EuRBPDB

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TCGA tumor abbreviations
  • ACCAdrenocortical carcinoma
  • BLCABladder Urothelial Carcinoma
  • BRCABreast invasive carcinoma
  • CESCCervical squamous cell carcinoma and endocervical adenocarcinoma
  • CHOLCholangio carcinoma
  • COADColon adenocarcinoma
  • DLBCLymphoid Neoplasm Diffuse Large B-cell Lymphoma
  • ESCAEsophageal carcinoma
  • GBMGlioblastoma multiforme
  • HNSCHead and Neck squamous cell carcinoma
  • KICHKidney Chromophobe
  • KIRCKidney renal clear cell carcinoma
  • KIRPKidney renal papillary cell carcinoma
  • LAMLAcute Myeloid Leukemia
  • LGGBrain Lower Grade Glioma
  • LIHCLiver hepatocellular carcinoma
  • LUADLung adenocarcinoma
  • LUSCLung squamous cell carcinoma
  • MESOMesothelioma
  • OVOvarian serous cystadenocarcinoma
  • PAADPancreatic adenocarcinoma
  • PCPGPheochromocytoma and Paraganglioma
  • PRADProstate adenocarcinoma
  • READRectum adenocarcinoma
  • SARCSarcoma
  • SKCMSkin Cutaneous Melanoma
  • STADStomach adenocarcinoma
  • TGCTThyroid carcinoma
  • THCAThyroid carcinoma
  • THYMThymoma
  • UCECUterine Corpus Endometrial Carcinoma
  • UCSUterine Carcinosarcoma
  • UVMUveal Melanoma

Note: Click here to get the extension of tumor abbreviations.


  • Cancer Related Information
  • Basic Information

Cancer associated literatures
PIDTitleArticle TimeAuthorDoi
23966470Tissue-specific and SRSF1-dependent splicing of fibronectin, a matrix protein that controls host cell invasion.Mol Biol Cell2013 OctLopez-Mejia ICdoi: 10.1091/mbc.E13-03-0142
28677791miR30c suppresses prostate cancer survival by targeting the ASF/SF2 splicing factor oncoprotein.Mol Med Rep2017 SepHuang YQdoi: 10.3892/mmr.2017.6910
29120871A SRSF1 self-binding mechanism restrains Mir505-3p from inhibiting proliferation of neural tumor cell lines.Anticancer Drugs2018 JanYang Kdoi: 10.1097/CAD.0000000000000564.
19602482Antagonistic SR proteins regulate alternative splicing of tumor-related Rac1b downstream of the PI3-kinase and Wnt pathways.Hum Mol Genet2009 Oct 1Gonalves Vdoi: 10.1093/hmg/ddp317
30429088SRSF1 modulates PTPMT1 alternative splicing to regulate lung cancer cell radioresistance.EBioMedicine2018 DecSheng Jdoi: 10.1016/j.ebiom.2018.11.007
20682707The oncoprotein SF2/ASF promotes non-small cell lung cancer survival by enhancing survivin expression.Clin Cancer Res2010 Aug 15Ezponda Tdoi: 10.1158/1078-0432.CCR-10-0076
23748175Alterations in expression pattern of splicing factors in epithelial ovarian cancer and its clinical impact.Int J Gynecol Cancer2013 JulIborra Sdoi: 10.1097/IGC.0b013e31829783e3.
24857172MALAT1 promotes cell proliferation in gastric cancer by recruiting SF2/ASF.Biomed Pharmacother2014 JunWang Jdoi: 10.1016/j.biopha.2014.04.007
24371231Identification of alternative splicing events regulated by the oncogenic factor SRSF1 in lung cancer.Cancer Res2014 Feb 15de Miguel FJdoi: 10.1158/0008-5472.CAN-13-1481
26431027SRSF1-Regulated Alternative Splicing in Breast Cancer.Mol Cell2015 Oct 1Anczuk??w Odoi: 10.1016/j.molcel.2015.09.005.

Differential Expression

Expression in 33 cancers

Mutations
CancerChrPosition Mutation TypedbSNPProtein-change Allele FreqRBD
BLCAchr1758005956Missense_MutationnovelS133C0.43
BLCAchr1758006472SilentnovelL84L0.19
BLCAchr1758005902Missense_MutationNAD151H0.16
BLCAchr1758006980Missense_MutationnovelG53V0.32RRM_1
BLCAchr1758005570Missense_MutationNAD195H0.08
BLCAchr1758005440Missense_MutationNAS238F0.25
BLCAchr1758006405Missense_MutationnovelG106E0.16
BLCAchr1758006526Missense_MutationnovelD66H0.39RRM_1
BLCAchr17580071615'UTRnovel0.29
BRCAchr1758005926Missense_MutationnovelE143K0.5
BRCAchr1758006964SilentNAF58F0.3
BRCAchr1758005643Intronnovel0.18
BRCAchr1758005742Intronnovel0.41
BRCAchr17580053823'UTRnovel0.08
CESCchr17580053803'UTRnovel0.25
CESCchr17580042813'Flanknovel0.26
CESCchr1758005735Intronnovel0.2
CESCchr1758006980Missense_MutationNAG53E0.27RRM_1
CESCchr17580052723'UTRrs3707396040.33
CESCchr17580042893'Flanknovel0.42
CESCchr1758005937Missense_MutationNAD139G0.53
CESCchr17580049573'UTRnovel0.29
CESCchr17580071615'UTRnovel0.43
CHOLchr1758005553SilentnovelP200P0.31
CHOLchr17580037863'Flanknovel0.36
COADchr1758006493Missense_MutationnovelY77N0.36
COADchr17580053303'UTRnovel0.33
COADchr1758005601Splice_SiteNAX185_splice0.42
COADchr1758005950Nonsense_MutationnovelQ135*0.22
COADchr1758007105SilentnovelA11A0.24
COADchr1758005909SilentnovelC148C0.2
COADchr1758005948Missense_MutationnovelQ135H0.25
COADchr1758005669Intronnovel0.07
COADchr1758005939Missense_MutationNAK138N0.18
COADchr1758006404SilentNAG106G0.2
DLBCchr1758006506Nonsense_MutationnovelY72*0.25
ESCAchr17580037863'Flanknovel0.63
ESCAchr17580048553'UTRnovel0.21
ESCAchr17580050843'UTRnovel0.12
GBMchr1758006500SilentnovelR74R0.32
GBMchr17580072125'UTRnovel0.36
GBMchr17580071435'UTRrs7604613610.18
GBMchr1758007036Missense_MutationnovelD34E0.13RRM_1
HNSCchr1758006964Frame_Shift_InsnovelV59Rfs*20.39RRM_1
HNSCchr17580072025'UTRnovel0.31
HNSCchr1758005887Frame_Shift_InsnovelG156Ifs*270.04
KIRPchr1758006476Nonsense_MutationNAY82*0.1
LIHCchr1758005766IntronNA0.34
LIHCchr1758005435Missense_MutationnovelR240S0.28
LIHCchr1758005542Missense_MutationnovelR204K0.18
LIHCchr1758005519Missense_MutationnovelR212S0.44
LUADchr1758005449Missense_MutationNAP235L0.26
LUADchr1758006483Missense_MutationnovelD80G0.15
LUADchr1758007120SilentnovelV6V0.14
LUSCchr1758006952Missense_MutationNAE62D0.51RRM_1
LUSCchr1758005812Missense_MutationNAR181G0.12
LUSCchr1758006355Missense_MutationNAV123L0.75
OVchr1758005456Nonsense_MutationnovelG233*0.06
OVchr1758006987Missense_MutationNAR51C0.94RRM_1
OVchr1758005933Missense_MutationNAH140Q0.16
OVchr1758006432Missense_MutationNAR97Q0.55
PAADchr1758006433Missense_MutationnovelR97G0.13
PRADchr1758007058Missense_MutationnovelI27N0.08RRM_1
PRADchr17580071395'UTRnovel0.2
PRADchr1758005887Frame_Shift_InsnovelG156Wfs*220.3
PRADchr1758005826Missense_MutationNAD176G0.42
READchr17580053423'UTRnovel0.4
SARCchr17580038583'Flanknovel0.91
SARCchr1758007070Missense_MutationnovelL23S0.21RRM_1
SARCchr1758007071Missense_MutationnovelL23I0.21RRM_1
SARCchr17580045113'Flanknovel0.21
SARCchr17580037863'Flanknovel0.47
SKCMchr1758005588Missense_MutationNAY189H0.93
SKCMchr17580073035'UTRnovel0.3
STADchr1758006507Frame_Shift_InsnovelY72Ffs*170.17
STADchr1758007102SilentNAG12G0.18
STADchr1758005440Frame_Shift_InsnovelS238Ffs*50.4
STADchr17580053253'UTRnovel0.2
STADchr17580052283'UTRnovel0.38
UCECchr17580037863'Flanknovel0.31
UCECchr17580037863'Flanknovel0.44
UCECchr1758005422Missense_MutationNAS244Y0.35
UCECchr1758006460Missense_MutationnovelF88V0.09
UCECchr1758005900Silentrs781290395D151D0.33
UCECchr17580037863'Flanknovel0.47
UCECchr17580037863'Flanknovel0.42
UCECchr17580052433'UTRnovel0.75
UCECchr17580042313'Flanknovel0.32
UCECchr17580037863'Flanknovel0.33
UCECchr17580053343'UTRnovel0.08
UCECchr17580040203'Flanknovel0.54
UCECchr17580037813'Flankrs5532226340.27
UCECchr17580037863'Flanknovel0.37
UCECchr1758007084SilentnovelI18I0.17
UCECchr17580038223'Flanknovel0.39
UCECchr17580039053'Flanknovel0.26
UCECchr1758005836Nonsense_MutationnovelR173*0.17
UCECchr17580052823'UTRnovel0.31
UCECchr1758006516Missense_MutationnovelD69G0.32RRM_1
UCECchr17580046893'FlankNA0.54
UCECchr17580037103'Flanknovel0.17
UCECchr1758007093Missense_MutationnovelD15E0.21
UCECchr1758005875Missense_MutationNAV160M0.07
UCECchr17580037863'Flanknovel0.27
UCECchr17580047043'Flanknovel0.31
UCECchr17580037863'Flanknovel0.44
UCECchr17580047053'Flanknovel0.38
UCECchr17580038423'Flanknovel0.4
UCECchr17580042723'Flanknovel0.39
UCECchr17580040883'Flanknovel0.42
UCECchr17580037863'Flanknovel0.36
UCECchr17580037863'Flanknovel0.49
UCECchr17580050173'UTRnovel0.25
UCECchr1758006977Missense_MutationnovelP54Q0.33RRM_1
UCECchr1758005912SilentNAV147V0.4
UCECchr1758005711Intronnovel0.32
UCECchr17580052973'UTRNA0.29
UCECchr17580038103'Flanknovel0.35
UCECchr1758005722Intronnovel0.17
UCECchr17580046613'Flanknovel0.53
UCECchr1758005572Missense_MutationnovelV194A0.28
UCECchr17580037863'Flanknovel0.42
UCECchr17580042893'Flanknovel0.33
UCECchr1758005777Intronnovel0.24
UCSchr1758007109Missense_MutationnovelP10L0.08

Copy Number Variations (CNVs)
CancerTypeFreq Q-value
DLBCDEL0.04170.18166
KIRPAMP0.66320.14801
PAADDEL0.21741.3088e-08
READAMP0.16970.15915
THCADEL0.0020.221
UVMAMP0.16250.054583

Survival Analysis
CancerP-value Q-value
THYM0.0082

Kaplan-Meier Survival Analysis

KIRC0.024

Kaplan-Meier Survival Analysis

STAD0.019

Kaplan-Meier Survival Analysis

SARC0.0089

Kaplan-Meier Survival Analysis

ACC0.0048

Kaplan-Meier Survival Analysis

PRAD0.039

Kaplan-Meier Survival Analysis

KIRP0.029

Kaplan-Meier Survival Analysis

COAD0.0015

Kaplan-Meier Survival Analysis

BLCA0.011

Kaplan-Meier Survival Analysis

CESC0.00085

Kaplan-Meier Survival Analysis

READ0.00071

Kaplan-Meier Survival Analysis

LIHC0.00014

Kaplan-Meier Survival Analysis

LGG0.0039

Kaplan-Meier Survival Analysis

LUAD0.018

Kaplan-Meier Survival Analysis

UVM0.014

Kaplan-Meier Survival Analysis

Drugs

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Eesembl ID



Cell lines and drugs in GSE70138 or GSE92742

  • Description
  • RBDs
  • RBPome
  • PRI
  • Literatures
  • Expression
  • Transcripts
  • Gene Model
  • Pathways
  • Phenotypes
  • PPI
  • Paralogs
  • Orthologs
  • Gene Ontology
Description
Ensembl ID
ENSG00000136450 (Gene tree)
Gene ID
6426
Gene Symbol
SRSF1
Alias
ASF|SF2|SRp30a|SF2p33|MGC5228|SFRS1
Full Name
serine and arginine rich splicing factor 1
Gene Type
protein_coding
Species
Homo_sapiens
Status
confidence
Strand
Minus strand
Length
6,428 bases
Position
chr17:58,000,919-58,007,346
Accession
10780
RBP type
canonical RBP
Summary
This gene encodes a member of the arginine/serine-rich splicing factor protein family. The encoded protein can either activate or repress splicing, depending on its phosphorylation state and its interaction partners. Multiple transcript variants have been found for this gene. There is a pseudogene of this gene on chromosome 13. [provided by RefSeq, Jun 2014]
RNA binding domains(RBDs)
Protein IDDomain Pfam IDE-value Domain number Total number
ENSP00000462215RRM_1PF00076.221.3e-3312
ENSP00000462215RRM_1PF00076.221.3e-3322
ENSP00000258962RRM_1PF00076.225.1e-3312
ENSP00000258962RRM_1PF00076.225.1e-3322
ENSP00000463042RRM_1PF00076.225.5e-3312
ENSP00000463042RRM_1PF00076.225.5e-3322
ENSP00000462687RRM_1PF00076.222.1e-1511
RNA binding proteome (RBPome)
PIDTitleMethod TimeAuthorDoi
22681889The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts4SURIC & HEK2932012 MayBaltz AGDOI: 10.1016/j.molcel.2012.05.021
30607034Comprehensive identification of RNA protein interactions in any organism using orthogonal organic phase separation (OOPS)OOPS & HEK2932019 Jan 3Queiroz RMLDOI: 10.1038/s41587-018-0001-2
29431736Capturing the interactome of newly transcribed RNANascentRICK & Hela2018 Feb 12Bao XDOI: 10.1038/nmeth.4595
29431736Capturing the interactome of newly transcribed RNAPolyT-RICK & Hela2018 Feb 12Bao XDOI: 10.1038/nmeth.4595
29431736Capturing the interactome of newly transcribed RNARIC & Hela2018 Feb 12Bao XDOI: 10.1038/nmeth.4595
29431736Capturing the interactome of newly transcribed RNARICK & Hela2018 Feb 12Bao XDOI: 10.1038/nmeth.4595
22658674Insights into RNA biology from an atlas of mammalian mRNA-binding proteinsRIC & Hela2012 May 31Castello ADOI: 10.1016/j.cell.2012.04.031
30528433The Human RNA-Binding Proteome and Its Dynamics during Translational ArrestXRNAX & Hela2018 Dec 6Trendel JDOI: 10.1016/j.cell.2018.11.004
30607034Comprehensive identification of RNA protein interactions in any organism using orthogonal organic phase separation (OOPS)OOPS & MCF10A2019 Jan 3Queiroz RMLDOI: 10.1038/s41587-018-0001-2
30528433The Human RNA-Binding Proteome and Its Dynamics during Translational ArrestXRNAX & MCF72018 Dec 6Trendel JDOI: 10.1016/j.cell.2018.11.004
30607034Comprehensive identification of RNA protein interactions in any organism using orthogonal organic phase separation (OOPS)OOPS & U2OS2019 Jan 3Queiroz RMLDOI: 10.1038/s41587-018-0001-2
27453046Comprehensive Identification of RNA-Binding Domains in Human CellsRIC & Hela2016 Aug 18Castello ADOI: 10.1016/j.molcel.2016.06.029
30352994Discovery of RNA-binding proteins and characterization of their dynamic responses by enhanced RNA interactome captureRIC & Jurkat2018 Oct 23Perez-Perri JIDOI:10.1038/s41467-018-06557-8
Protein-RNA interaction(RNA-Binding Site)
Click here to download all RNA binding sites
Click here to download all RNA binding sites

Literatures on RNA binding capacity
PIDTitleArticle TimeAuthorDoi
26282582SRSF1 and hnRNP H antagonistically regulate splicing of COLQ exon 16 in a congenital myasthenic syndrome.Sci Rep2015 Aug 18Rahman MAdoi: 10.1038/srep13208.
23836656Isolated pseudo-RNA-recognition motifs of SR proteins can regulate splicing using a noncanonical mode of RNA recognition.Proc Natl Acad Sci U S A2013 Jul 23Clery Adoi: 10.1073/pnas.1303445110
23975767catRAPID omics: a web server for large-scale prediction of protein-RNA interactions.Bioinformatics2013 Nov 15Agostini Fdoi: 10.1093/bioinformatics/btt495
25878250Heterogeneous Nuclear Ribonucleoprotein C Proteins Interact with the Human Papillomavirus Type 16 (HPV16) Early 3'-Untranslated Region and Alleviate Suppression of HPV16 Late L1 mRNA Splicing.J Biol Chem2015 May 22Dhanjal Sdoi: 10.1074/jbc.M115.638098
27935425How is Herstatin, a tumor suppressor splice variant of the oncogene HER2, regulated?RNA Biol2017 May 4Silipo Mdoi: 10.1080/15476286.2016.1267074
7512732The human splicing factor ASF/SF2 can specifically recognize pre-mRNA 5' splice sites.Proc Natl Acad Sci U S A1994 Apr 12Zuo P-
10022843The splicing factor-associated protein, p32, regulates RNA splicing by inhibiting ASF/SF2 RNA binding and phosphorylation.EMBO J1999 Feb 15Petersen-Mahrt SK-
8690088The RNA helicase CI from plum pox potyvirus has two regions involved in binding to RNA.FEBS Lett1996 Jun 17Fernandez A-
21536904Interaction between the RNA binding domains of Ser-Arg splicing factor 1 and U1-70K snRNP protein determines early spliceosome assembly.Proc Natl Acad Sci U S A2011 May 17Cho Sdoi: 10.1073/pnas.1017700108
20477871The splicing factor ASF/SF2 is associated with TIA-1-related/TIA-1-containing ribonucleoproteic complexes and contributes to post-transcriptional repression of gene expression.FEBS J2010 JunDelestienne Ndoi: 10.1111/j.1742-4658.2010.07664.x
26965252Characterization of RNA-Protein Interactions: Lessons from Two RNA-Binding Proteins, SRSF1 and SRSF2.Methods Mol Biol2016Skrdlant Ldoi: 10.1007/978-1-4939-3591-8_1.
28064149Emerging roles for RNA-binding proteins as effectors and regulators of cardiovascular disease.Eur Heart J2017 May 7de Bruin RGdoi: 10.1093/eurheartj/ehw567.
20120036The deep intronic c.903+469T>C mutation in the MTRR gene creates an SF2/ASF binding exonic splicing enhancer, which leads to pseudoexon activation and causes the cblE type of homocystinuria.Hum Mutat2010 AprHomolova Kdoi: 10.1002/humu.21206.
22369183Predicting sequence and structural specificities of RNA binding regions recognized by splicing factor SRSF1.BMC Genomics2011 Dec 23Wang Xdoi: 10.1186/1471-2164-12-S5-S8
21777388TDP-43: new aspects of autoregulation mechanisms in RNA binding proteins and their connection with human disease.FEBS J2011 OctBuratti Edoi: 10.1111/j.1742-4658.2011.08257.x
28990926IRAK2 directs stimulus-dependent nuclear export of inflammatory mRNAs.Elife2017 Oct 9Zhou Hdoi: 10.7554/eLife.29630.
7543047The human splicing factors ASF/SF2 and SC35 possess distinct, functionally significant RNA binding specificities.EMBO J1995 Jul 17Tacke R-
9761791The plant U1 small nuclear ribonucleoprotein particle 70K protein interacts with two novel serine/arginine-rich proteins.Plant Cell1998 OctGolovkin M-
1855257Primary structure of the human splicing factor ASF reveals similarities with Drosophila regulators.Cell1991 Jul 26Ge H-
1830244Functional expression of cloned human splicing factor SF2: homology to RNA-binding proteins, U1 70K, and Drosophila splicing regulators.Cell1991 Jul 26Krainer AR-
1340470The Drosophila RNA-binding protein RBP1 is localized to transcriptionally active sites of chromosomes and shows a functional similarity to human splicing factor ASF/SF2.Genes Dev1992 DecKim YJ-
9420331A specific subset of SR proteins shuttles continuously between the nucleus and the cytoplasm.Genes Dev1998 Jan 1Caceres JF-
8610170Pre-mRNA splicing in plants: characterization of Ser/Arg splicing factors.Proc Natl Acad Sci U S A1996 Apr 2Lopato S-
8223481Functional domains of the human splicing factor ASF/SF2.EMBO J1993 DecZuo P-
8013463Characterization and cloning of the human splicing factor 9G8: a novel 35 kDa factor of the serine/arginine protein family.EMBO J1994 Jun 1Cavaloc Y-
7667103U1 snRNP-ASF/SF2 interaction and 5' splice site recognition: characterization of required elements.Nucleic Acids Res1995 Aug 25Jamison SF-
16641292Cellular splicing and transcription regulatory protein p32 represses adenovirus major late transcription and causes hyperphosphorylation of RNA polymerase II.J Virol2006 MayOhrmalm C-
11801589Human splicing factor ASF/SF2 encodes for a repressor domain required for its inhibitory activity on pre-mRNA splicing.J Biol Chem2002 Apr 12Dauksaite V-
11072076Regulation of SRp20 exon 4 splicing.Biochim Biophys Acta2000 Nov 15Jumaa H-
15302913RNA recognition motif 2 directs the recruitment of SF2/ASF to nuclear stress bodies.Nucleic Acids Res2004 Aug 9Chiodi I-
15068396The second RNA-binding domain of the human splicing factor ASF/SF2 is the critical domain controlling adenovirus E1A alternative 5'-splice site selection.Biochem J2004 Jul 15Dauksaite V-
19906640Regulation of vascular endothelial growth factor (VEGF) splicing from pro-angiogenic to anti-angiogenic isoforms: a novel therapeutic strategy for angiogenesis.J Biol Chem2010 Feb 19Nowak DGdoi: 10.1074/jbc.M109.074930
19319956Increased expression of cellular RNA-binding proteins in HPV-induced neoplasia and cervical cancer.J Med Virol2009 MayFay Jdoi: 10.1002/jmv.21406.
18841201Identification of nuclear and cytoplasmic mRNA targets for the shuttling protein SF2/ASF.PLoS One2008 Oct 8Sanford JRdoi: 10.1371/journal.pone.0003369.
18463151Epstein-Barr virus SM protein functions as an alternative splicing factor.J Virol2008 JulVerma Ddoi: 10.1128/JVI.00344-08
17959926The RNA binding protein RNPS1 alleviates ASF/SF2 depletion-induced genomic instability.RNA2007 DecLi X-
17668007Structural and functional analysis of RNA and TAP binding to SF2/ASF.EMBO Rep2007 AugTintaru AM-
17176074A phosphoproteomic analysis of the ErbB2 receptor tyrosine kinase signaling pathways.Biochemistry2006 Dec 26Mukherji M-
22393468Protein kinase a-dependent phosphorylation of serine 119 in the proto-oncogenic serine/arginine-rich splicing factor 1 modulates its activity as a splicing enhancer protein.Genes Cancer2011 AugAksaas AKdoi: 10.1177/1947601911430226.
22172722WT1 mutants reveal SRPK1 to be a downstream angiogenesis target by altering VEGF splicing.Cancer Cell2011 Dec 13Amin EMdoi: 10.1016/j.ccr.2011.10.016.
21921418Skipping of an alternative intron in the srsf1 3' untranslated region increases transcript stability.J Med Invest2011 AugAkaike Y-
21852328The SRSF1 linker induces semi-conservative ESE binding by cooperating with the RRMs.Nucleic Acids Res2011 NovCho Sdoi: 10.1093/nar/gkr663
21822258Treatment with IL-17 prolongs the half-life of chemokine CXCL1 mRNA via the adaptor TRAF5 and the splicing-regulatory factor SF2 (ASF).Nat Immunol2011 Aug 7Sun Ddoi: 10.1038/ni.2081.
23284704Regulation of Mcl-1 by SRSF1 and SRSF5 in cancer cells.PLoS One2012Gautrey HLdoi: 10.1371/journal.pone.0051497
20460515Identification of ASF/SF2 as a critical, allele-specific effector of the cyclin D1b oncogene.Cancer Res2010 May 15Olshavsky NAdoi: 10.1158/0008-5472.CAN-09-3468
24926617p53-directed translational control can shape and expand the universe of p53 target genes.Cell Death Differ2014 OctZaccara Sdoi: 10.1038/cdd.2014.79
23592547SRSF1 and SRSF9 RNA binding proteins promote Wnt signalling-mediated tumorigenesis by enhancing β-catenin biosynthesis.EMBO Mol Med2013 MayFu Ydoi: 10.1002/emmm.201202218
24290757Hexanucleotide repeats in ALS/FTD form length-dependent RNA foci, sequester RNA binding proteins, and are neurotoxic.Cell Rep2013 Dec 12Lee YBdoi: 10.1016/j.celrep.2013.10.049
27091468Directional Phosphorylation and Nuclear Transport of the Splicing Factor SRSF1 Is Regulated by an RNA Recognition Motif.J Mol Biol2016 Jun 5Serrano Pdoi: 10.1016/j.jmb.2016.04.009
25855733SRSF1 RNA Recognition Motifs Are Strong Inhibitors of HIV-1 Replication.J Virol2015 JunPaz Sdoi: 10.1128/JVI.00693-15
28444861LncRNA MALAT1 is dysregulated in diabetic nephropathy and involved in high glucose-induced podocyte injury via its interplay with β-catenin.J Cell Mol Med2017 NovHu Mdoi: 10.1111/jcmm.13189
28721276Metformin decreases progerin expression and alleviates pathological defects of Hutchinson-Gilford progeria syndrome cells.NPJ Aging Mech Dis2016 Nov 10Egesipe ALdoi: 10.1038/npjamd.2016.26
27528402Human satellite-III non-coding RNAs modulate heat-shock-induced transcriptional repression.J Cell Sci2016 Oct 1Goenka A-
30087231Disruption by SaCas9 Endonuclease of HERV-Kenv, a Retroviral Gene with Oncogenic and Neuropathogenic Potential, Inhibits Molecules Involved in Cancer and Amyotrophic Lateral Sclerosis.Viruses2018 Aug 7Ibba Gdoi: 10.3390/v10080412.
30181552The oncogenic RNA-binding protein SRSF1 regulates LIG1 in non-small cell lung cancer.Lab Invest2018 DecMartinez-Terroba Edoi: 10.1038/s41374-018-0128-2
31142587c-MYC regulates mRNA translation efficiency and start-site selection in lymphoma.J Exp Med2019 Jul 1Singh Kdoi: 10.1084/jem.20181726
31200124The RNA-binding protein SRSF1 is a key cell cycle regulator via stabilizing NEAT1 in glioma.Int J Biochem Cell Biol2019 AugZhou Xdoi: 10.1016/j.biocel.2019.06.003
20617199RNAcontext: a new method for learning the sequence and structure binding preferences of RNA-binding proteins.PLoS Comput Biol2010 Jul 1Kazan Hdoi: 10.1371/journal.pcbi.1000832.
23349975Identification of a binding site for ASF/SF2 on an RNA fragment derived from the hepatitis delta virus genome.PLoS One2013Sikora Ddoi: 10.1371/journal.pone.0054832
23658645HnRNP A1/A2 and SF2/ASF regulate alternative splicing of interferon regulatory factor-3 and affect immunomodulatory functions in human non-small cell lung cancer cells.PLoS One2013 Apr 29Guo Rdoi: 10.1371/journal.pone.0062729
9023367HIV Rev-dependent binding of SF2/ASF to the Rev response element: possible role in Rev-mediated inhibition of HIV RNA splicing.Proc Natl Acad Sci U S A1997 Feb 4Powell DM-
9030686Phosphorylation of the ASF/SF2 RS domain affects both protein-protein and protein-RNA interactions and is necessary for splicing.Genes Dev1997 Feb 1Xiao SH-
8223480Functional analysis of pre-mRNA splicing factor SF2/ASF structural domains.EMBO J1993 DecCaceres JF-
12419255A Janus splicing regulatory element modulates HIV-1 tat and rev mRNA production by coordination of hnRNP A1 cooperative binding.J Mol Biol2002 Nov 1Marchand V-
11278454Binding sites for Rev and ASF/SF2 map to a 55-nucleotide purine-rich exonic element in equine infectious anemia virus RNA.J Biol Chem2001 Jun 1Chung H-
10880506Mapping the SF2/ASF binding sites in the bovine growth hormone exonic splicing enhancer.J Biol Chem2000 Sep 15Dirksen WP-
19047369SRp20 and CUG-BP1 modulate insulin receptor exon 11 alternative splicing.Mol Cell Biol2009 FebSen Sdoi: 10.1128/MCB.01709-08
20558599Alternative splicing of CD200 is regulated by an exonic splicing enhancer and SF2/ASF.Nucleic Acids Res2010 OctChen Zdoi: 10.1093/nar/gkq554
24869919N-terminus of the protein kinase CLK1 induces SR protein hyperphosphorylation.Biochem J2014 Aug 15Aubol BEdoi: 10.1042/BJ20140494.
24371143TMPyP4 porphyrin distorts RNA G-quadruplex structures of the disease-associated r(GGGGCC)n repeat of the C9orf72 gene and blocks interaction of RNA-binding proteins.J Biol Chem2014 Feb 21Zamiri Bdoi: 10.1074/jbc.C113.502336
23851510Mechanisms of the androgen receptor splicing in prostate cancer cells.Oncogene2014 Jun 12Liu LLdoi: 10.1038/onc.2013.284
28286323switchSENSE: A new technology to study protein-RNA interactions.Methods2017 Apr 15Clery Adoi: 10.1016/j.ymeth.2017.03.004
27999187Targeting the pro-angiogenic forms of VEGF or inhibiting their expression as anti-cancer strategies.Oncotarget2017 Feb 7Guyot Mdoi: 10.18632/oncotarget.13942.
28874828SRSF1 suppresses selection of intron-distal 5' splice site of DOK7 intron 4 to generate functional full-length Dok-7 protein.Sci Rep2017 Sep 5Ahsan KBdoi: 10.1038/s41598-017-11036-z.
30185622Molecular interactions connecting the function of the serine-arginine-rich protein SRSF1 to protein phosphatase 1.J Biol Chem2018 Oct 26Aubol BEdoi: 10.1074/jbc.RA118.004587
31208978SRSF1 and PTBP1 are trans-acting factors that suppress the formation of a CD33 splicing isoform linked to Alzheimer's disease risk.Mol Cell Biol2019 Jun 17van Bergeijk Pdoi: 10.1128/MCB.00568-18
Expression
Transcripts
Transcript IDNameLengthRefSeq ID Protein IDLengthRefSeq IDUniportKB ID
ENST00000584668SRSF1-207758-ENSP00000462616143 (aa)-J3KSR8
ENST00000584773SRSF1-2081317-ENSP00000463042253 (aa)-J3KTL2
ENST00000581979SRSF1-2041720-ENSP00000463223201 (aa)-Q07955
ENST00000582730SRSF1-2053117-ENSP00000462215201 (aa)-Q07955
ENST00000583741SRSF1-2061465-ENSP0000046391765 (aa)-J3QQV5
ENST00000578430SRSF1-202689--- (aa)--
ENST00000581497SRSF1-203438--- (aa)--
ENST00000258962SRSF1-2011513-ENSP00000258962248 (aa)-Q07955
ENST00000585096SRSF1-209568-ENSP0000046268773 (aa)-J3KSW7
Gene Model
Click here to download ENSG00000136450's gene model file
Pathways
Pathway IDPathway NameSource
hsa03040SpliceosomeKEGG
hsa04657IL-17 signaling pathwayKEGG
hsa05168Herpes simplex virus 1 infectionKEGG
Phenotypes
ensgIDTraitpValuePubmed ID
ENSG00000136450Stroke4.8610530E-00419369658
Protein-Protein Interaction (PPI)

Clik here to download ENSG00000136450's network

* RBP PPI network refers to all genes directly bind to RBP
Paralogs
Ensembl IDGene SymbolCoverageIdentiy ParalogGene SymbolCoverageIdentiy
ENSG00000136450SRSF17948.276ENSG00000115875SRSF75548.649
ENSG00000136450SRSF110067.692ENSG00000111786SRSF99762.698
ENSG00000136450SRSF17861.404ENSG00000100650SRSF59643.548
ENSG00000136450SRSF17740.678ENSG00000147274RBMX7640.678
ENSG00000136450SRSF17950.000ENSG00000112081SRSF36350.000
ENSG00000136450SRSF18444.828ENSG00000116350SRSF46044.770
ENSG00000136450SRSF17750.000ENSG00000124193SRSF65840.670
Orthologs
Ensembl IDGene SymbolCoverageIdentiy OrthologGene SymbolCoverageIdentiy Species
ENSG00000136450SRSF110090.769ENSAPOG00000008542-10086.220Acanthochromis_polyacanthus
ENSG00000136450SRSF19591.935ENSAPOG00000002748-9884.362Acanthochromis_polyacanthus
ENSG00000136450SRSF1100100.000ENSAMEG00000002635SRSF110097.177Ailuropoda_melanoleuca
ENSG00000136450SRSF19591.935ENSACIG00000008091srsf1a9878.926Amphilophus_citrinellus
ENSG00000136450SRSF19591.935ENSAOCG00000010671-9885.185Amphiprion_ocellaris
ENSG00000136450SRSF110090.769ENSAOCG00000000337-10086.508Amphiprion_ocellaris
ENSG00000136450SRSF110090.769ENSAPEG00000023352-9986.561Amphiprion_percula
ENSG00000136450SRSF19591.935ENSAPEG00000009915-9885.185Amphiprion_percula
ENSG00000136450SRSF19591.935ENSATEG00000022403-9884.898Anabas_testudineus
ENSG00000136450SRSF110087.692ENSATEG00000021567-10084.959Anabas_testudineus
ENSG00000136450SRSF110098.462ENSACAG00000005542-10098.387Anolis_carolinensis
ENSG00000136450SRSF17892.157ENSANAG00000025417-9976.016Aotus_nancymaae
ENSG00000136450SRSF1100100.000ENSANAG00000020583-100100.000Aotus_nancymaae
ENSG00000136450SRSF19996.479ENSAMXG00000024373-9477.778Astyanax_mexicanus
ENSG00000136450SRSF19596.774ENSAMXG00000035996srsf1a9893.145Astyanax_mexicanus
ENSG00000136450SRSF1100100.000ENSBTAG00000014766SRSF1100100.000Bos_taurus
ENSG00000136450SRSF1100100.000ENSCJAG00000041713-100100.000Callithrix_jacchus
ENSG00000136450SRSF19890.625ENSCJAG00000008111-8891.371Callithrix_jacchus
ENSG00000136450SRSF1100100.000ENSCAFG00000017430SRSF1100100.000Canis_familiaris
ENSG00000136450SRSF1100100.000ENSCAFG00020025632-100100.000Canis_lupus_dingo
ENSG00000136450SRSF1100100.000ENSCHIG00000010787SRSF1100100.000Capra_hircus
ENSG00000136450SRSF1100100.000ENSTSYG00000013899-100100.000Carlito_syrichta
ENSG00000136450SRSF1100100.000ENSCPOG00000032681-100100.000Cavia_porcellus
ENSG00000136450SRSF1100100.000ENSCCAG00000029484-100100.000Cebus_capucinus
ENSG00000136450SRSF1100100.000ENSCATG00000042294-100100.000Cercocebus_atys
ENSG00000136450SRSF110096.923ENSCATG00000005962-7596.629Cercocebus_atys
ENSG00000136450SRSF1100100.000ENSCLAG00000014707-100100.000Chinchilla_lanigera
ENSG00000136450SRSF110099.209ENSCSAG00000005642-10099.209Chlorocebus_sabaeus
ENSG00000136450SRSF1100100.000ENSCHOG00000001899SRSF1100100.000Choloepus_hoffmanni
ENSG00000136450SRSF1100100.000ENSCPBG00000009851-10098.814Chrysemys_picta_bellii
ENSG00000136450SRSF1100100.000ENSCANG00000029726-100100.000Colobus_angolensis_palliatus
ENSG00000136450SRSF1100100.000ENSCGRG00001000670Srsf1100100.000Cricetulus_griseus_chok1gshd
ENSG00000136450SRSF1100100.000ENSCGRG00000005590Srsf1100100.000Cricetulus_griseus_crigri
ENSG00000136450SRSF110090.769ENSCSEG00000009973-10080.303Cynoglossus_semilaevis
ENSG00000136450SRSF19493.443ENSCSEG00000014272-9884.553Cynoglossus_semilaevis
ENSG00000136450SRSF19591.935ENSCVAG00000018617-9885.185Cyprinodon_variegatus
ENSG00000136450SRSF19486.458ENSCVAG00000005458-9886.179Cyprinodon_variegatus
ENSG00000136450SRSF19996.735ENSDARG00000017843srsf1b9996.735Danio_rerio
ENSG00000136450SRSF19596.774ENSDARG00000057691srsf1a9892.095Danio_rerio
ENSG00000136450SRSF1100100.000ENSDNOG00000011737-100100.000Dasypus_novemcinctus
ENSG00000136450SRSF1100100.000ENSDORG00000015082Srsf1100100.000Dipodomys_ordii
ENSG00000136450SRSF110096.923ENSETEG00000005349-6398.913Echinops_telfairi
ENSG00000136450SRSF1100100.000ENSEASG00005002922-100100.000Equus_asinus_asinus
ENSG00000136450SRSF1100100.000ENSECAG00000016654SRSF1100100.000Equus_caballus
ENSG00000136450SRSF1100100.000ENSEEUG00000009255-63100.000Erinaceus_europaeus
ENSG00000136450SRSF19595.161ENSELUG00000021646srsf1a9879.839Esox_lucius
ENSG00000136450SRSF1100100.000ENSFCAG00000002250-100100.000Felis_catus
ENSG00000136450SRSF19897.857ENSFALG00000005062-10082.213Ficedula_albicollis
ENSG00000136450SRSF1100100.000ENSFDAG00000010646-100100.000Fukomys_damarensis
ENSG00000136450SRSF19591.935ENSFHEG00000003174srsf1a9885.185Fundulus_heteroclitus
ENSG00000136450SRSF19493.443ENSGMOG00000014787-9982.645Gadus_morhua
ENSG00000136450SRSF1100100.000ENSGALG00000005525SRSF110098.790Gallus_gallus
ENSG00000136450SRSF110090.769ENSGACG00000020621srsf1b10074.390Gasterosteus_aculeatus
ENSG00000136450SRSF1100100.000ENSGAGG00000022965-10098.814Gopherus_agassizii
ENSG00000136450SRSF1100100.000ENSGGOG00000004386SRSF1100100.000Gorilla_gorilla
ENSG00000136450SRSF19493.443ENSHBUG00000016788srsf1a9884.774Haplochromis_burtoni
ENSG00000136450SRSF199100.000ENSHGLG00000000669-100100.000Heterocephalus_glaber_female
ENSG00000136450SRSF199100.000ENSHGLG00000000600-100100.000Heterocephalus_glaber_female
ENSG00000136450SRSF1100100.000ENSHGLG00100016906-100100.000Heterocephalus_glaber_male
ENSG00000136450SRSF19590.323ENSHCOG00000018918srsf1a9781.928Hippocampus_comes
ENSG00000136450SRSF110096.923ENSIPUG00000008750srsf1b10095.968Ictalurus_punctatus
ENSG00000136450SRSF19496.721ENSIPUG00000017039srsf1a9893.145Ictalurus_punctatus
ENSG00000136450SRSF1100100.000ENSSTOG00000000243-100100.000Ictidomys_tridecemlineatus
ENSG00000136450SRSF1100100.000ENSJJAG00000000102-100100.000Jaculus_jaculus
ENSG00000136450SRSF110098.462ENSJJAG00000014464-9588.189Jaculus_jaculus
ENSG00000136450SRSF19591.935ENSKMAG00000019232srsf1a9883.951Kryptolebias_marmoratus
ENSG00000136450SRSF19591.935ENSLBEG00000020864-9884.362Labrus_bergylta
ENSG00000136450SRSF110078.462ENSLBEG00000015294-9883.133Labrus_bergylta
ENSG00000136450SRSF195100.000ENSLACG00000014160srsf1a9293.878Latimeria_chalumnae
ENSG00000136450SRSF1100100.000ENSLOCG00000005994srsf1a10097.177Lepisosteus_oculatus
ENSG00000136450SRSF1100100.000ENSLAFG00000025743SRSF1100100.000Loxodonta_africana
ENSG00000136450SRSF1100100.000ENSMFAG00000040003-100100.000Macaca_fascicularis
ENSG00000136450SRSF1100100.000ENSMMUG00000004725SRSF1100100.000Macaca_mulatta
ENSG00000136450SRSF110098.462ENSMMUG00000003260-10097.233Macaca_mulatta
ENSG00000136450SRSF1100100.000ENSMNEG00000027680-100100.000Macaca_nemestrina
ENSG00000136450SRSF110096.923ENSMNEG00000015983-10096.838Macaca_nemestrina
ENSG00000136450SRSF110096.923ENSMLEG00000015243-10094.466Mandrillus_leucophaeus
ENSG00000136450SRSF1100100.000ENSMLEG00000040509SRSF1100100.000Mandrillus_leucophaeus
ENSG00000136450SRSF110095.385ENSMAMG00000019691-10088.211Mastacembelus_armatus
ENSG00000136450SRSF110089.231ENSMAMG00000019687-10085.081Mastacembelus_armatus
ENSG00000136450SRSF19591.935ENSMAMG00000018454-9885.185Mastacembelus_armatus
ENSG00000136450SRSF15380.263ENSMGAG00000008204-5698.387Meleagris_gallopavo
ENSG00000136450SRSF1100100.000ENSMAUG00000021845Srsf1100100.000Mesocricetus_auratus
ENSG00000136450SRSF1100100.000ENSMICG00000013639-100100.000Microcebus_murinus
ENSG00000136450SRSF1100100.000ENSMOCG00000001996Srsf1100100.000Microtus_ochrogaster
ENSG00000136450SRSF19493.443ENSMMOG00000014354srsf1a9878.099Mola_mola
ENSG00000136450SRSF1100100.000ENSMODG00000014781-6398.919Monodelphis_domestica
ENSG00000136450SRSF110092.308ENSMALG00000007763-7979.695Monopterus_albus
ENSG00000136450SRSF19591.935ENSMALG00000017129-7588.601Monopterus_albus
ENSG00000136450SRSF1100100.000MGP_CAROLIEiJ_G0016943Srsf1100100.000Mus_caroli
ENSG00000136450SRSF1100100.000ENSMUSG00000018379Srsf1100100.000Mus_musculus
ENSG00000136450SRSF1100100.000MGP_PahariEiJ_G0018074Srsf1100100.000Mus_pahari
ENSG00000136450SRSF1100100.000MGP_SPRETEiJ_G0017790Srsf1100100.000Mus_spretus
ENSG00000136450SRSF1100100.000ENSMPUG00000015369SRSF1100100.000Mustela_putorius_furo
ENSG00000136450SRSF19997.183ENSMLUG00000023995-10090.323Myotis_lucifugus
ENSG00000136450SRSF1100100.000ENSMLUG00000011040SRSF1100100.000Myotis_lucifugus
ENSG00000136450SRSF1100100.000ENSNGAG00000011395Srsf1100100.000Nannospalax_galili
ENSG00000136450SRSF110092.308ENSNBRG00000008041srsf1b8082.741Neolamprologus_brichardi
ENSG00000136450SRSF1100100.000ENSNLEG00000008088-100100.000Nomascus_leucogenys
ENSG00000136450SRSF1100100.000ENSMEUG00000002783-10098.425Notamacropus_eugenii
ENSG00000136450SRSF199100.000ENSOPRG00000001234-100100.000Ochotona_princeps
ENSG00000136450SRSF110099.597ENSODEG00000011481-10099.597Octodon_degus
ENSG00000136450SRSF19591.935ENSONIG00000013160-9884.774Oreochromis_niloticus
ENSG00000136450SRSF110095.385ENSONIG00000004860-8190.863Oreochromis_niloticus
ENSG00000136450SRSF110072.308ENSOCUG00000010894-7771.795Oryctolagus_cuniculus
ENSG00000136450SRSF19591.935ENSORLG00000004580srsf1a9885.185Oryzias_latipes
ENSG00000136450SRSF19591.935ENSORLG00020009456srsf1a9885.185Oryzias_latipes_hni
ENSG00000136450SRSF19493.443ENSORLG00015014384srsf1a9884.774Oryzias_latipes_hsok
ENSG00000136450SRSF18487.719ENSOMEG00000004106srsf1a9282.743Oryzias_melastigma
ENSG00000136450SRSF1100100.000ENSOGAG00000025950-100100.000Otolemur_garnettii
ENSG00000136450SRSF110098.462ENSOARG00000008323SRSF110095.161Ovis_aries
ENSG00000136450SRSF1100100.000ENSPPAG00000043403-100100.000Pan_paniscus
ENSG00000136450SRSF1100100.000ENSPPRG00000004238-100100.000Panthera_pardus
ENSG00000136450SRSF1100100.000ENSPTRG00000049077SRSF1100100.000Pan_troglodytes
ENSG00000136450SRSF19797.826ENSPANG00000030275-10076.680Papio_anubis
ENSG00000136450SRSF1100100.000ENSPANG00000022305-100100.000Papio_anubis
ENSG00000136450SRSF110098.462ENSPKIG00000012857srsf1b10095.968Paramormyrops_kingsleyae
ENSG00000136450SRSF19995.102ENSPKIG00000007204srsf1a9995.102Paramormyrops_kingsleyae
ENSG00000136450SRSF19997.887ENSPSIG00000009000-10092.000Pelodiscus_sinensis
ENSG00000136450SRSF19493.443ENSPMGG00000013112-9985.654Periophthalmus_magnuspinnatus
ENSG00000136450SRSF19691.971ENSPMGG00000005467-9985.470Periophthalmus_magnuspinnatus
ENSG00000136450SRSF1100100.000ENSPEMG00000021416Srsf1100100.000Peromyscus_maniculatus_bairdii
ENSG00000136450SRSF1100100.000ENSPCIG00000006076-10099.197Phascolarctos_cinereus
ENSG00000136450SRSF19486.911ENSPFOG00000018325-8685.714Poecilia_formosa
ENSG00000136450SRSF19486.911ENSPLAG00000008416srsf1b9885.714Poecilia_latipinna
ENSG00000136450SRSF19486.911ENSPMEG00000002388-9885.714Poecilia_mexicana
ENSG00000136450SRSF19493.443ENSPMEG00000020607-9887.805Poecilia_mexicana
ENSG00000136450SRSF19493.443ENSPMEG00000014312-9887.805Poecilia_mexicana
ENSG00000136450SRSF19591.935ENSPREG00000009667srsf1a9885.185Poecilia_reticulata
ENSG00000136450SRSF1100100.000ENSPPYG00000008240SRSF1100100.000Pongo_abelii
ENSG00000136450SRSF1100100.000ENSPCAG00000005199SRSF1100100.000Procavia_capensis
ENSG00000136450SRSF1100100.000ENSPCOG00000023654-100100.000Propithecus_coquereli
ENSG00000136450SRSF110087.692ENSPCOG00000025736-9576.531Propithecus_coquereli
ENSG00000136450SRSF1100100.000ENSPVAG00000000519-75100.000Pteropus_vampyrus
ENSG00000136450SRSF19596.774ENSPNAG00000022241srsf1a9890.947Pygocentrus_nattereri
ENSG00000136450SRSF110098.462ENSPNAG00000014601srsf1b10094.355Pygocentrus_nattereri
ENSG00000136450SRSF1100100.000ENSRNOG00000050323Srsf1100100.000Rattus_norvegicus
ENSG00000136450SRSF1100100.000ENSRBIG00000034445-100100.000Rhinopithecus_bieti
ENSG00000136450SRSF1100100.000ENSRROG00000041506-100100.000Rhinopithecus_roxellana
ENSG00000136450SRSF1100100.000ENSSBOG00000025377-100100.000Saimiri_boliviensis_boliviensis
ENSG00000136450SRSF1100100.000ENSSHAG00000002552-10099.197Sarcophilus_harrisii
ENSG00000136450SRSF16681.250ENSSFOG00015010677-5983.077Scleropages_formosus
ENSG00000136450SRSF19898.438ENSSFOG00015004800srsf1a9996.356Scleropages_formosus
ENSG00000136450SRSF18279.245ENSSFOG00015001585-7280.519Scleropages_formosus
ENSG00000136450SRSF19591.935ENSSMAG00000007018-9883.128Scophthalmus_maximus
ENSG00000136450SRSF110089.231ENSSMAG00000009719-10086.275Scophthalmus_maximus
ENSG00000136450SRSF19591.935ENSSDUG00000011303-9884.362Seriola_dumerili
ENSG00000136450SRSF110089.231ENSSDUG00000003929-9977.510Seriola_dumerili
ENSG00000136450SRSF19591.935ENSSLDG00000010543-9884.362Seriola_lalandi_dorsalis
ENSG00000136450SRSF110086.154ENSSLDG00000016895-9976.113Seriola_lalandi_dorsalis
ENSG00000136450SRSF110089.231ENSSLDG00000016868-9982.661Seriola_lalandi_dorsalis
ENSG00000136450SRSF1100100.000ENSSARG00000010949-63100.000Sorex_araneus
ENSG00000136450SRSF1100100.000ENSSPUG00000000804-10098.814Sphenodon_punctatus
ENSG00000136450SRSF110089.231ENSSPAG00000014152-9984.556Stegastes_partitus
ENSG00000136450SRSF19591.935ENSSPAG00000022562-9885.597Stegastes_partitus
ENSG00000136450SRSF1100100.000ENSSSCG00000017626-100100.000Sus_scrofa
ENSG00000136450SRSF19997.887ENSTGUG00000008416-10098.370Taeniopygia_guttata
ENSG00000136450SRSF19591.935ENSTRUG00000003691srsf1a9884.362Takifugu_rubripes
ENSG00000136450SRSF19591.935ENSTNIG00000016223srsf1a9884.362Tetraodon_nigroviridis
ENSG00000136450SRSF110095.385ENSTBEG00000015378-6398.370Tupaia_belangeri
ENSG00000136450SRSF199100.000ENSTTRG00000007310SRSF1100100.000Tursiops_truncatus
ENSG00000136450SRSF1100100.000ENSUAMG00000009858SRSF1100100.000Ursus_americanus
ENSG00000136450SRSF1100100.000ENSUMAG00000000455-100100.000Ursus_maritimus
ENSG00000136450SRSF1100100.000ENSVPAG00000010094SRSF110099.597Vicugna_pacos
ENSG00000136450SRSF1100100.000ENSVVUG00000011882-100100.000Vulpes_vulpes
ENSG00000136450SRSF1100100.000ENSXETG00000008954srsf110091.386Xenopus_tropicalis
ENSG00000136450SRSF19591.935ENSXMAG00000011766srsf1a9885.185Xiphophorus_maculatus
Gene Ontology
Go IDGo_termPubmedIDEvidenceCategory
GO:0000380alternative mRNA splicing, via spliceosome8940107.IDAProcess
GO:0000381regulation of alternative mRNA splicing, via spliceosome21873635.IBAProcess
GO:0000395mRNA 5'-splice site recognition8940107.9885563.IDAProcess
GO:0000398mRNA splicing, via spliceosome11991638.ICProcess
GO:0000398mRNA splicing, via spliceosome-TASProcess
GO:0001701in utero embryonic development-IEAProcess
GO:0003723RNA binding22658674.22681889.HDAFunction
GO:0003723RNA binding21873635.IBAFunction
GO:0003723RNA binding19561594.IDAFunction
GO:0003723RNA binding20797886.IPIFunction
GO:0003729mRNA binding21984414.IDAFunction
GO:0005515protein binding9237760.9885563.10196197.15184380.15243141.15652350.15798186.18559666.18596238.20926688.21296756.21822258.21988832.23602568.23604122.IPIFunction
GO:0005634nucleus21630459.HDAComponent
GO:0005634nucleus21873635.IBAComponent
GO:0005634nucleus21984414.IDAComponent
GO:0005654nucleoplasm9885563.IDAComponent
GO:0005654nucleoplasm-TASComponent
GO:0005737cytoplasm-IEAComponent
GO:0006376mRNA splice site selection1830244.TASProcess
GO:0006397mRNA processing1830244.TASProcess
GO:0006405RNA export from nucleus-TASProcess
GO:0006406mRNA export from nucleus-TASProcess
GO:0016607nuclear speck21873635.IBAComponent
GO:0016607nuclear speck20797886.IDAComponent
GO:0031124mRNA 3'-end processing-TASProcess
GO:0033120positive regulation of RNA splicing-IEAProcess
GO:0035145exon-exon junction complex16314458.IDAComponent
GO:0043422protein kinase B binding-IEAFunction
GO:0044547DNA topoisomerase binding9611241.IPIFunction
GO:0045292mRNA cis splicing, via spliceosome21873635.IBAProcess
GO:0048709oligodendrocyte differentiation-IEAProcess
GO:0050733RS domain binding-IEAFunction
GO:0060048cardiac muscle contraction-IEAProcess
GO:0071013catalytic step 2 spliceosome11991638.IDAComponent
GO:0097421liver regeneration-IEAProcess
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