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Protein

DNA-directed RNA polymerases I, II, and III subunit RPABC3

Gene

POLR2H

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. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-113418. Formation of the Early Elongation Complex.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167158. Formation of the HIV-1 Early Elongation Complex.
R-HSA-167160. RNA Pol II CTD phosphorylation and interaction with CE.
R-HSA-167161. HIV Transcription Initiation.
R-HSA-167162. RNA Polymerase II HIV Promoter Escape.
R-HSA-167172. Transcription of the HIV genome.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167238. Pausing and recovery of Tat-mediated HIV elongation.
R-HSA-167242. Abortive elongation of HIV-1 transcript in the absence of Tat.
R-HSA-167243. Tat-mediated HIV elongation arrest and recovery.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-167287. HIV elongation arrest and recovery.
R-HSA-167290. Pausing and recovery of HIV elongation.
R-HSA-168325. Viral Messenger RNA Synthesis.
R-HSA-1834949. Cytosolic sensors of pathogen-associated DNA.
R-HSA-203927. MicroRNA (miRNA) biogenesis.
R-HSA-427413. NoRC negatively regulates rRNA expression.
R-HSA-452723. Transcriptional regulation of pluripotent stem cells.
R-HSA-5250924. B-WICH complex positively regulates rRNA expression.
R-HSA-5578749. Transcriptional regulation by small RNAs.
R-HSA-5601884. PIWI-interacting RNA (piRNA) biogenesis.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6781823. Formation of TC-NER Pre-Incision Complex.
R-HSA-6781827. Transcription-Coupled Nucleotide Excision Repair (TC-NER).
R-HSA-6782135. Dual incision in TC-NER.
R-HSA-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-6803529. FGFR2 alternative splicing.
R-HSA-6807505. RNA polymerase II transcribes snRNA genes.
R-HSA-72086. mRNA Capping.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72165. mRNA Splicing - Minor Pathway.
R-HSA-72203. Processing of Capped Intron-Containing Pre-mRNA.
R-HSA-73762. RNA Polymerase I Transcription Initiation.
R-HSA-73772. RNA Polymerase I Promoter Escape.
R-HSA-73776. RNA Polymerase II Promoter Escape.
R-HSA-73777. RNA Polymerase I Chain Elongation.
R-HSA-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-HSA-73780. RNA Polymerase III Chain Elongation.
R-HSA-73863. RNA Polymerase I Transcription Termination.
R-HSA-73980. RNA Polymerase III Transcription Termination.
R-HSA-749476. RNA Polymerase III Abortive And Retractive Initiation.
R-HSA-75953. RNA Polymerase II Transcription Initiation.
R-HSA-75955. RNA Polymerase II Transcription Elongation.
R-HSA-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.
R-HSA-76061. RNA Polymerase III Transcription Initiation From Type 1 Promoter.
R-HSA-76066. RNA Polymerase III Transcription Initiation From Type 2 Promoter.
R-HSA-76071. RNA Polymerase III Transcription Initiation From Type 3 Promoter.
R-HSA-77075. RNA Pol II CTD phosphorylation and interaction with CE.
R-HSA-8851708. Signaling by FGFR2 IIIa TM.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed RNA polymerases I, II, and III subunit RPABC3
Short name:
RNA polymerases I, II, and III subunit ABC3
Alternative name(s):
DNA-directed RNA polymerase II subunit H
DNA-directed RNA polymerases I, II, and III 17.1 kDa polypeptide
RPB17
RPB8 homolog
Short name:
hRPB8
Gene namesi
Name:POLR2H
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:9195. POLR2H.

Subcellular locationi

  • Nucleusnucleolus 2 Publications

GO - Cellular componenti

  • cytosol Source: Reactome
  • DNA-directed RNA polymerase I complex Source: GO_Central
  • DNA-directed RNA polymerase II, core complex Source: UniProtKB
  • DNA-directed RNA polymerase III complex Source: GO_Central
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33515.

Polymorphism and mutation databases

DMDMi20178325.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 150149DNA-directed RNA polymerases I, II, and III subunit RPABC3PRO_0000073997Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP52434.
MaxQBiP52434.
PaxDbiP52434.
PeptideAtlasiP52434.
PRIDEiP52434.
TopDownProteomicsiP52434-1. [P52434-1]

PTM databases

iPTMnetiP52434.
PhosphoSiteiP52434.

Expressioni

Gene expression databases

BgeeiP52434.
CleanExiHS_POLR2H.
ExpressionAtlasiP52434. baseline and differential.
GenevisibleiP52434. HS.

Organism-specific databases

HPAiHPA037745.
HPA055813.

Interactioni

Subunit structurei

Component of the RNA polymerase I (Pol I), RNA polymerase II (Pol II) and RNA polymerase III (Pol III) complexes consisting of at least 13, 12 and 17 subunits, respectively. Directly interacts with POLR2A.3 Publications

Protein-protein interaction databases

BioGridi111433. 61 interactions.
DIPiDIP-27556N.
IntActiP52434. 9 interactions.
MINTiMINT-1162805.
STRINGi9606.ENSP00000296223.

Structurei

Secondary structure

1
150
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 1610Combined sources
Beta strandi25 – 3511Combined sources
Beta strandi38 – 447Combined sources
Beta strandi48 – 503Combined sources
Beta strandi56 – 594Combined sources
Beta strandi66 – 705Combined sources
Turni71 – 733Combined sources
Beta strandi75 – 773Combined sources
Turni85 – 884Combined sources
Beta strandi89 – 924Combined sources
Beta strandi94 – 974Combined sources
Beta strandi104 – 1074Combined sources
Beta strandi110 – 1189Combined sources
Beta strandi121 – 1277Combined sources
Helixi129 – 1324Combined sources
Beta strandi142 – 1476Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F3INMR-A1-150[»]
5IY6electron microscopy7.20H1-150[»]
5IY7electron microscopy8.60H1-150[»]
5IY8electron microscopy7.90H1-150[»]
5IY9electron microscopy6.30H1-150[»]
5IYAelectron microscopy5.40H1-150[»]
5IYBelectron microscopy3.90H1-150[»]
5IYCelectron microscopy3.90H1-150[»]
5IYDelectron microscopy3.90H1-150[»]
DisProtiDP00504.
ProteinModelPortaliP52434.
SMRiP52434. Positions 1-150.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52434.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni16 – 4025Non-specific ssDNA bindingAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3400. Eukaryota.
ENOG4111FT0. LUCA.
GeneTreeiENSGT00390000018195.
HOGENOMiHOG000175572.
HOVERGENiHBG036116.
InParanoidiP52434.
KOiK03016.
OMAiEIAHARP.
OrthoDBiEOG7SN8DR.
PhylomeDBiP52434.
TreeFamiTF103043.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR005570. RNA_pol_Rpb8.
[Graphical view]
PANTHERiPTHR10917. PTHR10917. 1 hit.
PfamiPF03870. RNA_pol_Rpb8. 1 hit.
[Graphical view]
PIRSFiPIRSF000779. RNA_pol_Rpb8. 1 hit.
SMARTiSM00658. RPOL8c. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P52434-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAGILFEDIF DVKDIDPEGK KFDRVSRLHC ESESFKMDLI LDVNIQIYPV
60 70 80 90 100
DLGDKFRLVI ASTLYEDGTL DDGEYNPTDD RPSRADQFEY VMYGKVYRIE
110 120 130 140 150
GDETSTEAAT RLSAYVSYGG LLMRLQGDAN NLHGFEVDSR VYLLMKKLAF
Length:150
Mass (Da):17,143
Last modified:January 23, 2007 - v4
Checksum:i944D0860809F1425
GO
Isoform 2 (identifier: P52434-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     84-112: RADQFEYVMYGKVYRIEGDETSTEAATRL → S

Note: No experimental confirmation available. Gene prediction based on EST data.
Show »
Length:122
Mass (Da):13,849
Checksum:i67D60212F40AC1DC
GO
Isoform 3 (identifier: P52434-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: Missing.

Note: No experimental confirmation available. Gene prediction based on EST data.
Show »
Length:114
Mass (Da):12,959
Checksum:i6ED22DDC8CC5EB96
GO
Isoform 4 (identifier: P52434-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     113-150: SAYVSYGGLL...VYLLMKKLAF → LRLRAAEWQC...DEEASLLNLA

Note: No experimental confirmation available. Gene prediction based on EST data.
Show »
Length:175
Mass (Da):19,767
Checksum:i2544A688EC043228
GO
Isoform 5 (identifier: P52434-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: Missing.
     84-112: RADQFEYVMYGKVYRIEGDETSTEAATRL → S

Note: No experimental confirmation available. Gene prediction based on EST data.
Show »
Length:86
Mass (Da):9,664
Checksum:iB038E50425F19FCF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191G → A in AAA91458 (PubMed:8524256).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3636Missing in isoform 3 and isoform 5. CuratedVSP_055017Add
BLAST
Alternative sequencei84 – 11229RADQF…AATRL → S in isoform 2 and isoform 5. CuratedVSP_055018Add
BLAST
Alternative sequencei113 – 15038SAYVS…KKLAF → LRLRAAEWQCSRITGWGLLF QLCVRVLWGPAHEAAGGCQQ PAWIRGGLQSLSPDEEASLL NLA in isoform 4. CuratedVSP_055019Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37689 mRNA. Translation: AAA91458.1.
Z49199 mRNA. Translation: CAA89060.1.
AJ252079, AJ252080 Genomic DNA. Translation: CAB92189.1.
AC078797 Genomic DNA. No translation available.
BC000739 mRNA. Translation: AAH00739.1.
CCDSiCCDS3264.1. [P52434-1]
CCDS63859.1. [P52434-4]
CCDS63860.1. [P52434-2]
CCDS63861.1. [P52434-3]
CCDS63862.1. [P52434-5]
PIRiS55370.
RefSeqiNP_001265627.1. NM_001278698.1. [P52434-4]
NP_001265628.1. NM_001278699.1. [P52434-3]
NP_001265629.1. NM_001278700.1. [P52434-3]
NP_001265643.1. NM_001278714.1. [P52434-2]
NP_001265644.1. NM_001278715.1. [P52434-5]
NP_006223.2. NM_006232.3. [P52434-1]
XP_005247598.1. XM_005247541.2. [P52434-4]
XP_006713729.1. XM_006713666.2. [P52434-4]
XP_006713730.1. XM_006713667.2. [P52434-4]
XP_006713731.1. XM_006713668.2. [P52434-1]
XP_006713733.1. XM_006713670.2. [P52434-3]
UniGeneiHs.432574.

Genome annotation databases

EnsembliENST00000429568; ENSP00000415536; ENSG00000163882. [P52434-4]
ENST00000430783; ENSP00000411883; ENSG00000163882. [P52434-2]
ENST00000438240; ENSP00000398622; ENSG00000163882. [P52434-3]
ENST00000443489; ENSP00000393773; ENSG00000163882. [P52434-5]
ENST00000452961; ENSP00000399882; ENSG00000163882. [P52434-3]
ENST00000456318; ENSP00000392913; ENSG00000163882. [P52434-1]
GeneIDi5437.
KEGGihsa:5437.
UCSCiuc032smc.2. human. [P52434-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37689 mRNA. Translation: AAA91458.1.
Z49199 mRNA. Translation: CAA89060.1.
AJ252079, AJ252080 Genomic DNA. Translation: CAB92189.1.
AC078797 Genomic DNA. No translation available.
BC000739 mRNA. Translation: AAH00739.1.
CCDSiCCDS3264.1. [P52434-1]
CCDS63859.1. [P52434-4]
CCDS63860.1. [P52434-2]
CCDS63861.1. [P52434-3]
CCDS63862.1. [P52434-5]
PIRiS55370.
RefSeqiNP_001265627.1. NM_001278698.1. [P52434-4]
NP_001265628.1. NM_001278699.1. [P52434-3]
NP_001265629.1. NM_001278700.1. [P52434-3]
NP_001265643.1. NM_001278714.1. [P52434-2]
NP_001265644.1. NM_001278715.1. [P52434-5]
NP_006223.2. NM_006232.3. [P52434-1]
XP_005247598.1. XM_005247541.2. [P52434-4]
XP_006713729.1. XM_006713666.2. [P52434-4]
XP_006713730.1. XM_006713667.2. [P52434-4]
XP_006713731.1. XM_006713668.2. [P52434-1]
XP_006713733.1. XM_006713670.2. [P52434-3]
UniGeneiHs.432574.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F3INMR-A1-150[»]
5IY6electron microscopy7.20H1-150[»]
5IY7electron microscopy8.60H1-150[»]
5IY8electron microscopy7.90H1-150[»]
5IY9electron microscopy6.30H1-150[»]
5IYAelectron microscopy5.40H1-150[»]
5IYBelectron microscopy3.90H1-150[»]
5IYCelectron microscopy3.90H1-150[»]
5IYDelectron microscopy3.90H1-150[»]
DisProtiDP00504.
ProteinModelPortaliP52434.
SMRiP52434. Positions 1-150.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111433. 61 interactions.
DIPiDIP-27556N.
IntActiP52434. 9 interactions.
MINTiMINT-1162805.
STRINGi9606.ENSP00000296223.

PTM databases

iPTMnetiP52434.
PhosphoSiteiP52434.

Polymorphism and mutation databases

DMDMi20178325.

Proteomic databases

EPDiP52434.
MaxQBiP52434.
PaxDbiP52434.
PeptideAtlasiP52434.
PRIDEiP52434.
TopDownProteomicsiP52434-1. [P52434-1]

Protocols and materials databases

DNASUi5437.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000429568; ENSP00000415536; ENSG00000163882. [P52434-4]
ENST00000430783; ENSP00000411883; ENSG00000163882. [P52434-2]
ENST00000438240; ENSP00000398622; ENSG00000163882. [P52434-3]
ENST00000443489; ENSP00000393773; ENSG00000163882. [P52434-5]
ENST00000452961; ENSP00000399882; ENSG00000163882. [P52434-3]
ENST00000456318; ENSP00000392913; ENSG00000163882. [P52434-1]
GeneIDi5437.
KEGGihsa:5437.
UCSCiuc032smc.2. human. [P52434-1]

Organism-specific databases

CTDi5437.
GeneCardsiPOLR2H.
HGNCiHGNC:9195. POLR2H.
HPAiHPA037745.
HPA055813.
MIMi606023. gene.
neXtProtiNX_P52434.
PharmGKBiPA33515.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3400. Eukaryota.
ENOG4111FT0. LUCA.
GeneTreeiENSGT00390000018195.
HOGENOMiHOG000175572.
HOVERGENiHBG036116.
InParanoidiP52434.
KOiK03016.
OMAiEIAHARP.
OrthoDBiEOG7SN8DR.
PhylomeDBiP52434.
TreeFamiTF103043.

Enzyme and pathway databases

ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-113418. Formation of the Early Elongation Complex.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167158. Formation of the HIV-1 Early Elongation Complex.
R-HSA-167160. RNA Pol II CTD phosphorylation and interaction with CE.
R-HSA-167161. HIV Transcription Initiation.
R-HSA-167162. RNA Polymerase II HIV Promoter Escape.
R-HSA-167172. Transcription of the HIV genome.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167238. Pausing and recovery of Tat-mediated HIV elongation.
R-HSA-167242. Abortive elongation of HIV-1 transcript in the absence of Tat.
R-HSA-167243. Tat-mediated HIV elongation arrest and recovery.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-167287. HIV elongation arrest and recovery.
R-HSA-167290. Pausing and recovery of HIV elongation.
R-HSA-168325. Viral Messenger RNA Synthesis.
R-HSA-1834949. Cytosolic sensors of pathogen-associated DNA.
R-HSA-203927. MicroRNA (miRNA) biogenesis.
R-HSA-427413. NoRC negatively regulates rRNA expression.
R-HSA-452723. Transcriptional regulation of pluripotent stem cells.
R-HSA-5250924. B-WICH complex positively regulates rRNA expression.
R-HSA-5578749. Transcriptional regulation by small RNAs.
R-HSA-5601884. PIWI-interacting RNA (piRNA) biogenesis.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6781823. Formation of TC-NER Pre-Incision Complex.
R-HSA-6781827. Transcription-Coupled Nucleotide Excision Repair (TC-NER).
R-HSA-6782135. Dual incision in TC-NER.
R-HSA-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-6803529. FGFR2 alternative splicing.
R-HSA-6807505. RNA polymerase II transcribes snRNA genes.
R-HSA-72086. mRNA Capping.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72165. mRNA Splicing - Minor Pathway.
R-HSA-72203. Processing of Capped Intron-Containing Pre-mRNA.
R-HSA-73762. RNA Polymerase I Transcription Initiation.
R-HSA-73772. RNA Polymerase I Promoter Escape.
R-HSA-73776. RNA Polymerase II Promoter Escape.
R-HSA-73777. RNA Polymerase I Chain Elongation.
R-HSA-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-HSA-73780. RNA Polymerase III Chain Elongation.
R-HSA-73863. RNA Polymerase I Transcription Termination.
R-HSA-73980. RNA Polymerase III Transcription Termination.
R-HSA-749476. RNA Polymerase III Abortive And Retractive Initiation.
R-HSA-75953. RNA Polymerase II Transcription Initiation.
R-HSA-75955. RNA Polymerase II Transcription Elongation.
R-HSA-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.
R-HSA-76061. RNA Polymerase III Transcription Initiation From Type 1 Promoter.
R-HSA-76066. RNA Polymerase III Transcription Initiation From Type 2 Promoter.
R-HSA-76071. RNA Polymerase III Transcription Initiation From Type 3 Promoter.
R-HSA-77075. RNA Pol II CTD phosphorylation and interaction with CE.
R-HSA-8851708. Signaling by FGFR2 IIIa TM.

Miscellaneous databases

ChiTaRSiPOLR2H. human.
EvolutionaryTraceiP52434.
GeneWikiiPOLR2H.
GenomeRNAii5437.
PROiP52434.
SOURCEiSearch...

Gene expression databases

BgeeiP52434.
CleanExiHS_POLR2H.
ExpressionAtlasiP52434. baseline and differential.
GenevisibleiP52434. HS.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR005570. RNA_pol_Rpb8.
[Graphical view]
PANTHERiPTHR10917. PTHR10917. 1 hit.
PfamiPF03870. RNA_pol_Rpb8. 1 hit.
[Graphical view]
PIRSFiPIRSF000779. RNA_pol_Rpb8. 1 hit.
SMARTiSM00658. RPOL8c. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Six human RNA polymerase subunits functionally substitute for their yeast counterparts."
    McKune K., Moore P.A., Hull M.W., Woychik N.A.
    Mol. Cell. Biol. 15:6895-6900(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Four subunits that are shared by the three classes of RNA polymerase are functionally interchangeable between Homo sapiens and Saccharomyces cerevisiae."
    Shpakovski G.V., Acker J., Wintzerith M., Lacroix J.F., Thuriaux P., Vigneron M.
    Mol. Cell. Biol. 15:4702-4710(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Organization of genes encoding subunits of eucaryotic nuclear RNA polymerases shows non random intron distribution and correlates with the subunit modular structure."
    Shpakovski G.V., Lebedenko E.N., Grandemange S., Schaller S., Vigneron M., Kedinger C.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Placenta.
  4. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1).
    Tissue: Placenta.
  6. Bienvenut W.V.
    Submitted (AUG-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-13 AND 99-111, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma and Cervix carcinoma.
  7. "Immunoaffinity purification and functional characterization of human transcription factor IIH and RNA polymerase II from clonal cell lines that conditionally express epitope-tagged subunits of the multiprotein complexes."
    Kershnar E., Wu S.-Y., Chiang C.-M.
    J. Biol. Chem. 273:34444-34453(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE RNA POLYMERASE II CORE-COMPLEX, SUBCELLULAR LOCATION.
  8. "RNA polymerase I-specific subunit CAST/hPAF49 has a role in the activation of transcription by upstream binding factor."
    Panov K.I., Panova T.B., Gadal O., Nishiyama K., Saito T., Russell J., Zomerdijk J.C.B.M.
    Mol. Cell. Biol. 26:5436-5448(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE RNA POL I COMPLEX.
  9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Structural, biochemical, and dynamic characterizations of the hRPB8 subunit of human RNA polymerases."
    Kang X., Hu Y., Li Y., Guo X., Jiang X., Lai L., Xia B., Jin C.
    J. Biol. Chem. 281:18216-18226(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, DNA-BINDING REGION, SUBUNIT, INTERACTION WITH POLR2A.

Entry informationi

Entry nameiRPAB3_HUMAN
AccessioniPrimary (citable) accession number: P52434
Secondary accession number(s): C9J413
, C9JBJ6, C9JCU7, C9JUA8, P53802, Q969R0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 168 of the entry and version 4 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.