Details for: SNRNP200
Associated with
Other Information
Genular Protein ID: 1905003090
Symbol: U520_HUMAN
Name: U5 small nuclear ribonucleoprotein 200 kDa helicase
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 16723661
Title: The network of protein-protein interactions within the human U4/U6.U5 tri-snRNP.
PubMed ID: 16723661
DOI: 10.1261/rna.55406
PubMed ID: 14702039
Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.
PubMed ID: 14702039
DOI: 10.1038/ng1285
PubMed ID: 9872452
Title: Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro.
PubMed ID: 9872452
PubMed ID: 12168954
Title: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones.
PubMed ID: 12168954
PubMed ID: 8670905
Title: The HeLa 200 kDa U5 snRNP-specific protein and its homologue in Saccharomyces cerevisiae are members of the DEXH-box protein family of putative RNA helicases.
PubMed ID: 8670905
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 9539711
Title: The human U5-200kD DEXH-box protein unwinds U4/U6 RNA duplices in vitro.
PubMed ID: 9539711
PubMed ID: 11991638
Title: Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis.
PubMed ID: 11991638
PubMed ID: 17081983
Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
PubMed ID: 17081983
PubMed ID: 19367720
Title: Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment.
PubMed ID: 19367720
DOI: 10.1021/pr800500r
PubMed ID: 18691976
Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.
PubMed ID: 18691976
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 18318008
Title: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.
PubMed ID: 18318008
PubMed ID: 19413330
Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
PubMed ID: 19413330
DOI: 10.1021/ac9004309
PubMed ID: 19690332
Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
PubMed ID: 19690332
PubMed ID: 19608861
Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.
PubMed ID: 19608861
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
PubMed ID: 28112733
Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.
PubMed ID: 28112733
DOI: 10.1038/nsmb.3366
PubMed ID: 23045696
Title: Structural basis for functional cooperation between tandem helicase cassettes in Brr2-mediated remodeling of the spliceosome.
PubMed ID: 23045696
PubMed ID: 26912367
Title: Molecular architecture of the human U4/U6.U5 tri-snRNP.
PubMed ID: 26912367
PubMed ID: 28502770
Title: An Atomic Structure of the Human Spliceosome.
PubMed ID: 28502770
PubMed ID: 28781166
Title: Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for Activation.
PubMed ID: 28781166
PubMed ID: 29361316
Title: Structure and Conformational Dynamics of the Human Spliceosomal Bact Complex.
PubMed ID: 29361316
PubMed ID: 30315277
Title: Structures of the human pre-catalytic spliceosome and its precursor spliceosome.
PubMed ID: 30315277
PubMed ID: 29360106
Title: Structure of the human activated spliceosome in three conformational states.
PubMed ID: 29360106
DOI: 10.1038/cr.2018.14
PubMed ID: 29301961
Title: Structure of a human catalytic step I spliceosome.
PubMed ID: 29301961
PubMed ID: 30728453
Title: Structures of the human spliceosomes before and after release of the ligated exon.
PubMed ID: 30728453
PubMed ID: 30705154
Title: A human postcatalytic spliceosome structure reveals essential roles of metazoan factors for exon ligation.
PubMed ID: 30705154
PubMed ID: 33509932
Title: Structure of the activated human minor spliceosome.
PubMed ID: 33509932
PubMed ID: 35241646
Title: A multi-factor trafficking site on the spliceosome remodeling enzyme BRR2 recruits C9ORF78 to regulate alternative splicing.
PubMed ID: 35241646
PubMed ID: 35188580
Title: The intrinsically disordered TSSC4 protein acts as a helicase inhibitor, placeholder and multi-interaction coordinator during snRNP assembly and recycling.
PubMed ID: 35188580
DOI: 10.1093/nar/gkac087
PubMed ID: 16959974
Title: The consensus coding sequences of human breast and colorectal cancers.
PubMed ID: 16959974
PubMed ID: 19878916
Title: Autosomal-dominant retinitis pigmentosa caused by a mutation in SNRNP200, a gene required for unwinding of U4/U6 snRNAs.
PubMed ID: 19878916
PubMed ID: 19710410
Title: Mutations in ASCC3L1 on 2q11.2 are associated with autosomal dominant retinitis pigmentosa in a Chinese family.
PubMed ID: 19710410
DOI: 10.1167/iovs.09-3725
PubMed ID: 21618346
Title: Next generation sequencing of pooled samples reveals new SNRNP200 mutations associated with retinitis pigmentosa.
PubMed ID: 21618346
DOI: 10.1002/humu.21485
PubMed ID: 23029027
Title: A novel missense SNRNP200 mutation associated with autosomal dominant retinitis pigmentosa in a Chinese family.
PubMed ID: 23029027
PubMed ID: 23887765
Title: Contribution of SNRNP200 sequence variations to retinitis pigmentosa.
PubMed ID: 23887765
DOI: 10.1038/eye.2013.137
PubMed ID: 24319334
Title: Mutations in the small nuclear riboprotein 200 kDa gene (SNRNP200) cause 1.6% of autosomal dominant retinitis pigmentosa.
PubMed ID: 24319334
Sequence Information:
- Length: 2136
- Mass: 244508
- Checksum: 3F3811BDCCC9DDB7
- Sequence:
MADVTARSLQ YEYKANSNLV LQADRSLIDR TRRDEPTGEV LSLVGKLEGT RMGDKAQRTK PQMQEERRAK RRKRDEDRHD INKMKGYTLL SEGIDEMVGI IYKPKTKETR ETYEVLLSFI QAALGDQPRD ILCGAADEVL AVLKNEKLRD KERRKEIDLL LGQTDDTRYH VLVNLGKKIT DYGGDKEIQN MDDNIDETYG VNVQFESDEE EGDEDVYGEV REEASDDDME GDEAVVRCTL SANLVASGEL MSSKKKDLHP RDIDAFWLQR QLSRFYDDAI VSQKKADEVL EILKTASDDR ECENQLVLLL GFNTFDFIKV LRQHRMMILY CTLLASAQSE AEKERIMGKM EADPELSKFL YQLHETEKED LIREERSRRE RVRQSRMDTD LETMDLDQGG EALAPRQVLD LEDLVFTQGS HFMANKRCQL PDGSFRRQRK GYEEVHVPAL KPKPFGSEEQ LLPVEKLPKY AQAGFEGFKT LNRIQSKLYR AALETDENLL LCAPTGAGKT NVALMCMLRE IGKHINMDGT INVDDFKIIY IAPMRSLVQE MVGSFGKRLA TYGITVAELT GDHQLCKEEI SATQIIVCTP EKWDIITRKG GERTYTQLVR LIILDEIHLL HDDRGPVLEA LVARAIRNIE MTQEDVRLIG LSATLPNYED VATFLRVDPA KGLFYFDNSF RPVPLEQTYV GITEKKAIKR FQIMNEIVYE KIMEHAGKNQ VLVFVHSRKE TGKTARAIRD MCLEKDTLGL FLREGSASTE VLRTEAEQCK NLELKDLLPY GFAIHHAGMT RVDRTLVEDL FADKHIQVLV STATLAWGVN LPAHTVIIKG TQVYSPEKGR WTELGALDIL QMLGRAGRPQ YDTKGEGILI TSHGELQYYL SLLNQQLPIE SQMVSKLPDM LNAEIVLGNV QNAKDAVNWL GYAYLYIRML RSPTLYGISH DDLKGDPLLD QRRLDLVHTA ALMLDKNNLV KYDKKTGNFQ VTELGRIASH YYITNDTVQT YNQLLKPTLS EIELFRVFSL SSEFKNITVR EEEKLELQKL LERVPIPVKE SIEEPSAKIN VLLQAFISQL KLEGFALMAD MVYVTQSAGR LMRAIFEIVL NRGWAQLTDK TLNLCKMIDK RMWQSMCPLR QFRKLPEEVV KKIEKKNFPF ERLYDLNHNE IGELIRMPKM GKTIHKYVHL FPKLELSVHL QPITRSTLKV ELTITPDFQW DEKVHGSSEA FWILVEDVDS EVILHHEYFL LKAKYAQDEH LITFFVPVFE PLPPQYFIRV VSDRWLSCET QLPVSFRHLI LPEKYPPPTE LLDLQPLPVS ALRNSAFESL YQDKFPFFNP IQTQVFNTVY NSDDNVFVGA PTGSGKTICA EFAILRMLLQ SSEGRCVYIT PMEALAEQVY MDWYEKFQDR LNKKVVLLTG ETSTDLKLLG KGNIIISTPE KWDILSRRWK QRKNVQNINL FVVDEVHLIG GENGPVLEVI CSRMRYISSQ IERPIRIVAL SSSLSNAKDV AHWLGCSATS TFNFHPNVRP VPLELHIQGF NISHTQTRLL SMAKPVYHAI TKHSPKKPVI VFVPSRKQTR LTAIDILTTC AADIQRQRFL HCTEKDLIPY LEKLSDSTLK ETLLNGVGYL HEGLSPMERR LVEQLFSSGA IQVVVASRSL CWGMNVAAHL VIIMDTQYYN GKIHAYVDYP IYDVLQMVGH ANRPLQDDEG RCVIMCQGSK KDFFKKFLYE PLPVESHLDH CMHDHFNAEI VTKTIENKQD AVDYLTWTFL YRRMTQNPNY YNLQGISHRH LSDHLSELVE QTLSDLEQSK CISIEDEMDV APLNLGMIAA YYYINYTTIE LFSMSLNAKT KVRGLIEIIS NAAEYENIPI RHHEDNLLRQ LAQKVPHKLN NPKFNDPHVK TNLLLQAHLS RMQLSAELQS DTEEILSKAI RLIQACVDVL SSNGWLSPAL AAMELAQMVT QAMWSKDSYL KQLPHFTSEH IKRCTDKGVE SVFDIMEMED EERNALLQLT DSQIADVARF CNRYPNIELS YEVVDKDSIR SGGPVVVLVQ LEREEEVTGP VIAPLFPQKR EEGWWVVIGD AKSNSLISIK RLTLQQKAKV KLDFVAPATG AHNYTLYFMS DAYMGCDQEY KFSVDVKEAE TDSDSD
Database document:
This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.