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Protein Page:
POLR3A (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
POLR3A 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. 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. Defects in POLR3A are the cause of leukodystrophy hypomyelinating type 7 with or without oligodontia and/or hypogonadotropic hypogonadism (HLD7). An autosomal recessive neurodegenerative disorder characterized by childhood onset of progressive motor decline manifest as spasticity, ataxia, tremor, and cerebellar signs, as well as mild cognitive regression. Other features may include hypodontia or oligodontia and hypogonadotropic hypogonadism. There is considerable inter- and intrafamilial variability. Belongs to the RNA polymerase beta' chain family. Note: This description may include information from UniProtKB.
Protein type: Nucleotide Metabolism - purine; EC 2.7.7.6; Nucleotide Metabolism - pyrimidine; Transcription initiation complex; Transferase
Cellular Component: nucleoplasm; DNA-directed RNA polymerase III complex; membrane; cytosol
Molecular Function: DNA binding; zinc ion binding; DNA-directed RNA polymerase activity; ribonucleoside binding; chromatin binding
Biological Process: transcription from RNA polymerase III promoter; termination of RNA polymerase III transcription; transcription, DNA-dependent; positive regulation of interferon-beta production; positive regulation of interferon type I production; innate immune response; gene expression; defense response to virus; RNA elongation from RNA polymerase III promoter
Reference #:  O14802 (UniProtKB)
Alt. Names/Synonyms: DNA-directed RNA polymerase III largest subunit; DNA-directed RNA polymerase III subunit A; DNA-directed RNA polymerase III subunit RPC1; hRPC155; POLR3A; polymerase (RNA) III (DNA directed) polypeptide A, 155kDa; RNA polymerase III 155 kDa subunit; RNA polymerase III subunit C1; RNA polymerase III subunit C160; RNA polymerase III subunit RPC155-D; RPC1; RPC155
Gene Symbols: POLR3A
Molecular weight: 155,642 Da
Basal Isoelectric point: 8.76  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

POLR3A

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 K23-ac SHICFGMksPEEMRQ
0 1 S24-p HICFGMksPEEMRQQ
0 20 Y53-p NQHAPLLyGVLDHRM
0 2 K184-ub EKYKTNKkVVDPIVS
0 1 K228-ub LVVLNLFkRIPAEDV
0 3 K346-ac RGFVQRLkGkQGRFR
0 2 K348-ac FVQRLkGkQGRFRGN
0 1 K359-ac FRGNLSGkRVDFSGR
0 1 K388-ub AVPVHVAkILTFPEK
0 1 K406-ub ANINFLRkLVQNGPE
0 1 Y434-p QMKRFLKyGNREKMA
0 3 K445-ac EKMAQELkYGDIVER
0 1 K445-ub EKMAQELkYGDIVER
0 1 T525-p EALVLMGtkANLVTP
0 1 K526-ub ALVLMGtkANLVTPR
0 1 T593-p PTILKPVtLWtGKQI
0 1 T596-p LKPVtLWtGKQIFSV
0 1 S681-p NEAADAMsRLARLAP
0 2 K711-ub TPGQGLLkAkyELLN
0 1 K713-ub GQGLLkAkyELLNAG
0 1 Y714-p QGLLkAkyELLNAGY
0 1 S774 CLRELDKSNSPLTMA
0 1 K864-ub GLVDTAVkTAETGYM
0 1 T948-p SKNELILttESIMKK
0 1 T949-p KNELILttESIMKKS
0 1 S977-p KKFIKGVsEKIKKTR
0 1 K986-ub KIKKTRDkYGINDNG
0 1 K1013-ub ITPTQVEkFLETCRD
0 1 T1046-p QSIGEPGtQMtLKTF
0 1 T1049-p GEPGtQMtLKTFHFA
0 1 S1181-p CVTPRENsKSSMYYV
0 1 T1247-p GVKGTRTtSNNtYEV
0 1 T1251-p TRTtSNNtYEVEkTL
0 1 K1256-ub NNtYEVEkTLGIEAA
0 2 T1304-p KGEVLGItRFGLAKM
0 1 K1365-ac GLFKLLHkADRDPNP
  mouse

 
K23 SHICFGMKSPEEMRQ
S24 HICFGMKSPEEMRQQ
Y53 NNHAPLLYGVLDHRM
K184-ub EKYKTNKkVVDPIVS
K228 LVVLNLFKRIPAEDV
K346-ac RGFVQRLkGkQGRFR
K348-ac FVQRLkGkQGRFRGN
K359 FRGNLSGKRVDFSGR
K388 AVPVHVAKILTFPEK
K406 ANINFLRKLVRNGPD
Y434 QMKRFLKYGNREKMA
K445 EKMAQELKFGDIVER
K445 EKMAQELKFGDIVER
T525 EALVLMGTKANLVTP
K526 ALVLMGTKANLVTPR
T593 PTILKPVTLWTGKQI
T596 LKPVTLWTGKQIFSV
S681 NEAADAMSRLARLAP
K711-ub TPGQGLLkAKYELLN
K713 GQGLLkAKYELLNAG
Y714 QGLLkAKYELLNAGY
S774-p CLRELDKsNSPLTMA
K864 GLVDTAVKTAETGYM
T948 SKNDLTLTAEAIMKK
A949 KNDLTLTAEAIMKKN
S977 KTFIKGVSEKIKKTR
K986 KIKKTRDKYGINDNG
K1013 ITPTQIEKFLETCRD
T1046 QSIGEPGTQMTLKTF
T1049 GEPGTQMTLKTFHFA
S1181 CVTPRENSKSSMYYV
T1247 GVKGTRTTSNNTYEV
T1251 TRTTSNNTYEVEKTL
K1256 NNTYEVEKTLGIEAA
T1304 KGEVLGITRFGLAKM
K1365 GLFKLLHKANRDPKP
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