SNW1_MOUSE - dbPTM
SNW1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNW1_MOUSE
UniProt AC Q9CSN1
Protein Name SNW domain-containing protein 1
Gene Name Snw1
Organism Mus musculus (Mouse).
Sequence Length 536
Subcellular Localization Nucleus .
Protein Description Involved in pre-mRNA splicing as component of the spliceosome. Is required in the specific splicing of CDKN1A pre-mRNA; the function probably involves the recruitment of U2AF2 to the mRNA. Is proposed to recruit PPIL1 to the spliceosome. May be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. Involved in transcriptional regulation. Modulates TGF-beta-mediated transcription via association with SMAD proteins, MYOD1-mediated transcription via association with PABPN1, RB1-mediated transcriptional repression, and retinoid-X receptor (RXR)- and vitamin D receptor (VDR)-dependent gene transcription in a cell line-specific manner probably involving coactivators NCOA1 and GRIP1. Is involved in NOTCH1-mediated transcriptional activation. Binds to multimerized forms of Notch intracellular domain (NICD) and is proposed to recruit transcriptional coactivators such as MAML1 to form an intermediate preactivation complex which associates with DNA-bound CBF-1/RBPJ to form a transcriptional activation complex by releasing SNW1 and redundant NOTCH1 NICD..
Protein Sequence MALTSFLPAPTQLSQDQLEAEERARSQRSLQTSLVSSRREPPPYGYRKGWIPRLLEDFGDGGAFPEIHVAQYPLDMGRKKKMSNALAIQVDPEGKIKYDAIARQGQSKDKVIYSKYTDLVPKEVMNADDPDLQRPDEEAIKEITEKTRVALEKSVSQKVAAAMPVRAADKLAPAQYIRYTPSQQGVAFNSGAKQRVIRMVEMQKEPMEPPRFKINKKIPRGPPSPPAPVMHSPSRKMTVKEQQEWKIPPCISNWKNAKGYTIPIDKRLAADGRGLQTVHINENFAKLAEALYIADRKAREAVEMRAQVERKMAQKEKEKHEEKLREMAQKARERRAGIKTHVEKEDGEARERDEIRHDRRKERQHDRNLSRAAPDKRSKLQRNENRDISEVIALGVPNPRTSNEVQYDQRLFNQSKGMDSGFAGGEDEIYNVYDQAWRGGKDMAQSIYRPSKNLDKDMYGDDLEARIKTNRFVPDKEFSGSDRKQRGREGPVQFEEDPFGLDKFLEEAKQHGGSKRPSDSSRPKEHEHEGKKRRKE
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MALTSFLPA
------CCCCCCCCC		21.39-
4Phosphorylation----MALTSFLPAPT
----CCCCCCCCCCC		14.1126745281
5Phosphorylation---MALTSFLPAPTQ
---CCCCCCCCCCCC		26.1526745281
11PhosphorylationTSFLPAPTQLSQDQL
CCCCCCCCCCCHHHH		44.2228066266
14PhosphorylationLPAPTQLSQDQLEAE
CCCCCCCCHHHHHHH		23.1525266776
29PhosphorylationERARSQRSLQTSLVS
HHHHHHHHHHHHHHH		19.7222802335
32PhosphorylationRSQRSLQTSLVSSRR
HHHHHHHHHHHHCCC		29.3528066266
33PhosphorylationSQRSLQTSLVSSRRE
HHHHHHHHHHHCCCC		17.5128066266
36PhosphorylationSLQTSLVSSRREPPP
HHHHHHHHCCCCCCC		24.3428066266
37PhosphorylationLQTSLVSSRREPPPY
HHHHHHHCCCCCCCC		28.0728066266
83PhosphorylationMGRKKKMSNALAIQV
CCCCCCHHCCEEEEE		28.0328833060
153AcetylationKTRVALEKSVSQKVA
HHHHHHHHHHHHHHH		57.9422826441
158AcetylationLEKSVSQKVAAAMPV
HHHHHHHHHHHCCCC		26.7422826441
170AcetylationMPVRAADKLAPAQYI
CCCHHHHHCCCHHHE		41.6523806337
176PhosphorylationDKLAPAQYIRYTPSQ
HHCCCHHHEEECHHH		6.8929514104
179PhosphorylationAPAQYIRYTPSQQGV
CCHHHEEECHHHCCC		17.2828066266
180PhosphorylationPAQYIRYTPSQQGVA
CHHHEEECHHHCCCC		13.4528066266
182PhosphorylationQYIRYTPSQQGVAFN
HHEEECHHHCCCCCC		27.6028066266
190PhosphorylationQQGVAFNSGAKQRVI
HCCCCCCCCCCHHHH		33.4028066266
193UbiquitinationVAFNSGAKQRVIRMV
CCCCCCCCHHHHHHH		42.0122790023
224PhosphorylationKIPRGPPSPPAPVMH
CCCCCCCCCCCCCCC		46.8027087446
230OxidationPSPPAPVMHSPSRKM
CCCCCCCCCCCCCCC		2.2317242355
232PhosphorylationPPAPVMHSPSRKMTV
CCCCCCCCCCCCCCH		13.3827087446
234PhosphorylationAPVMHSPSRKMTVKE
CCCCCCCCCCCCHHH		47.7727087446
292PhosphorylationAKLAEALYIADRKAR
HHHHHHHHHHCHHHH		10.9125159016
339AcetylationRERRAGIKTHVEKED
HHHHHCCCCCEECCC		31.4922826441
401PhosphorylationLGVPNPRTSNEVQYD
CCCCCCCCCCCHHHH		36.8425338131
402PhosphorylationGVPNPRTSNEVQYDQ
CCCCCCCCCCHHHHH		32.07-
415PhosphorylationDQRLFNQSKGMDSGF
HHHHHHHCCCCCCCC		32.0822006019
420PhosphorylationNQSKGMDSGFAGGED
HHCCCCCCCCCCCCH		27.2425159016
430PhosphorylationAGGEDEIYNVYDQAW
CCCCHHHHHHHHHHH		9.1325159016
433PhosphorylationEDEIYNVYDQAWRGG
CHHHHHHHHHHHCCC		9.9425159016
441AcetylationDQAWRGGKDMAQSIY
HHHHCCCHHHHHHHH		47.3422826441
446PhosphorylationGGKDMAQSIYRPSKN
CCHHHHHHHHCCCCC		16.4329514104
448PhosphorylationKDMAQSIYRPSKNLD
HHHHHHHHCCCCCCC		23.0128066266
451PhosphorylationAQSIYRPSKNLDKDM
HHHHHCCCCCCCCCC		25.7728066266
459PhosphorylationKNLDKDMYGDDLEAR
CCCCCCCCCCHHHHH		27.7725159016
469PhosphorylationDLEARIKTNRFVPDK
HHHHHHHCCCCCCCC		29.2922871156
479PhosphorylationFVPDKEFSGSDRKQR
CCCCCCCCCCCHHHC		38.1828066266
481PhosphorylationPDKEFSGSDRKQRGR
CCCCCCCCCHHHCCC		32.8028066266
518PhosphorylationHGGSKRPSDSSRPKE
CCCCCCCCCCCCCCC		54.9125266776
520PhosphorylationGSKRPSDSSRPKEHE
CCCCCCCCCCCCCCC		32.3628066266
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of SNW1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNW1_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of SNW1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
U520_HUMANSNRNP200physical
20360068
U5S1_HUMANEFTUD2physical
20360068
SAAL1_HUMANSAAL1physical
20360068
PPIL1_HUMANPPIL1physical
20360068
PRP19_HUMANPRPF19physical
20360068
SYF2_HUMANSYF2physical
20360068
AQR_HUMANAQRphysical
20360068
RSRC1_HUMANRSRC1physical
20360068
SYF1_HUMANXAB2physical
20360068
SNR40_HUMANSNRNP40physical
20360068
PRP17_HUMANCDC40physical
20360068
RUXE_HUMANSNRPEphysical
20360068
HOME3_HUMANHOMER3physical
20360068
PPIE_HUMANPPIEphysical
20360068
SNW1_HUMANSNW1physical
20360068
SMD2_HUMANSNRPD2physical
20360068
HOME1_HUMANHOMER1physical
20360068
CDC5L_HUMANCDC5Lphysical
20360068
SMD3_HUMANSNRPD3physical
20360068
SMD1_HUMANSNRPD1physical
20360068
PAXB1_HUMANPAXBP1physical
20360068
CWC15_HUMANCWC15physical
20360068
CRNL1_HUMANCRNKL1physical
20360068
DHX15_HUMANDHX15physical
20360068
AAR2_HUMANAAR2physical
20360068
PRP8_HUMANPRPF8physical
20360068
CCD12_HUMANCCDC12physical
20360068
PLRG1_HUMANPLRG1physical
20360068
SIR1_MOUSESirt1physical
19934264
CDC5L_HUMANCDC5Lphysical
26496610
DHX8_HUMANDHX8physical
26496610
G6PD_HUMANG6PDphysical
26496610
GOGA4_HUMANGOLGA4physical
26496610
PLRG1_HUMANPLRG1physical
26496610
RREB1_HUMANRREB1physical
26496610
DGC14_HUMANDGCR14physical
26496610
KCAB2_HUMANKCNAB2physical
26496610
ARK72_HUMANAKR7A2physical
26496610
FA50A_HUMANFAM50Aphysical
26496610
ZNHI3_HUMANZNHIT3physical
26496610
SNR40_HUMANSNRNP40physical
26496610
HOME3_HUMANHOMER3physical
26496610
HOME1_HUMANHOMER1physical
26496610
AQR_HUMANAQRphysical
26496610
SPF27_HUMANBCAS2physical
26496610
PPIE_HUMANPPIEphysical
26496610
SLU7_HUMANSLU7physical
26496610
PRP8_HUMANPRPF8physical
26496610
PRS23_HUMANPRSS23physical
26496610
CLASR_HUMANCLASRPphysical
26496610
U520_HUMANSNRNP200physical
26496610
SYF2_HUMANSYF2physical
26496610
PRP19_HUMANPRPF19physical
26496610
CRNL1_HUMANCRNKL1physical
26496610
HOOK1_HUMANHOOK1physical
26496610
PRP17_HUMANCDC40physical
26496610
CWC15_HUMANCWC15physical
26496610
PPIL1_HUMANPPIL1physical
26496610
RBM22_HUMANRBM22physical
26496610
TM165_HUMANTMEM165physical
26496610
SYF1_HUMANXAB2physical
26496610
ISY1_HUMANISY1physical
26496610
WDR26_HUMANWDR26physical
26496610
ACTL8_HUMANACTL8physical
26496610
KLF16_HUMANKLF16physical
26496610
PCGF5_HUMANPCGF5physical
26496610
SAAL1_HUMANSAAL1physical
26496610
TOE1_HUMANTOE1physical
26496610
CA052_HUMANC1orf52physical
26496610
CCD12_HUMANCCDC12physical
26496610
ZBED6_HUMANZBED6physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SNW1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND SER-232, ANDMASS 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-224, AND MASSSPECTROMETRY.
"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-224, AND MASSSPECTROMETRY.
"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-224 AND SER-232, ANDMASS SPECTROMETRY.
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line.";
Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
Mol. Cell. Proteomics 3:279-286(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND SER-232, ANDMASS SPECTROMETRY.

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