Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q55GJ6

- PSB6_DICDI

UniProt

Q55GJ6 - PSB6_DICDI

Protein

Proteasome subunit beta type-6

Gene

psmB6

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (24 May 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.1 Publication

    Catalytic activityi

    Cleavage of peptide bonds with very broad specificity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei15 – 151NucleophileBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. proteolysis Source: dictyBase
    2. proteolysis involved in cellular protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    Enzyme and pathway databases

    ReactomeiREACT_204617. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_210566. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_212010. Regulation of activated PAK-2p34 by proteasome mediated degradation.
    REACT_214682. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_217211. ER-Phagosome pathway.
    REACT_217636. Autodegradation of the E3 ubiquitin ligase COP1.
    REACT_221036. Separation of Sister Chromatids.
    REACT_225025. APC/C:Cdc20 mediated degradation of Securin.
    REACT_226311. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_226712. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_95813. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.

    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):
    Differentiation-associated proteasome subunit 1
    Short name:
    DAPS-1
    Gene namesi
    Name:psmB6
    Synonyms:dapA
    ORF Names:DDB_G0267390
    OrganismiDictyostelium discoideum (Slime mold)
    Taxonomic identifieri44689 [NCBI]
    Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
    ProteomesiUP000002195: Chromosome 1, UP000002195: Unassembled WGS sequence

    Organism-specific databases

    dictyBaseiDDB_G0267390. psmB6.

    Subcellular locationi

    Cytoplasm 1 PublicationPROSITE-ProRule annotation. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: dictyBase
    2. nucleus Source: dictyBase
    3. proteasome core complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei1 – 1414Removed in mature form1 PublicationPRO_0000327384Add
    BLAST
    Chaini15 – 214200Proteasome subunit beta type-6PRO_0000327385Add
    BLAST

    Keywords - PTMi

    Zymogen

    Proteomic databases

    PRIDEiQ55GJ6.

    Expressioni

    Developmental stagei

    Maximally expressed 4-6 hours after starvation (around the aggregation-stream stage), followed by a drastic decrease from the mound to tipped aggregate stage.1 Publication

    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 By similarity.By similarity

    Protein-protein interaction databases

    STRINGi44689.DDB_0191199.

    Structurei

    3D structure databases

    ProteinModelPortaliQ55GJ6.
    SMRiQ55GJ6. Positions 15-211.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1B family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    KOiK02738.
    OMAiTSIMAVQ.
    PhylomeDBiQ55GJ6.

    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.

    Q55GJ6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEAPEWLDNA VDLGTSIMAV EYDGGVIMGA DSRTTTGAYI ANRVTNKITP    50
    IHERIYCCRS GSAADTQAIS DYVRYYLEMH TSELCDEPDV KTAASLFQLL 100
    CYSNKNNLMA GIIVAGWDKH QGGSVYNISL GGSMVKQPFA IGGSGSTYIY 150
    GYCDSKFKPK MTKDECIEFV QNSLALAMFR DGSSGGVIRL CIIDKNGVER 200
    KMIPGNNLPR FWEG 214
    Length:214
    Mass (Da):23,446
    Last modified:May 24, 2005 - v1
    Checksum:i1EA0E6921D37AAE2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251G → R AA sequence (PubMed:8130037)Curated
    Sequence conflicti28 – 281M → A AA sequence (PubMed:8130037)Curated
    Sequence conflicti95 – 951S → C in BAA25923. (PubMed:9535814)Curated
    Sequence conflicti122 – 1221Missing in BAA25923. (PubMed:9535814)Curated
    Sequence conflicti165 – 1651E → R in BAA25923. (PubMed:9535814)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB007024 mRNA. Translation: BAA25923.1.
    AAFI02000003 Genomic DNA. Translation: EAL73147.1.
    PIRiJE0101.
    RefSeqiXP_647188.1. XM_642096.1.

    Genome annotation databases

    EnsemblProtistsiDDB0191199; DDB0191199; DDB_G0267390.
    GeneIDi8615992.
    KEGGiddi:DDB_G0267390.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB007024 mRNA. Translation: BAA25923.1 .
    AAFI02000003 Genomic DNA. Translation: EAL73147.1 .
    PIRi JE0101.
    RefSeqi XP_647188.1. XM_642096.1.

    3D structure databases

    ProteinModelPortali Q55GJ6.
    SMRi Q55GJ6. Positions 15-211.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 44689.DDB_0191199.

    Protein family/group databases

    MEROPSi T01.010.

    Proteomic databases

    PRIDEi Q55GJ6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblProtistsi DDB0191199 ; DDB0191199 ; DDB_G0267390 .
    GeneIDi 8615992.
    KEGGi ddi:DDB_G0267390.

    Organism-specific databases

    dictyBasei DDB_G0267390. psmB6.

    Phylogenomic databases

    eggNOGi COG0638.
    KOi K02738.
    OMAi TSIMAVQ.
    PhylomeDBi Q55GJ6.

    Enzyme and pathway databases

    Reactomei REACT_204617. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_210566. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_212010. Regulation of activated PAK-2p34 by proteasome mediated degradation.
    REACT_214682. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_217211. ER-Phagosome pathway.
    REACT_217636. Autodegradation of the E3 ubiquitin ligase COP1.
    REACT_221036. Separation of Sister Chromatids.
    REACT_225025. APC/C:Cdc20 mediated degradation of Securin.
    REACT_226311. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_226712. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_95813. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.

    Miscellaneous databases

    PROi Q55GJ6.

    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

    1. "Preferential expression of the cDNA encoding the proteasome subunit during the growth/differentiation transition of Dictyostelium cells."
      Chae S.-C., Maeda Y.
      Biochem. Biophys. Res. Commun. 245:231-234(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
      Strain: AX2.
    2. "The genome of the social amoeba Dictyostelium discoideum."
      Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N.
      , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
      Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: AX4.
    3. "Proteasomes from Dictyostelium discoideum: characterization of structure and function."
      Schauer T.M., Nesper M., Kehl M., Lottspeich F., Mueller-Taubenberger A., Gerisch G., Baumeister W.
      J. Struct. Biol. 111:135-147(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 15-32, FUNCTION, SUBCELLULAR LOCATION.
      Strain: AX2.

    Entry informationi

    Entry nameiPSB6_DICDI
    AccessioniPrimary (citable) accession number: Q55GJ6
    Secondary accession number(s): O60953
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 8, 2008
    Last sequence update: May 24, 2005
    Last modified: October 1, 2014
    This is version 69 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Dictyostelium discoideum
      Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3