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Q9H0W8

- SMG9_HUMAN

UniProt

Q9H0W8 - SMG9_HUMAN

Protein

Protein SMG9

Gene

SMG9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons. Is recruited by release factors to stalled ribosomes together with SMG1 and SMG8 (forming the SMG1C protein kinase complex) and, in the SMG1C complex, is required for the efficient association between SMG1 and SMG8.1 Publication

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. gene expression Source: Reactome
    2. mRNA metabolic process Source: Reactome
    3. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
    4. RNA metabolic process Source: Reactome

    Keywords - Biological processi

    Nonsense-mediated mRNA decay

    Enzyme and pathway databases

    ReactomeiREACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein SMG9
    Alternative name(s):
    Protein smg-9 homolog
    Gene namesi
    Name:SMG9
    Synonyms:C19orf61
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:25763. SMG9.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. intracellular Source: LIFEdb

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162378734.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 520519Protein SMG9PRO_0000289163Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei7 – 71Phosphoserine4 Publications
    Modified residuei32 – 321Phosphoserine4 Publications
    Modified residuei53 – 531Phosphoserine3 Publications
    Modified residuei451 – 4511Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated by SMG1.6 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9H0W8.
    PaxDbiQ9H0W8.
    PRIDEiQ9H0W8.

    PTM databases

    PhosphoSiteiQ9H0W8.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9H0W8.
    BgeeiQ9H0W8.
    CleanExiHS_C19orf61.
    GenevestigatoriQ9H0W8.

    Organism-specific databases

    HPAiHPA041763.
    HPA042096.

    Interactioni

    Subunit structurei

    Component of the SMG1C complex composed of SMG1, SMG8 and SMG9. Self-associates to form homodimers and forms heterodimers with SMG8; these assembly forms may represent SMG1C intermediate forms.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-2872322,EBI-2872322
    SMG8Q8ND044EBI-2872322,EBI-3903643

    Protein-protein interaction databases

    BioGridi121029. 7 interactions.
    IntActiQ9H0W8. 5 interactions.
    MINTiMINT-4711590.
    STRINGi9606.ENSP00000270066.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H0W8.
    SMRiQ9H0W8. Positions 198-229.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi71 – 13363Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the SMG9 family.Curated

    Phylogenomic databases

    eggNOGiNOG255645.
    HOGENOMiHOG000006915.
    OMAiHAENPHH.
    OrthoDBiEOG7MPRF3.
    PhylomeDBiQ9H0W8.
    TreeFamiTF319763.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR027417. P-loop_NTPase.
    IPR019354. Smg8/Smg9.
    [Graphical view]
    PfamiPF10220. DUF2146. 1 hit.
    [Graphical view]

    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: Q9H0W8-1) [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

    MSESGHSQPG LYGIERRRRW KEPGSGGPQN LSGPGGRERD YIAPWERERR    50
    DASEETSTSV MQKTPIILSK PPAERSKQPP PPTAPAAPPA PAPLEKPIVL 100
    MKPREEGKGP VAVTGASTPE GTAPPPPAAP APPKGEKEGQ RPTQPVYQIQ 150
    NRGMGTAAPA AMDPVVGQAK LLPPERMKHS IKLVDDQMNW CDSAIEYLLD 200
    QTDVLVVGVL GLQGTGKSMV MSLLSANTPE EDQRTYVFRA QSAEMKERGG 250
    NQTSGIDFFI TQERIVFLDT QPILSPSILD HLINNDRKLP PEYNLPHTYV 300
    EMQSLQIAAF LFTVCHVVIV VQDWFTDLSL YRFLQTAEMV KPSTPSPSHE 350
    SSSSSGSDEG TEYYPHLVFL QNKARREDFC PRKLRQMHLM IDQLMAHSHL 400
    RYKGTLSMLQ CNVFPGLPPD FLDSEVNLFL VPFMDSEAES ENPPRAGPGS 450
    SPLFSLLPGY RGHPSFQSLV SKLRSQVMSM ARPQLSHTIL TEKNWFHYAA 500
    RIWDGVRKSS ALAEYSRLLA 520
    Length:520
    Mass (Da):57,651
    Last modified:March 1, 2001 - v1
    Checksum:iAA68A473F7F6BBCC
    GO
    Isoform 2 (identifier: Q9H0W8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         496-520: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:495
    Mass (Da):54,787
    Checksum:i7831F793135ECF1D
    GO

    Sequence cautioni

    The sequence AAC17932.1 differs from that shown. Reason: Erroneous gene model prediction.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei496 – 52025Missing in isoform 2. 1 PublicationVSP_025946Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL136606 mRNA. Translation: CAB66541.1.
    AK022948 mRNA. Translation: BAB14323.1.
    AC004780 Genomic DNA. Translation: AAC17932.1. Sequence problems.
    BC008869 mRNA. Translation: AAH08869.1.
    CCDSiCCDS33043.2. [Q9H0W8-1]
    RefSeqiNP_061981.2. NM_019108.2. [Q9H0W8-1]
    UniGeneiHs.466875.

    Genome annotation databases

    EnsembliENST00000270066; ENSP00000270066; ENSG00000105771. [Q9H0W8-1]
    ENST00000601170; ENSP00000471398; ENSG00000105771. [Q9H0W8-2]
    GeneIDi56006.
    KEGGihsa:56006.
    UCSCiuc002oxj.2. human. [Q9H0W8-1]

    Polymorphism databases

    DMDMi74733529.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL136606 mRNA. Translation: CAB66541.1 .
    AK022948 mRNA. Translation: BAB14323.1 .
    AC004780 Genomic DNA. Translation: AAC17932.1 . Sequence problems.
    BC008869 mRNA. Translation: AAH08869.1 .
    CCDSi CCDS33043.2. [Q9H0W8-1 ]
    RefSeqi NP_061981.2. NM_019108.2. [Q9H0W8-1 ]
    UniGenei Hs.466875.

    3D structure databases

    ProteinModelPortali Q9H0W8.
    SMRi Q9H0W8. Positions 198-229.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121029. 7 interactions.
    IntActi Q9H0W8. 5 interactions.
    MINTi MINT-4711590.
    STRINGi 9606.ENSP00000270066.

    PTM databases

    PhosphoSitei Q9H0W8.

    Polymorphism databases

    DMDMi 74733529.

    Proteomic databases

    MaxQBi Q9H0W8.
    PaxDbi Q9H0W8.
    PRIDEi Q9H0W8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000270066 ; ENSP00000270066 ; ENSG00000105771 . [Q9H0W8-1 ]
    ENST00000601170 ; ENSP00000471398 ; ENSG00000105771 . [Q9H0W8-2 ]
    GeneIDi 56006.
    KEGGi hsa:56006.
    UCSCi uc002oxj.2. human. [Q9H0W8-1 ]

    Organism-specific databases

    CTDi 56006.
    GeneCardsi GC19M044236.
    HGNCi HGNC:25763. SMG9.
    HPAi HPA041763.
    HPA042096.
    MIMi 613176. gene.
    neXtProti NX_Q9H0W8.
    PharmGKBi PA162378734.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG255645.
    HOGENOMi HOG000006915.
    OMAi HAENPHH.
    OrthoDBi EOG7MPRF3.
    PhylomeDBi Q9H0W8.
    TreeFami TF319763.

    Enzyme and pathway databases

    Reactomei REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

    Miscellaneous databases

    GenomeRNAii 56006.
    NextBioi 61462.
    PROi Q9H0W8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H0W8.
    Bgeei Q9H0W8.
    CleanExi HS_C19orf61.
    Genevestigatori Q9H0W8.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    IPR019354. Smg8/Smg9.
    [Graphical view ]
    Pfami PF10220. DUF2146. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Teratocarcinoma.
    3. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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).
      Tissue: Muscle.
    5. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-53 AND SER-451, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "SMG-8 and SMG-9, two novel subunits of the SMG-1 complex, regulate remodeling of the mRNA surveillance complex during nonsense-mediated mRNA decay."
      Yamashita A., Izumi N., Kashima I., Ohnishi T., Saari B., Katsuhata Y., Muramatsu R., Morita T., Iwamatsu A., Hachiya T., Kurata R., Hirano H., Anderson P., Ohno S.
      Genes Dev. 23:1091-1105(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SMG1C COMPLEX.
    9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 AND SER-32, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "The nonsense-mediated mRNA decay SMG-1 kinase is regulated by large-scale conformational changes controlled by SMG-8."
      Arias-Palomo E., Yamashita A., Fernandez I.S., Nunez-Ramirez R., Bamba Y., Izumi N., Ohno S., Llorca O.
      Genes Dev. 25:153-164(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SMG1 AND SMG8, ELECTRON MICROSCOPY OF THE SMG1C COMPLEX.
    13. "Characterization of SMG-9, an essential component of the nonsense-mediated mRNA decay SMG1C complex."
      Fernandez I.S., Yamashita A., Arias-Palomo E., Bamba Y., Bartolome R.A., Canales M.A., Teixido J., Ohno S., Llorca O.
      Nucleic Acids Res. 39:347-358(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 AND SER-32, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSMG9_HUMAN
    AccessioniPrimary (citable) accession number: Q9H0W8
    Secondary accession number(s): O60429, Q9H9A9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 29, 2007
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 96 of the entry and version 1 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 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3