixi96 – 10914Combined sources
Turni110 – 1134Combined sources
Beta strandi118 – 1247Combined sources
Turni125 – 1273Combined sources
Beta strandi128 – 1336Combined sources
Helixi135 – 1373Combined sources
Beta strandi143 – 1486Combined sources
Helixi149 – 1546Combined sources
Helixi155 – 1617Combined sources
Helixi168 – 18518Combined sources
Beta strandi193 – 1986Combined sources
Beta strandi203 – 2086Combined sources
Helixi210 – 2123Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UNFX-ray2.90N/b21-219[»]
3UNHX-ray3.20N/b21-219[»]
ProteinModelPortaliP28076.
SMRiP28076. Positions 21-219.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG291022.
HOGENOMiHOG000091079.
HOVERGENiHBG000123.
InParanoidiP28076.
KOiK02741.
OrthoDBiEOG79GT80.
PhylomeDBiP28076.
TreeFamiTF106221.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
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.

P28076-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRAGAPTAG SFRTEEVHTG TTIMAVEFDG GVVVGSDSRV SAGTAVVNRV
60 70 80 90 100
FDKLSPLHQR IFCALSGSAA DAQAIADMAA YQLELHGLEL EEPPLVLAAA
110 120 130 140 150
NVVKNISYKY REDLLAHLIV AGWDQREGGQ VYGTMGGMLI RQPFTIGGSG
160 170 180 190 200
SSYIYGYVDA AYKPGMTPEE CRRFTTNAIT LAMNRDGSSG GVIYLVTITA
210
AGVDHRVILG DELPKFYDE
Length:219
Mass (Da):23,397
Last modified:August 1, 1992 - v1
Checksum:i036BC558E770BD3E
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti60 – 601R → H in LMP-2b.
Natural varianti126 – 1261R → C in LMP-2b.
Natural varianti177 – 1771N → D in LMP-2b and LMP-2q.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS28642.1.
PIRiJC2019.
RefSeqiNP_038613.1. NM_013585.2.
UniGeneiMm.390983.

Genome annotation databases

GeneIDi16912.
KEGGimmu:16912.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS28642.1.
PIRiJC2019.
RefSeqiNP_038613.1. NM_013585.2.
UniGeneiMm.390983.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UNFX-ray2.90N/b21-219[»]
3UNHX-ray3.20N/b21-219[»]
ProteinModelPortaliP28076.
SMRiP28076. Positions 21-219.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP28076. 7 interactions.
MINTiMINT-4108888.

Chemistry

ChEMBLiCHEMBL1944491.

Protein family/group databases

MEROPSiT01.013.

PTM databases

PhosphoSiteiP28076.

Proteomic databases

MaxQBiP28076.
PaxDbiP28076.
PRIDEiP28076.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi16912.
KEGGimmu:16912.

Organism-specific databases

CTDi5698.
MGIiMGI:1346526. Psmb9.

Phylogenomic databases

eggNOGiNOG291022.
HOGENOMiHOG000091079.
HOVERGENiHBG000123.
InParanoidiP28076.
KOiK02741.
OrthoDBiEOG79GT80.
PhylomeDBiP28076.
TreeFamiTF106221.

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

NextBioi290956.
PROiP28076.
SOURCEiSearch...

Gene expression databases

BgeeiP28076.
ExpressionAtlasiP28076. baseline and differential.
GenevestigatoriP28076.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
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. "Homology of proteasome subunits to a major histocompatibility complex-linked LMP gene."
    Martinez C.K., Monaco J.J.
    Nature 353:664-667(1990) [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(1992) [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(1992) [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(1992) [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(1995) [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(1995) [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 (SEP-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(1995) [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 (SEP-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.
    , 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(2004) [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(2004) [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(2005) [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(2005) [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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY EGR1.
  15. Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.
  16. 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(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 20S IMMUNOPROTEASOME, SUBUNIT, FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiPSB9_MOUSE
AccessioniPrimary (citable) accession number: P28076
Secondary accession number(s): O09085
, O09151, Q07704, Q60827, Q64278
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: April 1, 2015
This is version 147 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, 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.