Details for: SF3B2
Associated with
Other Information
Genular Protein ID: 825840430
Symbol: SF3B2_HUMAN
Name: Splicing factor 3B subunit 2
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 14702039
Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.
PubMed ID: 14702039
DOI: 10.1038/ng1285
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: 8566756
Title: Evidence that sequence-independent binding of highly conserved U2 snRNP proteins upstream of the branch site is required for assembly of spliceosomal complex A.
PubMed ID: 8566756
DOI: 10.1101/gad.10.2.233
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: 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: 16923959
Title: Human immunodeficiency virus type 1 Vpr induces G2 checkpoint activation by interacting with the splicing factor SAP145.
PubMed ID: 16923959
DOI: 10.1128/mcb.01170-06
PubMed ID: 17525332
Title: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.
PubMed ID: 17525332
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: 24129315
Title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.
PubMed ID: 24129315
PubMed ID: 25218447
Title: Uncovering global SUMOylation signaling networks in a site-specific manner.
PubMed ID: 25218447
DOI: 10.1038/nsmb.2890
PubMed ID: 25772364
Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.
PubMed ID: 25772364
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: 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: 25737013
Title: PRMT9 is a type II methyltransferase that methylates the splicing factor SAP145.
PubMed ID: 25737013
DOI: 10.1038/ncomms7428
PubMed ID: 25979344
Title: Unique features of human protein arginine methyltransferase 9 (PRMT9) and its substrate RNA splicing factor SF3B2.
PubMed ID: 25979344
PubMed ID: 26030138
Title: Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin Dynamics.
PubMed ID: 26030138
PubMed ID: 27720643
Title: Molecular architecture of SF3b and structural consequences of its cancer-related mutations.
PubMed ID: 27720643
PubMed ID: 27905398
Title: Structure of the RBM7-ZCCHC8 core of the NEXT complex reveals connections to splicing factors.
PubMed ID: 27905398
DOI: 10.1038/ncomms13573
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: 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
PubMed ID: 34344887
Title: Haploinsufficiency of SF3B2 causes craniofacial microsomia.
PubMed ID: 34344887
Sequence Information:
- Length: 895
- Mass: 100228
- Checksum: D372AFA679443AD6
- Sequence:
MATEHPEPPK AELQLPPPPP PGHYGAWAAQ ELQAKLAEIG APIQGNREEL VERLQSYTRQ TGIVLNRPVL RGEDGDKAAP PPMSAQLPGI PMPPPPLGLP PLQPPPPPPP PPPGLGLGFP MAHPPNLGPP PPLRVGEPVA LSEEERLKLA QQQAALLMQQ EERAKQQGDH SLKEHELLEQ QKRAAVLLEQ ERQQEIAKMG TPVPRPPQDM GQIGVRTPLG PRVAAPVGPV GPTPTVLPMG APVPRPRGPP PPPGDENREM DDPSVGPKIP QALEKILQLK ESRQEEMNSQ QEEEEMETDA RSSLGQSASE TEEDTVSVSK KEKNRKRRNR KKKKKPQRVR GVSSESSGDR EKDSTRSRGS DSPAADVEIE YVTEEPEIYE PNFIFFKRIF EAFKLTDDVK KEKEKEPEKL DKLENSAAPK KKGFEEEHKD SDDDSSDDEQ EKKPEAPKLS KKKLRRMNRF TVAELKQLVA RPDVVEMHDV TAQDPKLLVH LKATRNSVPV PRHWCFKRKY LQGKRGIEKP PFELPDFIKR TGIQEMREAL QEKEEQKTMK SKMREKVRPK MGKIDIDYQK LHDAFFKWQT KPKLTIHGDL YYEGKEFETR LKEKKPGDLS DELRISLGMP VGPNAHKVPP PWLIAMQRYG PPPSYPNLKI PGLNSPIPES CSFGYHAGGW GKPPVDETGK PLYGDVFGTN AAEFQTKTEE EEIDRTPWGE LEPSDEESSE EEEEEESDED KPDETGFITP ADSGLITPGG FSSVPAGMET PELIELRKKK IEEAMDGSET PQLFTVLPEK RTATVGGAMM GSTHIYDMST VMSRKGPAPE LQGVEVALAP EELELDPMAM TQKYEEHVRE QQAQVEKEDF SDMVAEHAAK QKQKKRKAQP QDSRGGSKKY KEFKF
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.