Details for: SF3B1
Associated with
Other Information
Genular Protein ID: 1795467971
Symbol: SF3B1_HUMAN
Name: Splicing factor 3B subunit 1
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 9585501
Title: Phosphorylation of spliceosomal protein SAP 155 coupled with splicing catalysis.
PubMed ID: 9585501
PubMed ID: 15815621
Title: Generation and annotation of the DNA sequences of human chromosomes 2 and 4.
PubMed ID: 15815621
DOI: 10.1038/nature03466
PubMed ID: 10882114
Title: Functional association of U2 snRNP with the ATP-independent spliceosomal complex E.
PubMed ID: 10882114
PubMed ID: 12234937
Title: Characterization of novel SF3b and 17S U2 snRNP proteins, including a human Prp5p homologue and an SF3b DEAD-box protein.
PubMed ID: 12234937
DOI: 10.1093/emboj/cdf480
PubMed ID: 12105215
Title: Phosphorylation-dependent interaction between the splicing factors SAP155 and NIPP1.
PubMed ID: 12105215
PubMed ID: 11991638
Title: Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis.
PubMed ID: 11991638
PubMed ID: 12738865
Title: Molecular architecture of the multiprotein splicing factor SF3b.
PubMed ID: 12738865
PubMed ID: 15146077
Title: The human 18S U11/U12 snRNP contains a set of novel proteins not found in the U2-dependent spliceosome.
PubMed ID: 15146077
DOI: 10.1261/rna.7320604
PubMed ID: 17081983
Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
PubMed ID: 17081983
PubMed ID: 16603771
Title: The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear proteins in transcription.
PubMed ID: 16603771
PubMed ID: 16964243
Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.
PubMed ID: 16964243
DOI: 10.1038/nbt1240
PubMed ID: 17924679
Title: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.
PubMed ID: 17924679
DOI: 10.1021/pr070152u
PubMed ID: 18220336
Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.
PubMed ID: 18220336
DOI: 10.1021/pr0705441
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: 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: 21700224
Title: Human senataxin resolves RNA/DNA hybrids formed at transcriptional pause sites to promote Xrn2-dependent termination.
PubMed ID: 21700224
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
PubMed ID: 23512658
Title: PQBP1, a factor linked to intellectual disability, affects alternative splicing associated with neurite outgrowth.
PubMed ID: 23512658
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: 25218447
Title: Uncovering global SUMOylation signaling networks in a site-specific manner.
PubMed ID: 25218447
DOI: 10.1038/nsmb.2890
PubMed ID: 25114211
Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.
PubMed ID: 25114211
PubMed ID: 26575292
Title: Cross-talk between PRMT1-mediated methylation and ubiquitylation on RBM15 controls RNA splicing.
PubMed ID: 26575292
DOI: 10.7554/elife.07938
PubMed ID: 25755297
Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.
PubMed ID: 25755297
PubMed ID: 28541300
Title: Splicing modulators act at the branch point adenosine binding pocket defined by the PHF5A-SF3b complex.
PubMed ID: 28541300
DOI: 10.1038/ncomms15522
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: 34023904
Title: SANS (USH1G) regulates pre-mRNA splicing by mediating the intra-nuclear transfer of tri-snRNP complexes.
PubMed ID: 34023904
DOI: 10.1093/nar/gkab386
PubMed ID: 34365507
Title: SDE2 is an essential gene required for ribosome biogenesis and the regulation of alternative splicing.
PubMed ID: 34365507
DOI: 10.1093/nar/gkab647
PubMed ID: 16432215
Title: Crystal structure of a core spliceosomal protein interface.
PubMed ID: 16432215
PubMed ID: 17589525
Title: U2AF-homology motif interactions are required for alternative splicing regulation by SPF45.
PubMed ID: 17589525
DOI: 10.1038/nsmb1260
PubMed ID: 21062891
Title: Structural model of the p14/SF3b155 - branch duplex complex.
PubMed ID: 21062891
DOI: 10.1261/rna.2224411
PubMed ID: 24795046
Title: Cancer-relevant splicing factor CAPERalpha engages the essential splicing factor SF3b155 in a specific ternary complex.
PubMed ID: 24795046
PubMed ID: 27720643
Title: Molecular architecture of SF3b and structural consequences of its cancer-related mutations.
PubMed ID: 27720643
PubMed ID: 30567737
Title: The pre-mRNA splicing and transcription factor Tat-SF1 is a functional partner of the spliceosome SF3b1 subunit via a U2AF homology motif interface.
PubMed ID: 30567737
PubMed ID: 32494006
Title: Molecular architecture of the human 17S U2 snRNP.
PubMed ID: 32494006
PubMed ID: 33509932
Title: Structure of the activated human minor spliceosome.
PubMed ID: 33509932
PubMed ID: 34822310
Title: Structural basis of branch site recognition by the human spliceosome.
PubMed ID: 34822310
PubMed ID: 36797247
Title: Mechanisms of the RNA helicases DDX42 and DDX46 in human U2 snRNP assembly.
PubMed ID: 36797247
Sequence Information:
- Length: 1304
- Mass: 145830
- Checksum: 12F051757D2B9DEE
- Sequence:
MAKIAKTHED IEAQIREIQG KKAALDEAQG VGLDSTGYYD QEIYGGSDSR FAGYVTSIAA TELEDDDDDY SSSTSLLGQK KPGYHAPVAL LNDIPQSTEQ YDPFAEHRPP KIADREDEYK KHRRTMIISP ERLDPFADGG KTPDPKMNAR TYMDVMREQH LTKEEREIRQ QLAEKAKAGE LKVVNGAAAS QPPSKRKRRW DQTADQTPGA TPKKLSSWDQ AETPGHTPSL RWDETPGRAK GSETPGATPG SKIWDPTPSH TPAGAATPGR GDTPGHATPG HGGATSSARK NRWDETPKTE RDTPGHGSGW AETPRTDRGG DSIGETPTPG ASKRKSRWDE TPASQMGGST PVLTPGKTPI GTPAMNMATP TPGHIMSMTP EQLQAWRWER EIDERNRPLS DEELDAMFPE GYKVLPPPAG YVPIRTPARK LTATPTPLGG MTGFHMQTED RTMKSVNDQP SGNLPFLKPD DIQYFDKLLV DVDESTLSPE EQKERKIMKL LLKIKNGTPP MRKAALRQIT DKAREFGAGP LFNQILPLLM SPTLEDQERH LLVKVIDRIL YKLDDLVRPY VHKILVVIEP LLIDEDYYAR VEGREIISNL AKAAGLATMI STMRPDIDNM DEYVRNTTAR AFAVVASALG IPSLLPFLKA VCKSKKSWQA RHTGIKIVQQ IAILMGCAIL PHLRSLVEII EHGLVDEQQK VRTISALAIA ALAEAATPYG IESFDSVLKP LWKGIRQHRG KGLAAFLKAI GYLIPLMDAE YANYYTREVM LILIREFQSP DEEMKKIVLK VVKQCCGTDG VEANYIKTEI LPPFFKHFWQ HRMALDRRNY RQLVDTTVEL ANKVGAAEII SRIVDDLKDE AEQYRKMVME TIEKIMGNLG AADIDHKLEE QLIDGILYAF QEQTTEDSVM LNGFGTVVNA LGKRVKPYLP QICGTVLWRL NNKSAKVRQQ AADLISRTAV VMKTCQEEKL MGHLGVVLYE YLGEEYPEVL GSILGALKAI VNVIGMHKMT PPIKDLLPRL TPILKNRHEK VQENCIDLVG RIADRGAEYV SAREWMRICF ELLELLKAHK KAIRRATVNT FGYIAKAIGP HDVLATLLNN LKVQERQNRV CTTVAIAIVA ETCSPFTVLP ALMNEYRVPE LNVQNGVLKS LSFLFEYIGE MGKDYIYAVT PLLEDALMDR DLVHRQTASA VVQHMSLGVY GFGCEDSLNH LLNYVWPNVF ETSPHVIQAV MGALEGLRVA IGPCRMLQYC LQGLFHPARK VRDVYWKIYN SIYIGSQDAL IAHYPRIYND DKNTYIRYEL DYIL
Genular Protein ID: 301012572
Symbol: B4DGZ4_HUMAN
Name: N/A
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 15815621
Title: Generation and annotation of the DNA sequences of human chromosomes 2 and 4.
PubMed ID: 15815621
DOI: 10.1038/nature03466
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
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
Sequence Information:
- Length: 154
- Mass: 17409
- Checksum: 5A440D6CC1A9412F
- Sequence:
MAKIAKTHED IEAQIREIQG KKAALDEAQG VGLDSTGYYD QEIYGGSDSR FAGYVTSIAA TELEDDDDDY SSSTSLLGQK KPGYHAPVAL LNDIPQSTEQ YDPFAEHRPP KIADREDEYK KHRRTMIISP ERLDPFADGN SFPLFYKYSE IYLY
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.