Metabolism of non-coding RNA (Homo sapiens)

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1612, 219, 15, 183-5, 8, 11...1, 2114cytosolnucleoplasmRAE1 U6 snRNA SNRPE GEMIN4 NUP133 DDX20 U2 snRNA PHAX Nup45 U5 snRNA GEMIN8 2xMe-SNRPB GEMIN4 2xMe-SNRPD3 2xMe-SNRPD1 SNRPE GEMIN2 SMN1 GEMIN2 SNRPF m7G cappedSpliceosomal snRNAU6 snRNA GEMIN5 GEMIN8 3-methylguanosine cap AAAS 3-methylguanosine cap U4 snRNA GEMIN5 SNRPF U6 snRNA SNRPE 2xMe-SNRPD1 SNRPE GEMIN4 U1 snRNA U1 snRNA AdoMetGEMIN8 SNRPD2 SMN1 Nuclear Pore Complex(NPC)2xMe-SNRPB 2xMe-SNRPD3NUPL2 DDX20 NUPL1-2 GEMIN7 7-methylguanosine cap GEMIN5 U5 snRNA SNRPG 2xMe-SNRPD3 GEMIN6 SNRPG U2 snRNA 2xMe-SNRPD1 GEMIN7 7-methylguanosine cap NUP85 GEMIN6 GEMIN7 NUP98-5 NUP205 GEMIN7 NUP62 NDC1 NUP153 NUP160 SMN1 NUP98-3 GEMIN4 NUP54 SMN1 NUP210 GEMIN6 GEMIN2 Spliceosomalm3GcappedsnRNA:SMN:SM:Snurportin complexCLNS1A NUP214 U5 snRNA SMN1 SNRPBGEMIN8 U2 snRNA GEMIN5 U1 snRNA Spliceosomal m7Gcapped snRNAs withSMN:SM proteincomplex boundU1 snRNA m7G cappedsnRNA:CBC:PHAXcomplexSNRPF DDX20 Spliceosomal m3Gcapped snRNA loadedwith the SM complexGEMIN5 NCBP2 DDX20 NUP93 SNRPG U6 snRNA 2xMe-SNRPD3 TGS1PRMT5 DDX20 GEMIN7 NUP107 GEMIN6 U4 snRNA SMN1 2xMe-SNRPD3 SNRPG GEMIN8 2xMe-SNRPB U5 snRNA GEMIN4 SNRPD2 WDR77 SNRPD1U5 snRNA GEMIN7 NUP37 SNUPN RANBP2 U2 snRNA SNRPFGEMIN6 SNRPGSNRPE NUP188 SNRPF U4 snRNA SNRPD2 7-methylguanosine cap U1 snRNA SNRPG NUP98-4 TPR SNRPD2U6 snRNA POM121C GEMIN5 SNRPF Spliceosomal m3Gcapped snRNAs withSMN:SM proteincomplex bound2xMe-SNRPD3 2xMe-SNRPB SNUPNGEMIN2 NCBP2 SMN complexSMN complexMethylosomeNUP88 U4 snRNA NUP35 GEMIN8 SNRPD2 GEMIN2 PHAXDDX20 NCBP1 3-methylguanosine cap 3-methylguanosine cap NUP50 POM121 U2 snRNA GEMIN2 2xMe-SNRPD1 SNRPESMN:SM proteincomplexGEMIN6 U4 snRNA Cap Binding Complex(CBC)GEMIN4 Me2-R108,R112-SNRPB NUP155 2xMe-SNRPD1 SNRPD2 NUP43 NCBP1 SEH1L-2 76, 10, 19, 2217, 20217, 20


Description

The term non-coding is commonly employed for RNA that does not encode a protein, but this does not mean that such RNAs do not contain information nor have function. There is considerable evidence that the majority of mammalian and other complex organism's genomes is transcribed into non-coding RNAs, many of which are alternatively spliced and/or processed into smaller products. Around 98% of all transcriptional output in humans is non-coding RNA. RNA-mediated gene regulation is widespread in higher eukaryotes and complex genetic phenomena like RNA interference are mediated by such RNAs. These non-coding RNAs are a growing list and include rRNAs, tRNAs, snRNAs, snoRNAs siRNAs, 7SL RNA, 7SK RNA, the RNA component of RNase P RNA, the RNA component of RNase MRP, and the RNA component of telomerase. View original pathway at:Reactome.

Comments

Reactome-Converter 
Pathway is converted from Reactome ID: 194441
Reactome-version 
Reactome version: 66

Quality Tags

Ontology Terms

 

Bibliography

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  1. Plessel G, Fischer U, Lührmann R.; ''m3G cap hypermethylation of U1 small nuclear ribonucleoprotein (snRNP) in vitro: evidence that the U1 small nuclear RNA-(guanosine-N2)-methyltransferase is a non-snRNP cytoplasmic protein that requires a binding site on the Sm core domain.''; PubMed
  2. Fontoura BM, Blobel G, Matunis MJ.; ''A conserved biogenesis pathway for nucleoporins: proteolytic processing of a 186-kilodalton precursor generates Nup98 and the novel nucleoporin, Nup96.''; PubMed
  3. Charroux B, Pellizzoni L, Perkinson RA, Shevchenko A, Mann M, Dreyfuss G.; ''Gemin3: A novel DEAD box protein that interacts with SMN, the spinal muscular atrophy gene product, and is a component of gems.''; PubMed
  4. Charroux B, Pellizzoni L, Perkinson RA, Yong J, Shevchenko A, Mann M, Dreyfuss G.; ''Gemin4. A novel component of the SMN complex that is found in both gems and nucleoli.''; PubMed
  5. Friesen WJ, Dreyfuss G.; ''Specific sequences of the Sm and Sm-like (Lsm) proteins mediate their interaction with the spinal muscular atrophy disease gene product (SMN).''; PubMed
  6. Suntharalingam M, Wente SR.; ''Peering through the pore: nuclear pore complex structure, assembly, and function.''; PubMed
  7. Brahms H, Meheus L, de Brabandere V, Fischer U, Lührmann R.; ''Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B' and the Sm-like protein LSm4, and their interaction with the SMN protein.''; PubMed
  8. Baccon J, Pellizzoni L, Rappsilber J, Mann M, Dreyfuss G.; ''Identification and characterization of Gemin7, a novel component of the survival of motor neuron complex.''; PubMed
  9. Bühler D, Raker V, Lührmann R, Fischer U.; ''Essential role for the tudor domain of SMN in spliceosomal U snRNP assembly: implications for spinal muscular atrophy.''; PubMed
  10. Ori A, Banterle N, Iskar M, Iskar M, Andrés-Pons A, Escher C, Khanh Bui H, Sparks L, Solis-Mezarino V, Rinner O, Bork P, Lemke EA, Beck M.; ''Cell type-specific nuclear pores: a case in point for context-dependent stoichiometry of molecular machines.''; PubMed
  11. Gubitz AK, Mourelatos Z, Abel L, Rappsilber J, Mann M, Dreyfuss G.; ''Gemin5, a novel WD repeat protein component of the SMN complex that binds Sm proteins.''; PubMed
  12. Narayanan U, Ospina JK, Frey MR, Hebert MD, Matera AG.; ''SMN, the spinal muscular atrophy protein, forms a pre-import snRNP complex with snurportin1 and importin beta.''; PubMed
  13. Pellizzoni L, Baccon J, Rappsilber J, Mann M, Dreyfuss G.; ''Purification of native survival of motor neurons complexes and identification of Gemin6 as a novel component.''; PubMed
  14. Sleeman JE, Lamond AI.; ''Newly assembled snRNPs associate with coiled bodies before speckles, suggesting a nuclear snRNP maturation pathway.''; PubMed
  15. Meister G, Eggert C, Fischer U.; ''SMN-mediated assembly of RNPs: a complex story.''; PubMed
  16. Segref A, Mattaj IW, Ohno M.; ''The evolutionarily conserved region of the U snRNA export mediator PHAX is a novel RNA-binding domain that is essential for U snRNA export.''; PubMed
  17. Carissimi C, Saieva L, Gabanella F, Pellizzoni L.; ''Gemin8 is required for the architecture and function of the survival motor neuron complex.''; PubMed
  18. Pellizzoni L, Kataoka N, Charroux B, Dreyfuss G.; ''A novel function for SMN, the spinal muscular atrophy disease gene product, in pre-mRNA splicing.''; PubMed
  19. Rabut G, Doye V, Ellenberg J.; ''Mapping the dynamic organization of the nuclear pore complex inside single living cells.''; PubMed
  20. Neuenkirchen N, Englbrecht C, Ohmer J, Ziegenhals T, Chari A, Fischer U.; ''Reconstitution of the human U snRNP assembly machinery reveals stepwise Sm protein organization.''; PubMed
  21. Mouaikel J, Narayanan U, Verheggen C, Matera AG, Bertrand E, Tazi J, Bordonné R.; ''Interaction between the small-nuclear-RNA cap hypermethylase and the spinal muscular atrophy protein, survival of motor neuron.''; PubMed
  22. Cronshaw JM, Krutchinsky AN, Zhang W, Chait BT, Matunis MJ.; ''Proteomic analysis of the mammalian nuclear pore complex.''; PubMed

History

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CompareRevisionActionTimeUserComment
101423view11:30, 1 November 2018ReactomeTeamreactome version 66
100961view21:07, 31 October 2018ReactomeTeamreactome version 65
100498view19:41, 31 October 2018ReactomeTeamreactome version 64
100044view16:25, 31 October 2018ReactomeTeamreactome version 63
99596view14:58, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
99214view12:43, 31 October 2018ReactomeTeamreactome version 62
94040view13:53, 16 August 2017ReactomeTeamreactome version 61
93664view11:30, 9 August 2017ReactomeTeamreactome version 61
86970view13:51, 15 July 2016MkutmonOntology Term : 'non-coding RNA pathway' added !
86786view09:26, 11 July 2016ReactomeTeamreactome version 56
83121view10:02, 18 November 2015ReactomeTeamVersion54
81460view12:59, 21 August 2015ReactomeTeamVersion53
76932view08:20, 17 July 2014ReactomeTeamFixed remaining interactions
76637view12:01, 16 July 2014ReactomeTeamFixed remaining interactions
75967view10:02, 11 June 2014ReactomeTeamRe-fixing comment source
75670view10:58, 10 June 2014ReactomeTeamReactome 48 Update
75025view13:53, 8 May 2014AnweshaFixing comment source for displaying WikiPathways description
74669view08:44, 30 April 2014ReactomeTeamNew pathway

External references

DataNodes

View all...
NameTypeDatabase referenceComment
2xMe-SNRPB ProteinP14678 (Uniprot-TrEMBL)
2xMe-SNRPD1 ProteinP62314 (Uniprot-TrEMBL)
2xMe-SNRPD3 ProteinP62318 (Uniprot-TrEMBL)
2xMe-SNRPD3ProteinP62318 (Uniprot-TrEMBL)
3-methylguanosine cap MetaboliteCHEBI:1604 (ChEBI)
7-methylguanosine cap MetaboliteCHEBI:17825 (ChEBI)
7-methylguanosine cap MetaboliteCHEBI:2274 (ChEBI)
AAAS ProteinQ9NRG9 (Uniprot-TrEMBL)
AdoMetMetaboliteCHEBI:15414 (ChEBI)
CLNS1A ProteinP54105 (Uniprot-TrEMBL)
Cap Binding Complex (CBC)ComplexR-HSA-162460 (Reactome)
DDX20 ProteinQ9UHI6 (Uniprot-TrEMBL)
GEMIN2 ProteinO14893 (Uniprot-TrEMBL)
GEMIN4 ProteinP57678 (Uniprot-TrEMBL)
GEMIN5 ProteinQ8TEQ6 (Uniprot-TrEMBL)
GEMIN6 ProteinQ8WXD5 (Uniprot-TrEMBL)
GEMIN7 ProteinQ9H840 (Uniprot-TrEMBL)
GEMIN8 ProteinQ9NWZ8 (Uniprot-TrEMBL)
Me2-R108,R112-SNRPB ProteinP14678 (Uniprot-TrEMBL)
MethylosomeComplexR-HSA-191849 (Reactome)
NCBP1 ProteinQ09161 (Uniprot-TrEMBL)
NCBP2 ProteinP52298 (Uniprot-TrEMBL)
NDC1 ProteinQ9BTX1 (Uniprot-TrEMBL)
NUP107 ProteinP57740 (Uniprot-TrEMBL)
NUP133 ProteinQ8WUM0 (Uniprot-TrEMBL)
NUP153 ProteinP49790 (Uniprot-TrEMBL)
NUP155 ProteinO75694 (Uniprot-TrEMBL)
NUP160 ProteinQ12769 (Uniprot-TrEMBL)
NUP188 ProteinQ5SRE5 (Uniprot-TrEMBL)
NUP205 ProteinQ92621 (Uniprot-TrEMBL)
NUP210 ProteinQ8TEM1 (Uniprot-TrEMBL)
NUP214 ProteinP35658 (Uniprot-TrEMBL)
NUP35 ProteinQ8NFH5 (Uniprot-TrEMBL)
NUP37 ProteinQ8NFH4 (Uniprot-TrEMBL)
NUP43 ProteinQ8NFH3 (Uniprot-TrEMBL)
NUP50 ProteinQ9UKX7 (Uniprot-TrEMBL)
NUP54 ProteinQ7Z3B4 (Uniprot-TrEMBL)
NUP62 ProteinP37198 (Uniprot-TrEMBL)
NUP85 ProteinQ9BW27 (Uniprot-TrEMBL)
NUP88 ProteinQ99567 (Uniprot-TrEMBL)
NUP93 ProteinQ8N1F7 (Uniprot-TrEMBL)
NUP98-3 ProteinP52948-3 (Uniprot-TrEMBL)
NUP98-4 ProteinP52948-4 (Uniprot-TrEMBL)
NUP98-5 ProteinP52948-5 (Uniprot-TrEMBL)
NUPL1-2 ProteinQ9BVL2-1 (Uniprot-TrEMBL)
NUPL2 ProteinO15504 (Uniprot-TrEMBL)
Nuclear Pore Complex (NPC)ComplexR-HSA-157689 (Reactome)
Nup45 ProteinQ9BVL2-2 (Uniprot-TrEMBL)
PHAX ProteinQ9H814 (Uniprot-TrEMBL)
PHAXProteinQ9H814 (Uniprot-TrEMBL)
POM121 ProteinQ96HA1 (Uniprot-TrEMBL)
POM121C ProteinA8CG34 (Uniprot-TrEMBL)
PRMT5 ProteinO14744 (Uniprot-TrEMBL)
RAE1 ProteinP78406 (Uniprot-TrEMBL)
RANBP2 ProteinP49792 (Uniprot-TrEMBL)
SEH1L-2 ProteinQ96EE3-2 (Uniprot-TrEMBL)
SMN complexComplexR-HSA-191762 (Reactome)
SMN complexComplexR-HSA-191881 (Reactome)
SMN1 ProteinQ16637 (Uniprot-TrEMBL)
SMN:SM protein complexComplexR-HSA-191791 (Reactome)
SNRPBProteinP14678 (Uniprot-TrEMBL)
SNRPD1ProteinP62314 (Uniprot-TrEMBL)
SNRPD2 ProteinP62316 (Uniprot-TrEMBL)
SNRPD2ProteinP62316 (Uniprot-TrEMBL)
SNRPE ProteinP62304 (Uniprot-TrEMBL)
SNRPEProteinP62304 (Uniprot-TrEMBL)
SNRPF ProteinP62306 (Uniprot-TrEMBL)
SNRPFProteinP62306 (Uniprot-TrEMBL)
SNRPG ProteinP62308 (Uniprot-TrEMBL)
SNRPGProteinP62308 (Uniprot-TrEMBL)
SNUPN ProteinO95149 (Uniprot-TrEMBL)
SNUPNProteinO95149 (Uniprot-TrEMBL)
Spliceosomal

m3G capped

snRNA:SMN:SM:Snurportin complex
ComplexR-HSA-191778 (Reactome)
Spliceosomal m3G

capped snRNA loaded

with the SM complex
ComplexR-HSA-191870 (Reactome)
Spliceosomal m3G

capped snRNAs with SMN:SM protein

complex bound
ComplexR-HSA-191891 (Reactome)
Spliceosomal m7G

capped snRNAs with SMN:SM protein

complex bound
ComplexR-HSA-191813 (Reactome)
TGS1ProteinQ96RS0 (Uniprot-TrEMBL)
TPR ProteinP12270 (Uniprot-TrEMBL)
U1 snRNA ProteinV00590 (EMBL)
U2 snRNA ProteinX59360 (EMBL)
U4 snRNA ProteinX59361 (EMBL)
U5 snRNA ProteinX04293 (EMBL)
U6 snRNA ProteinX59362 (EMBL)
WDR77 ProteinQ9BQA1 (Uniprot-TrEMBL)
m7G capped Spliceosomal snRNAComplexR-HSA-191853 (Reactome)
m7G capped

snRNA:CBC:PHAX

complex
ComplexR-HSA-191887 (Reactome)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
2xMe-SNRPD3R-HSA-191790 (Reactome)
AdoMetR-HSA-191790 (Reactome)
Cap Binding Complex (CBC)ArrowR-HSA-191825 (Reactome)
Methylosomemim-catalysisR-HSA-191790 (Reactome)
Nuclear Pore Complex (NPC)ArrowR-HSA-191825 (Reactome)
Nuclear Pore Complex (NPC)ArrowR-HSA-191830 (Reactome)
PHAXArrowR-HSA-191825 (Reactome)
R-HSA-191763 (Reactome) The nuclear import signal has two parts; Cap hypermethylation triggers nuclear import via snurportin1 binding and by receptor recognition of the Sm proteins. Snurportin1 (SPN) is an adaptor that links the assembled snRNP to the nuclear transport machinery, recruiting importin beta for nuclear import. The import receptor that recognizes the Sm proteins is not yet known.
R-HSA-191784 (Reactome) The snRNA:SMN:SM protein complex is engaged by a hypermethylase that hypermethylates the snRNA cap from m7G (7-methylguanosine) to m3G (2,2,7-trimethylguanosine).
R-HSA-191786 (Reactome) To facilitate snRNP assembly, the SMN complex must bring together the Sm proteins and an Sm-site-containing snRNA. The SMN:Sm protein complex binds to the m7G capped snRNAs in the cytoplasm.
R-HSA-191790 (Reactome) The survival of motor neurons (SMN) complex binds to Sm proteins and small nuclear RNAs (snRNAs) in the cytoplasm. Sm is part the SMN multiprotein complex that contains Gemins 2 – 7, including the DEAD-box RNA helicase Gemin3. The binding of the SMN complex to the snRNAs depends on the presence of specific, high-affinity (nanomolar) binding domains in the snRNAs. The SMN complex binds the Sm proteins through the Sm domains interaction with the Gemins, the TUDOR domain, and through unique arginine- and glycine-rich (RG) domains found in three of these, SmB, SmD1 and SmD3. The association with RG domains is strongly enhanced by the post-translational symmetric dimethylation of specific arginines in these domains, a process that is carried out by the methylosome (JBP1 or PRMT5) complex.
R-HSA-191825 (Reactome) The snRNAs, except U6 snRNA, are transcribed by RNA polymerase II, co-transcriptionally capped and exported rapidly to the cytoplasm in association with a cap-binding complex and the export factor PHAX.
R-HSA-191830 (Reactome) A properly assembled Sm core and the m3G cap structure are prerequisites for small nuclear ribonucleoprotein (snRNP) import into the nucleus. Once imported into the nucleus, the snRNPs are initially concentrated in Cajal bodies (CBs), where there is further processing of the snRNAs plus binding of additional proteins, from CRBs they transit to "speckles", from where they are engaged for pre-mRNA splicing. The SMN complexes in the nucleus are found throughout the nucleoplasm but are particularly concentrated in Gems, the "twins" of the snRNP-rich CBs.
SMN complexArrowR-HSA-191830 (Reactome)
SMN complexR-HSA-191790 (Reactome)
SMN:SM protein complexArrowR-HSA-191790 (Reactome)
SMN:SM protein complexR-HSA-191786 (Reactome)
SNRPBR-HSA-191790 (Reactome)
SNRPD1R-HSA-191790 (Reactome)
SNRPD2R-HSA-191790 (Reactome)
SNRPER-HSA-191790 (Reactome)
SNRPFR-HSA-191790 (Reactome)
SNRPGR-HSA-191790 (Reactome)
SNUPNArrowR-HSA-191830 (Reactome)
SNUPNR-HSA-191763 (Reactome)
Spliceosomal

m3G capped

snRNA:SMN:SM:Snurportin complex
ArrowR-HSA-191763 (Reactome)
Spliceosomal

m3G capped

snRNA:SMN:SM:Snurportin complex
R-HSA-191830 (Reactome)
Spliceosomal m3G

capped snRNA loaded

with the SM complex
ArrowR-HSA-191830 (Reactome)
Spliceosomal m3G

capped snRNAs with SMN:SM protein

complex bound
ArrowR-HSA-191784 (Reactome)
Spliceosomal m3G

capped snRNAs with SMN:SM protein

complex bound
R-HSA-191763 (Reactome)
Spliceosomal m7G

capped snRNAs with SMN:SM protein

complex bound
ArrowR-HSA-191786 (Reactome)
Spliceosomal m7G

capped snRNAs with SMN:SM protein

complex bound
R-HSA-191784 (Reactome)
TGS1mim-catalysisR-HSA-191784 (Reactome)
m7G capped Spliceosomal snRNAArrowR-HSA-191825 (Reactome)
m7G capped Spliceosomal snRNAR-HSA-191786 (Reactome)
m7G capped

snRNA:CBC:PHAX

complex
R-HSA-191825 (Reactome)
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