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Protein

Proteasome subunit beta type-6

Gene

Psmb6

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. May catalyze basal processing of intracellular antigens.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei34 – 341NucleophileBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. proteolysis involved in cellular protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

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

MEROPSiT01.010.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Psmb6
Synonyms:Lmp19
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:104880. Psmb6.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: MGI
  4. Golgi apparatus Source: MGI
  5. nucleoplasm Source: MGI
  6. nucleus Source: MGI
  7. proteasome complex Source: MGI
  8. proteasome core complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Propeptidei2 – 3332Removed in mature formBy similarityPRO_0000026615Add
BLAST
Chaini34 – 238205Proteasome subunit beta type-6PRO_0000026616Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation, Zymogen

Proteomic databases

MaxQBiQ60692.
PaxDbiQ60692.
PRIDEiQ60692.

2D gel databases

REPRODUCTION-2DPAGEQ60692.

PTM databases

PhosphoSiteiQ60692.

Expressioni

Inductioni

Up-regulated by the antioxidant dithiolethione (D3T) in liver, lung and small intestine (at protein level).1 Publication

Gene expression databases

BgeeiQ60692.
GenevestigatoriQ60692.

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. This subunit can be displaced by the equivalent immune-specific subunit PSMB9.1 Publication

Protein-protein interaction databases

BioGridi202423. 2 interactions.
IntActiQ60692. 9 interactions.
MINTiMINT-1850570.

Structurei

Secondary structure

1
238
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi36 – 405Combined sources
Beta strandi42 – 498Combined sources
Beta strandi53 – 553Combined sources
Beta strandi58 – 636Combined sources
Beta strandi67 – 693Combined sources
Beta strandi71 – 8010Combined sources
Helixi82 – 10322Combined sources
Helixi109 – 12214Combined sources
Turni123 – 1264Combined sources
Beta strandi129 – 1379Combined sources
Turni138 – 1403Combined sources
Beta strandi141 – 1477Combined sources
Beta strandi157 – 1626Combined sources
Helixi163 – 1686Combined sources
Helixi169 – 1757Combined sources
Helixi182 – 19918Combined sources
Beta strandi200 – 2023Combined sources
Beta strandi207 – 2137Combined sources
Beta strandi216 – 2227Combined sources
Helixi224 – 2263Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.904/N/b/p34-238[»]
3UNEX-ray3.204/N/b/p34-238[»]
ProteinModelPortaliQ60692.
SMRiQ60692. Positions 34-235.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00510000046484.
HOGENOMiHOG000091079.
HOVERGENiHBG000123.
InParanoidiQ60692.
KOiK02738.
OMAiTSIMAVQ.
OrthoDBiEOG79GT80.
PhylomeDBiQ60692.
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.

Q60692-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAALAVRRA GSAPAFGPEA LTPDWENREV STGTTIMAVQ FNGGVVLGAD
60 70 80 90 100
SRTTTGSYIA NRVTDKLTPI HDHIFCCRSG SAADTQAVAD AVTYQLGFHS
110 120 130 140 150
IELNEPPLVH TAASLFKEMC YRYREDLMAG IIIAGWDPQE GGQVYSVPMG
160 170 180 190 200
GMMVRQSFAI GGSGSSYIYG YVDATYREGM TKDECLQFTA NALALAMERD
210 220 230
GSSGGVIRLA AIQESGVERQ VLLGDQIPKF TIATLPPP
Length:238
Mass (Da):25,379
Last modified:December 19, 2005 - v3
Checksum:i5A4EB82C4374C6FE
GO

Sequence cautioni

The sequence AAA75375.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAA75376.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH13897.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE20959.1 differs from that shown. Reason: Frameshift at position 224. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21A → T (PubMed:7797265).Curated
Sequence conflicti6 – 61A → S (PubMed:7797265).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti38 – 381A → T.1 Publication
Natural varianti89 – 891A → T.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS48836.1.
RefSeqiNP_032972.3. NM_008946.4.
UniGeneiMm.98.

Genome annotation databases

EnsembliENSMUST00000018430; ENSMUSP00000018430; ENSMUSG00000018286.
GeneIDi19175.
KEGGimmu:19175.
UCSCiuc007jve.2. mouse.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS48836.1.
RefSeqiNP_032972.3. NM_008946.4.
UniGeneiMm.98.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.904/N/b/p34-238[»]
3UNEX-ray3.204/N/b/p34-238[»]
ProteinModelPortaliQ60692.
SMRiQ60692. Positions 34-235.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202423. 2 interactions.
IntActiQ60692. 9 interactions.
MINTiMINT-1850570.

Chemistry

ChEMBLiCHEMBL1944493.

Protein family/group databases

MEROPSiT01.010.

PTM databases

PhosphoSiteiQ60692.

2D gel databases

REPRODUCTION-2DPAGEQ60692.

Proteomic databases

MaxQBiQ60692.
PaxDbiQ60692.
PRIDEiQ60692.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000018430; ENSMUSP00000018430; ENSMUSG00000018286.
GeneIDi19175.
KEGGimmu:19175.
UCSCiuc007jve.2. mouse.

Organism-specific databases

CTDi5694.
MGIiMGI:104880. Psmb6.

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00510000046484.
HOGENOMiHOG000091079.
HOVERGENiHBG000123.
InParanoidiQ60692.
KOiK02738.
OMAiTSIMAVQ.
OrthoDBiEOG79GT80.
PhylomeDBiQ60692.
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

ChiTaRSiPsmb6. mouse.
NextBioi295856.
PROiQ60692.
SOURCEiSearch...

Gene expression databases

BgeeiQ60692.
GenevestigatoriQ60692.

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. "Characterization and mapping of the gene encoding mouse proteasome subunit DELTA (Lmp19)."
    Woodward E.C., Monaco J.J.
    Immunogenetics 42:28-34(1994) [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.
    , 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: Hippocampus and Wolffian duct.
  3. 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(2003) [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 (MAR-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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY DITHIOLETHIONE.
  7. Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.

Entry informationi

Entry nameiPSB6_MOUSE
AccessioniPrimary (citable) accession number: Q60692
Secondary accession number(s): Q3V240
, Q60693, Q8BJX9, Q91VH5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 17, 2001
Last sequence update: December 19, 2005
Last modified: March 31, 2015
This is version 136 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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.