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Q9ER88

- RT29_MOUSE

UniProt

Q9ER88 - RT29_MOUSE

Protein

28S ribosomal protein S29, mitochondrial

Gene

Dap3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Involved in mediating interferon-gamma-induced cell death.By similarity

    GO - Biological processi

    1. apoptotic mitochondrial changes Source: MGI

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Keywords - Biological processi

    Apoptosis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    28S ribosomal protein S29, mitochondrial
    Short name:
    MRP-S29
    Short name:
    S29mt
    Alternative name(s):
    Death-associated protein 3
    Short name:
    DAP-3
    Gene namesi
    Name:Dap3
    Synonyms:Mrps29
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:1929538. Dap3.

    Subcellular locationi

    Mitochondrion By similarity

    GO - Cellular componenti

    1. mitochondrial matrix Source: MGI
    2. mitochondrial ribosome Source: InterPro
    3. mitochondrion Source: MGI
    4. small ribosomal subunit Source: InterPro

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 1717MitochondrionBy similarityAdd
    BLAST
    Chaini18 – 39137428S ribosomal protein S29, mitochondrialPRO_0000087718Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei168 – 1681N6-acetyllysineBy similarity
    Modified residuei200 – 2001N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9ER88.
    PaxDbiQ9ER88.
    PRIDEiQ9ER88.

    PTM databases

    PhosphoSiteiQ9ER88.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9ER88.
    BgeeiQ9ER88.
    CleanExiMM_DAP3.
    GenevestigatoriQ9ER88.

    Interactioni

    Subunit structurei

    Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins. Interacts with KIAA0141. Interacts with NOA1 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi211134. 8 interactions.
    IntActiQ9ER88. 2 interactions.
    MINTiMINT-1849208.
    STRINGi10090.ENSMUSP00000088456.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9ER88.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiNOG260931.
    GeneTreeiENSGT00390000015248.
    HOVERGENiHBG025946.
    InParanoidiQ9ER88.
    KOiK17408.
    PhylomeDBiQ9ER88.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR019368. Ribosomal_S23/S29_mit.
    IPR008092. Ribosomal_S29_mit.
    [Graphical view]
    PfamiPF10236. DAP3. 1 hit.
    [Graphical view]
    PRINTSiPR01716. DEATHASSOCP3.

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9ER88-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MLTGITRLFS RVQKLDPRCF LHMSVQATQN SQVPAERPRT VSRTSDSDPA    50
    KHGEQHEGQH YSIPLQDLKT VFPHGLPPRY MMQVKTFGEA CLMVRKPALE 100
    LLGYLKNTNF AHPAVRYLLY GEKGTGKTLS LCHAVHFCAR HDWLILHIPD 150
    AHLWVKNCRE LLQSTHNKQR FDQPLEASTW LKNFKTTNER FLSQIKVQEK 200
    YVWNKRESTE KGSPLGEVVE QGLTRVRNAT DAVGVVLKEL KAQSALGLFH 250
    LLVAVDGVNA LWGRTTLKKE DRTLIAPEEL SLVHNLRKMV KNDWHGGAIV 300
    LSLSQTGSLF KSRTAYLPHE LLGKEGFNAL EPFLPILIPN YNPKEFESSF 350
    QYYLENNWLQ HEKASTEEGR KELRFLSNCN PEQLERLCAS L 391
    Length:391
    Mass (Da):44,699
    Last modified:March 1, 2001 - v1
    Checksum:i038AC9DA7A61FFF4
    GO
    Isoform 2 (identifier: Q9ER88-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         295-324: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:361
    Mass (Da):41,536
    Checksum:i2F708608DB27B4D1
    GO

    Sequence cautioni

    The sequence BAB29240.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAB29605.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAC27790.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAC40673.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti90 – 901A → R in BAB29605. (PubMed:16141072)Curated
    Sequence conflicti141 – 1411H → N in BAC27790. (PubMed:16141072)Curated
    Sequence conflicti177 – 1771A → G in BAB29605. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei295 – 32430Missing in isoform 2. 1 PublicationVSP_008916Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ250375 mRNA. Translation: CAC05583.1.
    AK014889 mRNA. Translation: BAB29605.1. Different initiation.
    AK014280 mRNA. Translation: BAB29240.3. Different initiation.
    AK021250 mRNA. No translation available.
    AK032275 mRNA. Translation: BAC27790.1. Different initiation.
    AK088960 mRNA. Translation: BAC40673.1. Different initiation.
    BC019566 mRNA. Translation: AAH19566.2.
    RefSeqiNP_001158005.1. NM_001164533.1.
    NP_075370.2. NM_022994.3.
    XP_006501925.1. XM_006501862.1. [Q9ER88-1]
    XP_006501926.1. XM_006501863.1. [Q9ER88-1]
    XP_006501927.1. XM_006501864.1. [Q9ER88-1]
    XP_006501932.1. XM_006501869.1. [Q9ER88-1]
    UniGeneiMm.29028.
    Mm.400397.

    Genome annotation databases

    EnsembliENSMUST00000107491; ENSMUSP00000103115; ENSMUSG00000068921.
    ENSMUST00000173135; ENSMUSP00000134422; ENSMUSG00000068921. [Q9ER88-1]
    GeneIDi65111.
    KEGGimmu:65111.
    UCSCiuc008pxh.2. mouse. [Q9ER88-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ250375 mRNA. Translation: CAC05583.1 .
    AK014889 mRNA. Translation: BAB29605.1 . Different initiation.
    AK014280 mRNA. Translation: BAB29240.3 . Different initiation.
    AK021250 mRNA. No translation available.
    AK032275 mRNA. Translation: BAC27790.1 . Different initiation.
    AK088960 mRNA. Translation: BAC40673.1 . Different initiation.
    BC019566 mRNA. Translation: AAH19566.2 .
    RefSeqi NP_001158005.1. NM_001164533.1.
    NP_075370.2. NM_022994.3.
    XP_006501925.1. XM_006501862.1. [Q9ER88-1 ]
    XP_006501926.1. XM_006501863.1. [Q9ER88-1 ]
    XP_006501927.1. XM_006501864.1. [Q9ER88-1 ]
    XP_006501932.1. XM_006501869.1. [Q9ER88-1 ]
    UniGenei Mm.29028.
    Mm.400397.

    3D structure databases

    ProteinModelPortali Q9ER88.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 211134. 8 interactions.
    IntActi Q9ER88. 2 interactions.
    MINTi MINT-1849208.
    STRINGi 10090.ENSMUSP00000088456.

    PTM databases

    PhosphoSitei Q9ER88.

    Proteomic databases

    MaxQBi Q9ER88.
    PaxDbi Q9ER88.
    PRIDEi Q9ER88.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000107491 ; ENSMUSP00000103115 ; ENSMUSG00000068921 .
    ENSMUST00000173135 ; ENSMUSP00000134422 ; ENSMUSG00000068921 . [Q9ER88-1 ]
    GeneIDi 65111.
    KEGGi mmu:65111.
    UCSCi uc008pxh.2. mouse. [Q9ER88-2 ]

    Organism-specific databases

    CTDi 7818.
    MGIi MGI:1929538. Dap3.

    Phylogenomic databases

    eggNOGi NOG260931.
    GeneTreei ENSGT00390000015248.
    HOVERGENi HBG025946.
    InParanoidi Q9ER88.
    KOi K17408.
    PhylomeDBi Q9ER88.

    Miscellaneous databases

    NextBioi 320301.
    PROi Q9ER88.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9ER88.
    Bgeei Q9ER88.
    CleanExi MM_DAP3.
    Genevestigatori Q9ER88.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR019368. Ribosomal_S23/S29_mit.
    IPR008092. Ribosomal_S29_mit.
    [Graphical view ]
    Pfami PF10236. DAP3. 1 hit.
    [Graphical view ]
    PRINTSi PR01716. DEATHASSOCP3.
    ProtoNeti Search...

    Publicationsi

    1. "The apoptosis mediator mDAP-3 is a novel member of a conserved family of mitochondrial proteins."
      Berger T., Brigl M., Herrmann J.M., Vielhauer V., Luckow B., Schloendorff D., Kretzler M.
      J. Cell Sci. 113:3603-3612(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Embryonic kidney.
    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] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J, FVB/N and NOD.
      Tissue: Embryo, Embryonic head, Olfactory bulb, Testis and Thymus.
    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] (ISOFORM 1).
      Strain: FVB/N.
      Tissue: Kidney.

    Entry informationi

    Entry nameiRT29_MOUSE
    AccessioniPrimary (citable) accession number: Q9ER88
    Secondary accession number(s): Q8C2B2
    , Q8CCQ8, Q8VCK8, Q9CRT4, Q9CS11, Q9D5V9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 19, 2002
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 97 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

    External Data

    Dasty 3