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Q9CWH6

- PSA7L_MOUSE

UniProt

Q9CWH6 - PSA7L_MOUSE

Protein

Proteasome subunit alpha type-7-like

Gene

Psma8

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Component of the spermatoproteasome, a form of the proteasome specifically found in testis that promotes degradation of histones, thereby participating actively to the exchange of histones during spermatogenesis. 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.1 Publication

    Catalytic activityi

    Cleavage of peptide bonds with very broad specificity.PROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Threonine protease

    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_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_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.

    Protein family/group databases

    MEROPSiT01.978.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit alpha type-7-like (EC:3.4.25.1)
    Gene namesi
    Name:Psma8
    Synonyms:Psma7l
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 18

    Organism-specific databases

    MGIiMGI:1920927. Psma8.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleus Source: UniProtKB-SubCell
    3. proteasome core complex, alpha-subunit complex Source: InterPro
    4. spermatoproteasome complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Proteasome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 250250Proteasome subunit alpha type-7-likePRO_0000124150Add
    BLAST

    Proteomic databases

    PaxDbiQ9CWH6.
    PRIDEiQ9CWH6.

    PTM databases

    PhosphoSiteiQ9CWH6.

    Expressioni

    Gene expression databases

    BgeeiQ9CWH6.
    GenevestigatoriQ9CWH6.

    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. Component of the spermatoproteasome, a form of the proteasome specifically found in testis.By similarity1 Publication

    Protein-protein interaction databases

    IntActiQ9CWH6. 2 interactions.
    MINTiMINT-4108848.
    STRINGi10090.ENSMUSP00000042590.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9CWH6.
    SMRiQ9CWH6. Positions 5-240.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0638.
    GeneTreeiENSGT00550000074753.
    HOGENOMiHOG000091085.
    HOVERGENiHBG003005.
    InParanoidiQ14A44.
    KOiK02731.
    OMAiPLKMLDR.
    OrthoDBiEOG71VSTG.
    PhylomeDBiQ9CWH6.
    TreeFamiTF106212.

    Family and domain databases

    Gene3Di3.60.20.10. 1 hit.
    InterProiIPR029055. Ntn_hydrolases_N.
    IPR000426. Proteasome_asu_N.
    IPR023332. Proteasome_suA-type.
    IPR001353. Proteasome_sua/b.
    [Graphical view]
    PfamiPF00227. Proteasome. 1 hit.
    PF10584. Proteasome_A_N. 1 hit.
    [Graphical view]
    SMARTiSM00948. Proteasome_A_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF56235. SSF56235. 1 hit.
    PROSITEiPS00388. PROTEASOME_ALPHA_1. 1 hit.
    PS51475. PROTEASOME_ALPHA_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9CWH6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASRYDRAIT VFSPDGHLFQ VEYAQEAVKK GSTAVGIRGT NIVVLGVEKK    50
    SVAKLQDERT VRKICALDDH VCMAFAGLTA DARVVISRAR VECQSHKLTV 100
    EDPVTVEYIT RFIATLKQKY TQSNGRRPFG ISALIVGFDD DGIPRLYQTD 150
    PSGTYHAWKA NAIGRSAKTV REFLEKNYTE DAISNDKEAI KLAIKALLEV 200
    VQSGGKNIEL AIIRRDQPLK MFSAKEIELE VSEIEREKDE AEKTKSKKST 250
    Length:250
    Mass (Da):27,866
    Last modified:June 1, 2001 - v1
    Checksum:i86258DBE01B0C0E6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK010717 mRNA. Translation: BAB27139.1.
    BC116990 mRNA. Translation: AAI16991.1.
    BC116992 mRNA. Translation: AAI16993.1.
    CCDSiCCDS50226.1.
    RefSeqiNP_001157081.1. NM_001163609.1.
    UniGeneiMm.87277.

    Genome annotation databases

    EnsembliENSMUST00000040860; ENSMUSP00000042590; ENSMUSG00000036743.
    GeneIDi73677.
    KEGGimmu:73677.
    UCSCiuc008edj.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK010717 mRNA. Translation: BAB27139.1 .
    BC116990 mRNA. Translation: AAI16991.1 .
    BC116992 mRNA. Translation: AAI16993.1 .
    CCDSi CCDS50226.1.
    RefSeqi NP_001157081.1. NM_001163609.1.
    UniGenei Mm.87277.

    3D structure databases

    ProteinModelPortali Q9CWH6.
    SMRi Q9CWH6. Positions 5-240.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9CWH6. 2 interactions.
    MINTi MINT-4108848.
    STRINGi 10090.ENSMUSP00000042590.

    Protein family/group databases

    MEROPSi T01.978.

    PTM databases

    PhosphoSitei Q9CWH6.

    Proteomic databases

    PaxDbi Q9CWH6.
    PRIDEi Q9CWH6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000040860 ; ENSMUSP00000042590 ; ENSMUSG00000036743 .
    GeneIDi 73677.
    KEGGi mmu:73677.
    UCSCi uc008edj.2. mouse.

    Organism-specific databases

    CTDi 143471.
    MGIi MGI:1920927. Psma8.

    Phylogenomic databases

    eggNOGi COG0638.
    GeneTreei ENSGT00550000074753.
    HOGENOMi HOG000091085.
    HOVERGENi HBG003005.
    InParanoidi Q14A44.
    KOi K02731.
    OMAi PLKMLDR.
    OrthoDBi EOG71VSTG.
    PhylomeDBi Q9CWH6.
    TreeFami TF106212.

    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_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_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.

    Miscellaneous databases

    NextBioi 338777.
    PROi Q9CWH6.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9CWH6.
    Genevestigatori Q9CWH6.

    Family and domain databases

    Gene3Di 3.60.20.10. 1 hit.
    InterProi IPR029055. Ntn_hydrolases_N.
    IPR000426. Proteasome_asu_N.
    IPR023332. Proteasome_suA-type.
    IPR001353. Proteasome_sua/b.
    [Graphical view ]
    Pfami PF00227. Proteasome. 1 hit.
    PF10584. Proteasome_A_N. 1 hit.
    [Graphical view ]
    SMARTi SM00948. Proteasome_A_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56235. SSF56235. 1 hit.
    PROSITEi PS00388. PROTEASOME_ALPHA_1. 1 hit.
    PS51475. PROTEASOME_ALPHA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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.
      Tissue: Embryonic stem cell.
    2. "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].
      Tissue: Brain.
    3. Cited for: FUNCTION, IDENTIFICATION IN THE SPERMATOPROTEASOME.

    Entry informationi

    Entry nameiPSA7L_MOUSE
    AccessioniPrimary (citable) accession number: Q9CWH6
    Secondary accession number(s): Q14A44
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2002
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 104 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3