dbPTM

RPA43_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RPA43_HUMAN
UniProt AC	Q3B726
Protein Name	DNA-directed RNA polymerase I subunit RPA43
Gene Name	TWISTNB
Organism	Homo sapiens (Human).
Sequence Length	338
Subcellular Localization	Nucleus, nucleolus.
Protein Description	DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I which synthesizes ribosomal RNA precursors. Through its association with RRN3/TIF-IA may be involved in recruitment of Pol I to rDNA promoters..
Protein Sequence	MAAGCSEAPRPAAASDGSLVGQAGVLPCLELPTYAAACALVNSRYSCLVAGPHQRHIALSPRYLNRKRTGIREQLDAELLRYSESLLGVPIAYDNIKVVGELGDIYDDQGHIHLNIEADFVIFCPEPGQKLMGIVNKVSSSHIGCLVHGCFNASIPKPEQLSAEQWQTMEINMGDELEFEVFRLDSDAAGVFCIRGKLNITSLQFKRSEVSEEVTENGTEEAAKKPKKKKKKKDPETYEVDSGTTKLADDADDTPMEESALQNTNNANGIWEEEPKKKKKKKKHQEVQDQDPVFQGSDSSGYQSDHKKKKKKRKHSEEAEFTPPLKCSPKRKGKSNFL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MAAGCSEAPRPAA --CCCCCCCCCCCCC	35.56	20860994
60	Phosphorylation	HQRHIALSPRYLNRK CHHEEECCHHHHCCC	9.79	23401153
83	Phosphorylation	DAELLRYSESLLGVP HHHHHHHHHHHHCCC	17.80	27251275
85	Phosphorylation	ELLRYSESLLGVPIA HHHHHHHHHHCCCEE	23.97	21815630
93	Phosphorylation	LLGVPIAYDNIKVVG HHCCCEEECCEEEEE	15.39	20068231
197	Acetylation	GVFCIRGKLNITSLQ EEEEEECEEEECEEE	28.63	25953088
211	Phosphorylation	QFKRSEVSEEVTENG EEEHHHHCHHHHHCC	24.80	25627689
215	Phosphorylation	SEVSEEVTENGTEEA HHHCHHHHHCCCHHH	27.32	25159151
237	Phosphorylation	KKKKDPETYEVDSGT CCCCCCCCEECCCCC	30.30	30108239
238	Phosphorylation	KKKDPETYEVDSGTT CCCCCCCEECCCCCC	16.58	23403867
242	Phosphorylation	PETYEVDSGTTKLAD CCCEECCCCCCEECC	43.12	25159151
244	Phosphorylation	TYEVDSGTTKLADDA CEECCCCCCEECCCC	25.39	23403867
245	Phosphorylation	YEVDSGTTKLADDAD EECCCCCCEECCCCC	27.82	21815630
254	Phosphorylation	LADDADDTPMEESAL ECCCCCCCCCHHHHH	25.69	25159151
259	Phosphorylation	DDTPMEESALQNTNN CCCCCHHHHHHCCCC	22.45	30576142
264	Phosphorylation	EESALQNTNNANGIW HHHHHHCCCCCCCCC	19.52	22210691
297	Phosphorylation	QDPVFQGSDSSGYQS CCCCCCCCCCCCCCC	24.44	23401153
299	Phosphorylation	PVFQGSDSSGYQSDH CCCCCCCCCCCCCHH	27.62	23401153
300	Phosphorylation	VFQGSDSSGYQSDHK CCCCCCCCCCCCHHH	46.65	30266825
302	Phosphorylation	QGSDSSGYQSDHKKK CCCCCCCCCCHHHHH	13.54	23927012
304	Phosphorylation	SDSSGYQSDHKKKKK CCCCCCCCHHHHHHH	32.95	29255136
316	Phosphorylation	KKKKRKHSEEAEFTP HHHHHCCCCCCCCCC	39.92	29255136
322	Phosphorylation	HSEEAEFTPPLKCSP CCCCCCCCCCCCCCC	18.59	29255136
328	Phosphorylation	FTPPLKCSPKRKGKS CCCCCCCCCCCCCCC	31.69	29255136
335	Phosphorylation	SPKRKGKSNFL---- CCCCCCCCCCC----	41.29	26074081

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 RPA43_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RPA43_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 RPA43_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RPA2_HUMAN	POLR1B	physical	26186194
RPA1_HUMAN	POLR1A	physical	26186194
RRN3_HUMAN	RRN3	physical	26186194
RRN3_HUMAN	RRN3	physical	28514442
RPAC1_HUMAN	POLR1C	physical	28514442
RPA1_HUMAN	POLR1A	physical	28514442
RPA2_HUMAN	POLR1B	physical	28514442

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 RPA43_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-316 AND SER-328, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; SER-316 AND SER-328,AND MASS SPECTROMETRY.	17081983 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-302, AND MASSSPECTROMETRY.	18220336 [Abstract]