PRPF3_MOUSE - dbPTM
PRPF3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRPF3_MOUSE
UniProt AC Q922U1
Protein Name U4/U6 small nuclear ribonucleoprotein Prp3
Gene Name Prpf3
Organism Mus musculus (Mouse).
Sequence Length 683
Subcellular Localization Nucleus speckle . Colocalizes with spliceosomal snRNPs..
Protein Description Participates in pre-mRNA splicing. Part of the U4/U5/U6 tri-snRNP complex, one of the building blocks of the spliceosome..
Protein Sequence MALSKRELDELKPWIEKTVKRVLGFSEPTVVTAALNCVGKGMDKKKAADHLKPFLDDSTLRFVDKLFEAVEEGRSSRHSKSSSDRSRKRELKEVFGDDSEISKESSGVKKRRIPRFEEVEEEPEVIPGPPSESPGMLTKLQIKQMMEAATRQIEERKKQLSFISPPAPQPKTPSSSQPERLPIGNTIQPSQAATFMNDAIEKARKAAELQARIQAQLALKPGLIGNANMVGLANLHAMGIAPPKVELKDQTKPTPLILDEQGRTVDATGKEVELTHRMPTLKANIRAVKREQFKQQLKEKPSEDMESNTFFDPRVSIAPSQRQRRTFKFHDKGKFEKIAQRLRTKAQLEKLQAEISQAARKTGIHTSTRLALIAPKKELKEGDIPEIEWWDSYIIPNGFDLTEENPKREDYFGITNLVEHPAQLNPPVDNDTPVTLGVYLTKKEQKKLRRQTRREAQKELQEKVRLGLTPPPEPKVRISNLMRVLGTEAVQDPTKVEAHVRAQMAKRQKAHEEANAARKLTAEQRKVKKIKKLKEDISQGVHISVYRVRNLSNPAKKFKIEANAGQLYLTGVVVLHKDVNVVVVEGGPKAQKKFKRLMLHRIKWDEQTSNTKGDDDEESDEEAVKKTNKCVLVWEGTAKDRSFGEMKFKQCPTENMAREHFKKHGAEHYWDLALSESVLESTD
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
65AcetylationSTLRFVDKLFEAVEE
HHHHHHHHHHHHHHH		50.1822826441
99PhosphorylationKEVFGDDSEISKESS
HHHHCCCCHHHHCCC		41.3828725479
102PhosphorylationFGDDSEISKESSGVK
HCCCCHHHHCCCCCC		26.7330482847
131PhosphorylationEVIPGPPSESPGMLT
CCCCCCCCCCCCHHC		54.5721149613
133PhosphorylationIPGPPSESPGMLTKL
CCCCCCCCCCHHCHH		30.9621149613
138PhosphorylationSESPGMLTKLQIKQM
CCCCCHHCHHHHHHH		22.3326643407
161PhosphorylationEERKKQLSFISPPAP
HHHHHHHCCCCCCCC		20.3128066266
164PhosphorylationKKQLSFISPPAPQPK
HHHHCCCCCCCCCCC		23.8729233185
172PhosphorylationPPAPQPKTPSSSQPE
CCCCCCCCCCCCCCC		34.7826643407
174PhosphorylationAPQPKTPSSSQPERL
CCCCCCCCCCCCCCC		48.1026643407
175PhosphorylationPQPKTPSSSQPERLP
CCCCCCCCCCCCCCC		33.9126643407
176PhosphorylationQPKTPSSSQPERLPI
CCCCCCCCCCCCCCC		54.8426643407
186PhosphorylationERLPIGNTIQPSQAA
CCCCCCCCCCHHHHH		18.7726643407
190PhosphorylationIGNTIQPSQAATFMN
CCCCCCHHHHHHHHH		18.9728059163
302PhosphorylationQQLKEKPSEDMESNT
HHHHHCCCHHCCCCC		58.2427180971
307PhosphorylationKPSEDMESNTFFDPR
CCCHHCCCCCCCCCC		34.2427180971
309PhosphorylationSEDMESNTFFDPRVS
CHHCCCCCCCCCCCC		34.6527180971
392PhosphorylationPEIEWWDSYIIPNGF
CCCCCHHHEECCCCC		12.4317203969
393PhosphorylationEIEWWDSYIIPNGFD
CCCCHHHEECCCCCC		10.6117203969
469PhosphorylationEKVRLGLTPPPEPKV
HHHHCCCCCCCCCCC		31.7626824392
479PhosphorylationPEPKVRISNLMRVLG
CCCCCCHHHHHHHHC		17.2227600695
495AcetylationEAVQDPTKVEAHVRA
CHHCCCHHHHHHHHH		43.3922826441
608PhosphorylationRIKWDEQTSNTKGDD
HHCCCHHCCCCCCCC		23.1525619855
609PhosphorylationIKWDEQTSNTKGDDD
HCCCHHCCCCCCCCC		42.0425619855
611PhosphorylationWDEQTSNTKGDDDEE
CCHHCCCCCCCCCHH		35.8525619855
619PhosphorylationKGDDDEESDEEAVKK
CCCCCHHCHHHHHHH		48.5527087446
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 PRPF3_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRPF3_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 PRPF3_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NH2L1_HUMANNHP2L1physical
26496610
RBBP5_HUMANRBBP5physical
26496610
RFC2_HUMANRFC2physical
26496610
RL31_HUMANRPL31physical
26496610
RL38_HUMANRPL38physical
26496610
SNUT1_HUMANSART1physical
26496610
PRP4_HUMANPRPF4physical
26496610
DDX23_HUMANDDX23physical
26496610
H2AY_HUMANH2AFYphysical
26496610
SART3_HUMANSART3physical
26496610
PUR6_HUMANPAICSphysical
26496610
WBP4_HUMANWBP4physical
26496610
ATX2L_HUMANATXN2Lphysical
26496610
DJC13_HUMANDNAJC13physical
26496610
PRP6_HUMANPRPF6physical
26496610
PRP31_HUMANPRPF31physical
26496610
RT02_HUMANMRPS2physical
26496610
DC2L1_HUMANDYNC2LI1physical
26496610
PHF6_HUMANPHF6physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PRPF3_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-619, AND MASSSPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, AND MASSSPECTROMETRY.

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