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P82933

- RT09_HUMAN

UniProt

P82933 - RT09_HUMAN

Protein

28S ribosomal protein S9, mitochondrial

Gene

MRPS9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 2 (16 Dec 2008)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. structural constituent of ribosome Source: InterPro

    GO - Biological processi

    1. DNA damage response, detection of DNA damage Source: UniProtKB
    2. peptide biosynthetic process Source: UniProtKB
    3. translation Source: InterPro

    Keywords - Molecular functioni

    Ribonucleoprotein, Ribosomal protein

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    28S ribosomal protein S9, mitochondrial
    Short name:
    MRP-S9
    Short name:
    S9mt
    Gene namesi
    Name:MRPS9
    Synonyms:RPMS9
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:14501. MRPS9.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial small ribosomal subunit Source: UniProtKB
    2. mitochondrion Source: HPA
    3. nucleolus Source: HPA

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31028.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 39628S ribosomal protein S9, mitochondrialPRO_0000030655
    Transit peptidei1 – ?MitochondrionSequence Analysis

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei287 – 2871N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP82933.
    PaxDbiP82933.
    PRIDEiP82933.

    PTM databases

    PhosphoSiteiP82933.

    Expressioni

    Gene expression databases

    ArrayExpressiP82933.
    BgeeiP82933.
    CleanExiHS_MRPS9.
    GenevestigatoriP82933.

    Organism-specific databases

    HPAiHPA043476.
    HPA048479.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    revP046182EBI-721385,EBI-6164309From a different organism.

    Protein-protein interaction databases

    BioGridi122360. 42 interactions.
    IntActiP82933. 9 interactions.
    MINTiMINT-1379488.
    STRINGi9606.ENSP00000258455.

    Structurei

    3D structure databases

    ProteinModelPortaliP82933.
    SMRiP82933. Positions 274-389.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein S9P family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0103.
    HOGENOMiHOG000020877.
    HOVERGENiHBG023132.
    InParanoidiP82933.
    KOiK02996.
    OMAiARPVMKH.
    OrthoDBiEOG79PJPF.
    PhylomeDBiP82933.
    TreeFamiTF106154.

    Family and domain databases

    Gene3Di3.30.230.10. 1 hit.
    InterProiIPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    IPR000754. Ribosomal_S9.
    IPR020574. Ribosomal_S9_CS.
    [Graphical view]
    PANTHERiPTHR21569. PTHR21569. 1 hit.
    PfamiPF00380. Ribosomal_S9. 1 hit.
    [Graphical view]
    SUPFAMiSSF54211. SSF54211. 1 hit.
    PROSITEiPS00360. RIBOSOMAL_S9. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P82933-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAPCVSYGG AVSYRLLLWG RGSLARKQGL WKTAAPELQT NVRSQILRLR    50
    HTAFVIPKKN VPTSKRETYT EDFIKKQIEE FNIGKRHLAN MMGEDPETFT 100
    QEDIDRAIAY LFPSGLFEKR ARPVMKHPEQ IFPRQRAIQW GEDGRPFHYL 150
    FYTGKQSYYS LMHDVYGMLL NLEKHQSHLQ AKSLLPEKTV TRDVIGSRWL 200
    IKEELEEMLV EKLSDLDYMQ FIRLLEKLLT SQCGAAEEEF VQRFRRSVTL 250
    ESKKQLIEPV QYDEQGMAFS KSEGKRKTAK AEAIVYKHGS GRIKVNGIDY 300
    QLYFPITQDR EQLMFPFHFV DRLGKHDVTC TVSGGGRSAQ AGAIRLAMAK 350
    ALCSFVTEDE VEWMRQAGLL TTDPRVRERK KPGQEGARRK FTWKKR 396
    Length:396
    Mass (Da):45,835
    Last modified:December 16, 2008 - v2
    Checksum:i74412E34F0926360
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti13 – 131S → L.
    Corresponds to variant rs13399067 [ dbSNP | Ensembl ].
    VAR_047902

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC010884 Genomic DNA. No translation available.
    AC107080 Genomic DNA. No translation available.
    AC104655 Genomic DNA. No translation available.
    CH471127 Genomic DNA. Translation: EAX01767.1.
    BC057240 mRNA. Translation: AAH57240.1.
    CCDSiCCDS2065.1.
    RefSeqiNP_872578.1. NM_182640.2.
    UniGeneiHs.590900.

    Genome annotation databases

    EnsembliENST00000258455; ENSP00000258455; ENSG00000135972.
    GeneIDi64965.
    KEGGihsa:64965.
    UCSCiuc002tcn.4. human.

    Polymorphism databases

    DMDMi218511769.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC010884 Genomic DNA. No translation available.
    AC107080 Genomic DNA. No translation available.
    AC104655 Genomic DNA. No translation available.
    CH471127 Genomic DNA. Translation: EAX01767.1 .
    BC057240 mRNA. Translation: AAH57240.1 .
    CCDSi CCDS2065.1.
    RefSeqi NP_872578.1. NM_182640.2.
    UniGenei Hs.590900.

    3D structure databases

    ProteinModelPortali P82933.
    SMRi P82933. Positions 274-389.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122360. 42 interactions.
    IntActi P82933. 9 interactions.
    MINTi MINT-1379488.
    STRINGi 9606.ENSP00000258455.

    PTM databases

    PhosphoSitei P82933.

    Polymorphism databases

    DMDMi 218511769.

    Proteomic databases

    MaxQBi P82933.
    PaxDbi P82933.
    PRIDEi P82933.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000258455 ; ENSP00000258455 ; ENSG00000135972 .
    GeneIDi 64965.
    KEGGi hsa:64965.
    UCSCi uc002tcn.4. human.

    Organism-specific databases

    CTDi 64965.
    GeneCardsi GC02P105654.
    HGNCi HGNC:14501. MRPS9.
    HPAi HPA043476.
    HPA048479.
    MIMi 611975. gene.
    neXtProti NX_P82933.
    PharmGKBi PA31028.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0103.
    HOGENOMi HOG000020877.
    HOVERGENi HBG023132.
    InParanoidi P82933.
    KOi K02996.
    OMAi ARPVMKH.
    OrthoDBi EOG79PJPF.
    PhylomeDBi P82933.
    TreeFami TF106154.

    Miscellaneous databases

    GenomeRNAii 64965.
    NextBioi 67144.
    PROi P82933.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P82933.
    Bgeei P82933.
    CleanExi HS_MRPS9.
    Genevestigatori P82933.

    Family and domain databases

    Gene3Di 3.30.230.10. 1 hit.
    InterProi IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    IPR000754. Ribosomal_S9.
    IPR020574. Ribosomal_S9_CS.
    [Graphical view ]
    PANTHERi PTHR21569. PTHR21569. 1 hit.
    Pfami PF00380. Ribosomal_S9. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54211. SSF54211. 1 hit.
    PROSITEi PS00360. RIBOSOMAL_S9. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
    4. "The small subunit of the mammalian mitochondrial ribosome: identification of the full complement of ribosomal proteins present."
      Koc E.C., Burkhart W., Blackburn K., Moseley A., Spremulli L.L.
      J. Biol. Chem. 276:19363-19374(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION.
    5. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-287, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRT09_HUMAN
    AccessioniPrimary (citable) accession number: P82933
    Secondary accession number(s): Q6PG40
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2002
    Last sequence update: December 16, 2008
    Last modified: October 1, 2014
    This is version 110 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Ribosomal proteins
      Ribosomal proteins families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3