dbPTM

TTF1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TTF1_HUMAN
UniProt AC	Q15361
Protein Name	Transcription termination factor 1
Gene Name	TTF1
Organism	Homo sapiens (Human).
Sequence Length	905
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	MEGESSRFEIHTPVSDKKKKKCSIHKERPQKHSHEIFRDSSLVNEQSQITRRKKRKKDFQHLISSPLKKSRICDETANATSTLKKRKKRRYSALEVDEEAGVTVVLVDKENINNTPKHFRKDVDVVCVDMSIEQKLPRKPKTDKFQVLAKSHAHKSEALHSKVREKKNKKHQRKAASWESQRARDTLPQSESHQEESWLSVGPGGEITELPASAHKNKSKKKKKKSSNREYETLAMPEGSQAGREAGTDMQESQPTVGLDDETPQLLGPTHKKKSKKKKKKKSNHQEFEALAMPEGSQVGSEVGADMQESRPAVGLHGETAGIPAPAYKNKSKKKKKKSNHQEFEAVAMPESLESAYPEGSQVGSEVGTVEGSTALKGFKESNSTKKKSKKRKLTSVKRARVSGDDFSVPSKNSESTLFDSVEGDGAMMEEGVKSRPRQKKTQACLASKHVQEAPRLEPANEEHNVETAEDSEIRYLSADSGDADDSDADLGSAVKQLQEFIPNIKDRATSTIKRMYRDDLERFKEFKAQGVAIKFGKFSVKENKQLEKNVEDFLALTGIESADKLLYTDRYPEEKSVITNLKRRYSFRLHIGRNIARPWKLIYYRAKKMFDVNNYKGRYSEGDTEKLKMYHSLLGNDWKTIGEMVARSSLSVALKFSQISSQRNRGAWSKSETRKLIKAVEEVILKKMSPQELKEVDSKLQENPESCLSIVREKLYKGISWVEVEAKVQTRNWMQCKSKWTEILTKRMTNGRRIYYGMNALRAKVSLIERLYEINVEDTNEIDWEDLASAIGDVPPSYVQTKFSRLKAVYVPFWQKKTFPEIIDYLYETTLPLLKEKLEKMMEKKGTKIQTPAAPKQVFPFRDIFYYEDDSEGEDIEKESEGQAPCMAHACNSSTLGGQGRWII

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	Phosphorylation	SSRFEIHTPVSDKKK CCCEEECCCCCCCCC	30.92	30266825
15	Phosphorylation	FEIHTPVSDKKKKKC EEECCCCCCCCCCCC	44.94	30266825
40	Phosphorylation	SHEIFRDSSLVNEQS CHHHHCCHHHHCCHH	22.70	19691289
41	Phosphorylation	HEIFRDSSLVNEQSQ HHHHCCHHHHCCHHH	40.40	25159151
47	Phosphorylation	SSLVNEQSQITRRKK HHHHCCHHHHHHHHH	19.85	20068231
50	Phosphorylation	VNEQSQITRRKKRKK HCCHHHHHHHHHHHH	19.45	20068231
64	Phosphorylation	KDFQHLISSPLKKSR HHHHHHHCCCCHHHC	32.06	29255136
65	Phosphorylation	DFQHLISSPLKKSRI HHHHHHCCCCHHHCC	27.53	29255136
70	Phosphorylation	ISSPLKKSRICDETA HCCCCHHHCCCHHHC	25.87	28111955
76	Phosphorylation	KSRICDETANATSTL HHCCCHHHCCCCHHH	16.38	30576142
80	Phosphorylation	CDETANATSTLKKRK CHHHCCCCHHHHHHH	23.27	25159151
81	Phosphorylation	DETANATSTLKKRKK HHHCCCCHHHHHHHH	29.36	21815630
82	Phosphorylation	ETANATSTLKKRKKR HHCCCCHHHHHHHHH	37.94	21815630
84	Ubiquitination	ANATSTLKKRKKRRY CCCCHHHHHHHHHCC	51.09	-
85	Ubiquitination	NATSTLKKRKKRRYS CCCHHHHHHHHHCCC	72.98	-
92	Phosphorylation	KRKKRRYSALEVDEE HHHHHCCCCEEECCC	25.27	22468782
115	Phosphorylation	DKENINNTPKHFRKD CHHHCCCCCCHHCCC	29.26	28348404
144	Acetylation	PRKPKTDKFQVLAKS CCCCCCCHHHHHHHH	42.82	25953088
144	Ubiquitination	PRKPKTDKFQVLAKS CCCCCCCHHHHHHHH	42.82	-
150	Ubiquitination	DKFQVLAKSHAHKSE CHHHHHHHHHCCHHH	38.32	-
161	Phosphorylation	HKSEALHSKVREKKN CHHHHHHHHHHHHHH	33.42	-
177	Phosphorylation	KHQRKAASWESQRAR HHHHHHHHHHHHHHH	35.91	25159151
213	Phosphorylation	EITELPASAHKNKSK CCCCCCCHHCCCCCC	29.03	25159151
226	Phosphorylation	SKKKKKKSSNREYET CCCCCCCCCCHHHHH	41.55	28555341
227	Phosphorylation	KKKKKKSSNREYETL CCCCCCCCCHHHHHH	49.11	25159151
231	Phosphorylation	KKSSNREYETLAMPE CCCCCHHHHHHHCCC	15.81	18669648
233	Phosphorylation	SSNREYETLAMPEGS CCCHHHHHHHCCCCH	20.93	20068231
240	Phosphorylation	TLAMPEGSQAGREAG HHHCCCCHHHHHHCC	18.39	17525332
248	Phosphorylation	QAGREAGTDMQESQP HHHHHCCCCCCCCCC	35.03	23663014
253	Phosphorylation	AGTDMQESQPTVGLD CCCCCCCCCCCCCCC	25.27	23663014
256	Phosphorylation	DMQESQPTVGLDDET CCCCCCCCCCCCCCC	21.40	23663014
263	Phosphorylation	TVGLDDETPQLLGPT CCCCCCCCCHHCCCC	24.27	23401153
270	Phosphorylation	TPQLLGPTHKKKSKK CCHHCCCCCCCCCCC	44.52	23401153
297	Phosphorylation	ALAMPEGSQVGSEVG HHHCCCCCCCCCCCC	21.74	-
301	Phosphorylation	PEGSQVGSEVGADMQ CCCCCCCCCCCCCHH	30.19	-
357	Phosphorylation	PESLESAYPEGSQVG CHHHHHHCCCCCCCC	15.88	-
361	Phosphorylation	ESAYPEGSQVGSEVG HHHCCCCCCCCCCCC	21.74	-
365	Phosphorylation	PEGSQVGSEVGTVEG CCCCCCCCCCCEECC	30.19	-
398	Acetylation	KRKLTSVKRARVSGD HCCCCCCEEEECCCC	39.86	7708271
403	Phosphorylation	SVKRARVSGDDFSVP CCEEEECCCCCCCCC	30.83	29255136
408	Phosphorylation	RVSGDDFSVPSKNSE ECCCCCCCCCCCCCC	39.86	29255136
434	Ubiquitination	AMMEEGVKSRPRQKK HHHCCCCCCCCCHHH	52.16	-
449	Acetylation	TQACLASKHVQEAPR HHHHHHHHHHHHCCC	42.03	23749302
449	Ubiquitination	TQACLASKHVQEAPR HHHHHHHHHHHHCCC	42.03	-
468	Phosphorylation	NEEHNVETAEDSEIR CCCCCCCCCCCCCCE	30.94	27732954
472	Phosphorylation	NVETAEDSEIRYLSA CCCCCCCCCCEEEEC	26.82	25850435
476	Phosphorylation	AEDSEIRYLSADSGD CCCCCCEEEECCCCC	15.63	23927012
478	Phosphorylation	DSEIRYLSADSGDAD CCCCEEEECCCCCCC	22.54	23927012
481	Phosphorylation	IRYLSADSGDADDSD CEEEECCCCCCCCCC	37.99	23927012
487	Phosphorylation	DSGDADDSDADLGSA CCCCCCCCCCCHHHH	34.93	29255136
493	Phosphorylation	DSDADLGSAVKQLQE CCCCCHHHHHHHHHH	36.87	30266825
506	Ubiquitination	QEFIPNIKDRATSTI HHHCCCCHHHHHHHH	48.04	-
510	Phosphorylation	PNIKDRATSTIKRMY CCCHHHHHHHHHHHH	27.57	28634120
514	Ubiquitination	DRATSTIKRMYRDDL HHHHHHHHHHHHHHH	31.07	-
528	Methylation	LERFKEFKAQGVAIK HHHHHHHHHHCEEEE	40.67	115979431
528	Ubiquitination	LERFKEFKAQGVAIK HHHHHHHHHHCEEEE	40.67	-
535	Ubiquitination	KAQGVAIKFGKFSVK HHHCEEEEECCCCHH	38.02	-
538	Ubiquitination	GVAIKFGKFSVKENK CEEEEECCCCHHHCH	37.28	-
542	Ubiquitination	KFGKFSVKENKQLEK EECCCCHHHCHHHHH	55.14	-
549	Ubiquitination	KENKQLEKNVEDFLA HHCHHHHHHHHHHHH	74.92	-
565	Ubiquitination	TGIESADKLLYTDRY HCCCCHHHHHHCCCC	39.86	-
568	Phosphorylation	ESADKLLYTDRYPEE CCHHHHHHCCCCCHH	19.61	30177828
569	Phosphorylation	SADKLLYTDRYPEEK CHHHHHHCCCCCHHH	17.61	30177828
572	Phosphorylation	KLLYTDRYPEEKSVI HHHHCCCCCHHHHHH	20.15	30177828
583	Ubiquitination	KSVITNLKRRYSFRL HHHHHHHCHHEEEEE	36.58	-
587	Phosphorylation	TNLKRRYSFRLHIGR HHHCHHEEEEEEECC	11.33	29496963
617	Ubiquitination	MFDVNNYKGRYSEGD HCCCCCCCCCCCCCC	38.75	-
621	Phosphorylation	NNYKGRYSEGDTEKL CCCCCCCCCCCHHHH	33.47	25159151
627	Ubiquitination	YSEGDTEKLKMYHSL CCCCCHHHHHHHHHH	56.34	-
629	Ubiquitination	EGDTEKLKMYHSLLG CCCHHHHHHHHHHHC	48.78	-
640	Ubiquitination	SLLGNDWKTIGEMVA HHHCCCHHHHHHHHH	32.88	-
650	Phosphorylation	GEMVARSSLSVALKF HHHHHHHHHHHHHHH	21.07	20860994
652	Phosphorylation	MVARSSLSVALKFSQ HHHHHHHHHHHHHHH	13.80	29759185
658	Phosphorylation	LSVALKFSQISSQRN HHHHHHHHHHHCCCC	25.64	29759185
661	Phosphorylation	ALKFSQISSQRNRGA HHHHHHHHCCCCCCC	16.87	29759185
662	Phosphorylation	LKFSQISSQRNRGAW HHHHHHHCCCCCCCC	34.49	29759185
671	Ubiquitination	RNRGAWSKSETRKLI CCCCCCCHHHHHHHH	41.43	-
687	Ubiquitination	AVEEVILKKMSPQEL HHHHHHHHHCCHHHH	34.99	-
688	Acetylation	VEEVILKKMSPQELK HHHHHHHHCCHHHHH	40.96	20167786
688	Ubiquitination	VEEVILKKMSPQELK HHHHHHHHCCHHHHH	40.96	-
690	Phosphorylation	EVILKKMSPQELKEV HHHHHHCCHHHHHHH	32.10	25159151
695	Ubiquitination	KMSPQELKEVDSKLQ HCCHHHHHHHHHHHH	55.74	-
700	Acetylation	ELKEVDSKLQENPES HHHHHHHHHHHCHHH	50.13	20167786
700	Sumoylation	ELKEVDSKLQENPES HHHHHHHHHHHCHHH	50.13	28112733
700	Ubiquitination	ELKEVDSKLQENPES HHHHHHHHHHHCHHH	50.13	-
710	Phosphorylation	ENPESCLSIVREKLY HCHHHHHHHHHHHHH	24.30	25159151
738	Ubiquitination	TRNWMQCKSKWTEIL HCCHHHCHHHHHHHH	37.87	-
740	Ubiquitination	NWMQCKSKWTEILTK CHHHCHHHHHHHHHH	43.56	-
747	Ubiquitination	KWTEILTKRMTNGRR HHHHHHHHHHCCCCC	36.41	-
765	Ubiquitination	GMNALRAKVSLIERL CHHHHHHHHHHHHHH	26.39	-
808	Ubiquitination	QTKFSRLKAVYVPFW HHHHHHCEEEEECCC	34.39	-
818	Ubiquitination	YVPFWQKKTFPEIID EECCCCCCCHHHHHH	40.05	-
838	Ubiquitination	TLPLLKEKLEKMMEK CHHHHHHHHHHHHHH	61.43	-
846	Ubiquitination	LEKMMEKKGTKIQTP HHHHHHHCCCCCCCC	59.51	-
857	Acetylation	IQTPAAPKQVFPFRD CCCCCCCCCEECCCC	55.13	7339563
857	Ubiquitination	IQTPAAPKQVFPFRD CCCCCCCCCEECCCC	55.13	-
867	Phosphorylation	FPFRDIFYYEDDSEG ECCCCEEEEECCCCC	13.28	23403867
868	Phosphorylation	PFRDIFYYEDDSEGE CCCCEEEEECCCCCC	11.35	26657352
872	Phosphorylation	IFYYEDDSEGEDIEK EEEEECCCCCCCCCH	60.88	25159151
881	Phosphorylation	GEDIEKESEGQAPCM CCCCCHHCCCCCCCH	59.08	25002506
894	Phosphorylation	CMAHACNSSTLGGQG CHHHHCCCCCCCCCC	25.28	25627689
895	Phosphorylation	MAHACNSSTLGGQGR HHHHCCCCCCCCCCC	17.41	25627689
896	Phosphorylation	AHACNSSTLGGQGRW HHHCCCCCCCCCCCC	29.28	25627689

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
-	K	Ubiquitination	E3 ubiquitin ligase	MDM2	Q00987	PMID:22383580

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TTF1_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CAVN1_HUMAN	PTRF	physical	9582279
KAT2B_HUMAN	KAT2B	physical	11250901
BAZ2A_HUMAN	BAZ2A	physical	15292447
MDM2_HUMAN	MDM2	physical	22383580
CDN2A_HUMAN	CDKN2A	physical	22383580
ARF_HUMAN	CDKN2A	physical	22383580

Drug and Disease Associations

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

Regulatory Network of TTF1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-476; SER-481 ANDSER-487, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-476; SER-481 ANDSER-487, AND MASS SPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-403; SER-478;SER-481 AND SER-487, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-47, AND MASSSPECTROMETRY.	19007248 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, AND MASSSPECTROMETRY.	17525332 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-872, AND MASSSPECTROMETRY.	16565220 [Abstract]