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Protein

DNA-directed RNA polymerase III subunit RPC1

Gene

POLR3A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity2 Publications

Catalytic activityi

Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi69 – 691Zinc 1By similarity
Metal bindingi72 – 721Zinc 1By similarity
Metal bindingi79 – 791Zinc 1By similarity
Metal bindingi82 – 821Zinc 1By similarity
Metal bindingi109 – 1091Zinc 2By similarity
Metal bindingi112 – 1121Zinc 2By similarity
Metal bindingi156 – 1561Zinc 2By similarity
Metal bindingi499 – 4991Magnesium; catalyticBy similarity
Metal bindingi501 – 5011Magnesium; catalyticBy similarity
Metal bindingi503 – 5031Magnesium; catalyticBy similarity

GO - Molecular functioni

GO - Biological processi

  • defense response to virus Source: UniProtKB-KW
  • gene expression Source: Reactome
  • innate immune response Source: UniProtKB
  • positive regulation of interferon-beta production Source: UniProtKB
  • positive regulation of protein targeting to mitochondrion Source: ParkinsonsUK-UCL
  • positive regulation of type I interferon production Source: Reactome
  • regulation of mitochondrion degradation Source: ParkinsonsUK-UCL
  • termination of RNA polymerase III transcription Source: Reactome
  • transcription, DNA-templated Source: UniProtKB
  • transcription elongation from RNA polymerase III promoter Source: Reactome
  • transcription from RNA polymerase III promoter Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity, Transcription

Keywords - Ligandi

Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_1036. RNA Polymerase III Transcription Initiation From Type 2 Promoter.
REACT_118823. Cytosolic sensors of pathogen-associated DNA.
REACT_22339. RNA Polymerase III Abortive And Retractive Initiation.
REACT_347. RNA Polymerase III Transcription Initiation From Type 1 Promoter.
REACT_571. RNA Polymerase III Transcription Initiation From Type 3 Promoter.
REACT_63. RNA Polymerase III Transcription Termination.
REACT_756. RNA Polymerase III Chain Elongation.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed RNA polymerase III subunit RPC1 (EC:2.7.7.6)
Short name:
RNA polymerase III subunit C1
Alternative name(s):
DNA-directed RNA polymerase III largest subunit
DNA-directed RNA polymerase III subunit A
RNA polymerase III 155 kDa subunit
Short name:
RPC155
RNA polymerase III subunit C160
Gene namesi
Name:POLR3A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:30074. POLR3A.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • DNA-directed RNA polymerase III complex Source: MGI
  • membrane Source: UniProtKB
  • nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

Pathology & Biotechi

Involvement in diseasei

Leukodystrophy, hypomyelinating, 7, with or without oligodontia and/or hypogonadotropic hypogonadism (HLD7)4 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn 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.

See also OMIM:607694
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti91 – 911P → L in HLD7. 1 Publication
VAR_072338
Natural varianti310 – 3101W → C in HLD7. 1 Publication
VAR_072339
Natural varianti372 – 3721D → N in HLD7. 1 Publication
VAR_066516
Natural varianti387 – 3871A → G in HLD7. 1 Publication
VAR_072340
Natural varianti558 – 5581F → L in HLD7. 1 Publication
VAR_066517
Natural varianti602 – 6021S → R in HLD7. 1 Publication
VAR_072341
Natural varianti636 – 6361S → Y in HLD7. 1 Publication
VAR_066518
Natural varianti672 – 6721G → E in HLD7. 1 Publication
VAR_066519
Natural varianti724 – 7241C → Y in HLD7. 1 Publication
VAR_066520
Natural varianti775 – 7751N → I in HLD7. 1 Publication
VAR_066521
Natural varianti804 – 8041I → T in HLD7. 1 Publication
VAR_072342
Natural varianti852 – 8521M → V in HLD7. 2 Publications
VAR_066522
Natural varianti897 – 8971I → N in HLD7. 1 Publication
VAR_067004
Natural varianti1005 – 10051R → C in HLD7. 2 Publications
VAR_066523
Natural varianti1247 – 12471T → TT in HLD7. 1 Publication
VAR_066524
Natural varianti1261 – 12611E → K in HLD7. 1 Publication
VAR_072343

Keywords - Diseasei

Disease mutation, Leukodystrophy

Organism-specific databases

MIMi607694. phenotype.
Orphaneti88637. Hypomyelination - hypogonadotropic hypogonadism - hypodontia.
77295. Odontoleukodystrophy.
PharmGKBiPA134900426.

Polymorphism and mutation databases

BioMutaiPOLR3A.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13901390DNA-directed RNA polymerase III subunit RPC1PRO_0000073947Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei445 – 4451N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO14802.
PaxDbiO14802.
PRIDEiO14802.

PTM databases

PhosphoSiteiO14802.

Expressioni

Tissue specificityi

Expressed in the brain, in the cortex and the white matter (at protein level).1 Publication

Gene expression databases

BgeeiO14802.
CleanExiHS_POLR3A.
ExpressionAtlasiO14802. baseline and differential.
GenevisibleiO14802. HS.

Organism-specific databases

HPAiHPA037926.
HPA037927.

Interactioni

Subunit structurei

Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits.By similarity

Protein-protein interaction databases

BioGridi116301. 36 interactions.
IntActiO14802. 10 interactions.
STRINGi9606.ENSP00000361446.

Structurei

3D structure databases

ProteinModelPortaliO14802.
SMRiO14802. Positions 13-1363.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni844 – 85613Bridging helixBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the RNA polymerase beta' chain family.Curated

Phylogenomic databases

eggNOGiCOG0086.
GeneTreeiENSGT00730000110946.
HOGENOMiHOG000222974.
HOVERGENiHBG004339.
InParanoidiO14802.
KOiK03018.
OMAiHKADRDP.
OrthoDBiEOG761BSV.
PhylomeDBiO14802.
TreeFamiTF103054.

Family and domain databases

InterProiIPR000722. RNA_pol_asu.
IPR006592. RNA_pol_N.
IPR007080. RNA_pol_Rpb1_1.
IPR007066. RNA_pol_Rpb1_3.
IPR007083. RNA_pol_Rpb1_4.
IPR007081. RNA_pol_Rpb1_5.
IPR015700. RPC1.
[Graphical view]
PANTHERiPTHR19376:SF31. PTHR19376:SF31. 1 hit.
PfamiPF04997. RNA_pol_Rpb1_1. 1 hit.
PF00623. RNA_pol_Rpb1_2. 1 hit.
PF04983. RNA_pol_Rpb1_3. 1 hit.
PF05000. RNA_pol_Rpb1_4. 1 hit.
PF04998. RNA_pol_Rpb1_5. 1 hit.
[Graphical view]
SMARTiSM00663. RPOLA_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O14802-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKEQFRETD VAKKISHICF GMKSPEEMRQ QAHIQVVSKN LYSQDNQHAP
60 70 80 90 100
LLYGVLDHRM GTSEKDRPCE TCGKNLADCL GHYGYIDLEL PCFHVGYFRA
110 120 130 140 150
VIGILQMICK TCCHIMLSQE EKKQFLDYLK RPGLTYLQKR GLKKKISDKC
160 170 180 190 200
RKKNICHHCG AFNGTVKKCG LLKIIHEKYK TNKKVVDPIV SNFLQSFETA
210 220 230 240 250
IEHNKEVEPL LGRAQENLNP LVVLNLFKRI PAEDVPLLLM NPEAGKPSDL
260 270 280 290 300
ILTRLLVPPL CIRPSVVSDL KSGTNEDDLT MKLTEIIFLN DVIKKHRISG
310 320 330 340 350
AKTQMIMEDW DFLQLQCALY INSELSGIPL NMAPKKWTRG FVQRLKGKQG
360 370 380 390 400
RFRGNLSGKR VDFSGRTVIS PDPNLRIDEV AVPVHVAKIL TFPEKVNKAN
410 420 430 440 450
INFLRKLVQN GPEVHPGANF IQQRHTQMKR FLKYGNREKM AQELKYGDIV
460 470 480 490 500
ERHLIDGDVV LFNRQPSLHK LSIMAHLARV KPHRTFRFNE CVCTPYNADF
510 520 530 540 550
DGDEMNLHLP QTEEAKAEAL VLMGTKANLV TPRNGEPLIA AIQDFLTGAY
560 570 580 590 600
LLTLKDTFFD RAKACQIIAS ILVGKDEKIK VRLPPPTILK PVTLWTGKQI
610 620 630 640 650
FSVILRPSDD NPVRANLRTK GKQYCGKGED LCANDSYVTI QNSELMSGSM
660 670 680 690 700
DKGTLGSGSK NNIFYILLRD WGQNEAADAM SRLARLAPVY LSNRGFSIGI
710 720 730 740 750
GDVTPGQGLL KAKYELLNAG YKKCDEYIEA LNTGKLQQQP GCTAEETLEA
760 770 780 790 800
LILKELSVIR DHAGSACLRE LDKSNSPLTM ALCGSKGSFI NISQMIACVG
810 820 830 840 850
QQAISGSRVP DGFENRSLPH FEKHSKLPAA KGFVANSFYS GLTPTEFFFH
860 870 880 890 900
TMAGREGLVD TAVKTAETGY MQRRLVKSLE DLCSQYDLTV RSSTGDIIQF
910 920 930 940 950
IYGGDGLDPA AMEGKDEPLE FKRVLDNIKA VFPCPSEPAL SKNELILTTE
960 970 980 990 1000
SIMKKSEFLC CQDSFLQEIK KFIKGVSEKI KKTRDKYGIN DNGTTEPRVL
1010 1020 1030 1040 1050
YQLDRITPTQ VEKFLETCRD KYMRAQMEPG SAVGALCAQS IGEPGTQMTL
1060 1070 1080 1090 1100
KTFHFAGVAS MNITLGVPRI KEIINASKAI STPIITAQLD KDDDADYARL
1110 1120 1130 1140 1150
VKGRIEKTLL GEISEYIEEV FLPDDCFILV KLSLERIRLL RLEVNAETVR
1160 1170 1180 1190 1200
YSICTSKLRV KPGDVAVHGE AVVCVTPREN SKSSMYYVLQ FLKEDLPKVV
1210 1220 1230 1240 1250
VQGIPEVSRA VIHIDEQSGK EKYKLLVEGD NLRAVMATHG VKGTRTTSNN
1260 1270 1280 1290 1300
TYEVEKTLGI EAARTTIINE IQYTMVNHGM SIDRRHVMLL SDLMTYKGEV
1310 1320 1330 1340 1350
LGITRFGLAK MKESVLMLAS FEKTADHLFD AAYFGQKDSV CGVSECIIMG
1360 1370 1380 1390
IPMNIGTGLF KLLHKADRDP NPPKRPLIFD TNEFHIPLVT
Length:1,390
Mass (Da):155,641
Last modified:September 23, 2008 - v2
Checksum:i56F30900848E3DB9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151I → T in AAB86536 (PubMed:9331371).Curated
Sequence conflicti262 – 2621I → F in AAB86536 (PubMed:9331371).Curated
Sequence conflicti283 – 2831L → P in AAM12029 (PubMed:12384934).Curated
Sequence conflicti1056 – 10561A → G in AAB86536 (PubMed:9331371).Curated
Sequence conflicti1275 – 12751M → MV in AAB86536 (PubMed:9331371).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti91 – 911P → L in HLD7. 1 Publication
VAR_072338
Natural varianti310 – 3101W → C in HLD7. 1 Publication
VAR_072339
Natural varianti372 – 3721D → N in HLD7. 1 Publication
VAR_066516
Natural varianti387 – 3871A → G in HLD7. 1 Publication
VAR_072340
Natural varianti558 – 5581F → L in HLD7. 1 Publication
VAR_066517
Natural varianti582 – 5821R → L.
Corresponds to variant rs34588967 [ dbSNP | Ensembl ].
VAR_051873
Natural varianti602 – 6021S → R in HLD7. 1 Publication
VAR_072341
Natural varianti636 – 6361S → Y in HLD7. 1 Publication
VAR_066518
Natural varianti672 – 6721G → E in HLD7. 1 Publication
VAR_066519
Natural varianti713 – 7131K → N.
Corresponds to variant rs35354908 [ dbSNP | Ensembl ].
VAR_051874
Natural varianti724 – 7241C → Y in HLD7. 1 Publication
VAR_066520
Natural varianti775 – 7751N → I in HLD7. 1 Publication
VAR_066521
Natural varianti804 – 8041I → T in HLD7. 1 Publication
VAR_072342
Natural varianti852 – 8521M → V in HLD7. 2 Publications
VAR_066522
Natural varianti897 – 8971I → N in HLD7. 1 Publication
VAR_067004
Natural varianti1005 – 10051R → C in HLD7. 2 Publications
VAR_066523
Natural varianti1247 – 12471T → TT in HLD7. 1 Publication
VAR_066524
Natural varianti1261 – 12611E → K in HLD7. 1 Publication
VAR_072343

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF021351 mRNA. Translation: AAB86536.1.
AL512628 Genomic DNA. Translation: CAI16466.1.
CH471083 Genomic DNA. Translation: EAW54617.1.
BC041089 mRNA. Translation: AAH41089.1.
AY091459 mRNA. Translation: AAM12029.1.
CCDSiCCDS7354.1.
RefSeqiNP_008986.2. NM_007055.3.
UniGeneiHs.436896.

Genome annotation databases

EnsembliENST00000372371; ENSP00000361446; ENSG00000148606.
GeneIDi11128.
KEGGihsa:11128.
UCSCiuc001jzn.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF021351 mRNA. Translation: AAB86536.1.
AL512628 Genomic DNA. Translation: CAI16466.1.
CH471083 Genomic DNA. Translation: EAW54617.1.
BC041089 mRNA. Translation: AAH41089.1.
AY091459 mRNA. Translation: AAM12029.1.
CCDSiCCDS7354.1.
RefSeqiNP_008986.2. NM_007055.3.
UniGeneiHs.436896.

3D structure databases

ProteinModelPortaliO14802.
SMRiO14802. Positions 13-1363.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116301. 36 interactions.
IntActiO14802. 10 interactions.
STRINGi9606.ENSP00000361446.

PTM databases

PhosphoSiteiO14802.

Polymorphism and mutation databases

BioMutaiPOLR3A.

Proteomic databases

MaxQBiO14802.
PaxDbiO14802.
PRIDEiO14802.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000372371; ENSP00000361446; ENSG00000148606.
GeneIDi11128.
KEGGihsa:11128.
UCSCiuc001jzn.3. human.

Organism-specific databases

CTDi11128.
GeneCardsiGC10M079729.
GeneReviewsiPOLR3A.
HGNCiHGNC:30074. POLR3A.
HPAiHPA037926.
HPA037927.
MIMi607694. phenotype.
614258. gene.
neXtProtiNX_O14802.
Orphaneti88637. Hypomyelination - hypogonadotropic hypogonadism - hypodontia.
77295. Odontoleukodystrophy.
PharmGKBiPA134900426.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0086.
GeneTreeiENSGT00730000110946.
HOGENOMiHOG000222974.
HOVERGENiHBG004339.
InParanoidiO14802.
KOiK03018.
OMAiHKADRDP.
OrthoDBiEOG761BSV.
PhylomeDBiO14802.
TreeFamiTF103054.

Enzyme and pathway databases

ReactomeiREACT_1036. RNA Polymerase III Transcription Initiation From Type 2 Promoter.
REACT_118823. Cytosolic sensors of pathogen-associated DNA.
REACT_22339. RNA Polymerase III Abortive And Retractive Initiation.
REACT_347. RNA Polymerase III Transcription Initiation From Type 1 Promoter.
REACT_571. RNA Polymerase III Transcription Initiation From Type 3 Promoter.
REACT_63. RNA Polymerase III Transcription Termination.
REACT_756. RNA Polymerase III Chain Elongation.

Miscellaneous databases

ChiTaRSiPOLR3A. human.
GenomeRNAii11128.
NextBioi42292.
PROiO14802.
SOURCEiSearch...

Gene expression databases

BgeeiO14802.
CleanExiHS_POLR3A.
ExpressionAtlasiO14802. baseline and differential.
GenevisibleiO14802. HS.

Family and domain databases

InterProiIPR000722. RNA_pol_asu.
IPR006592. RNA_pol_N.
IPR007080. RNA_pol_Rpb1_1.
IPR007066. RNA_pol_Rpb1_3.
IPR007083. RNA_pol_Rpb1_4.
IPR007081. RNA_pol_Rpb1_5.
IPR015700. RPC1.
[Graphical view]
PANTHERiPTHR19376:SF31. PTHR19376:SF31. 1 hit.
PfamiPF04997. RNA_pol_Rpb1_1. 1 hit.
PF00623. RNA_pol_Rpb1_2. 1 hit.
PF04983. RNA_pol_Rpb1_3. 1 hit.
PF05000. RNA_pol_Rpb1_4. 1 hit.
PF04998. RNA_pol_Rpb1_5. 1 hit.
[Graphical view]
SMARTiSM00663. RPOLA_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The largest subunit of human RNA polymerase III is closely related to the largest subunit of yeast and trypanosome RNA polymerase III."
    Sepehri S., Hernandez N.
    Genome Res. 7:1006-1019(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Uterus.
  5. "Identification of an immunodominant epitope on RNA polymerase III recognized by systemic sclerosis sera: application to enzyme-linked immunosorbent assay."
    Kuwana M., Kimura K., Kawakami Y.
    Arthritis Rheum. 46:2742-2747(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-374.
  6. "Characterization of human RNA polymerase III identifies orthologues for Saccharomyces cerevisiae RNA polymerase III subunits."
    Hu P., Wu S., Sun Y., Yuan C.-C., Kobayashi R., Myers M.P., Hernandez N.
    Mol. Cell. Biol. 22:8044-8055(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE RNA POL III COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway."
    Chiu Y.-H., Macmillan J.B., Chen Z.J.
    Cell 138:576-591(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate."
    Ablasser A., Bauernfeind F., Hartmann G., Latz E., Fitzgerald K.A., Hornung V.
    Nat. Immunol. 10:1065-1072(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: VARIANTS HLD7 ASN-372; LEU-558; TYR-636; GLU-672; TYR-724; ILE-775; VAL-852 AND THR-1247 INS, INVOLVEMENT IN HLD7, TISSUE SPECIFICITY.
  12. "Mutations in POLR3A and POLR3B encoding RNA Polymerase III subunits cause an autosomal-recessive hypomyelinating leukoencephalopathy."
    Saitsu H., Osaka H., Sasaki M., Takanashi J., Hamada K., Yamashita A., Shibayama H., Shiina M., Kondo Y., Nishiyama K., Tsurusaki Y., Miyake N., Doi H., Ogata K., Inoue K., Matsumoto N.
    Am. J. Hum. Genet. 89:644-651(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HLD7 ASN-897 AND CYS-1005.
  13. "Mutations in POLR3A and POLR3B are a major cause of hypomyelinating leukodystrophies with or without dental abnormalities and/or hypogonadotropic hypogonadism."
    Daoud H., Tetreault M., Gibson W., Guerrero K., Cohen A., Gburek-Augustat J., Synofzik M., Brais B., Stevens C.A., Sanchez-Carpintero R., Goizet C., Naidu S., Vanderver A., Bernard G.
    J. Med. Genet. 50:194-197(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HLD7 LEU-91; GLY-387; ARG-602; VAL-852; CYS-1005 AND LYS-1261.
  14. "Novel compound heterozygous mutations of POLR3A revealed by whole-exome sequencing in a patient with hypomyelination."
    Shimojima K., Shimada S., Tamasaki A., Akaboshi S., Komoike Y., Saito A., Furukawa T., Yamamoto T.
    Brain Dev. 36:315-321(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HLD7 CYS-310 AND THR-804.

Entry informationi

Entry nameiRPC1_HUMAN
AccessioniPrimary (citable) accession number: O14802
Secondary accession number(s): Q8IW34, Q8TCW5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: September 23, 2008
Last modified: June 24, 2015
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.