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

UniProtKB / Swiss-Prot ID :  SON_MOUSE

Gene Name (Synonyms) : 
Son, Nrebp  

Species :  Mus musculus (Mouse). 

Subcellular Localization :  Nucleus speckle (By similarity). Note=Colocalizes with the pre-mRNA splicing factor SRSF2 (By similarity). 

Protein Function :  RNA-binding protein that acts as a mRNA splicing cofactor by promoting efficient splicing of transcripts that posses weak splice sites. Specifically promotes splicing of many cell-cycle and DNA-repair transcripts that posses weak splice sites, such as TUBG1, KATNB1, TUBGCP2, AURKB, PCNT, AKT1, RAD23A, and FANCG. Probably acts by facilitating the interaction between Serine/arginine-rich proteins such as SRSF2 and the RNA polymerase II. Also binds to DNA; binds to the consensus DNA sequence: 5'- GA[GT]AN[CG][AG]CC-3' (By similarity). May also regulate the ghrelin signaling in hypothalamic neuron by acting as a negative regulator of GHSR expression. 

Protein Sequence MAADIEQVFRSFVVSKFREIQQELSSGRSEGQLNGETNPPIEGNQAGDTAASARSLPNEEIVQKIEEVLS...
Predicted Secondary Structure CCCCHHHHHHHHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCCCCCCCCCHHHHCCCHHHHHHHHHHHHH...
Protein Variant -
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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
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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
55PhosphoserineASARSLPNE
HHHHCCCHH
48.14Phosphositeplus
Link-
150PhosphoserineGNLESDSFL
CCCCCCCEE
41.54Phosphositeplus
Link-
152PhosphoserineLESDSFLKF
CCCCCEECC
41.58Phosphositeplus
Link-
256PhosphoserineAALKSPEPV
CCCCCCCCE
35.03Phosphositeplus
Link-
267PhosphotyrosineMSVEYQKSV
CCCCCCCCC
21.05Phosphositeplus
Link-
317PhosphoserineHPEPSPSTM
CCCCCCCCC
29.80Phosphositeplus
Link-
319PhosphoserineEPSPSTMDF
CCCCCCCCC
40.47Phosphositeplus
Link-
905PhosphoserineMGSKSPDPY
CCCCCCCCC
35.91Phosphositeplus
Link-
971PhosphoserineIAPRSYRIA
CCCCCCCCC
20.08Phosphositeplus
Link-
972PhosphotyrosineAPRSYRIAP
CCCCCCCCC
13.81Phosphositeplus
Link-
993PhosphoserineASRRSMMMS
CCCCCCCCC
15.21Phosphositeplus
Link-
1021PhosphoserineRSMMSPMAE
ECCCCCCHH
11.68Phosphositeplus
Link-
1046PhosphoserineRSMMSPMAE
CCCCEEEEE
11.68Phosphositeplus
Link-
1068PhosphoserineAYERSMMSP
CCCCCCCCC
13.59Phosphositeplus
Link-
1071PhosphoserineRSMMSPMAD
CCCCCCCCC
11.68Phosphositeplus
Link-
1708PhosphoserineDVEDSLPIK
CCCCCCCCC
23.65Phosphositeplus
Link-
1714PhosphoserinePIKESAQAV
CCCCCCCCC
22.22PhosphoELM
Link-
1714PhosphoserinePIKESAQAV
CCCCCCCCC
22.22Phosphositeplus
Link-
1714Phosphoserine.PIKESAQAV
CCCCCCCCC
22.22UniProtKB
Link-
1723PhosphoserineAVALSPKES
CCCCCCCCC
24.96PhosphoELM
Link-
1723PhosphoserineAVALSPKES
CCCCCCCCC
24.96Phosphositeplus
Link-
1723PhosphoserineAVALSPKES
CCCCCCCCC
24.96SysPTM
Link-
1723Phosphoserine.AVALSPKES
CCCCCCCCC
24.96UniProtKB
Link-
1791PhosphoserineERDKSAASP
CCCCCCCCC
33.10Phosphositeplus
Link-
1794PhosphoserineKSAASPVVI
CCCCCCCCC
20.24Phosphositeplus
Link-
1799PhosphoserinePVVISIPER
CCCCCCCCC
22.08Phosphositeplus
Link-
1805PhosphoserinePERASESSS
CCCCCCCCC
44.20Phosphositeplus
Link-
1807PhosphoserineRASESSSEE
CCCCCCCCC
36.35Phosphositeplus
Link-
1807PhosphoserineRASESSSEE
CCCCCCCCC
36.35SysPTM
Link-
1808PhosphoserineASESSSEEK
CCCCCCCCC
37.40Phosphositeplus
Link-
1808PhosphoserineASESSSEEK
CCCCCCCCC
37.40SysPTM
Link-
1809PhosphoserineSESSSEEKD
CCCCCCCCC
60.08PhosphoELM
Link-
1809PhosphoserineSESSSEEKD
CCCCCCCCC
60.08Phosphositeplus
Link-
1809PhosphoserineSESSSEEKD
CCCCCCCCC
60.08SysPTM
Link-
1809Phosphoserine.SESSSEEKD
CCCCCCCCC
60.08UniProtKB
Link-
1815PhosphotyrosineEKDDYEIFV
CCCCCCCHH
22.51Phosphositeplus
Link-
1845PhosphoserineKKRDSSLRS
CCCCCCCCC
34.99Phosphositeplus
Link-
1845Phosphoserine.KKRDSSLRS
CCCCCCCCC
34.99UniProtKB
Link-
1846PhosphoserineKRDSSLRSR
CCCCCCCCC
31.90Phosphositeplus
Link-
1846Phosphoserine.KRDSSLRSR
CCCCCCCCC
31.90UniProtKB
Link-
1849PhosphoserineSSLRSRSKR
CCCCCCCCC
46.31Phosphositeplus
Link-
1849Phosphoserine.SSLRSRSKR
CCCCCCCCC
46.31UniProtKB
Link-
1935PhosphoserineRKRSSSRDN
CCCCCCCCC
33.16PhosphoELM
Link-
1935PhosphoserineRKRSSSRDN
CCCCCCCCC
33.16SysPTM
Link-
1949PhosphothreonineARSRTPSRR
CCCCCCCCC
27.19Phosphositeplus
Link-
1951PhosphoserineSRTPSRRSR
CCCCCCCCC
39.45Phosphositeplus
Link-
1954PhosphoserinePSRRSRSHT
CCCCCCCCC
36.70Phosphositeplus
Link-
1956PhosphoserineRRSRSHTPS
CCCCCCCCC
32.72Phosphositeplus
Link-
1958PhosphothreonineSRSHTPSRR
CCCCCCCCC
24.98Phosphositeplus
Link-
1973PhosphoserineGRRRSFSIS
CCCCCCCCC
22.87PhosphoELM
Link-
1973PhosphoserineGRRRSFSIS
CCCCCCCCC
22.87Phosphositeplus
Link-
1973PhosphoserineGRRRSFSIS
CCCCCCCCC
22.87SysPTM
Link-
1973Phosphoserine.GRRRSFSIS
CCCCCCCCC
22.87UniProtKB
Link-
1975PhosphoserineRRSFSISPS
CCCCCCCCC
24.33Phosphositeplus
Link-
1975Phosphoserine.RRSFSISPS
CCCCCCCCC
24.33UniProtKB
Link-
1977PhosphoserineSFSISPSRR
CCCCCCCCC
18.67Phosphositeplus
Link-
1979PhosphoserineSISPSRRSR
CCCCCCCCC
33.27PhosphoELM
Link-
1979PhosphoserineSISPSRRSR
CCCCCCCCC
33.27Phosphositeplus
Link-
1979PhosphoserineSISPSRRSR
CCCCCCCCC
33.27SysPTM
Link-
1979Phosphoserine.SISPSRRSR
CCCCCCCCC
33.27UniProtKB
Link-
1982PhosphoserinePSRRSRTPS
CCCCCCCCC
39.12Phosphositeplus
Link-
1984PhosphothreonineRRSRTPSRR
CCCCCCCCC
27.19Phosphositeplus
Link-
1986PhosphoserineSRTPSRRSR
CCCCCCCCC
39.45Phosphositeplus
Link-
1989PhosphoserinePSRRSRTPS
CCCCCCCCC
39.12Phosphositeplus
Link-
1991PhosphothreonineRRSRTPSRR
CCCCCCCCC
27.19Phosphositeplus
Link-
1993PhosphoserineSRTPSRRSR
CCCCCCCCC
39.45Phosphositeplus
Link-
1996PhosphoserinePSRRSRTPS
CCCCCCCCC
39.12Phosphositeplus
Link-
1998PhosphothreonineRRSRTPSRR
CCCCCCCCC
27.19Phosphositeplus
Link-
2000PhosphoserineSRTPSRRSR
CCCCCCCCC
39.45Phosphositeplus
Link-
2003PhosphoserinePSRRSRTPS
CCCCCCCCC
39.12Phosphositeplus
Link-
2005PhosphothreonineRRSRTPSRR
CCCCCCCCC
27.19Phosphositeplus
Link-
2007PhosphoserineSRTPSRRSR
CCCCCCCCC
39.45Phosphositeplus
Link-
2010PhosphoserinePSRRSRTPS
CCCCCCCCC
39.12Phosphositeplus
Link-
2012PhosphothreonineRRSRTPSRR
CCCCCCCCC
27.19Phosphositeplus
Link-
2014PhosphoserineSRTPSRRRR
CCCCCCCCC
37.49Phosphositeplus
Link-
2027PhosphoserineVRRRSFSIS
CCCCCCCCC
22.87Phosphositeplus
Link-
2027Phosphoserine.VRRRSFSIS
CCCCCCCCC
22.87UniProtKB
Link-
2029PhosphoserineRRSFSISPV
CCCCCCCCC
24.33Phosphositeplus
Link-
2029Phosphoserine.RRSFSISPV
CCCCCCCCC
24.33UniProtKB
Link-
2031PhosphoserineSFSISPVRL
CCCCCCCCC
19.02Phosphositeplus
Link-
2031Phosphoserine.SFSISPVRL
CCCCCCCCC
19.02UniProtKB
Link-
2038PhosphoserineRLRRSRTPL
CCCCCCCCC
33.79Phosphositeplus
Link-
2040PhosphothreonineRRSRTPLRR
CCCCCCCCC
28.11Phosphositeplus
Link-
2047PhosphoserineRRRFSRSPI
CCCCCCCCC
30.00Phosphositeplus
Link-
2049PhosphoserineRFSRSPIRR
CCCCCCCCC
24.39Phosphositeplus
Link-
2147PhosphoserineKPHVSDEEE
CCCCCCCCC
35.95Phosphositeplus
Link-
2157PhosphotyrosineEPPFYHHPF
CCCCCCCCC
12.66Phosphositeplus
Link-
2256PhosphoserineQKRLSENAF
CCEEEEEHH
32.60Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1714; SER-1809;SER-1973; SER-1975 AND SER-1979, AND MASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1845; SER-1846;SER-1849; SER-1973; SER-1975; SER-1979; SER-2027; SER-2029 ANDSER-2031, AND MASS SPECTROMETRY.
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1723, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures