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Protein

Small nuclear ribonucleoprotein G

Gene

SNRPG

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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.2 Publications

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. gene expression Source: Reactome
  2. histone mRNA metabolic process Source: Reactome
  3. mRNA 3'-end processing Source: Reactome
  4. mRNA splicing, via spliceosome Source: UniProtKB
  5. ncRNA metabolic process Source: Reactome
  6. RNA splicing Source: UniProtKB
  7. spliceosomal complex assembly Source: UniProtKB
  8. spliceosomal snRNP assembly Source: UniProtKB
  9. termination of RNA polymerase II transcription Source: Reactome
  10. transcription from RNA polymerase II promoter Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_11066. snRNP Assembly.
REACT_1364. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
REACT_1753. mRNA Splicing - Minor Pathway.
REACT_185. SLBP independent Processing of Histone Pre-mRNAs.
REACT_387. Cleavage of Growing Transcript in the Termination Region.
REACT_467. 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
Synonyms:PBSCG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:11163. SNRPG.

Subcellular locationi

Cytoplasmcytosol 1 Publication. Nucleus 1 Publication
Note: SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes.

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. methylosome Source: UniProtKB
  4. nucleoplasm Source: Reactome
  5. small nuclear ribonucleoprotein complex Source: UniProtKB
  6. SMN-Sm protein complex Source: UniProtKB
  7. spliceosomal complex Source: UniProtKB
  8. U12-type spliceosomal complex Source: UniProtKB
  9. U1 snRNP Source: UniProtKB
  10. U4 snRNP Source: UniProtKB
  11. U7 snRNP Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36004.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7676Small nuclear ribonucleoprotein GPRO_0000125545Add
BLAST

Proteomic databases

MaxQBiP62308.
PeptideAtlasiP62308.
PRIDEiP62308.

PTM databases

PhosphoSiteiP62308.

Expressioni

Gene expression databases

BgeeiP62308.
CleanExiHS_SNRPG.
ExpressionAtlasiP62308. baseline.
GenevestigatoriP62308.

Organism-specific databases

HPAiHPA064152.

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 TACC1.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SNRPEP623044EBI-624585,EBI-348082
TACC1O75410-15EBI-624585,EBI-624252

Protein-protein interaction databases

BioGridi112521. 42 interactions.
DIPiDIP-34627N.
IntActiP62308. 23 interactions.
MINTiMINT-1527983.
STRINGi9606.ENSP00000272348.

Structurei

Secondary structure

1
76
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni11 – 144Combined sources
Beta strandi16 – 216Combined sources
Turni22 – 243Combined sources
Beta strandi25 – 3410Combined sources
Beta strandi40 – 478Combined sources
Beta strandi57 – 626Combined sources
Beta strandi64 – 718Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CW1X-ray5.493/4/5/G1-76[»]
3PGWX-ray4.40G/J1-76[»]
3S6NX-ray2.50G1-76[»]
4F7UX-ray1.90G/J1-76[»]
4PJOX-ray3.30G/U/g/u1-76[»]
4V98X-ray3.10A4/AH/AP/AX/Af/An/Av/B4/BH/BP/BX/Bf/Bn/Bv/CH/CP/CX/Cf/Cn/Cv1-76[»]
4WZJX-ray3.60AG/AN/AU/BG/BN/BU/CG/CN/CU/DG/DN/DU1-76[»]
ProteinModelPortaliP62308.
SMRiP62308. Positions 7-74.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62308.

Family & Domainsi

Sequence similaritiesi

Belongs to the snRNP Sm proteins family.Curated

Phylogenomic databases

GeneTreeiENSGT00510000046985.
HOVERGENiHBG000513.
InParanoidiP62308.
KOiK11099.
OMAiEKERIGM.
OrthoDBiEOG7S221K.
TreeFamiTF315099.

Family and domain databases

InterProiIPR017132. Lsm7/snRNP-G.
IPR010920. LSM_dom.
IPR001163. Ribonucl_LSM.
IPR006649. Ribonucl_LSM_euk/arc.
[Graphical view]
PfamiPF01423. LSM. 1 hit.
[Graphical view]
PIRSFiPIRSF037188. U6_snRNA_Lsm7. 1 hit.
SMARTiSM00651. Sm. 1 hit.
[Graphical view]
SUPFAMiSSF50182. SSF50182. 1 hit.

Sequencei

Sequence statusi: Complete.

P62308-1 [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
X85373 mRNA. Translation: CAA59689.1.
CR456918 mRNA. Translation: CAG33199.1.
AC079338 Genomic DNA. Translation: AAX81996.1.
CH471053 Genomic DNA. Translation: EAW99817.1.
CH471053 Genomic DNA. Translation: EAW99818.1.
BC000070 mRNA. Translation: AAH00070.1.
BC022432 mRNA. Translation: AAH22432.1.
BC066302 mRNA. Translation: AAH66302.1.
BC070166 mRNA. Translation: AAH70166.1.
BC071880 mRNA. Translation: AAH71880.1.
BC106055 mRNA. Translation: AAI06056.1.
CCDSiCCDS1903.1.
PIRiS55054.
RefSeqiNP_003087.1. NM_003096.2.
UniGeneiHs.465167.
Hs.516076.
Hs.631639.
Hs.654528.

Genome annotation databases

EnsembliENST00000272348; ENSP00000272348; ENSG00000143977.
GeneIDi6637.
KEGGihsa:6637.
UCSCiuc002sgp.3. human.

Polymorphism databases

DMDMi59800216.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85373 mRNA. Translation: CAA59689.1.
CR456918 mRNA. Translation: CAG33199.1.
AC079338 Genomic DNA. Translation: AAX81996.1.
CH471053 Genomic DNA. Translation: EAW99817.1.
CH471053 Genomic DNA. Translation: EAW99818.1.
BC000070 mRNA. Translation: AAH00070.1.
BC022432 mRNA. Translation: AAH22432.1.
BC066302 mRNA. Translation: AAH66302.1.
BC070166 mRNA. Translation: AAH70166.1.
BC071880 mRNA. Translation: AAH71880.1.
BC106055 mRNA. Translation: AAI06056.1.
CCDSiCCDS1903.1.
PIRiS55054.
RefSeqiNP_003087.1. NM_003096.2.
UniGeneiHs.465167.
Hs.516076.
Hs.631639.
Hs.654528.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CW1X-ray5.493/4/5/G1-76[»]
3PGWX-ray4.40G/J1-76[»]
3S6NX-ray2.50G1-76[»]
4F7UX-ray1.90G/J1-76[»]
4PJOX-ray3.30G/U/g/u1-76[»]
4V98X-ray3.10A4/AH/AP/AX/Af/An/Av/B4/BH/BP/BX/Bf/Bn/Bv/CH/CP/CX/Cf/Cn/Cv1-76[»]
4WZJX-ray3.60AG/AN/AU/BG/BN/BU/CG/CN/CU/DG/DN/DU1-76[»]
ProteinModelPortaliP62308.
SMRiP62308. Positions 7-74.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112521. 42 interactions.
DIPiDIP-34627N.
IntActiP62308. 23 interactions.
MINTiMINT-1527983.
STRINGi9606.ENSP00000272348.

PTM databases

PhosphoSiteiP62308.

Polymorphism databases

DMDMi59800216.

Proteomic databases

MaxQBiP62308.
PeptideAtlasiP62308.
PRIDEiP62308.

Protocols and materials databases

DNASUi6637.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000272348; ENSP00000272348; ENSG00000143977.
GeneIDi6637.
KEGGihsa:6637.
UCSCiuc002sgp.3. human.

Organism-specific databases

CTDi6637.
GeneCardsiGC02M070508.
HGNCiHGNC:11163. SNRPG.
HPAiHPA064152.
MIMi603542. gene.
neXtProtiNX_P62308.
PharmGKBiPA36004.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00510000046985.
HOVERGENiHBG000513.
InParanoidiP62308.
KOiK11099.
OMAiEKERIGM.
OrthoDBiEOG7S221K.
TreeFamiTF315099.

Enzyme and pathway databases

ReactomeiREACT_11066. snRNP Assembly.
REACT_1364. SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs.
REACT_1753. mRNA Splicing - Minor Pathway.
REACT_185. SLBP independent Processing of Histone Pre-mRNAs.
REACT_387. Cleavage of Growing Transcript in the Termination Region.
REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSiSNRPG. human.
EvolutionaryTraceiP62308.
GeneWikiiSNRPG.
GenomeRNAii6637.
NextBioi25857.
PROiP62308.
SOURCEiSearch...

Gene expression databases

BgeeiP62308.
CleanExiHS_SNRPG.
ExpressionAtlasiP62308. baseline.
GenevestigatoriP62308.

Family and domain databases

InterProiIPR017132. Lsm7/snRNP-G.
IPR010920. LSM_dom.
IPR001163. Ribonucl_LSM.
IPR006649. Ribonucl_LSM_euk/arc.
[Graphical view]
PfamiPF01423. LSM. 1 hit.
[Graphical view]
PIRSFiPIRSF037188. U6_snRNA_Lsm7. 1 hit.
SMARTiSM00651. Sm. 1 hit.
[Graphical view]
SUPFAMiSSF50182. SSF50182. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "snRNP Sm proteins share two evolutionarily conserved sequence motifs which are involved in Sm protein-protein interactions."
    Hermann H., Fabrizio P., Raker V.A., Foulaki K., Hornig H., Brahms H., Luehrmann R.
    EMBO J. 14:2076-2088(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Bone, Brain, Pancreas and Placenta.
  6. "Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10, a new 14 kDa Sm D1-like protein."
    Pillai R.S., Will C.L., Luehrmann R., Schuemperli D., Mueller B.
    EMBO J. 20:5470-5479(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE U7 SNRNP COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Carcinogenesis and translational controls: TACC1 is down-regulated in human cancers and associates with mRNA regulators."
    Conte N., Charafe-Jauffret E., Delaval B., Adelaide J., Ginestier C., Geneix J., Isnardon D., Jacquemier J., Birnbaum D.
    Oncogene 21:5619-5630(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TACC1.
  8. "Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
    Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
    RNA 8:426-439(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
  9. "The human 18S U11/U12 snRNP contains a set of novel proteins not found in the U2-dependent spliceosome."
    Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R., Elbashir S., Tuschl T., Luehrmann R.
    RNA 10:929-941(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH THE U11/U12 SPLICEOSOME, IDENTIFICATION BY MASS SPECTROMETRY.
  10. "An assembly chaperone collaborates with the SMN complex to generate spliceosomal SnRNPs."
    Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B., Englbrecht C., Sickmann A., Stark H., Fischer U.
    Cell 135:497-509(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SNRNP BIOGENESIS, IDENTIFICATION IN 6S PICLN-SM COMPLEX, IDENTIFICATION IN SMN-SM COMPLEX, SUBCELLULAR LOCATION.
  11. "Crystal structure of human spliceosomal U1 snRNP at 5.5 A resolution."
    Pomeranz Krummel D.A., Oubridge C., Leung A.K., Li J., Nagai K.
    Nature 458:475-480(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (5.49 ANGSTROMS) OF 1-174 IN SPLICEOSOMAL U1 SNRNP.
  12. "Structure of the spliceosomal U4 snRNP core domain and its implication for snRNP biogenesis."
    Leung A.K., Nagai K., Li J.
    Nature 473:536-539(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) IN SPLICEOSOMAL CORE U4 SNRNP.
  13. "Structural basis of assembly chaperone-mediated snRNP formation."
    Grimm C., Chari A., Pelz J.P., Kuper J., Kisker C., Diederichs K., Stark H., Schindelin H., Fischer U.
    Mol. Cell 49:692-703(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN 6S PICLN-SM COMPLEX, IDENTIFICATION IN 6S PICLN-SM COMPLEX, FUNCTION IN CORE U1 SNRNP BIOGENESIS.

Entry informationi

Entry nameiRUXG_HUMAN
AccessioniPrimary (citable) accession number: P62308
Secondary accession number(s): D6W5G6, Q15357, Q6IB86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: July 5, 2004
Last modified: April 1, 2015
This is version 115 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.