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Q6P9V6

- Q6P9V6_RAT

UniProt

Q6P9V6 - Q6P9V6_RAT

Protein

Proteasome subunit alpha type

Gene

Psma5

Organism
Rattus norvegicus (Rat)
Status
Unreviewed - Annotation score: 2 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    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.UniRule annotation

    Catalytic activityi

    Cleavage of peptide bonds with very broad specificity.UniRule 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 proteaseUniRule annotation

    Enzyme and pathway databases

    ReactomeiREACT_194781. Separation of Sister Chromatids.
    REACT_196424. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_198391. Asymmetric localization of PCP proteins.
    REACT_199194. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_199197. ER-Phagosome pathway.
    REACT_199247. Activation of NF-kappaB in B cells.
    REACT_199254. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_204983. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_206488. degradation of DVL.
    REACT_206997. CDT1 association with the CDC6:ORC:origin complex.
    REACT_211117. Orc1 removal from chromatin.
    REACT_212486. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_220232. Regulation of ornithine decarboxylase (ODC).
    REACT_227706. degradation of AXIN.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proteasome subunit alpha typeUniRule annotation (EC:3.4.25.1UniRule annotation)
    Gene namesi
    Name:Psma5Imported
    ORF Names:rCG_28817Imported
    OrganismiRattus norvegicus (Rat)Imported
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 2

    Organism-specific databases

    RGDi61848. Psma5.

    Subcellular locationi

    Cytoplasm UniRule annotation. Nucleus UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell
    3. proteasome core complex, alpha-subunit complex Source: InterPro

    Keywords - Cellular componenti

    CytoplasmUniRule annotation, NucleusUniRule annotationSAAS annotation, ProteasomeUniRule annotationImported

    Expressioni

    Gene expression databases

    GenevestigatoriQ6P9V6.

    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.UniRule annotation

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase T1A family.UniRule annotation

    Phylogenomic databases

    GeneTreeiENSGT00550000074958.
    HOVERGENiHBG003005.
    InParanoidiQ6P9V6.
    OMAiCAMSGLT.
    OrthoDBiEOG769ZKB.
    TreeFamiTF106211.

    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.

    Q6P9V6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFLTRSEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGI QTSEGVCLAV    50
    EKRITSPLME PSSIEKIVEI DAHIGCAMSG LIADAKTLID KARVETQNHW 100
    FTYNETMTVE SVTQAVSNLA LQFGEEDADP GAMSRPFGVA LLFGGVDEKG 150
    PQLFHMDPSG TFVQCDARAI GSASEGAQSS LQEVYHKSMT LKEAIKSSLI 200
    ILKQVMEEKL NATNIELATV QPGQNFHMFT KEELEEVIKD I 241
    Length:241
    Mass (Da):26,411
    Last modified:July 5, 2004 - v1
    Checksum:i5610CDA00469120A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AABR06019891 Genomic DNA. No translation available.
    BC060575 mRNA. Translation: AAH60575.1.
    CH473952 Genomic DNA. Translation: EDL81928.1.
    UniGeneiRn.1276.

    Genome annotation databases

    EnsembliENSRNOT00000026928; ENSRNOP00000026928; ENSRNOG00000019868.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AABR06019891 Genomic DNA. No translation available.
    BC060575 mRNA. Translation: AAH60575.1 .
    CH473952 Genomic DNA. Translation: EDL81928.1 .
    UniGenei Rn.1276.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000026928 ; ENSRNOP00000026928 ; ENSRNOG00000019868 .

    Organism-specific databases

    RGDi 61848. Psma5.

    Phylogenomic databases

    GeneTreei ENSGT00550000074958.
    HOVERGENi HBG003005.
    InParanoidi Q6P9V6.
    OMAi CAMSGLT.
    OrthoDBi EOG769ZKB.
    TreeFami TF106211.

    Enzyme and pathway databases

    Reactomei REACT_194781. Separation of Sister Chromatids.
    REACT_196424. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_198391. Asymmetric localization of PCP proteins.
    REACT_199194. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_199197. ER-Phagosome pathway.
    REACT_199247. Activation of NF-kappaB in B cells.
    REACT_199254. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_204983. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_206488. degradation of DVL.
    REACT_206997. CDT1 association with the CDC6:ORC:origin complex.
    REACT_211117. Orc1 removal from chromatin.
    REACT_212486. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_220232. Regulation of ornithine decarboxylase (ODC).
    REACT_227706. degradation of AXIN.

    Miscellaneous databases

    PROi Q6P9V6.

    Gene expression databases

    Genevestigatori Q6P9V6.

    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 status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.
      , Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Pituitary glandImported.
    2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
      Rat Genome Sequencing Project Consortium
      Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
      , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
      Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Brown NorwayImported.
    3. Cited for: NUCLEOTIDE SEQUENCE.
      Strain: BNImported.
    4. Cited for: NUCLEOTIDE SEQUENCE.
      Strain: BNImported.
    5. Ensembl
      Submitted (FEB-2012) to UniProtKB
      Cited for: IDENTIFICATION.
      Strain: Brown NorwayImported.

    Entry informationi

    Entry nameiQ6P9V6_RAT
    AccessioniPrimary (citable) accession number: Q6P9V6
    Entry historyi
    Integrated into UniProtKB/TrEMBL: July 5, 2004
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 80 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiUnreviewed (UniProtKB/TrEMBL)

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteomeImported

    External Data

    Dasty 3