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P28063

- PSB8_MOUSE

UniProt

P28063 - PSB8_MOUSE

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Protein

Proteasome subunit beta type-8

Gene

Psmb8

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. May be involved in the inflammatory response pathway. Required for adipocyte differentiation.3 Publications

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei72 – 732Cleavage; by autocatalysis
Active sitei73 – 731Nucleophile1 Publication

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Keywords - Biological processi

Differentiation, 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_203336. Degradation of beta-catenin by the destruction complex.
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.
REACT_232069. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_232469. Hh ligand biogenesis disease.
REACT_233316. Hedgehog ligand biogenesis.
REACT_234963. Regulation of ornithine decarboxylase (ODC).
REACT_244558. CDT1 association with the CDC6:ORC:origin complex.
REACT_245230. Orc1 removal from chromatin.
REACT_249922. CDK-mediated phosphorylation and removal of Cdc6.
REACT_263467. Ubiquitin-dependent degradation of Cyclin D1.
REACT_268522. GLI3 is processed to GLI3R by the proteasome.
REACT_268705. Degradation of GLI1 by the proteasome.
REACT_270923. Degradation of GLI2 by the proteasome.

Protein family/group databases

MEROPSiT01.015.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-8 (EC:3.4.25.1)
Alternative name(s):
Low molecular mass protein 7
Macropain subunit C13
Multicatalytic endopeptidase complex subunit C13
Proteasome component C13
Proteasome subunit beta-5i
Gene namesi
Name:Psmb8
Synonyms:Lmp7, Mc13
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:1346527. Psmb8.

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 7272Removed in mature formBy similarityPRO_0000026599Add
BLAST
Chaini73 – 276204Proteasome subunit beta type-8PRO_0000026600Add
BLAST

Post-translational modificationi

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

Keywords - PTMi

Zymogen

Proteomic databases

MaxQBiP28063.
PaxDbiP28063.
PRIDEiP28063.

PTM databases

PhosphoSiteiP28063.

Expressioni

Tissue specificityi

Detected in liver (at protein level). Expressed in spleen, thymus, lung, liver, heart and, at a very low level, in kidney. Not expressed in brain nor testis.2 Publications

Inductioni

Up-regulated by interferon gamma (at protein level). Up-regulated by IRF1. Down-regulated in spleen by deoxynivalenol (DON), a mycotoxin that alters immune functions. Down-regulated by the selective inhibitor PR-957. Up-regulated by heat shock treatment. Down-regulated by EGR1 in neuronal cells.5 Publications

Gene expression databases

BgeeiP28063.
ExpressionAtlasiP28063. baseline and differential.
GenevestigatoriP28063.

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 housekeeping subunit PSMB5. Component of the spermatoproteasome, a form of the proteasome specifically found in testis. Directly interacts with POMP. Interacts with TAP1.3 Publications

Protein-protein interaction databases

IntActiP28063. 4 interactions.
MINTiMINT-1856641.

Structurei

Secondary structure

1
276
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi74 – 807Combined sources
Beta strandi83 – 886Combined sources
Beta strandi92 – 943Combined sources
Beta strandi97 – 1026Combined sources
Beta strandi106 – 1083Combined sources
Beta strandi113 – 1164Combined sources
Helixi121 – 14222Combined sources
Helixi148 – 16114Combined sources
Turni162 – 1643Combined sources
Beta strandi171 – 1777Combined sources
Beta strandi180 – 1867Combined sources
Beta strandi188 – 1903Combined sources
Beta strandi192 – 1943Combined sources
Beta strandi196 – 2016Combined sources
Helixi204 – 2129Combined sources
Helixi221 – 23818Combined sources
Beta strandi244 – 2529Combined sources
Beta strandi255 – 2639Combined sources
Helixi264 – 2718Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UNFX-ray2.90K/Y73-276[»]
3UNHX-ray3.20K/Y73-276[»]
ProteinModelPortaliP28063.
SMRiP28063. Positions 73-273.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00510000046395.
HOGENOMiHOG000091082.
HOVERGENiHBG108297.
InParanoidiP28063.
KOiK02740.
OMAiSDLMHQY.
PhylomeDBiP28063.
TreeFamiTF106223.

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.

P28063-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALLDLCGAA RGQRPEWAAL DAGSGGRSDP GHYSFSAQAP ELALPRGMQP
60 70 80 90 100
TAFLRSFGGD QERNVQIEMA HGTTTLAFKF QHGVIVAVDS RATAGSYISS
110 120 130 140 150
LRMNKVIEIN PYLLGTMSGC AADCQYWERL LAKECRLYYL RNGERISVSA
160 170 180 190 200
ASKLLSNMML QYRGMGLSMG SMICGWDKKG PGLYYVDDNG TRLSGQMFST
210 220 230 240 250
GSGNTYAYGV MDSGYRQDLS PEEAYDLGRR AIAYATHRDN YSGGVVNMYH
260 270
MKEDGWVKVE SSDVSDLLYK YGEAAL
Length:276
Mass (Da):30,260
Last modified:November 1, 1995 - v2
Checksum:iD9FCCF3EF83CD3C3
GO

Sequence cautioni

The sequence CAA45780.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti39 – 391A → R in CAB60065. (PubMed:8406612)Curated
Sequence conflicti148 – 1481V → M in BAE26960. (PubMed:16141072)Curated
Sequence conflicti199 – 1991S → P in AAH51450. (PubMed:15489334)Curated

Polymorphismi

The allele, LMP7k/LMP7s/LMPf/LMP7r/LMPcas4/LMPg7 found in strains NMRI, B10.BR, SJL, A.CA, B10.RIII, B10.cas4 and NOD may be post-translationally modified. Allele LMP7q is found in strain DBA/1J.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti272 – 2721G → R in LMP7k/LMP7s/LMPf/LMP7r/LMPcas4/LMPg7. 2 Publications
Natural varianti275 – 2751A → S in LMP7q. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64449 mRNA. Translation: CAA45779.1.
X64449 mRNA. Translation: CAA45780.1. Different initiation.
L11145 mRNA. Translation: AAB46392.1.
Z21847 Genomic DNA. Translation: CAB60065.1. Sequence problems.
U22031 mRNA. Translation: AAA75033.1.
U22032 mRNA. Translation: AAA75034.1.
U22033 mRNA. Translation: AAA75035.1.
U22034 mRNA. Translation: AAA75036.1.
U22035 mRNA. Translation: AAA75037.1.
AK031801 mRNA. Translation: BAC27555.1.
AK050627 mRNA. Translation: BAE20682.1.
AK146182 mRNA. Translation: BAE26960.1.
AK150674 mRNA. Translation: BAE29756.1.
AK159971 mRNA. Translation: BAE35524.1.
AF027865 Genomic DNA. Translation: AAB81532.1.
BC013785 mRNA. Translation: AAH13785.1.
BC051450 mRNA. Translation: AAH51450.1.
CCDSiCCDS50073.1.
PIRiI54513.
RefSeqiNP_034854.2. NM_010724.2.
UniGeneiMm.180191.
Mm.484878.

Genome annotation databases

EnsembliENSMUST00000025196; ENSMUSP00000025196; ENSMUSG00000024338.
GeneIDi16913.
KEGGimmu:16913.
UCSCiuc012apv.1. mouse.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64449 mRNA. Translation: CAA45779.1 .
X64449 mRNA. Translation: CAA45780.1 . Different initiation.
L11145 mRNA. Translation: AAB46392.1 .
Z21847 Genomic DNA. Translation: CAB60065.1 . Sequence problems.
U22031 mRNA. Translation: AAA75033.1 .
U22032 mRNA. Translation: AAA75034.1 .
U22033 mRNA. Translation: AAA75035.1 .
U22034 mRNA. Translation: AAA75036.1 .
U22035 mRNA. Translation: AAA75037.1 .
AK031801 mRNA. Translation: BAC27555.1 .
AK050627 mRNA. Translation: BAE20682.1 .
AK146182 mRNA. Translation: BAE26960.1 .
AK150674 mRNA. Translation: BAE29756.1 .
AK159971 mRNA. Translation: BAE35524.1 .
AF027865 Genomic DNA. Translation: AAB81532.1 .
BC013785 mRNA. Translation: AAH13785.1 .
BC051450 mRNA. Translation: AAH51450.1 .
CCDSi CCDS50073.1.
PIRi I54513.
RefSeqi NP_034854.2. NM_010724.2.
UniGenei Mm.180191.
Mm.484878.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3UNF X-ray 2.90 K/Y 73-276 [» ]
3UNH X-ray 3.20 K/Y 73-276 [» ]
ProteinModelPortali P28063.
SMRi P28063. Positions 73-273.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P28063. 4 interactions.
MINTi MINT-1856641.

Chemistry

ChEMBLi CHEMBL1944492.

Protein family/group databases

MEROPSi T01.015.

PTM databases

PhosphoSitei P28063.

Proteomic databases

MaxQBi P28063.
PaxDbi P28063.
PRIDEi P28063.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000025196 ; ENSMUSP00000025196 ; ENSMUSG00000024338 .
GeneIDi 16913.
KEGGi mmu:16913.
UCSCi uc012apv.1. mouse.

Organism-specific databases

CTDi 5696.
MGIi MGI:1346527. Psmb8.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00510000046395.
HOGENOMi HOG000091082.
HOVERGENi HBG108297.
InParanoidi P28063.
KOi K02740.
OMAi SDLMHQY.
PhylomeDBi P28063.
TreeFami TF106223.

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_203336. Degradation of beta-catenin by the destruction complex.
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.
REACT_232069. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_232469. Hh ligand biogenesis disease.
REACT_233316. Hedgehog ligand biogenesis.
REACT_234963. Regulation of ornithine decarboxylase (ODC).
REACT_244558. CDT1 association with the CDC6:ORC:origin complex.
REACT_245230. Orc1 removal from chromatin.
REACT_249922. CDK-mediated phosphorylation and removal of Cdc6.
REACT_263467. Ubiquitin-dependent degradation of Cyclin D1.
REACT_268522. GLI3 is processed to GLI3R by the proteasome.
REACT_268705. Degradation of GLI1 by the proteasome.
REACT_270923. Degradation of GLI2 by the proteasome.

Miscellaneous databases

NextBioi 290960.
PROi P28063.
SOURCEi Search...

Gene expression databases

Bgeei P28063.
ExpressionAtlasi P28063. baseline and differential.
Genevestigatori P28063.

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. "Isolation and characterization of the MHC linked beta-type proteasome subunit MC13 cDNA."
    Frentzel S., Graef U., Haemmerling G., Kloetzel P.-M.
    FEBS Lett. 302:121-125(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Lymphoma.
  2. "Different genomic structure of mouse and human Lmp7 genes: characterization of MHC-encoded proteasome genes."
    Meinhardt T., Graf U., Hammerling G.J.
    Immunogenetics 38:373-379(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Lymphoma.
  3. "Genomic organization and tissue expression of the mouse proteasome gene Lmp-7."
    Zanelli E.H., Zhou P., Hong C., Smart M.K., David C.S.
    Immunogenetics 38:400-407(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
    Strain: BALB/c.
  4. "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], VARIANTS LMP7K/LMP7S/LMPF/LMP7R/LMPCAS4/LMPG7 ARG-272 AND LMP7Q SER-275.
    Strain: A.CA, B10.BR, B10.CAS4, B10.RIII, BALB/c, DBA/1J, NOD and SJL.
    Tissue: Splenocyte and Thymocyte.
  5. "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 and DBA/2.
    Tissue: Bone marrow, Medulla oblongata and Thymus.
  6. "Sequence of the mouse major histocompatibility locus class II region."
    Rowen L., Qin S., Ahearn M.E., Loretz C., Faust J., Lasky S., Mahairas G., Hood L.
    Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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], VARIANT LMP7K/LMP7S/LMPF/LMP7R/LMPCAS4/LMPG7 ARG-272.
    Strain: C57BL/6NCr and NMRI.
    Tissue: Hematopoietic stem cell and Mammary tumor.
  8. "MHC class I expression in mice lacking the proteasome subunit LMP-7."
    Fehling H.J., Swat W., Laplace C., Kuehn R., Rajewsky K., Mueller U., von Boehmer H.
    Science 265:1234-1237(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Gene expression profiling in spleens of deoxynivalenol-exposed mice: immediate early genes as primary targets."
    Kinser S., Jia Q., Li M., Laughter A., Cornwell P., Corton J.C., Pestka J.
    J. Toxicol. Environ. Health Part A 67:1423-1441(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY DEOXYNIVALENOL.
  10. "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.
  11. "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.
  12. "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.
  13. Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.
  14. "A selective inhibitor of the immunoproteasome subunit LMP7 blocks cytokine production and attenuates progression of experimental arthritis."
    Muchamuel T., Basler M., Aujay M.A., Suzuki E., Kalim K.W., Lauer C., Sylvain C., Ring E.R., Shields J., Jiang J., Shwonek P., Parlati F., Demo S.D., Bennett M.K., Kirk C.J., Groettrup M.
    Nat. Med. 15:781-787(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY PR-957.
  15. Cited for: FUNCTION IN ADIPOCYTE DIFFERENTIATION.
  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 IN COMPLEX WITH SYNTHETIC INHIBITOR, SUBUNIT, FUNCTION, TISSUE SPECIFICITY, ACTIVE SITE, AUTOCLEAVAGE.

Entry informationi

Entry nameiPSB8_MOUSE
AccessioniPrimary (citable) accession number: P28063
Secondary accession number(s): Q3UK42
, Q64300, Q792S8, Q7TMX9, Q91VH7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: November 1, 1995
Last modified: November 26, 2014
This is version 139 of the entry and version 2 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