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Protein

Protein SMG8

Gene

Smg8

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 2 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 SMG9 (forming the SMG1C protein kinase complex) and, in the SMG1C complex, is required to mediate the recruitment of SMG1 to the ribosome:SURF complex and to suppress SMG1 kinase activity until the ribosome:SURF complex locates the exon junction complex (EJC). Acts as a regulator of kinase activity (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Nonsense-mediated mRNA decay

Enzyme and pathway databases

ReactomeiR-MMU-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
Protein SMG8
Alternative name(s):
Protein smg-8 homolog
Gene namesi
Name:Smg8
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1921383. Smg8.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 991991Protein SMG8PRO_0000304975Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei115 – 1151PhosphoserineBy similarity
Modified residuei469 – 4691PhosphoserineBy similarity
Modified residuei668 – 6681PhosphoserineBy similarity
Modified residuei742 – 7421PhosphoserineBy similarity
Modified residuei895 – 8951PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by SMG1.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8VE18.
MaxQBiQ8VE18.
PaxDbiQ8VE18.
PeptideAtlasiQ8VE18.
PRIDEiQ8VE18.

PTM databases

iPTMnetiQ8VE18.
PhosphoSiteiQ8VE18.

Expressioni

Gene expression databases

BgeeiQ8VE18.
CleanExiMM_1200011M11RIK.
ExpressionAtlasiQ8VE18. baseline and differential.
GenevisibleiQ8VE18. MM.

Interactioni

Subunit structurei

Component of the SMG1C complex composed of SMG1, SMG8 and SMG9; the recruitment of SMG8 to SMG1 N-terminus induces a large conformational change in the SMG1 C-terminal head domain containing the catalytic domain. Forms heterodimers with SMG9; this assembly form may represent a SMG1C intermediate form (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000020801.

Family & Domainsi

Sequence similaritiesi

Belongs to the SMG8 family.Curated

Phylogenomic databases

eggNOGiKOG3692. Eukaryota.
ENOG410Y30B. LUCA.
GeneTreeiENSGT00390000018533.
HOGENOMiHOG000154346.
InParanoidiQ8VE18.
KOiK18734.
OMAiNCGRTQG.
OrthoDBiEOG7S4X5N.
PhylomeDBiQ8VE18.
TreeFamiTF323445.

Family and domain databases

InterProiIPR028802. SMG8.
IPR019354. Smg8/Smg9.
[Graphical view]
PANTHERiPTHR13091:SF0. PTHR13091:SF0. 3 hits.
PfamiPF10220. DUF2146. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8VE18-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGPVSLREL LMGASAWLGS ESPGGPSAEG GGNAAGTPEP PWREDEICVV
60 70 80 90 100
GIFGKTALRL NSEKFSLVNT VCDRQVFPLF HHQDPGDPGT GIKTKAVSVG
110 120 130 140 150
EAGGAGDPGA AAGDSLRGGM ATAEGNRAEP GPQDFSLLQA YYNQESKVLY
160 170 180 190 200
LILTSICDNS QLLRACRALQ SGEAGGGLSL PHAETHEFWK HQEKLQCLSL
210 220 230 240 250
LYLFSVCHIL LLVHPTCSFD ITYDRVFRAL DGLRQKVLPL LKTAIKDCPV
260 270 280 290 300
GKDWKLNCRP CPPRLLFLFQ LNGALKVEPP RSQDTAHPDK PKKHSPKRRL
310 320 330 340 350
QHALEDQIYR IFRKSRVLTN QSINCLFTVP ANQAFVYIVP GSQEEDPIGM
360 370 380 390 400
LLDQLRSHCT VKDPESLLVP APLSGPRRYQ AMRQHSRQQL SFHIDSSTSS
410 420 430 440 450
SSGQLVDFTL REFLWQHVEL VLSKKGFDDS VGRNPQPSHF ELPTYQKWIS
460 470 480 490 500
AAAKLYEVAI DGKEEDLGSP TGELTSKILS SIKVLEGFLD IDTKFSENRC
510 520 530 540 550
QKALPMAHSA YQSNLPHNYT MTVHKNQLAQ ALRVYSQHAR GPAFHKYAMQ
560 570 580 590 600
LHEDCYKFWS NGHQLCEERS LTDQHCVHKF HSLPKSGEKP EADRNPPVLY
610 620 630 640 650
HNSRARSTGA CNCGRKQAPR DDPFDIKAAN YDFYQLLEEK CCGKLDHINF
660 670 680 690 700
PVFEPSTPDP APAKNEPSPA PPDSDAEKLK EKEPQTQGES TSLSLALSLG
710 720 730 740 750
QSTDSLGTYP ADPQAGGDNP EVHGQGEGKS EKRPNLVDRQ ASTVEYLPGM
760 770 780 790 800
LHSNCPKGLL PKFSSWSLVK LGPAKSYNFH TGLDQQGFVP GTNYLMPWDI
810 820 830 840 850
VIRTRAEDEG DLDTNSWPAP NKAIPGKRSA VVMGRGRRRD DIARAFVGFE
860 870 880 890 900
YEDSRGRRFM CSGPDKVMKV MGSGPKESAL KALNSDMPLY ILSSSQGRGL
910 920 930 940 950
KPHYAQLMRL FVVVPDAPLQ IILMPQVQPG PPPCPVFYPE KQEITLPPDG
960 970 980 990
LWVLRFPYAY VTERGPCFPP KENVQLMSYK VLRGVLKAVT Q
Length:991
Mass (Da):109,667
Last modified:March 1, 2002 - v1
Checksum:i14A43C60C8054413
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti222 – 2221T → N in BAC27255 (PubMed:16141072).Curated
Sequence conflicti829 – 8291S → R in BAC27255 (PubMed:16141072).Curated
Sequence conflicti845 – 8451A → D in BAC27255 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004714 mRNA. Translation: BAB23498.2.
AK031106 mRNA. Translation: BAC27255.1.
AK035089 mRNA. Translation: BAC28941.1.
AL713917 Genomic DNA. Translation: CAI25313.1.
CU407131 Genomic DNA. Translation: CAQ51995.1.
BC020005 mRNA. Translation: AAH20005.1.
CCDSiCCDS25207.1.
RefSeqiNP_077224.1. NM_024262.1.
UniGeneiMm.23257.

Genome annotation databases

EnsembliENSMUST00000020801; ENSMUSP00000020801; ENSMUSG00000020495.
GeneIDi74133.
KEGGimmu:74133.
UCSCiuc007ktg.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004714 mRNA. Translation: BAB23498.2.
AK031106 mRNA. Translation: BAC27255.1.
AK035089 mRNA. Translation: BAC28941.1.
AL713917 Genomic DNA. Translation: CAI25313.1.
CU407131 Genomic DNA. Translation: CAQ51995.1.
BC020005 mRNA. Translation: AAH20005.1.
CCDSiCCDS25207.1.
RefSeqiNP_077224.1. NM_024262.1.
UniGeneiMm.23257.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000020801.

PTM databases

iPTMnetiQ8VE18.
PhosphoSiteiQ8VE18.

Proteomic databases

EPDiQ8VE18.
MaxQBiQ8VE18.
PaxDbiQ8VE18.
PeptideAtlasiQ8VE18.
PRIDEiQ8VE18.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020801; ENSMUSP00000020801; ENSMUSG00000020495.
GeneIDi74133.
KEGGimmu:74133.
UCSCiuc007ktg.1. mouse.

Organism-specific databases

CTDi55181.
MGIiMGI:1921383. Smg8.

Phylogenomic databases

eggNOGiKOG3692. Eukaryota.
ENOG410Y30B. LUCA.
GeneTreeiENSGT00390000018533.
HOGENOMiHOG000154346.
InParanoidiQ8VE18.
KOiK18734.
OMAiNCGRTQG.
OrthoDBiEOG7S4X5N.
PhylomeDBiQ8VE18.
TreeFamiTF323445.

Enzyme and pathway databases

ReactomeiR-MMU-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

PROiQ8VE18.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VE18.
CleanExiMM_1200011M11RIK.
ExpressionAtlasiQ8VE18. baseline and differential.
GenevisibleiQ8VE18. MM.

Family and domain databases

InterProiIPR028802. SMG8.
IPR019354. Smg8/Smg9.
[Graphical view]
PANTHERiPTHR13091:SF0. PTHR13091:SF0. 3 hits.
PfamiPF10220. DUF2146. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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].
    Strain: C57BL/6J.
    Tissue: Embryo, Forelimb and Lung.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Liver, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiSMG8_MOUSE
AccessioniPrimary (citable) accession number: Q8VE18
Secondary accession number(s): B2KGQ4
, Q8BS62, Q8BSP7, Q9DBW6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: March 1, 2002
Last modified: July 6, 2016
This is version 98 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
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.