RPC1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RPC1_HUMAN
• UniProt AC: O14802
• Protein Name: DNA-directed RNA polymerase III subunit RPC1
• Gene Name: POLR3A
• Organism: Homo sapiens (Human).
• Sequence Length: 1390
• Subcellular Localization: Nucleus.
• Protein Description: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Forms the polymerase active center together with the second largest subunit. A single-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol III. A bridging helix emanates from RPC1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol III by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition (By similarity). Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway..
• Protein Sequence: MVKEQFRETDVAKKISHICFGMKSPEEMRQQAHIQVVSKNLYSQDNQHAPLLYGVLDHRMGTSEKDRPCETCGKNLADCLGHYGYIDLELPCFHVGYFRAVIGILQMICKTCCHIMLSQEEKKQFLDYLKRPGLTYLQKRGLKKKISDKCRKKNICHHCGAFNGTVKKCGLLKIIHEKYKTNKKVVDPIVSNFLQSFETAIEHNKEVEPLLGRAQENLNPLVVLNLFKRIPAEDVPLLLMNPEAGKPSDLILTRLLVPPLCIRPSVVSDLKSGTNEDDLTMKLTEIIFLNDVIKKHRISGAKTQMIMEDWDFLQLQCALYINSELSGIPLNMAPKKWTRGFVQRLKGKQGRFRGNLSGKRVDFSGRTVISPDPNLRIDEVAVPVHVAKILTFPEKVNKANINFLRKLVQNGPEVHPGANFIQQRHTQMKRFLKYGNREKMAQELKYGDIVERHLIDGDVVLFNRQPSLHKLSIMAHLARVKPHRTFRFNECVCTPYNADFDGDEMNLHLPQTEEAKAEALVLMGTKANLVTPRNGEPLIAAIQDFLTGAYLLTLKDTFFDRAKACQIIASILVGKDEKIKVRLPPPTILKPVTLWTGKQIFSVILRPSDDNPVRANLRTKGKQYCGKGEDLCANDSYVTIQNSELMSGSMDKGTLGSGSKNNIFYILLRDWGQNEAADAMSRLARLAPVYLSNRGFSIGIGDVTPGQGLLKAKYELLNAGYKKCDEYIEALNTGKLQQQPGCTAEETLEALILKELSVIRDHAGSACLRELDKSNSPLTMALCGSKGSFINISQMIACVGQQAISGSRVPDGFENRSLPHFEKHSKLPAAKGFVANSFYSGLTPTEFFFHTMAGREGLVDTAVKTAETGYMQRRLVKSLEDLCSQYDLTVRSSTGDIIQFIYGGDGLDPAAMEGKDEPLEFKRVLDNIKAVFPCPSEPALSKNELILTTESIMKKSEFLCCQDSFLQEIKKFIKGVSEKIKKTRDKYGINDNGTTEPRVLYQLDRITPTQVEKFLETCRDKYMRAQMEPGSAVGALCAQSIGEPGTQMTLKTFHFAGVASMNITLGVPRIKEIINASKAISTPIITAQLDKDDDADYARLVKGRIEKTLLGEISEYIEEVFLPDDCFILVKLSLERIRLLRLEVNAETVRYSICTSKLRVKPGDVAVHGEAVVCVTPRENSKSSMYYVLQFLKEDLPKVVVQGIPEVSRAVIHIDEQSGKEKYKLLVEGDNLRAVMATHGVKGTRTTSNNTYEVEKTLGIEAARTTIINEIQYTMVNHGMSIDRRHVMLLSDLMTYKGEVLGITRFGLAKMKESVLMLASFEKTADHLFDAAYFGQKDSVCGVSECIIMGIPMNIGTGLFKLLHKADRDPNPPKRPLIFDTNEFHIPLVT

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Methylation	-----MVKEQFRETD -----CCHHHHHHHH	58.62	115975349
9	Phosphorylation	VKEQFRETDVAKKIS CHHHHHHHHHHHHHH	31.36	30631047
23	Acetylation	SHICFGMKSPEEMRQ HHHHHCCCCHHHHHH	64.34	25953088
24	Phosphorylation	HICFGMKSPEEMRQQ HHHHCCCCHHHHHHH	28.75	29214152
53	Phosphorylation	NQHAPLLYGVLDHRM CCCHHHHHHHHHHCC	16.93	27642862
65	Acetylation	HRMGTSEKDRPCETC HCCCCCCCCCCCCCC	59.82	23749302
65	Ubiquitination	HRMGTSEKDRPCETC HCCCCCCCCCCCCCC	59.82	-
128	Phosphorylation	EKKQFLDYLKRPGLT HHHHHHHHHHCCCCH	19.10	28152594
139	Ubiquitination	PGLTYLQKRGLKKKI CCCHHHHHCCCHHHH	45.93	29967540
149	Ubiquitination	LKKKISDKCRKKNIC CHHHHCHHHHHCCCC	29.19	24816145
178	Ubiquitination	LLKIIHEKYKTNKKV HHHHHHHHHCCCCCC	37.57	29967540
184	Ubiquitination	EKYKTNKKVVDPIVS HHHCCCCCCCCHHHH	49.95	33845483
228	Ubiquitination	LVVLNLFKRIPAEDV HHHHHHHCCCCHHHC	53.21	21906983
246	Ubiquitination	LMNPEAGKPSDLILT EECCCCCCCCCCCHH	48.69	-
271	Ubiquitination	PSVVSDLKSGTNEDD HHHHCCCCCCCCHHH	52.40	29967540
281	Sulfoxidation	TNEDDLTMKLTEIIF CCHHHHHHHHHHHHH	4.32	21406390
320	Phosphorylation	LQLQCALYINSELSG HHHHHHHHHCHHHCC	4.59	23401153
323	Phosphorylation	QCALYINSELSGIPL HHHHHHCHHHCCCCC	30.29	23401153
326	Phosphorylation	LYINSELSGIPLNMA HHHCHHHCCCCCCCC	30.53	23401153
335	Acetylation	IPLNMAPKKWTRGFV CCCCCCCCCCCHHHH	51.94	25953088
336	Acetylation	PLNMAPKKWTRGFVQ CCCCCCCCCCHHHHH	53.38	25953088
346	Acetylation	RGFVQRLKGKQGRFR HHHHHHHCCCCCCCC	67.27	12650233
348	Acetylation	FVQRLKGKQGRFRGN HHHHHCCCCCCCCCC	48.25	19806641
353	Methylation	KGKQGRFRGNLSGKR CCCCCCCCCCCCCCE	31.56	115488171
359	Acetylation	FRGNLSGKRVDFSGR CCCCCCCCEEECCCC	45.96	12650243
388	Ubiquitination	AVPVHVAKILTFPEK CEECHHHHHHHCHHH	36.84	21906983
395	Acetylation	KILTFPEKVNKANIN HHHHCHHHHCHHHHH	51.88	25953088
395	Ubiquitination	KILTFPEKVNKANIN HHHHCHHHHCHHHHH	51.88	29967540
398	Malonylation	TFPEKVNKANINFLR HCHHHHCHHHHHHHH	45.88	26320211
398	Ubiquitination	TFPEKVNKANINFLR HCHHHHCHHHHHHHH	45.88	29967540
406	Ubiquitination	ANINFLRKLVQNGPE HHHHHHHHHHHCCCC	55.97	21906983
433	Acetylation	TQMKRFLKYGNREKM HHHHHHHHHCCHHHH	48.69	25953088
433	Ubiquitination	TQMKRFLKYGNREKM HHHHHHHHHCCHHHH	48.69	-
434	Phosphorylation	QMKRFLKYGNREKMA HHHHHHHHCCHHHHH	23.06	20068231
445	Acetylation	EKMAQELKYGDIVER HHHHHHCCCCCHHHH	46.57	19608861
445	Ubiquitination	EKMAQELKYGDIVER HHHHHHCCCCCHHHH	46.57	21906983
525	Phosphorylation	EALVLMGTKANLVTP HHHHHCCCCCCCCCC	17.02	21406692
526	Ubiquitination	ALVLMGTKANLVTPR HHHHCCCCCCCCCCC	29.55	21906983
531	Phosphorylation	GTKANLVTPRNGEPL CCCCCCCCCCCCCCC	21.50	24719451
580	Ubiquitination	VGKDEKIKVRLPPPT CCCCCCEEEECCCCC	32.16	-
590	Ubiquitination	LPPPTILKPVTLWTG CCCCCCCEEEEEECC	33.32	-
593	Phosphorylation	PTILKPVTLWTGKQI CCCCEEEEEECCCEE	25.71	-
596	Phosphorylation	LKPVTLWTGKQIFSV CEEEEEECCCEEEEE	37.30	-
652	Ubiquitination	LMSGSMDKGTLGSGS HCCCCCCCCCCCCCC	45.19	-
660	Ubiquitination	GTLGSGSKNNIFYIL CCCCCCCCCCEEEEE	58.50	-
681	Phosphorylation	NEAADAMSRLARLAP CHHHHHHHHHHHHHH	26.34	-
711	Ubiquitination	TPGQGLLKAKYELLN CCCCCHHHHHHHHHH	48.12	21906983
713	Ubiquitination	GQGLLKAKYELLNAG CCCHHHHHHHHHHHH	37.36	21906983
714	Phosphorylation	QGLLKAKYELLNAGY CCHHHHHHHHHHHHH	19.37	-
722	Ubiquitination	ELLNAGYKKCDEYIE HHHHHHHHHHHHHHH	46.11	29967540
723	Ubiquitination	LLNAGYKKCDEYIEA HHHHHHHHHHHHHHH	38.13	29967540
735	Ubiquitination	IEALNTGKLQQQPGC HHHHHCCCCCCCCCC	40.87	29967540
742	Glutathionylation	KLQQQPGCTAEETLE CCCCCCCCCHHHHHH	4.08	22555962
754	Ubiquitination	TLEALILKELSVIRD HHHHHHHHHHHHHHH	50.01	29967540
773	Ubiquitination	ACLRELDKSNSPLTM HHHHHHHCCCCCCEE	65.25	-
785	Phosphorylation	LTMALCGSKGSFINI CEEHHCCCCCCCCCH	32.61	24532841
788	Phosphorylation	ALCGSKGSFINISQM HHCCCCCCCCCHHHH	27.04	24532841
793	Phosphorylation	KGSFINISQMIACVG CCCCCCHHHHHHHHC	14.81	24532841
823	Ubiquitination	RSLPHFEKHSKLPAA CCCCCHHHHCCCCCC	52.84	29967540
826	Ubiquitination	PHFEKHSKLPAAKGF CCHHHHCCCCCCCCC	59.20	27667366
864	Ubiquitination	GLVDTAVKTAETGYM CCCCHHHHHHHHHHH	39.28	21906983
877	Ubiquitination	YMQRRLVKSLEDLCS HHHHHHHHHHHHHHH	54.65	-
922	Ubiquitination	KDEPLEFKRVLDNIK CCCCCCHHHHHHHEE	32.02	29967540
936	Phosphorylation	KAVFPCPSEPALSKN EEEEECCCCCCCCCC	64.03	18767875
941	Phosphorylation	CPSEPALSKNELILT CCCCCCCCCCCEEEE	35.23	18767875
948	Phosphorylation	SKNELILTTESIMKK CCCCEEEEHHHHHHH	22.86	-
949	Phosphorylation	KNELILTTESIMKKS CCCEEEEHHHHHHHC	25.04	-
951	Phosphorylation	ELILTTESIMKKSEF CEEEEHHHHHHHCCH	26.37	19690332
955	Ubiquitination	TTESIMKKSEFLCCQ EHHHHHHHCCHHHCC	37.53	29967540
970	Ubiquitination	DSFLQEIKKFIKGVS HHHHHHHHHHHHHHH	40.66	29967540
974	Ubiquitination	QEIKKFIKGVSEKIK HHHHHHHHHHHHHHH	57.29	29967540
977	Phosphorylation	KKFIKGVSEKIKKTR HHHHHHHHHHHHHHH	41.67	24719451
979	Ubiquitination	FIKGVSEKIKKTRDK HHHHHHHHHHHHHHH	52.93	27667366
981	Ubiquitination	KGVSEKIKKTRDKYG HHHHHHHHHHHHHCC	60.19	22817900
982	Ubiquitination	GVSEKIKKTRDKYGI HHHHHHHHHHHHCCC	52.87	22817900
983	Phosphorylation	VSEKIKKTRDKYGIN HHHHHHHHHHHCCCC	38.81	29978859
986	Ubiquitination	KIKKTRDKYGINDNG HHHHHHHHCCCCCCC	41.93	22817900
994	Phosphorylation	YGINDNGTTEPRVLY CCCCCCCCCCCEEEE	33.95	29978859
995	Phosphorylation	GINDNGTTEPRVLYQ CCCCCCCCCCEEEEE	45.44	29978859
1005	Methylation	RVLYQLDRITPTQVE EEEEEECCCCHHHHH	43.18	115488179
1013	Ubiquitination	ITPTQVEKFLETCRD CCHHHHHHHHHHHHH	57.29	22817900
1046	Phosphorylation	QSIGEPGTQMTLKTF HHCCCCCCEEEEEEE	26.36	18077418
1049	Phosphorylation	GEPGTQMTLKTFHFA CCCCCEEEEEEEECC	18.45	18077418
1071	Ubiquitination	TLGVPRIKEIINASK EECCHHHHHHHHHHH	44.11	-
1078	Ubiquitination	KEIINASKAISTPII HHHHHHHHHCCCCEE	47.53	29967540
1091	Ubiquitination	IITAQLDKDDDADYA EEEEECCCCCCHHHH	72.20	29967540
1102	Ubiquitination	ADYARLVKGRIEKTL HHHHHHHHHHHHHHH	47.25	29967540
1157	Ubiquitination	RYSICTSKLRVKPGD EEEEECCCCCCCCCC	23.35	-
1181	Phosphorylation	CVTPRENSKSSMYYV EECCCCCCCHHHHHH	29.21	20068231
1182	Ubiquitination	VTPRENSKSSMYYVL ECCCCCCCHHHHHHH	59.12	23503661
1183	Phosphorylation	TPRENSKSSMYYVLQ CCCCCCCHHHHHHHH	21.84	20068231
1184	Phosphorylation	PRENSKSSMYYVLQF CCCCCCHHHHHHHHH	17.97	20068231
1186	Phosphorylation	ENSKSSMYYVLQFLK CCCCHHHHHHHHHHH	7.74	20068231
1187	Phosphorylation	NSKSSMYYVLQFLKE CCCHHHHHHHHHHHH	6.00	20068231
1198	Ubiquitination	FLKEDLPKVVVQGIP HHHHCCCCEEEECCC	55.76	29967540
1222	Ubiquitination	DEQSGKEKYKLLVEG ECCCCCEEEEEEEEC	51.69	-
1224	Ubiquitination	QSGKEKYKLLVEGDN CCCCEEEEEEEECCC	46.54	29967540
1242	Ubiquitination	VMATHGVKGTRTTSN HHHHCCCCCEEECCC	60.19	29901268
1246	Phosphorylation	HGVKGTRTTSNNTYE CCCCCEEECCCCEEE	34.12	24719451
1247	Phosphorylation	GVKGTRTTSNNTYEV CCCCEEECCCCEEEE	26.60	24719451
1248	Phosphorylation	VKGTRTTSNNTYEVE CCCEEECCCCEEEEE	27.72	24719451
1251	Phosphorylation	TRTTSNNTYEVEKTL EEECCCCEEEEEEEC	25.88	-
1256	Ubiquitination	NNTYEVEKTLGIEAA CCEEEEEEECCCHHH	54.98	22817900
1265	Phosphorylation	LGIEAARTTIINEIQ CCCHHHHHHHHHHHH	20.02	25072903
1266	Phosphorylation	GIEAARTTIINEIQY CCHHHHHHHHHHHHH	17.82	25072903
1273	Phosphorylation	TIINEIQYTMVNHGM HHHHHHHHHHHHCCC	11.49	25072903
1274	Phosphorylation	IINEIQYTMVNHGMS HHHHHHHHHHHCCCC	9.77	25072903
1281	Phosphorylation	TMVNHGMSIDRRHVM HHHHCCCCCCHHHHH	26.40	25072903
1304	Phosphorylation	KGEVLGITRFGLAKM CCCHHCCCHHCHHHH	20.39	20068231
1365	Acetylation	GLFKLLHKADRDPNP HHHHHHHHCCCCCCC	52.53	7364655
1365	Ubiquitination	GLFKLLHKADRDPNP HHHHHHHHCCCCCCC	52.53	29967540
1374	Ubiquitination	DRDPNPPKRPLIFDT CCCCCCCCCCCEEEC	68.83	29967540

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RPC1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RPC1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RPC1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RPC5_HUMAN	POLR3E	physical	12391170
RPC8_HUMAN	POLR3H	physical	22939629
RPC4_HUMAN	POLR3D	physical	22939629
RPC2_HUMAN	POLR3B	physical	22939629
RPC9_HUMAN	CRCP	physical	22939629
RPC3_HUMAN	POLR3C	physical	22939629
SMCA5_HUMAN	SMARCA5	physical	22939629
VPS18_HUMAN	VPS18	physical	22939629
RPC9_HUMAN	CRCP	physical	26344197
TF3C3_HUMAN	GTF3C3	physical	26344197
HDAC1_HUMAN	HDAC1	physical	26344197
HDAC2_HUMAN	HDAC2	physical	26344197
IPO9_HUMAN	IPO9	physical	26344197
RM17_HUMAN	MRPL17	physical	26344197
RM22_HUMAN	MRPL22	physical	26344197
RM24_HUMAN	MRPL24	physical	26344197
RM54_HUMAN	MRPL54	physical	26344197
RT07_HUMAN	MRPS7	physical	26344197
RPA2_HUMAN	POLR1B	physical	26344197
RPAC1_HUMAN	POLR1C	physical	26344197
RPB1_HUMAN	POLR2A	physical	26344197
RPAB1_HUMAN	POLR2E	physical	26344197
RPAB3_HUMAN	POLR2H	physical	26344197
RPC2_HUMAN	POLR3B	physical	26344197
RPC3_HUMAN	POLR3C	physical	26344197
RPC4_HUMAN	POLR3D	physical	26344197
RPC5_HUMAN	POLR3E	physical	26344197
RPC6_HUMAN	POLR3F	physical	26344197
RPC7_HUMAN	POLR3G	physical	26344197
RPC8_HUMAN	POLR3H	physical	26344197
RPC10_HUMAN	POLR3K	physical	26344197
RS5_HUMAN	RPS5	physical	26344197
SMCA4_HUMAN	SMARCA4	physical	26344197
TSR1_HUMAN	TSR1	physical	26344197
EFTU_HUMAN	TUFM	physical	26344197

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 607694: Leukodystrophy, hypomyelinating, 7, with or without oligodontia and/or hypogonadotropic hypogonadism (HLD7)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Acetylation

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-445, AND MASS SPECTROMETRY.
PubMed: 19608861