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Q9H0W8

- SMG9_HUMAN

UniProt

Q9H0W8 - SMG9_HUMAN

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Protein

Protein SMG9

Gene

SMG9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

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
Complete GO annotation...

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
Complete GO annotation...

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 – 71Phosphoserine3 Publications
Modified residuei32 – 321Phosphoserine3 Publications
Modified residuei53 – 531Phosphoserine2 Publications
Modified residuei451 – 4511Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated by SMG1.6 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9H0W8.
PaxDbiQ9H0W8.
PRIDEiQ9H0W8.

PTM databases

PhosphoSiteiQ9H0W8.

Expressioni

Gene expression databases

BgeeiQ9H0W8.
CleanExiHS_C19orf61.
ExpressionAtlasiQ9H0W8. baseline and differential.
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 207-275.
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.
GeneTreeiENSGT00390000003568.
HOGENOMiHOG000006915.
InParanoidiQ9H0W8.
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

        10         20         30         40         50
MSESGHSQPG LYGIERRRRW KEPGSGGPQN LSGPGGRERD YIAPWERERR
60 70 80 90 100
DASEETSTSV MQKTPIILSK PPAERSKQPP PPTAPAAPPA PAPLEKPIVL
110 120 130 140 150
MKPREEGKGP VAVTGASTPE GTAPPPPAAP APPKGEKEGQ RPTQPVYQIQ
160 170 180 190 200
NRGMGTAAPA AMDPVVGQAK LLPPERMKHS IKLVDDQMNW CDSAIEYLLD
210 220 230 240 250
QTDVLVVGVL GLQGTGKSMV MSLLSANTPE EDQRTYVFRA QSAEMKERGG
260 270 280 290 300
NQTSGIDFFI TQERIVFLDT QPILSPSILD HLINNDRKLP PEYNLPHTYV
310 320 330 340 350
EMQSLQIAAF LFTVCHVVIV VQDWFTDLSL YRFLQTAEMV KPSTPSPSHE
360 370 380 390 400
SSSSSGSDEG TEYYPHLVFL QNKARREDFC PRKLRQMHLM IDQLMAHSHL
410 420 430 440 450
RYKGTLSMLQ CNVFPGLPPD FLDSEVNLFL VPFMDSEAES ENPPRAGPGS
460 470 480 490 500
SPLFSLLPGY RGHPSFQSLV SKLRSQVMSM ARPQLSHTIL TEKNWFHYAA
510 520
RIWDGVRKSS ALAEYSRLLA
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 207-275.
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.
GeneTreei ENSGT00390000003568.
HOGENOMi HOG000006915.
InParanoidi Q9H0W8.
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

Bgeei Q9H0W8.
CleanExi HS_C19orf61.
ExpressionAtlasi Q9H0W8. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 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
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