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P28076

- PSB9_MOUSE

UniProt

P28076 - PSB9_MOUSE

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Protein

Proteasome subunit beta type-9

Gene

Psmb9

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. 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 autocatalysisBy 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_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

MEROPSiT01.013.

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: Chromosome 17

Organism-specific databases

MGIiMGI:1346526. Psmb9.

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
  5. 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).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 – 276
Beta strandi32 – 365
Beta strandi40 – 423
Beta strandi45 – 506
Beta strandi54 – 585
Beta strandi61 – 655
Helixi69 – 8921
Helixi96 – 10914
Turni110 – 1134
Beta strandi118 – 1247
Turni125 – 1273
Beta strandi128 – 1336
Helixi135 – 1373
Beta strandi143 – 1486
Helixi149 – 1546
Helixi155 – 1617
Helixi168 – 18518
Beta strandi193 – 1986
Beta strandi203 – 2086
Helixi210 – 2123

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
GeneTreeiENSGT00510000046484.
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.

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:
EMBL
GenBank
DDBJ
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

EnsembliENSMUST00000174576; ENSMUSP00000133499; ENSMUSG00000096727.
GeneIDi16912.
KEGGimmu:16912.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS28642.1.
PIRi JC2019.
RefSeqi NP_038613.1. NM_013585.2.
UniGenei Mm.390983.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3UNF X-ray 2.90 N/b 21-219 [» ]
3UNH X-ray 3.20 N/b 21-219 [» ]
ProteinModelPortali P28076.
SMRi P28076. Positions 21-219.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P28076. 7 interactions.
MINTi MINT-4108888.

Chemistry

ChEMBLi CHEMBL1944491.

Protein family/group databases

MEROPSi T01.013.

PTM databases

PhosphoSitei P28076.

Proteomic databases

MaxQBi P28076.
PaxDbi P28076.
PRIDEi P28076.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000174576 ; ENSMUSP00000133499 ; ENSMUSG00000096727 .
GeneIDi 16912.
KEGGi mmu:16912.

Organism-specific databases

CTDi 5698.
MGIi MGI:1346526. Psmb9.

Phylogenomic databases

eggNOGi NOG291022.
GeneTreei ENSGT00510000046484.
HOGENOMi HOG000091079.
HOVERGENi HBG000123.
InParanoidi P28076.
KOi K02741.
OrthoDBi EOG79GT80.
PhylomeDBi P28076.
TreeFami TF106221.

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

NextBioi 290956.
PROi P28076.
SOURCEi Search...

Gene expression databases

Bgeei P28076.
ExpressionAtlasi P28076. baseline and differential.
Genevestigatori P28076.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view ]
Pfami PF00227. Proteasome. 1 hit.
[Graphical view ]
PRINTSi PR00141. PROTEASOME.
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. "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.
    , 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. 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(2012) [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: October 29, 2014
This is version 142 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