dbPTM

TFP11_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TFP11_MOUSE
UniProt AC	Q9ERA6
Protein Name	Tuftelin-interacting protein 11
Gene Name	Tfip11
Organism	Mus musculus (Mouse).
Sequence Length	838
Subcellular Localization	Cytoplasm. Nucleus. In the nucleus localizes to unique speckle domains in close proximity to nuclear speckles and not identical to paraspeckles.
Protein Description	Involved in pre-mRNA splicing, specifically in spliceosome disassembly during late-stage splicing events. Intron turnover seems to proceed through reactions in two lariat-intron associated complexes termed Intron Large (IL) and Intron Small (IS). In cooperation with DHX15 seems to mediate the transition of the U2, U5 and U6 snRNP-containing IL complex to the snRNP-free IS complex leading to efficient debranching and turnover of excised introns. May play a role in the differentiation of ameloblasts and odontoblasts or in the forming of the enamel extracellular matrix..
Protein Sequence	MSLSHLYRDGEGHLDDDDDDERENFEITDWDLQNEFNPNRQRHWQTKEEATYGVWAERDSDEERPSFGGKRARDYSAPVNFISAGLKKGAAEEADSEDSDAEEKPVKQEDFPKDLGPKKLKTGGNFKPSQKGFSGGTKSFMDFGSWERHTKGIGQKLLQKMGYVPGRGLGKNAQGIINPIEAKQRKGKGAVGAYGSERTTQSLQDFPVADSEEEAEEEFQKELSQWRKDPSGSKKKPKYSYKTVEELKAKGRVSKKLTAPQKELSQVKVIDMTGREQKVYYSYSQISHKHSVPDEGVPLLAQLPPTAGKEARMPGFALPELEHNLQLLIERTEQEIIQSDRQLQYERDMVVSLSHELEKTAEVLAHEERVISNLSKVLALVEECERRMQPHGADPLTLDECARIFETLQDKYYEEYRLADRADLAVAIVYPLVKDYFKDWHPLEDGSYGTQIISKWKSLLENDQLLSHSSQDLSSDAFHRLMWEVWMPFVRNVVAQWQPRNCEPMVDFLDSWAHIIPVWILDNILDQLIFPKLQKEVDNWNPLTDTVPIHSWIHPWLPLMQARLEPLYSPVRSKLSSALQKWHPSDASAKLILQPWKEVLTPGSWEAFMLRNIVPKLGMCLGELVINPHQQHMDAFYWVMDWEGMISVSSLVGLLEKHFFPKWLQVLCSWLSNSPNYEEITKWYLGWKSMFSDQVLAHPSVKDKFNEALDIMNRAVSSNVGAYMQPGARENIAYLTHTERRKDFQYEAMQERREAENMAQRGIGVAASSVPMNFKDLIETKAEEHNIVFMPVIGKRHEGKQLYTFGRIVIYIDRGVVFVQGEKTWVPTSLQSLIDMAK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSLSHLYRD ------CCHHHCCCC	38.28	26824392
4	Phosphorylation	----MSLSHLYRDGE ----CCHHHCCCCCC	12.25	28066266
51	Phosphorylation	WQTKEEATYGVWAER CCCHHHHHCCEEECC	24.88	25159016
52	Phosphorylation	QTKEEATYGVWAERD CCHHHHHCCEEECCC	19.41	25159016
60	Phosphorylation	GVWAERDSDEERPSF CEEECCCCCCCCCCC	53.82	25521595
66	Phosphorylation	DSDEERPSFGGKRAR CCCCCCCCCCCCCCC	42.62	25159016
87	Acetylation	NFISAGLKKGAAEEA HHHCHHHHCCHHHHC	48.52	23806337
88	Acetylation	FISAGLKKGAAEEAD HHCHHHHCCHHHHCC	59.84	30583177
96	Phosphorylation	GAAEEADSEDSDAEE CHHHHCCCCCCCCCC	50.80	27087446
99	Phosphorylation	EEADSEDSDAEEKPV HHCCCCCCCCCCCCC	34.37	27087446
138	Acetylation	KGFSGGTKSFMDFGS CCCCCCCCCCCCCCC	45.00	22826441
145	Phosphorylation	KSFMDFGSWERHTKG CCCCCCCCHHHHCCH	26.25	26643407
199	Phosphorylation	GAYGSERTTQSLQDF CCCCCCCCCCCHHHC	25.74	25619855
202	Phosphorylation	GSERTTQSLQDFPVA CCCCCCCCHHHCCCC	26.38	25619855
211	Phosphorylation	QDFPVADSEEEAEEE HHCCCCCCHHHHHHH	36.85	24925903
224	Phosphorylation	EEFQKELSQWRKDPS HHHHHHHHHHHCCCC	28.87	25159016
243	Phosphorylation	KPKYSYKTVEELKAK CCCCCCCCHHHHHHC	25.56	22817900
262	Acetylation	KKLTAPQKELSQVKV CCCCCCHHHHHCCEE	60.61	22826441
281	Phosphorylation	GREQKVYYSYSQISH CCCEEEEEEHHHCCC	12.24	-
467	Phosphorylation	LENDQLLSHSSQDLS HHCCCHHCCCCCCCC	29.89	25338131
469	Phosphorylation	NDQLLSHSSQDLSSD CCCHHCCCCCCCCHH	26.73	19060867
470	Phosphorylation	DQLLSHSSQDLSSDA CCHHCCCCCCCCHHH	23.45	21183079
568	Phosphorylation	QARLEPLYSPVRSKL HHHHCHHCHHHHHHH	22.95	28066266
569	Phosphorylation	ARLEPLYSPVRSKLS HHHCHHCHHHHHHHH	25.30	28418008
573	Phosphorylation	PLYSPVRSKLSSALQ HHCHHHHHHHHHHHH	37.88	-
704	Ubiquitination	AHPSVKDKFNEALDI CCHHHHHHHHHHHHH	44.35	-
781	Ubiquitination	FKDLIETKAEEHNIV HHHHHHHHHHHCCEE	40.80	-

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 TFP11_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TFP11_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 TFP11_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of TFP11_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TFP11_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-60; SER-96 AND SER-99,AND MASS SPECTROMETRY.	19367708 [Abstract]
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells."; Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.; J. Proteome Res. 6:3174-3186(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND SER-99, AND MASSSPECTROMETRY.	17622165 [Abstract]