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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

  • DNA-directed 5'-3' RNA polymerase activity Source: UniProtKB-KW
  • single-stranded DNA binding Source: CAFA

GO - Biological processi

Keywordsi

Molecular functionDNA-binding
Biological processTranscription

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 during HIV infection.
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

EuPathDBiHostDB:ENSG00000163882.9.
HGNCiHGNC:9195. POLR2H.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi5437.
OpenTargetsiENSG00000163882.
PharmGKBiPA33515.

Polymorphism and mutation databases

DMDMi20178325.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00000739972 – 150DNA-directed RNA polymerases I, II, and III subunit RPABC3Add BLAST149

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

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

PTM databases

iPTMnetiP52434.
PhosphoSitePlusiP52434.

Expressioni

Gene expression databases

BgeeiENSG00000163882.
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 interactors.
CORUMiP52434.
DIPiDIP-27556N.
IntActiP52434. 18 interactors.
MINTiMINT-1162805.
STRINGi9606.ENSP00000296223.

Structurei

Secondary structure

1150
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 16Combined sources10
Beta strandi25 – 35Combined sources11
Beta strandi38 – 44Combined sources7
Beta strandi48 – 50Combined sources3
Beta strandi56 – 59Combined sources4
Beta strandi66 – 70Combined sources5
Turni71 – 73Combined sources3
Beta strandi75 – 77Combined sources3
Turni85 – 88Combined sources4
Beta strandi89 – 92Combined sources4
Beta strandi94 – 97Combined sources4
Beta strandi104 – 107Combined sources4
Beta strandi110 – 118Combined sources9
Beta strandi121 – 127Combined sources7
Helixi129 – 132Combined sources4
Beta strandi142 – 147Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP52434.
SMRiP52434.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52434.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni16 – 40Non-specific ssDNA bindingAdd BLAST25

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3400. Eukaryota.
ENOG4111FT0. LUCA.
GeneTreeiENSGT00390000018195.
HOGENOMiHOG000175572.
HOVERGENiHBG036116.
InParanoidiP52434.
KOiK03016.
OMAiFEYVMFG.
OrthoDBiEOG091G0QJA.
PhylomeDBiP52434.
TreeFamiTF103043.

Family and domain databases

InterProiView protein in InterPro
IPR012340. NA-bd_OB-fold.
IPR005570. RNA_pol_Rpb8.
PANTHERiPTHR10917. PTHR10917. 1 hit.
PfamiView protein in Pfam
PF03870. RNA_pol_Rpb8. 1 hit.
PIRSFiPIRSF000779. RNA_pol_Rpb8. 1 hit.
SMARTiView protein in SMART
SM00658. RPOL8c. 1 hit.
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)DescriptionActionsGraphical viewLength
Sequence conflicti19G → A in AAA91458 (PubMed:8524256).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0550171 – 36Missing in isoform 3 and isoform 5. CuratedAdd BLAST36
Alternative sequenceiVSP_05501884 – 112RADQF…AATRL → S in isoform 2 and isoform 5. CuratedAdd BLAST29
Alternative sequenceiVSP_055019113 – 150SAYVS…KKLAF → LRLRAAEWQCSRITGWGLLF QLCVRVLWGPAHEAAGGCQQ PAWIRGGLQSLSPDEEASLL NLA in isoform 4. CuratedAdd BLAST38

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_001278699.2. [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_006232.4. [P52434-1]
XP_006713729.1. XM_006713666.2. [P52434-4]
XP_006713730.1. XM_006713667.2. [P52434-4]
XP_016862125.1. XM_017006636.1. [P52434-2]
XP_016862126.1. XM_017006637.1. [P52434-5]
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

Similar proteinsi

Entry informationi

Entry nameiRPAB3_HUMAN
AccessioniPrimary (citable) accession number: P52434
Secondary accession number(s): C9J413
, C9JBJ6, C9JCU7, C9JUA8, P53802, Q969R0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: September 27, 2017
This is version 179 of the entry and version 4 of the sequence. See 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