dbPTM

TTF1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TTF1_MOUSE
UniProt AC	Q62187
Protein Name	Transcription termination factor 1
Gene Name	Ttf1
Organism	Mus musculus (Mouse).
Sequence Length	859
Subcellular Localization	Nucleus . Nucleus, nucleolus .
Protein Description	Multifunctional nucleolar protein that terminates ribosomal gene transcription, mediates replication fork arrest and regulates RNA polymerase I transcription on chromatin. Plays a dual role in rDNA regulation, being involved in both activation and silencing of rDNA transcription. Interaction with BAZ2A/TIP5 recovers DNA-binding activity..
Protein Sequence	MKGGTSKFKTHTETLYKKKKWSSVSEKRPQKCPSQCLESKQPQVSVLGKRRRASQTPAQETLESEWPQKAKRKKRRREPQTPAQETLESEWPQKAKKKKRRGEPQTPTQESLESEQPPVSLLGKRRRESQTPAQENSESEQPRKAKRRRKKRKGSQQPTSSLLKTPETFLKAKKTTSAHKKKKNSVLEVDMETGIILVDKENMENLLETSRKDVDIVYVDMSKGQRSAKVRETGELPAAKPQEHGCRELLGDVRSRKKQKHLQKVAPWDVVQGSQPESISLPPSEPLSSEDLEGKSTEAAVFCKKKSKKNVFRSQELEPIPDSLDDSETISERLDSTHHGGAVGAGEECESTKESHSIKKKSKKKKHKSVALATSSDSASVTDSKAKNALVDSSEGSGAVREEDVDHRPAEAEAQACSTEKHREAMQRLEPTHEEESNSESASNSAARHISEDRRESDDSDVDLGSAVRQLREFIPDIQERAATTIRRMYRDDLGRFKEFKAQGVAIRFGKFSAKENKQIEKNVQDFLSLTGIESADKLLYTDRYPEEKTLITNLKRKHAFRLHIGKGIARPWKLVYYRAKKIFDVNNYKGRYNEEDTKKLKAYHSLHGNDWKKIGAMVARSSLSVALKFSQIGGTRNQGAWSKAETQRLIKAVEDVILKKMSPQELRELDSKLQEDPEGRLSIVREKLYKGISWVEVEARVETRNWMQCKSKWTEILTKRMTHGGFVYRGVNALQAKITLIERLYELNVNDANEIDWEDLASAIGDVPPPFVQAKFYKLKAACVPFWQKKTFPEIIDYLYKNSLPLLKEKLDKKMKKKDGQIQTPAAPKQDFLFKDIFHCDDDSDEGSPEEPSASDVQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
54	Phosphorylation	LGKRRRASQTPAQET HCCCCCCCCCCCHHH	32.54	25338131
56	Phosphorylation	KRRRASQTPAQETLE CCCCCCCCCCHHHHH	20.35	25338131
106	Phosphorylation	KRRGEPQTPTQESLE HCCCCCCCCCHHHHH	38.73	25338131
111	Phosphorylation	PQTPTQESLESEQPP CCCCCHHHHHCCCCC	27.85	27600695
129	Phosphorylation	LGKRRRESQTPAQEN HCHHHCCCCCCCCCC	37.23	27087446
131	Phosphorylation	KRRRESQTPAQENSE HHHCCCCCCCCCCCC	29.85	30635358
137	Phosphorylation	QTPAQENSESEQPRK CCCCCCCCCCHHHHH	41.57	25521595
139	Phosphorylation	PAQENSESEQPRKAK CCCCCCCCHHHHHHH	41.16	25159016
155	Phosphorylation	RRKKRKGSQQPTSSL HHHHCCCCCCCCHHH	28.78	27841257
227	Phosphorylation	DMSKGQRSAKVRETG ECCCCCCEECHHHCC	25.26	-
323	Phosphorylation	ELEPIPDSLDDSETI CCCCCCCCCCCHHHH	28.48	22705319
327	Phosphorylation	IPDSLDDSETISERL CCCCCCCHHHHHHHH	35.98	30635358
329	Phosphorylation	DSLDDSETISERLDS CCCCCHHHHHHHHHC	33.48	30635358
331	Phosphorylation	LDDSETISERLDSTH CCCHHHHHHHHHCCC	24.88	30635358
369	Phosphorylation	SKKKKHKSVALATSS CCCCCCCCEEECCCC	16.61	29895711
374	Phosphorylation	HKSVALATSSDSASV CCCEEECCCCCCCCC	29.61	29895711
375	Phosphorylation	KSVALATSSDSASVT CCEEECCCCCCCCCC	26.92	-
378	Phosphorylation	ALATSSDSASVTDSK EECCCCCCCCCCCHH	25.13	29895711
380	Phosphorylation	ATSSDSASVTDSKAK CCCCCCCCCCCHHHH	29.51	29895711
384	Phosphorylation	DSASVTDSKAKNALV CCCCCCCHHHHHHEE	25.75	22817900
432	Phosphorylation	AMQRLEPTHEEESNS HHHHHCCCCHHHCCC	32.32	25159016
437	Phosphorylation	EPTHEEESNSESASN CCCCHHHCCCHHHHH	49.27	27087446
439	Phosphorylation	THEEESNSESASNSA CCHHHCCCHHHHHHH	42.05	21082442
441	Phosphorylation	EEESNSESASNSAAR HHHCCCHHHHHHHHH	36.50	25159016
443	Phosphorylation	ESNSESASNSAARHI HCCCHHHHHHHHHHH	40.37	25777480
445	Phosphorylation	NSESASNSAARHISE CCHHHHHHHHHHHHC	22.32	25777480
451	Phosphorylation	NSAARHISEDRRESD HHHHHHHHCCHHCCC	27.59	21082442
457	Phosphorylation	ISEDRRESDDSDVDL HHCCHHCCCCCCCCH	44.93	27087446
460	Phosphorylation	DRRESDDSDVDLGSA CHHCCCCCCCCHHHH	44.52	27087446
466	Phosphorylation	DSDVDLGSAVRQLRE CCCCCHHHHHHHHHH	30.78	25159016
518	Acetylation	KFSAKENKQIEKNVQ CCCHHHHHHHHHHHH	54.46	22902405
683	Phosphorylation	EDPEGRLSIVREKLY HCCCCCHHHHHHHHH	20.06	24719451
845	Phosphorylation	IFHCDDDSDEGSPEE CEECCCCCCCCCCCC	44.55	25521595
849	Phosphorylation	DDDSDEGSPEEPSAS CCCCCCCCCCCCCCC	27.39	25619855

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 TTF1_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TTF1_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 TTF1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of TTF1_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of TTF1_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-457 AND SER-460, ANDMASS SPECTROMETRY.	19367708 [Abstract]
"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-457 AND SER-460, ANDMASS SPECTROMETRY.	17242355 [Abstract]