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Q80VJ2

- SRA1_MOUSE

UniProt

Q80VJ2 - SRA1_MOUSE

Protein

Steroid receptor RNA activator 1

Gene

Sra1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 3 (28 Jun 2011)
      Previous versions | rss
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    Functioni

    Functional RNA which acts as a transcriptional coactivator that selectively enhances steroid receptor-mediated transactivation ligand-independently through a mechanism involving the modulating N-terminal domain (AF-1) of steroid receptors. Also mediates transcriptional coactivation of steroid receptors ligand-dependently through the steroid-binding domain (AF-2). Enhances cellular proliferation and differentiation and promotes apoptosis in vivo. May play a role in tumorigenesis By similarity.By similarity

    GO - Molecular functioni

    1. DNA binding Source: MGI
    2. ligand-dependent nuclear receptor transcription coactivator activity Source: MGI
    3. thyroid hormone receptor activator activity Source: MGI
    4. transcription coactivator activity Source: UniProtKB
    5. transcription cofactor activity Source: MGI

    GO - Biological processi

    1. cell differentiation Source: UniProtKB
    2. cell proliferation Source: UniProtKB
    3. execution phase of apoptosis Source: Ensembl
    4. positive regulation of receptor activity Source: GOC
    5. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    6. regulation of apoptotic process Source: UniProtKB
    7. regulation of transcription from RNA polymerase II promoter Source: MGI
    8. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Receptor, Ribonucleoprotein

    Keywords - Biological processi

    Apoptosis, Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Steroid receptor RNA activator 1
    Alternative name(s):
    Steroid receptor RNA activator protein
    Short name:
    SRAP
    Gene namesi
    Name:Sra1Imported
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 18

    Organism-specific databases

    MGIiMGI:1344414. Sra1.

    Subcellular locationi

    Nucleus By similarity. Cytoplasm By similarity

    GO - Cellular componenti

    1. cell leading edge Source: MGI
    2. nucleus Source: UniProtKB
    3. ribonucleoprotein complex Source: UniProtKB
    4. steroid hormone aporeceptor complex Source: MGI
    5. transcription factor complex Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 232232Steroid receptor RNA activator 1PRO_0000234106Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei60 – 601PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ80VJ2.
    PaxDbiQ80VJ2.
    PRIDEiQ80VJ2.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00317966.

    PTM databases

    PhosphoSiteiQ80VJ2.

    Expressioni

    Gene expression databases

    BgeeiQ80VJ2.
    CleanExiMM_SRA1.
    GenevestigatoriQ80VJ2.

    Interactioni

    Subunit structurei

    SRA1 RNA exists in a ribonucleoprotein complex containing NCOA1. The RNA also forms a complex with PUS1 and RARG in the nucleus. Interacts with AR.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi204880. 2 interactions.
    IntActiQ80VJ2. 2 interactions.
    MINTiMINT-4125677.

    Structurei

    Secondary structure

    1
    232
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi109 – 12416
    Helixi129 – 14820
    Helixi153 – 16816
    Helixi171 – 18313
    Helixi186 – 1894
    Turni190 – 1923
    Helixi193 – 20614

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2YRUNMR-A102-206[»]
    ProteinModelPortaliQ80VJ2.
    SMRiQ80VJ2. Positions 99-207.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ80VJ2.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi56 – 10146Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the SRA1 family.Curated

    Phylogenomic databases

    eggNOGiNOG44276.
    GeneTreeiENSGT00390000001803.
    HOGENOMiHOG000127508.
    HOVERGENiHBG061820.
    InParanoidiQ80VJ2.
    OMAiQTQTGGP.
    OrthoDBiEOG790G2V.
    TreeFamiTF314789.

    Family and domain databases

    InterProiIPR009917. SRA1-protein/COPII_Sec31.
    [Graphical view]
    PfamiPF07304. SRA1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q80VJ2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMRCPAGGAE VEMAELYVKP GNKERGWNDP PQFSYGLQTQ TGGPKRTPLT    50
    KRVAAPQDGS PRAPETSGPP PVDHPPPSSK ASRPPPMGSC PATGVEPPSS 100
    PVIESETLIE DVLRPLEQAL EDCHGHTKKQ VCDDISRRLA LLREQWAGGK 150
    LSIPVKKRMA LLVQELLHHQ WDAADDIHRS LMVDHVTEVS QWMVGVKRLI 200
    AEKKSLSSEE TKEEKFTVEP ENQTIPGFQQ PS 232
    Length:232
    Mass (Da):25,557
    Last modified:June 28, 2011 - v3
    Checksum:i0838CA544C75A678
    GO

    Sequence cautioni

    The sequence AAH26480.1 differs from that shown. Reason: Contaminating sequence.
    The sequence AAH26480.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAH48362.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAB24943.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAB26893.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAE32451.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51P → A in BAB24943. (PubMed:16141072)Curated
    Sequence conflicti10 – 101E → G in BAB24943. (PubMed:16141072)Curated
    Sequence conflicti27 – 271W → G in BAB24943. (PubMed:16141072)Curated
    Sequence conflicti140 – 1401A → V in AAH48362. (PubMed:15489334)Curated
    Sequence conflicti185 – 1851H → Y in AAH48362. (PubMed:15489334)Curated
    Sequence conflicti204 – 2041K → R in AAH48362. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC115631 Genomic DNA. No translation available.
    AK007302 mRNA. Translation: BAB24943.1. Different initiation.
    AK010375 mRNA. Translation: BAB26893.1. Different initiation.
    AK154232 mRNA. Translation: BAE32451.1. Different initiation.
    BC026480 mRNA. Translation: AAH26480.1. Sequence problems.
    BC048362 mRNA. Translation: AAH48362.1. Different initiation.
    CN836515 mRNA. No translation available.
    CCDSiCCDS29156.2.
    RefSeqiNP_001157878.1. NM_001164406.1.
    NP_079567.2. NM_025291.3.
    UniGeneiMm.29058.

    Genome annotation databases

    EnsembliENSMUST00000173875; ENSMUSP00000133360; ENSMUSG00000006050.
    GeneIDi24068.
    KEGGimmu:24068.
    UCSCiuc008eny.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC115631 Genomic DNA. No translation available.
    AK007302 mRNA. Translation: BAB24943.1 . Different initiation.
    AK010375 mRNA. Translation: BAB26893.1 . Different initiation.
    AK154232 mRNA. Translation: BAE32451.1 . Different initiation.
    BC026480 mRNA. Translation: AAH26480.1 . Sequence problems.
    BC048362 mRNA. Translation: AAH48362.1 . Different initiation.
    CN836515 mRNA. No translation available.
    CCDSi CCDS29156.2.
    RefSeqi NP_001157878.1. NM_001164406.1.
    NP_079567.2. NM_025291.3.
    UniGenei Mm.29058.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2YRU NMR - A 102-206 [» ]
    ProteinModelPortali Q80VJ2.
    SMRi Q80VJ2. Positions 99-207.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204880. 2 interactions.
    IntActi Q80VJ2. 2 interactions.
    MINTi MINT-4125677.

    PTM databases

    PhosphoSitei Q80VJ2.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00317966.

    Proteomic databases

    MaxQBi Q80VJ2.
    PaxDbi Q80VJ2.
    PRIDEi Q80VJ2.

    Protocols and materials databases

    DNASUi 24068.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000173875 ; ENSMUSP00000133360 ; ENSMUSG00000006050 .
    GeneIDi 24068.
    KEGGi mmu:24068.
    UCSCi uc008eny.2. mouse.

    Organism-specific databases

    CTDi 10011.
    MGIi MGI:1344414. Sra1.

    Phylogenomic databases

    eggNOGi NOG44276.
    GeneTreei ENSGT00390000001803.
    HOGENOMi HOG000127508.
    HOVERGENi HBG061820.
    InParanoidi Q80VJ2.
    OMAi QTQTGGP.
    OrthoDBi EOG790G2V.
    TreeFami TF314789.

    Miscellaneous databases

    EvolutionaryTracei Q80VJ2.
    NextBioi 304045.
    PROi Q80VJ2.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q80VJ2.
    CleanExi MM_SRA1.
    Genevestigatori Q80VJ2.

    Family and domain databases

    InterProi IPR009917. SRA1-protein/COPII_Sec31.
    [Graphical view ]
    Pfami PF07304. SRA1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    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(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-232.
      Strain: C57BL/6JImported and NODImported.
      Tissue: Embryonic stem cellImported and TestisImported.
    3. "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 10-232.
      Strain: Czech IIImported.
      Tissue: EyeImported, Mammary glandImported and Testis.
    4. "Regulation of nuclear receptor activity by a pseudouridine synthase through posttranscriptional modification of steroid receptor RNA activator."
      Zhao X., Patton J.R., Davis S.L., Florence B., Ames S.J., Spanjaard R.A.
      Mol. Cell 15:549-558(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH PUS1 AND RARG.
    5. "Solution structure of mouse steroid receptor RNA activator 1 (SRA1) protein."
      RIKEN structural genomics initiative (RSGI)
      Submitted (APR-2008) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 99-207.

    Entry informationi

    Entry nameiSRA1_MOUSE
    AccessioniPrimary (citable) accession number: Q80VJ2
    Secondary accession number(s): E9QM44
    , Q8R0S3, Q9CWU7, Q9D973
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2006
    Last sequence update: June 28, 2011
    Last modified: October 1, 2014
    This is version 91 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Appears to be the first example of a new class of functional RNAs also able to encode a protein.By similarity

    Keywords - Technical termi

    3D-structure, Complete proteome, 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3