Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q60692 (PSB6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. 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-6

EC=3.4.25.1
Alternative name(s):
Low molecular mass protein 19
Macropain delta chain
Multicatalytic endopeptidase complex delta chain
Proteasome delta chain
Proteasome subunit Y
Gene names
Name:Psmb6
Synonyms:Lmp19
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length238 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. May catalyze basal processing of intracellular antigens.

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. This subunit can be displaced by the equivalent immune-specific subunit PSMB9. Ref.7

Subcellular location

Cytoplasm. Nucleus.

Induction

Up-regulated by the antioxidant dithiolethione (D3T) in liver, lung and small intestine (at protein level). Ref.6

Sequence similarities

Belongs to the peptidase T1B family.

Sequence caution

The sequence AAA75375.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAA75376.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH13897.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAE20959.1 differs from that shown. Reason: Frameshift at position 224.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Propeptide2 – 3332Removed in mature form By similarity
PRO_0000026615
Chain34 – 238205Proteasome subunit beta type-6
PRO_0000026616

Sites

Active site341Nucleophile By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Natural variations

Natural variant381A → T. Ref.1
Natural variant891A → T. Ref.1

Experimental info

Sequence conflict21A → T Ref.1
Sequence conflict61A → S Ref.1

Secondary structure

................................... 238
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q60692 [UniParc].

Last modified December 20, 2005. Version 3.
Checksum: 5A4EB82C4374C6FE

FASTA23825,379
        10         20         30         40         50         60 
MAAALAVRRA GSAPAFGPEA LTPDWENREV STGTTIMAVQ FNGGVVLGAD SRTTTGSYIA 

        70         80         90        100        110        120 
NRVTDKLTPI HDHIFCCRSG SAADTQAVAD AVTYQLGFHS IELNEPPLVH TAASLFKEMC 

       130        140        150        160        170        180 
YRYREDLMAG IIIAGWDPQE GGQVYSVPMG GMMVRQSFAI GGSGSSYIYG YVDATYREGM 

       190        200        210        220        230 
TKDECLQFTA NALALAMERD GSSGGVIRLA AIQESGVERQ VLLGDQIPKF TIATLPPP 

« Hide

References

« Hide 'large scale' references
[1]"Characterization and mapping of the gene encoding mouse proteasome subunit DELTA (Lmp19)."
Woodward E.C., Monaco J.J.
Immunogenetics 42:28-34(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANTS THR-38 AND THR-89.
Strain: DBA/2J.
Tissue: Liver.
[2]"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: Hippocampus and Wolffian duct.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"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] OF 7-238.
Strain: FVB/N.
Tissue: Mammary tumor.
[5]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 209-229, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[6]"Tissue specific increase of the catalytic subunits of the 26S proteasome by indirect antioxidant dithiolethione in mice: enhanced activity for degradation of abnormal protein."
Kwak M.K., Huang B., Chang H., Kim J.A., Kensler T.W.
Life Sci. 80:2411-2420(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY DITHIOLETHIONE.
[7]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U13393 mRNA. Translation: AAA75375.1. Different initiation.
U13394 Genomic DNA. Translation: AAA75376.1. Different initiation.
AK078437 mRNA. Translation: BAC37272.1.
AK132042 mRNA. Translation: BAE20959.1. Frameshift.
AK167123 mRNA. Translation: BAE39271.1.
AK167227 mRNA. Translation: BAE39351.1.
AL592547 Genomic DNA. Translation: CAI24014.1.
BC013897 mRNA. Translation: AAH13897.1. Different initiation.
CCDSCCDS48836.1.
RefSeqNP_032972.3. NM_008946.4.
UniGeneMm.98.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.904/N/b/p34-238[»]
3UNEX-ray3.204/N/b/p34-238[»]
ProteinModelPortalQ60692.
SMRQ60692. Positions 34-235.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202423. 2 interactions.
IntActQ60692. 9 interactions.
MINTMINT-1850570.

Chemistry

ChEMBLCHEMBL1944493.

Protein family/group databases

MEROPST01.010.

PTM databases

PhosphoSiteQ60692.

2D gel databases

REPRODUCTION-2DPAGEQ60692.

Proteomic databases

MaxQBQ60692.
PaxDbQ60692.
PRIDEQ60692.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000018430; ENSMUSP00000018430; ENSMUSG00000018286.
GeneID19175.
KEGGmmu:19175.
UCSCuc007jve.2. mouse.

Organism-specific databases

CTD5694.
MGIMGI:104880. Psmb6.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00510000046484.
HOGENOMHOG000091079.
HOVERGENHBG000123.
InParanoidQ60692.
KOK02738.
OMATSIMAVQ.
OrthoDBEOG79GT80.
PhylomeDBQ60692.
TreeFamTF106221.

Gene expression databases

BgeeQ60692.
GenevestigatorQ60692.

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

NextBio295856.
PROQ60692.
SOURCESearch...

Entry information

Entry namePSB6_MOUSE
AccessionPrimary (citable) accession number: Q60692
Secondary accession number(s): Q3V240 expand/collapse secondary AC list , Q60693, Q8BJX9, Q91VH5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: December 20, 2005
Last modified: July 9, 2014
This is version 128 of the entry and version 3 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