dbPTM

RRN3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RRN3_HUMAN
UniProt AC	Q9NYV6
Protein Name	RNA polymerase I-specific transcription initiation factor RRN3
Gene Name	RRN3
Organism	Homo sapiens (Human).
Sequence Length	651
Subcellular Localization	Nucleus, nucleolus .
Protein Description	Required for efficient transcription initiation by RNA polymerase I. Required for the formation of the competent preinitiation complex (PIC). Dissociates from pol I as a consequence of transcription. In vitro, cannot activate transcription in a subsequent transcription reaction (By similarity)..
Protein Sequence	MAAPLLHTRLPGDAAASSSAVKKLGASRTGISNMRALENDFFNSPPRKTVRFGGTVTEVLLKYKKGETNDFELLKNQLLDPDIKDDQIINWLLEFRSSIMYLTKDFEQLISIILRLPWLNRSQTVVEEYLAFLGNLVSAQTVFLRPCLSMIASHFVPPRVIIKEGDVDVSDSDDEDDNLPANFDTCHRALQIIARYVPSTPWFLMPILVEKFPFVRKSERTLECYVHNLLRISVYFPTLRHEILELIIEKLLKLDVNASRQGIEDAEETATQTCGGTDSTEGLFNMDEDEETEHETKAGPERLDQMVHPVAERLDILMSLVLSYMKDVCYVDGKVDNGKTKDLYRDLINIFDKLLLPTHASCHVQFFMFYLCSFKLGFAEAFLEHLWKKLQDPSNPAIIRQAAGNYIGSFLARAKFIPLITVKSCLDLLVNWLHIYLNNQDSGTKAFCDVALHGPFYSACQAVFYTFVFRHKQLLSGNLKEGLQYLQSLNFERIVMSQLNPLKICLPSVVNFFAAITNKYQLVFCYTIIERNNRQMLPVIRSTAGGDSVQICTNPLDTFFPFDPCVLKRSKKFIDPIYQVWEDMSAEELQEFKKPMKKDIVEDEDDDFLKGEVPQNDTVIGITPSSFDTHFRSPSSSVGSPPVLYMQPSPL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Methylation	AAPLLHTRLPGDAAA CCCCCCCCCCCCHHH	28.30	115368723
11 (in isoform 3)	Phosphorylation	-	35.01	25849741
17	Phosphorylation	LPGDAAASSSAVKKL CCCCHHHCHHHHHHH	21.79	23401153
18	Phosphorylation	PGDAAASSSAVKKLG CCCHHHCHHHHHHHC	20.00	29255136
19	Phosphorylation	GDAAASSSAVKKLGA CCHHHCHHHHHHHCC	34.29	29255136
22	Acetylation	AASSSAVKKLGASRT HHCHHHHHHHCCCCC	41.83	25953088
22	Ubiquitination	AASSSAVKKLGASRT HHCHHHHHHHCCCCC	41.83	21906983
22	Ubiquitination	AASSSAVKKLGASRT HHCHHHHHHHCCCCC	41.83	21906983
29	Ubiquitination	KKLGASRTGISNMRA HHHCCCCCCCCHHHH	36.05	-
32	Ubiquitination	GASRTGISNMRALEN CCCCCCCCHHHHHHC	26.39	-
44	Phosphorylation	LENDFFNSPPRKTVR HHCCCCCCCCCCEEE	30.99	19664994
49	Phosphorylation	FNSPPRKTVRFGGTV CCCCCCCEEEECCEE	20.42	24732914
55	Phosphorylation	KTVRFGGTVTEVLLK CEEEECCEEHHHHHH	25.32	28857561
62	Ubiquitination	TVTEVLLKYKKGETN EEHHHHHHHHCCCCC	51.36	21906983
62	Ubiquitination	TVTEVLLKYKKGETN EEHHHHHHHHCCCCC	51.36	21906983
65	Ubiquitination	EVLLKYKKGETNDFE HHHHHHHCCCCCHHH	59.91	-
75	Ubiquitination	TNDFELLKNQLLDPD CCHHHHHHHHCCCCC	56.10	-
170	Phosphorylation	KEGDVDVSDSDDEDD EECCCCCCCCCCCCC	27.25	26503892
172	Phosphorylation	GDVDVSDSDDEDDNL CCCCCCCCCCCCCCC	39.18	25463755
185	Phosphorylation	NLPANFDTCHRALQI CCCCCHHHHHHHHHH	13.18	20068231
196	Phosphorylation	ALQIIARYVPSTPWF HHHHHHHHCCCCCCH	14.00	20068231
199	Phosphorylation	IIARYVPSTPWFLMP HHHHHCCCCCCHHHH	36.74	20068231
200	Phosphorylation	IARYVPSTPWFLMPI HHHHCCCCCCHHHHH	20.61	20068231
233	Phosphorylation	VHNLLRISVYFPTLR HHHHHHHHEECHHHH	12.34	-
233	Ubiquitination	VHNLLRISVYFPTLR HHHHHHHHEECHHHH	12.34	-
253	Ubiquitination	LIIEKLLKLDVNASR HHHHHHHHCCCCHHH	53.75	21906983
253	Ubiquitination	LIIEKLLKLDVNASR HHHHHHHHCCCCHHH	53.75	21906983
271	Phosphorylation	EDAEETATQTCGGTD CCHHHHHCCCCCCCC	31.65	-
298	Ubiquitination	ETEHETKAGPERLDQ CCCCHHCCCHHHHHH	46.31	21906983
306	Sulfoxidation	GPERLDQMVHPVAER CHHHHHHHHHHHHHH	2.74	21406390
319	Phosphorylation	ERLDILMSLVLSYMK HHHHHHHHHHHHHHC	16.33	22468782
324	Phosphorylation	LMSLVLSYMKDVCYV HHHHHHHHHCCCEEE	12.20	22468782
330	Phosphorylation	SYMKDVCYVDGKVDN HHHCCCEEECCEECC	11.04	22468782
334	Ubiquitination	DVCYVDGKVDNGKTK CCEEECCEECCCCCH	41.79	-
386	Ubiquitination	AEAFLEHLWKKLQDP HHHHHHHHHHHHCCC	5.39	-
409	Phosphorylation	AAGNYIGSFLARAKF HCHHHHHHHHHHHCC	13.92	24719451
415	Ubiquitination	GSFLARAKFIPLITV HHHHHHHCCCCCEEH	37.97	-
428	Ubiquitination	TVKSCLDLLVNWLHI EHHHHHHHHHHHHHH	3.57	21906983
480	Ubiquitination	QLLSGNLKEGLQYLQ HHHCCCHHHHHHHHH	54.45	21906983
568	Ubiquitination	PFDPCVLKRSKKFID CCCHHHHHCCHHHCC	33.94	-
593	Ubiquitination	AEELQEFKKPMKKDI HHHHHHHHCCHHCCC	56.04	-
598	Ubiquitination	EFKKPMKKDIVEDED HHHCCHHCCCCCCCC	46.57	-
610	Ubiquitination	DEDDDFLKGEVPQND CCCCCCCCCCCCCCC	53.68	2190698
618	Phosphorylation	GEVPQNDTVIGITPS CCCCCCCCEEEECCH	22.90	29255136
623	Phosphorylation	NDTVIGITPSSFDTH CCCEEEECCHHHCCC	16.35	29255136
625	Phosphorylation	TVIGITPSSFDTHFR CEEEECCHHHCCCCC	34.68	22210691
626	Phosphorylation	VIGITPSSFDTHFRS EEEECCHHHCCCCCC	28.48	29255136
629	Phosphorylation	ITPSSFDTHFRSPSS ECCHHHCCCCCCCCC	22.39	26074081
633	Phosphorylation	SFDTHFRSPSSSVGS HHCCCCCCCCCCCCC	28.34	22115753
635	Phosphorylation	DTHFRSPSSSVGSPP CCCCCCCCCCCCCCC	36.17	30278072
636	Phosphorylation	THFRSPSSSVGSPPV CCCCCCCCCCCCCCE	32.21	25159151
637	Phosphorylation	HFRSPSSSVGSPPVL CCCCCCCCCCCCCEE	34.53	25159151
640	Phosphorylation	SPSSSVGSPPVLYMQ CCCCCCCCCCEEEEC	24.71	30278072
645	Phosphorylation	VGSPPVLYMQPSPL- CCCCCEEEECCCCC-	8.24	23403867
649	Phosphorylation	PVLYMQPSPL----- CEEEECCCCC-----	23.18	25159151

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
44	S	Phosphorylation	Kinase	CDK2	P24941	PSP
170	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
172	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
200	T	Phosphorylation	Kinase	MK09	P45984	PhosphoELM
633	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
635	S	Phosphorylation	Kinase	AMPKG2	Q9UGJ0	PSP
635	S	Phosphorylation	Kinase	PRKAA1	Q13131	GPS
649	S	Phosphorylation	Kinase	RPS6KA3	P51812	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
200	T	Phosphorylation		15805466
Phosphorylated at Thr-200 by MAPK9/JNK2, which abrogates initiation complex formation.

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 RRN3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RPA2_MOUSE	Polr1b	physical	15004009
EIF3L_MOUSE	Eif3l	physical	15004009
RPA1_HUMAN	POLR1A	physical	11250903
TBP_HUMAN	TBP	physical	11250903
TAF1B_HUMAN	TAF1B	physical	11250903
UBF1_HUMAN	UBTF	physical	11250903
TAF1C_HUMAN	TAF1C	physical	11250903
TAF1A_HUMAN	TAF1A	physical	11250903
RPA49_HUMAN	POLR1E	physical	19214185
RPA2_MOUSE	Polr1b	physical	12393749
TIF1B_MOUSE	Trim28	physical	12393749
RPA2_HUMAN	POLR1B	physical	15558034
ACTS_HUMAN	ACTA1	physical	15558034
RPA43_YEAST	RPA43	physical	23393135
TAF12_YEAST	TAF12	physical	23393135
MYO1C_HUMAN	MYO1C	physical	15558034

Drug and Disease Associations

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

Regulatory Network of RRN3_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 SER-640, AND MASSSPECTROMETRY.	19690332 [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-44; SER-170; SER-172 ANDSER-640, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, AND MASSSPECTROMETRY.	18691976 [Abstract]
"The nucleolus as a stress sensor: JNK2 inactivates the transcriptionfactor TIF-IA and down-regulates rRNA synthesis."; Mayer C., Bierhoff H., Grummt I.; Genes Dev. 19:933-941(2005). Cited for: PHOSPHORYLATION AT THR-200 BY MAPK9/JNK2, AND FUNCTION.	15805466 [Abstract]

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