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Protein

Small nuclear ribonucleoprotein G

Gene

Snrpg

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in an heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. Appears to function in the U7 snRNP complex that is involved in histone 3'-end processing (By similarity).By similarity

GO - Molecular functioni

  1. RNA binding Source: UniProtKB-KW

GO - Biological processi

  1. spliceosomal snRNP assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_206812. snRNP Assembly.
REACT_215668. SLBP independent Processing of Histone Pre-mRNAs.
REACT_235610. mRNA Splicing - Minor Pathway.
REACT_235695. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
REACT_260226. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Small nuclear ribonucleoprotein G
Short name:
snRNP-G
Alternative name(s):
Sm protein G
Short name:
Sm-G
Short name:
SmG
Gene namesi
Name:Snrpg
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17, UP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:1915261. Snrpg.

Subcellular locationi

Cytoplasmcytosol By similarity. Nucleus By similarity
Note: SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes.By similarity

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. methylosome Source: UniProtKB
  3. SMN-Sm protein complex Source: UniProtKB
  4. spliceosomal complex Source: UniProtKB-KW
  5. U1 snRNP Source: UniProtKB
  6. U4 snRNP Source: UniProtKB
  7. U7 snRNP Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7676Small nuclear ribonucleoprotein GPRO_0000125546Add
BLAST

Proteomic databases

MaxQBiP62309.
PaxDbiP62309.
PRIDEiP62309.

PTM databases

PhosphoSiteiP62309.

Expressioni

Gene expression databases

BgeeiP62309.
CleanExiMM_SNRPG.
ExpressionAtlasiP62309. baseline and differential.
GenevestigatoriP62309.

Interactioni

Subunit structurei

U1 snRNP is for instance composed of the 7 core Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in an heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP, and at least three U1 snRNP-specific proteins SNRNP70/U1-70K, SNRPA/U1-A and SNRPC/U1-C. Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Component of the heptameric ring U7 snRNP complex, or U7 Sm protein core complex, at least composed of LSM10, LSM11, SNRPB, SNRPD3, SNRPE, SNRPF, SNRPG and U7 snRNA. Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG; catalyzes core snRNPs assembly. Forms a 6S pICln-Sm complex composed of CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-like structure where CLNS1A/pICln mimics additional Sm proteins and which is unable to assemble into the core snRNP. Interacts with TACC1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi212595. 1 interaction.
IntActiP62309. 1 interaction.
MINTiMINT-4133513.

Structurei

3D structure databases

ProteinModelPortaliP62309.
SMRiP62309. Positions 7-74.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the snRNP Sm proteins family.Curated

Phylogenomic databases

eggNOGiCOG1958.
GeneTreeiENSGT00510000046985.
HOVERGENiHBG000513.
InParanoidiP62309.
KOiK11099.
OMAiEKERIGM.
OrthoDBiEOG7S221K.
PhylomeDBiP62309.
TreeFamiTF315099.

Family and domain databases

InterProiIPR010920. LSM_dom.
IPR001163. Ribonucl_LSM.
IPR006649. Ribonucl_LSM_euk/arc.
[Graphical view]
PfamiPF01423. LSM. 1 hit.
[Graphical view]
SMARTiSM00651. Sm. 1 hit.
[Graphical view]
SUPFAMiSSF50182. SSF50182. 1 hit.

Sequencei

Sequence statusi: Complete.

P62309-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKAHPPELK KFMDKKLSLK LNGGRHVQGI LRGFDPFMNL VIDECVEMAT
60 70
SGQQNNIGMV VIRGNSIIML EALERV
Length:76
Mass (Da):8,496
Last modified:July 5, 2004 - v1
Checksum:i623302BF6BE758FE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012802 mRNA. Translation: BAB28480.1.
AK013235 mRNA. Translation: BAB28732.1.
BC027499 mRNA. Translation: AAH27499.1.
BC051470 mRNA. Translation: AAH51470.1.
BC094411 mRNA. Translation: AAH94411.1.
CCDSiCCDS39541.1.
RefSeqiNP_080782.1. NM_026506.2.
UniGeneiMm.276802.

Genome annotation databases

EnsembliENSMUST00000053575; ENSMUSP00000137416; ENSMUSG00000049124.
ENSMUST00000089558; ENSMUSP00000086987; ENSMUSG00000057278.
GeneIDi68011.
KEGGimmu:68011.
UCSCiuc009crm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012802 mRNA. Translation: BAB28480.1.
AK013235 mRNA. Translation: BAB28732.1.
BC027499 mRNA. Translation: AAH27499.1.
BC051470 mRNA. Translation: AAH51470.1.
BC094411 mRNA. Translation: AAH94411.1.
CCDSiCCDS39541.1.
RefSeqiNP_080782.1. NM_026506.2.
UniGeneiMm.276802.

3D structure databases

ProteinModelPortaliP62309.
SMRiP62309. Positions 7-74.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212595. 1 interaction.
IntActiP62309. 1 interaction.
MINTiMINT-4133513.

PTM databases

PhosphoSiteiP62309.

Proteomic databases

MaxQBiP62309.
PaxDbiP62309.
PRIDEiP62309.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000053575; ENSMUSP00000137416; ENSMUSG00000049124.
ENSMUST00000089558; ENSMUSP00000086987; ENSMUSG00000057278.
GeneIDi68011.
KEGGimmu:68011.
UCSCiuc009crm.1. mouse.

Organism-specific databases

CTDi6637.
MGIiMGI:1915261. Snrpg.

Phylogenomic databases

eggNOGiCOG1958.
GeneTreeiENSGT00510000046985.
HOVERGENiHBG000513.
InParanoidiP62309.
KOiK11099.
OMAiEKERIGM.
OrthoDBiEOG7S221K.
PhylomeDBiP62309.
TreeFamiTF315099.

Enzyme and pathway databases

ReactomeiREACT_206812. snRNP Assembly.
REACT_215668. SLBP independent Processing of Histone Pre-mRNAs.
REACT_235610. mRNA Splicing - Minor Pathway.
REACT_235695. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
REACT_260226. mRNA Splicing - Major Pathway.

Miscellaneous databases

NextBioi25857.
PROiP62309.
SOURCEiSearch...

Gene expression databases

BgeeiP62309.
CleanExiMM_SNRPG.
ExpressionAtlasiP62309. baseline and differential.
GenevestigatoriP62309.

Family and domain databases

InterProiIPR010920. LSM_dom.
IPR001163. Ribonucl_LSM.
IPR006649. Ribonucl_LSM_euk/arc.
[Graphical view]
PfamiPF01423. LSM. 1 hit.
[Graphical view]
SMARTiSM00651. Sm. 1 hit.
[Graphical view]
SUPFAMiSSF50182. SSF50182. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
  2. "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: C57BL/6J.
    Tissue: Mammary gland and Thymus.
  3. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-10, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.

Entry informationi

Entry nameiRUXG_MOUSE
AccessioniPrimary (citable) accession number: P62309
Secondary accession number(s): Q15357, Q52KC7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: July 5, 2004
Last modified: January 7, 2015
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, Direct protein sequencing, 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

External Data

Dasty 3

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 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.