UniProt Accession

 RPC1_HUMAN; O14802; Q8IW34; Q8TCW5 

Genbank Protein ID

 AF021351; AL512628; CH471083; BC041089; AY091459 

Genbank Nucleotide ID

 AAB86536.1; CAI16466.1; EAW54617.1; AAH41089.1; AAM12029.1 

Protein Name

 DNA-directed RNA polymerase III subunit RPC1 

Protein Synonyms/Alias

 RNA polymerase III subunit C1; DNA-directed RNA polymerase III largest subunit; DNA-directed RNA polymerase III subunit A; RNA polymerase III 155 kDa subunit; RPC155; RNA polymerase III subunit C160 

Gene Name

 POLR3A 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
65	HRMGTSEKDRPCETC	acetylation	[1]
65	HRMGTSEKDRPCETC	ubiquitination	[2]
228	LVVLNLFKRIPAEDV	ubiquitination	[2, 3, 4]
246	LMNPEAGKPSDLILT	ubiquitination	[2]
271	PSVVSDLKSGTNEDD	ubiquitination	[2]
388	AVPVHVAKILTFPEK	ubiquitination	[1, 2, 5]
395	KILTFPEKVNKANIN	ubiquitination	[2]
398	TFPEKVNKANINFLR	ubiquitination	[2]
406	ANINFLRKLVQNGPE	ubiquitination	[2, 3]
433	TQMKRFLKYGNREKM	ubiquitination	[1, 2]
445	EKMAQELKYGDIVER	acetylation	[1, 6, 7]
445	EKMAQELKYGDIVER	ubiquitination	[2, 5]
526	ALVLMGTKANLVTPR	ubiquitination	[2, 4, 5]
580	VGKDEKIKVRLPPPT	ubiquitination	[2]
590	LPPPTILKPVTLWTG	ubiquitination	[2]
652	LMSGSMDKGTLGSGS	ubiquitination	[2]
660	GTLGSGSKNNIFYIL	ubiquitination	[2]
711	TPGQGLLKAKYELLN	ubiquitination	[2, 3, 4, 5]
713	GQGLLKAKYELLNAG	ubiquitination	[1, 2, 4, 5]
722	ELLNAGYKKCDEYIE	ubiquitination	[2, 5]
723	LLNAGYKKCDEYIEA	ubiquitination	[2]
773	ACLRELDKSNSPLTM	ubiquitination	[2]
823	RSLPHFEKHSKLPAA	ubiquitination	[2]
864	GLVDTAVKTAETGYM	ubiquitination	[2, 4, 5]
877	YMQRRLVKSLEDLCS	ubiquitination	[2]
986	KIKKTRDKYGINDNG	ubiquitination	[2, 5]
1013	ITPTQVEKFLETCRD	ubiquitination	[1, 2, 3]
1071	TLGVPRIKEIINASK	ubiquitination	[2]
1078	KEIINASKAISTPII	ubiquitination	[5]
1091	IITAQLDKDDDADYA	ubiquitination	[2]
1157	RYSICTSKLRVKPGD	ubiquitination	[2]
1182	VTPRENSKSSMYYVL	ubiquitination	[2, 4, 5]
1222	DEQSGKEKYKLLVEG	ubiquitination	[2]
1224	QSGKEKYKLLVEGDN	ubiquitination	[2]
1242	VMATHGVKGTRTTSN	ubiquitination	[1, 2]
1256	NNTYEVEKTLGIEAA	ubiquitination	[2, 5]

Reference

 [1] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [6] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [7] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 

Functional 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. 

Sequence Annotation

 REGION 844 856 Bridging helix (By similarity).
 METAL 69 69 Zinc 1 (By similarity).
 METAL 72 72 Zinc 1 (By similarity).
 METAL 79 79 Zinc 1 (By similarity).
 METAL 82 82 Zinc 1 (By similarity).
 METAL 109 109 Zinc 2 (By similarity).
 METAL 112 112 Zinc 2 (By similarity).
 METAL 156 156 Zinc 2 (By similarity).
 METAL 499 499 Magnesium; catalytic (By similarity).
 METAL 501 501 Magnesium; catalytic (By similarity).
 METAL 503 503 Magnesium; catalytic (By similarity).
 MOD_RES 445 445 N6-acetyllysine.  

Keyword

 Acetylation; Antiviral defense; Complete proteome; DNA-directed RNA polymerase; Immunity; Innate immunity; Leukodystrophy; Magnesium; Metal-binding; Nucleotidyltransferase; Nucleus; Polymorphism; Reference proteome; Transcription; Transferase; Zinc. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 1390 AA 

Protein Sequence

Gene Ontology

 GO:0005666; C:DNA-directed RNA polymerase III complex; NAS:UniProtKB.
 GO:0003682; F:chromatin binding; IEA:Compara.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0003899; F:DNA-directed RNA polymerase activity; NAS:UniProtKB.
 GO:0032549; F:ribonucleoside binding; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
 GO:0045087; P:innate immune response; IMP:UniProtKB.
 GO:0032728; P:positive regulation of interferon-beta production; IMP:UniProtKB.
 GO:0006386; P:termination of RNA polymerase III transcription; TAS:Reactome.
 GO:0006385; P:transcription elongation from RNA polymerase III promoter; TAS:Reactome. 

Interpro

 IPR009010; Asp_de-COase-like_dom.
 IPR000722; RNA_pol_asu.
 IPR015700; RNA_pol_III_lsu.
 IPR006592; RNA_pol_N.
 IPR007080; RNA_pol_Rpb1_1.
 IPR007066; RNA_pol_Rpb1_3.
 IPR007083; RNA_pol_Rpb1_4.
 IPR007081; RNA_pol_Rpb1_5. 

Pfam

 PF04997; RNA_pol_Rpb1_1
 PF00623; RNA_pol_Rpb1_2
 PF04983; RNA_pol_Rpb1_3
 PF05000; RNA_pol_Rpb1_4
 PF04998; RNA_pol_Rpb1_5 

SMART

 SM00663; RPOLA_N 

PROSITE

  

PRINTS