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P28063 (PSB8_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. 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-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 names
Name:Psmb8
Synonyms:Lmp7, Mc13
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length276 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. May be involved in the inflammatory response pathway. Required for adipocyte differentiation. Ref.8 Ref.15 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 housekeeping subunit PSMB5. Component of the spermatoproteasome, a form of the proteasome specifically found in testis. Directly interacts with POMP. Interacts with TAP1. Ref.13 Ref.16 Ref.17

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Tissue specificity

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. Ref.3 Ref.17

Induction

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. Ref.9 Ref.10 Ref.11 Ref.12 Ref.14

Post-translational modification

Autocleaved. The resulting N-terminal Thr residue of the mature subunit is responsible for the nucleophile proteolytic activity. Ref.17

Polymorphism

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.

Sequence similarities

Belongs to the peptidase T1B family.

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 7272Removed in mature form By similarity
PRO_0000026599
Chain73 – 276204Proteasome subunit beta type-8
PRO_0000026600

Sites

Active site731Nucleophile Ref.17
Site72 – 732Cleavage; by autocatalysis

Natural variations

Natural variant2721G → R in LMP7k/LMP7s/LMPf/LMP7r/LMPcas4/LMPg7. Ref.4 Ref.7
Natural variant2751A → S in LMP7q. Ref.4

Experimental info

Sequence conflict391A → R in CAB60065. Ref.3
Sequence conflict1481V → M in BAE26960. Ref.5
Sequence conflict1991S → P in AAH51450. Ref.7

Secondary structure

..................................... 276
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P28063 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: D9FCCF3EF83CD3C3

FASTA27630,260
        10         20         30         40         50         60 
MALLDLCGAA RGQRPEWAAL DAGSGGRSDP GHYSFSAQAP ELALPRGMQP TAFLRSFGGD 

        70         80         90        100        110        120 
QERNVQIEMA HGTTTLAFKF QHGVIVAVDS RATAGSYISS LRMNKVIEIN PYLLGTMSGC 

       130        140        150        160        170        180 
AADCQYWERL LAKECRLYYL RNGERISVSA ASKLLSNMML QYRGMGLSMG SMICGWDKKG 

       190        200        210        220        230        240 
PGLYYVDDNG TRLSGQMFST GSGNTYAYGV MDSGYRQDLS PEEAYDLGRR AIAYATHRDN 

       250        260        270 
YSGGVVNMYH MKEDGWVKVE SSDVSDLLYK YGEAAL 

« Hide

References

« Hide 'large scale' references
[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. 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 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]"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.
[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]"A mutation in the immunoproteasome subunit PSMB8 causes autoinflammation and lipodystrophy in humans."
Kitamura A., Maekawa Y., Uehara H., Izumi K., Kawachi I., Nishizawa M., Toyoshima Y., Takahashi H., Standley D.M., Tanaka K., Hamazaki J., Murata S., Obara K., Toyoshima I., Yasutomo K.
J. Clin. Invest. 121:4150-4160(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ADIPOCYTE DIFFERENTIATION.
[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 IN COMPLEX WITH SYNTHETIC INHIBITOR, SUBUNIT, FUNCTION, TISSUE SPECIFICITY, ACTIVE SITE, AUTOCLEAVAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS50073.1.
PIRI54513.
RefSeqNP_034854.2. NM_010724.2.
UniGeneMm.180191.
Mm.484878.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3UNFX-ray2.90K/Y73-276[»]
3UNHX-ray3.20K/Y73-276[»]
ProteinModelPortalP28063.
SMRP28063. Positions 73-273.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP28063. 4 interactions.
MINTMINT-1856641.

Chemistry

ChEMBLCHEMBL1944492.

Protein family/group databases

MEROPST01.015.

PTM databases

PhosphoSiteP28063.

Proteomic databases

MaxQBP28063.
PaxDbP28063.
PRIDEP28063.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025196; ENSMUSP00000025196; ENSMUSG00000024338.
GeneID16913.
KEGGmmu:16913.
UCSCuc012apv.1. mouse.

Organism-specific databases

CTD5696.
MGIMGI:1346527. Psmb8.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00510000046395.
HOGENOMHOG000091082.
HOVERGENHBG108297.
InParanoidP28063.
KOK02740.
OMASDLMHQY.
PhylomeDBP28063.
TreeFamTF106223.

Gene expression databases

ArrayExpressP28063.
BgeeP28063.
GenevestigatorP28063.

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

NextBio290960.
PROP28063.
SOURCESearch...

Entry information

Entry namePSB8_MOUSE
AccessionPrimary (citable) accession number: P28063
Secondary accession number(s): Q3UK42 expand/collapse secondary AC list , Q64300, Q792S8, Q7TMX9, Q91VH7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 135 of the entry and version 2 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