RU17_MOUSE - dbPTM
RU17_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RU17_MOUSE
UniProt AC Q62376
Protein Name U1 small nuclear ribonucleoprotein 70 kDa
Gene Name Snrnp70
Organism Mus musculus (Mouse).
Sequence Length 448
Subcellular Localization Nucleus speckle . Nucleus, nucleoplasm . Colocalizes with SCNM1 and LUC7L2 in nuclear speckles.
Protein Description Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. SNRNP70 binds to the loop I region of U1-snRNA. The truncated isoforms cannot bind U1-snRNA (By similarity)..
Protein Sequence MTQFLPPNLLALFAPRDPIPYLPPLEKLPHEKHHNQPYCGIAPYIREFEDPRDAPPPTRAETREERMERKRREKIERRQQEVETELKMWDPHNDPNAQGDAFKTLFVARVNYDTTESKLRREFEVYGPIKRIHMVYSKRSGKPRGYAFIEYEHERDMHSAYKHADGKKIDGRRVLVDVERGRTVKGWRPRRLGGGLGGTRRGGADVNIRHSGRDDTSRYDERPGPSPLPHRDRDRDRERERRERSRERDKERERRRSRSRDRRRRSRSRDKDERRRSRERSKDKDRDRKRRSSRSRERARRERERKEELRGGGGGGGGGSGGGGGGDMAEPSEAGDGAPDDGPPGELGPEGPDGPEEKGRDRDRERRRSHRSERERRRDRDRDRDREHKRGERGSERGRDEARGGGGSGQDNGLEGLGSDGRDMYMEAEGGDGYMAPENGYLMEAAPE
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------MTQFLPPNL
------CCCCCCHHH		28.20-
27AcetylationPYLPPLEKLPHEKHH
CCCCCHHHCCCCCCC		75.0123236377
27UbiquitinationPYLPPLEKLPHEKHH
CCCCCHHHCCCCCCC		75.01-
32AcetylationLEKLPHEKHHNQPYC
HHHCCCCCCCCCCCC		47.3222826441
38PhosphorylationEKHHNQPYCGIAPYI
CCCCCCCCCCCHHHH		8.1122817900
44PhosphorylationPYCGIAPYIREFEDP
CCCCCHHHHHCCCCC		12.0030165576
84PhosphorylationRRQQEVETELKMWDP
HHHHHHHHHHHHCCC		52.3627818261
112PhosphorylationLFVARVNYDTTESKL
EEEEEECCCCCHHHH		16.29-
117PhosphorylationVNYDTTESKLRREFE
ECCCCCHHHHHHHEE		34.5918779572
118UbiquitinationNYDTTESKLRREFEV
CCCCCHHHHHHHEEE		39.52-
118AcetylationNYDTTESKLRREFEV
CCCCCHHHHHHHEEE		39.5223806337
118MalonylationNYDTTESKLRREFEV
CCCCCHHHHHHHEEE		39.5226320211
126PhosphorylationLRREFEVYGPIKRIH
HHHHEEEECCEEEEE		15.2425263469
137PhosphorylationKRIHMVYSKRSGKPR
EEEEEEEECCCCCCC		15.3512548559
140PhosphorylationHMVYSKRSGKPRGYA
EEEEECCCCCCCEEE		55.7112548559
151PhosphorylationRGYAFIEYEHERDMH
CEEEEEEEECHHHHH		20.12-
162AcetylationRDMHSAYKHADGKKI
HHHHHHHCCCCCCEE		31.8423806337
199PhosphorylationLGGGLGGTRRGGADV
CCCCCCCCCCCCCCC		18.5229176673
201MethylationGGLGGTRRGGADVNI
CCCCCCCCCCCCCEE		47.9712018435
211PhosphorylationADVNIRHSGRDDTSR
CCCEEECCCCCCCCC		26.1923684622
216PhosphorylationRHSGRDDTSRYDERP
ECCCCCCCCCCCCCC		21.2825367039
217PhosphorylationHSGRDDTSRYDERPG
CCCCCCCCCCCCCCC		35.5225266776
219PhosphorylationGRDDTSRYDERPGPS
CCCCCCCCCCCCCCC		23.1725619855
226PhosphorylationYDERPGPSPLPHRDR
CCCCCCCCCCCCCCC		45.0121930439
245PhosphorylationERERRERSRERDKER
HHHHHHHHHHHHHHH		33.4729899451
266PhosphorylationSRDRRRRSRSRDKDE
HHHHHHHHHHCHHHH		32.5619367708
268PhosphorylationDRRRRSRSRDKDERR
HHHHHHHHCHHHHHH		46.1822817900
292PhosphorylationDRDRKRRSSRSRERA
HHHHHHHHHHHHHHH		33.8520531401
293PhosphorylationRDRKRRSSRSRERAR
HHHHHHHHHHHHHHH		32.2522802335
295PhosphorylationRKRRSSRSRERARRE
HHHHHHHHHHHHHHH		40.2020531401
320PhosphorylationGGGGGGGSGGGGGGD
CCCCCCCCCCCCCCC		37.2228833060
332PhosphorylationGGDMAEPSEAGDGAP
CCCCCCCCCCCCCCC		31.4225521595
369PhosphorylationRDRERRRSHRSERER
HHHHHHHHHHHHHHH		22.8019854140
372PhosphorylationERRRSHRSERERRRD
HHHHHHHHHHHHHHH		35.2719854140
395PhosphorylationHKRGERGSERGRDEA
HHHCCCCCHHCCCCC		30.2729899451
408PhosphorylationEARGGGGSGQDNGLE
CCCCCCCCCCCCCCC		36.2325521595
419PhosphorylationNGLEGLGSDGRDMYM
CCCCCCCCCCCEEEE		41.7728973931
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 RU17_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RU17_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 RU17_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CAN1_HUMANCAPN1physical
26496610
SMN_HUMANSMN1physical
26496610
RSMB_HUMANSNRPBphysical
26496610
RU1C_HUMANSNRPCphysical
26496610
SMD1_HUMANSNRPD1physical
26496610
SMD2_HUMANSNRPD2physical
26496610
SMD3_HUMANSNRPD3physical
26496610
RUXF_HUMANSNRPFphysical
26496610
RUXG_HUMANSNRPGphysical
26496610
THIO_HUMANTXNphysical
26496610
RBP56_HUMANTAF15physical
26496610
GEMI2_HUMANGEMIN2physical
26496610
ABC3B_HUMANAPOBEC3Bphysical
26496610
STRAP_HUMANSTRAPphysical
26496610
DDX20_HUMANDDX20physical
26496610
RPRD2_HUMANRPRD2physical
26496610
GEMI5_HUMANGEMIN5physical
26496610
ABT1_HUMANABT1physical
26496610
PKN3_HUMANPKN3physical
26496610
GEMI4_HUMANGEMIN4physical
26496610
PHAX_HUMANPHAXphysical
26496610
GEMI8_HUMANGEMIN8physical
26496610
ZN668_HUMANZNF668physical
26496610
GEMI7_HUMANGEMIN7physical
26496610
GEMI6_HUMANGEMIN6physical
26496610
ZN503_HUMANZNF503physical
26496610
TOE1_HUMANTOE1physical
26496610
LSM11_HUMANLSM11physical
26496610
KLHL8_HUMANKLHL8physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RU17_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-226, AND MASSSPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND MASSSPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, AND MASSSPECTROMETRY.

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