Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Splicing factor 1  

UniProtKB / Swiss-Prot ID :  SF01_HUMAN

Gene Name (Synonyms) : 
SF1, ZFM1, ZNF162  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. 

Protein Function :  Necessary for the ATP-dependent first step of spliceosome assembly. Binds to the intron branch point sequence (BPS) 5'-UACUAAC-3' of the pre-mRNA. May act as transcription repressor. 

Protein Sequence MATGANATPLDFPSKKRKRSRWNQDTMEQKTVIPGMPTVIPPGLTREQERAYIVQLQIEDLTRKLRTGDL...
Predicted Secondary Structure CCCCCCCCCCCCHHHHHHHHCCCCHHHHHHCCCCCCCCEECCCCCHHHHHHHHHHHHHHHHHHHHHHCCC...
Protein Variant
LocationDescription
357S -> T. VAR_017196
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MATGAN
---CCCCCC
18.10UniProtKB
Link-
20PhosphoserineKRKRSRWNQ
HHHHHCCCC
44.69SysPTM
Link-
20Phosphoserine (PKG1/cGK-I)KRKRSRWNQ
HHHHHCCCC
44.69PhosphoELM
Link-
20Phosphoserine (PRKG1)KRKRSRWNQ
HHHHHCCCC
44.69HPRD
Link-
20Phosphoserine; by PKG.KRKRSRWNQ
HHHHHCCCC
44.69UniProtKB
Link-
67PhosphothreonineRKLRTGDLG
HHHHHCCCC
45.55HPRD
Link-
80PhosphoserinePEDRSPSPE
CCCCCCCCC
41.89HPRD
Link-
80PhosphoserinePEDRSPSPE
CCCCCCCCC
41.89PhosphoELM
Link-
80PhosphoserinePEDRSPSPE
CCCCCCCCC
41.89SysPTM
Link-
80Phosphoserine.PEDRSPSPE
CCCCCCCCC
41.89UniProtKB
Link-
82PhosphoserineDRSPSPEPI
CCCCCCCCC
43.04HPRD
Link-
82PhosphoserineDRSPSPEPI
CCCCCCCCC
43.04PhosphoELM
Link-
82PhosphoserineDRSPSPEPI
CCCCCCCCC
43.04SysPTM
Link-
82Phosphoserine.DRSPSPEPI
CCCCCCCCC
43.04UniProtKB
Link-
87PhosphotyrosinePEPIYNSEG
CCCCCCCCC
24.29HPRD
Link-
87PhosphotyrosinePEPIYNSEG
CCCCCCCCC
24.29PhosphoELM
Link-
87PhosphotyrosinePEPIYNSEG
CCCCCCCCC
24.29SysPTM
Link-
87Phosphotyrosine.PEPIYNSEG
CCCCCCCCC
24.29UniProtKB
Link-
89PhosphoserinePIYNSEGKR
CCCCCCCCC
30.65HPRD
Link-
89PhosphoserinePIYNSEGKR
CCCCCCCCC
30.65SysPTM
Link-
89Phosphoserine.PIYNSEGKR
CCCCCCCCC
30.65UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
CD2B2_HUMANphysical interactionMINT-62843MINT15105431
SF3A2_HUMANphysical interactionMINT-5206115MINT17332742
SPF45_HUMANdirect interaction
direct interaction
DIP:58781EDIP17589525
17589525
DDX17_HUMANphysical interactionEBI-754810
intact16189514
WWP2_HUMANphysical interactionEBI-754882
intact16189514
RBPMS_HUMANphysical interactionEBI-756883
intact16189514
Q96HC5_HUMANphysical interactionEBI-760234
intact16189514
EWS_HUMANin vitro
yeast 2-hybrid
HPRD:03306HPRD9660765
FUS_HUMANin vitroHPRD:03306HPRD9660765
BCL2_HUMANin vitroHPRD:03306HPRD8668206
ARD1_HUMANyeast 2-hybridHPRD:03306HPRD16189514
WWP2_HUMANyeast 2-hybridHPRD:03306HPRD16189514
PLS1_HUMANyeast 2-hybridHPRD:03306HPRD16189514
DDX17_HUMANyeast 2-hybridHPRD:03306HPRD16189514
RBPMS_HUMANyeast 2-hybridHPRD:03306HPRD16189514
U2AF2_HUMANin vitro
yeast 2-hybrid
HPRD:03306HPRD9150140
9512519
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-80; SER-82; TYR-87 AND SER-89, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, AND MASSSPECTROMETRY.
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline.";
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
Electrophoresis 28:2027-2034(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-80; SER-82 ANDTYR-87, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-82 AND SER-89,PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-463 (ISOFORM 6), ANDMASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-80; SER-82; TYR-87 AND SER-89, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, AND MASSSPECTROMETRY.
"Phosphorylation of splicing factor SF1 on Ser20 by cGMP-dependentprotein kinase regulates spliceosome assembly.";
Wang X., Bruderer S., Rafi Z., Xue J., Milburn P.J., Kraemer A.,Robinson P.J.;
EMBO J. 18:4549-4559(1999).
Cited for: PROTEIN SEQUENCE OF 19-28; 94-103; 228-239 AND 298-308, FUNCTION,INTERACTION WITH U2AF2, MUTAGENESIS OF SER-20, AND PHOSPHORYLATION ATSER-20.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures