FIP1_MOUSE - dbPTM
FIP1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FIP1_MOUSE
UniProt AC Q9D824
Protein Name Pre-mRNA 3'-end-processing factor FIP1
Gene Name Fip1l1
Organism Mus musculus (Mouse).
Sequence Length 581
Subcellular Localization Nucleus.
Protein Description Component of the cleavage and polyadenylation specificity factor (CPSF) complex that plays a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. FIP1L1 contributes to poly(A) site recognition and stimulates poly(A) addition. Binds to U-rich RNA sequence elements surrounding the poly(A) site. May act to tether poly(A) polymerase to the CPSF complex (By similarity)..
Protein Sequence MSAGEVERLVELSGGTGGDEEEEWLYGGPWDVHVHSDLAKDLDENEVERPEEENASANPPSGIEEEAAENGVAKPKVTETEDDSDSDSDDDEDDVHVTIGDIKTGAPQYGSYGTAPVNLNIKAGGRVYGNTGTKVKGVDLDAPGSINGVPLLEVDLDSFEDKPWRKPGADLSDYFNYGFNEDTWKAYCEKQKRIRMGLEVIPVTSTTNKITVQQGRTGNSEKEAALPSTKAEFTSPPSLFKTGLPPSRNSTSSQSQTSTASRKASSSVGKWQDRYGRAESPDLRRLPGAIDVIGQTITISRVEGRRRANENSNIQVLSDRSATEVDNNFSKPPPFFPPGAPPTHLPPPPFLPPPPTVSTAPPLIPPPGIPITVPPPGFPPPPGAPPPSLIPTIESGHSSGYDSRSARAFPYGNVAFPHLTSSAPSWPSLVDTTKQWDYYARREKDRDRDRERDRDRERERDRDRERERTRERERERDHSPTPSVFNSDEERYRYREYAERGYERHRASREKEERHRERRHREKEETRHKSSRSNSRRRHESEEGDSHRRHKHKKSKRSKEGKEAGSEPVPEQESTEAAPAE
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
2Phosphorylation------MSAGEVERL
------CCHHHHHHE		45.0128066266
13PhosphorylationVERLVELSGGTGGDE
HHHEEECCCCCCCCC		22.9821183079
16PhosphorylationLVELSGGTGGDEEEE
EEECCCCCCCCCHHH		41.3321149613
26PhosphorylationDEEEEWLYGGPWDVH
CCHHHHHCCCCCCEE		22.5526643407
36PhosphorylationPWDVHVHSDLAKDLD
CCCEEECHHHHHCCC		32.9826643407
56PhosphorylationRPEEENASANPPSGI
CCHHHCCCCCCCCCH		39.9125266776
61PhosphorylationNASANPPSGIEEEAA
CCCCCCCCCHHHHHH		54.3721659605
78PhosphorylationGVAKPKVTETEDDSD
CCCCCCCCCCCCCCC		43.2328833060
80PhosphorylationAKPKVTETEDDSDSD
CCCCCCCCCCCCCCC		35.0428833060
84PhosphorylationVTETEDDSDSDSDDD
CCCCCCCCCCCCCCC		51.8727087446
86PhosphorylationETEDDSDSDSDDDED
CCCCCCCCCCCCCCC		42.8627087446
88PhosphorylationEDDSDSDSDDDEDDV
CCCCCCCCCCCCCCE		47.0627087446
98PhosphorylationDEDDVHVTIGDIKTG
CCCCEEEEECEECCC		12.3628833060
111PhosphorylationTGAPQYGSYGTAPVN
CCCCCCCCCCCCCCE		18.5624453211
114PhosphorylationPQYGSYGTAPVNLNI
CCCCCCCCCCCEEEE		21.3926643407
122UbiquitinationAPVNLNIKAGGRVYG
CCCEEEEEECCEEEC		39.65-
204O-linked_GlycosylationGLEVIPVTSTTNKIT
CCEEEECCCCCCCEE		18.2730059200
216 (in isoform 4)Phosphorylation-34.8130635358
220 (in isoform 4)Phosphorylation-51.9330635358
228PhosphorylationEKEAALPSTKAEFTS
HHHHCCCCCCCCCCC		43.3123984901
229PhosphorylationKEAALPSTKAEFTSP
HHHCCCCCCCCCCCC		32.1323984901
229O-linked_GlycosylationKEAALPSTKAEFTSP
HHHCCCCCCCCCCCC		32.1330059200
230AcetylationEAALPSTKAEFTSPP
HHCCCCCCCCCCCCC		50.7022826441
234PhosphorylationPSTKAEFTSPPSLFK
CCCCCCCCCCCHHHC		31.6522942356
235PhosphorylationSTKAEFTSPPSLFKT
CCCCCCCCCCHHHCC		39.8826824392
238PhosphorylationAEFTSPPSLFKTGLP
CCCCCCCHHHCCCCC		50.2322942356
253PhosphorylationPSRNSTSSQSQTSTA
CCCCCCCCCCHHHHC		33.6621183079
261O-linked_GlycosylationQSQTSTASRKASSSV
CCHHHHCCHHHHCHH		34.1155411941
261PhosphorylationQSQTSTASRKASSSV
CCHHHHCCHHHHCHH		34.1121183079
265PhosphorylationSTASRKASSSVGKWQ
HHCCHHHHCHHCHHH		26.6129514104
267PhosphorylationASRKASSSVGKWQDR
CCHHHHCHHCHHHHH		32.1829514104
270AcetylationKASSSVGKWQDRYGR
HHHCHHCHHHHHCCC		39.2523806337
275PhosphorylationVGKWQDRYGRAESPD
HCHHHHHCCCCCCCC		21.1827149854
280PhosphorylationDRYGRAESPDLRRLP
HHCCCCCCCCHHHCC		23.8027087446
312PhosphorylationRRRANENSNIQVLSD
CHHCCCCCCEEEECC		29.1829514104
411PhosphorylationRSARAFPYGNVAFPH
CCCCCCCCCCEECCC		18.19-
469PhosphorylationRDRERERTRERERER
HHHHHHHHHHHHHHH		31.93-
479PhosphorylationRERERDHSPTPSVFN
HHHHHCCCCCCCCCC		34.4627087446
481PhosphorylationRERDHSPTPSVFNSD
HHHCCCCCCCCCCCH		31.0727087446
483PhosphorylationRDHSPTPSVFNSDEE
HCCCCCCCCCCCHHH		41.6527087446
487PhosphorylationPTPSVFNSDEERYRY
CCCCCCCCHHHHHHH		34.6327087446
492PhosphorylationFNSDEERYRYREYAE
CCCHHHHHHHHHHHH		18.4427742792
502PhosphorylationREYAERGYERHRASR
HHHHHHHHHHHHHHH		18.9329514104
508PhosphorylationGYERHRASREKEERH
HHHHHHHHHHHHHHH		40.7123140645
535PhosphorylationHKSSRSNSRRRHESE
HHHHHCHHHHHHHCC		28.54-
541PhosphorylationNSRRRHESEEGDSHR
HHHHHHHCCCCHHHH		34.5226824392
546PhosphorylationHESEEGDSHRRHKHK
HHCCCCHHHHHHHCH		29.7425266776
558PhosphorylationKHKKSKRSKEGKEAG
HCHHCHHHHHHHHCC		38.5022802335
566PhosphorylationKEGKEAGSEPVPEQE
HHHHHCCCCCCCCHH		45.8621149613
575PhosphorylationPVPEQESTEAAPAE-
CCCCHHCCCCCCCC-		28.9629514104
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 FIP1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FIP1_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 FIP1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of FIP1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FIP1_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-280 AND SER-479, ANDMASS 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-86; SER-88 AND SER-479,AND MASS SPECTROMETRY.
"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-479; THR-481; SER-483AND SER-487, AND MASS SPECTROMETRY.

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