Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DNA-directed RNA polymerases I, II, and III subunit RPABC4

Gene

RPC10

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

DNA-dependent RNA polymerases catalyze 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 a small RNAs, such as 5S rRNA and tRNAs, respectively. RNA polymerases are composed of mobile elements that move relative to each other. In Pol II, the core element with the central large cleft comprises RPB3, RBP10, RPB11, RPB12 and regions of RPB1 and RPB2 forming the active center.3 Publications

Miscellaneous

Present with 907 molecules/cell in log phase SD medium.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi31Zinc1
Metal bindingi34Zinc1
Metal bindingi48Zinc1
Metal bindingi51Zinc1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri31 – 51C4-typeAdd BLAST21

GO - Molecular functioni

  • DNA binding Source: InterPro
  • RNA polymerase I activity Source: UniProtKB
  • zinc ion binding Source: SGD

GO - Biological processi

  • ribosome biogenesis Source: UniProtKB-KW
  • termination of RNA polymerase III transcription Source: Reactome
  • transcription, RNA-templated Source: GOC
  • transcription by RNA polymerase I Source: UniProtKB
  • transcription by RNA polymerase II Source: SGD
  • transcription by RNA polymerase III Source: SGD
  • tRNA transcription by RNA polymerase III Source: SGD

Keywordsi

Biological processRibosome biogenesis, Transcription
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-31179-MONOMER
ReactomeiR-SCE-113418 Formation of the Early Elongation Complex
R-SCE-674695 RNA Polymerase II Pre-transcription Events
R-SCE-6781823 Formation of TC-NER Pre-Incision Complex
R-SCE-6782135 Dual incision in TC-NER
R-SCE-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-SCE-6796648 TP53 Regulates Transcription of DNA Repair Genes
R-SCE-6807505 RNA polymerase II transcribes snRNA genes
R-SCE-72086 mRNA Capping
R-SCE-72165 mRNA Splicing - Minor Pathway
R-SCE-73762 RNA Polymerase I Transcription Initiation
R-SCE-73776 RNA Polymerase II Promoter Escape
R-SCE-73779 RNA Polymerase II Transcription Pre-Initiation And Promoter Opening
R-SCE-75953 RNA Polymerase II Transcription Initiation
R-SCE-76042 RNA Polymerase II Transcription Initiation And Promoter Clearance
R-SCE-77075 RNA Pol II CTD phosphorylation and interaction with CE
R-SCE-9018519 Estrogen-dependent gene expression

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed RNA polymerases I, II, and III subunit RPABC4
Short name:
RNA polymerases I, II, and III subunit ABC4
Alternative name(s):
ABC10-alpha
Gene namesi
Name:RPC10
Synonyms:RPB12
Ordered Locus Names:YHR143W-A
ORF Names:YHR143BW
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VIII

Organism-specific databases

EuPathDBiFungiDB:YHR143W-A
SGDiS000001185 RPC10

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole 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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001597531 – 70DNA-directed RNA polymerases I, II, and III subunit RPABC4Add BLAST70

Post-translational modificationi

The N-terminus is blocked.

Proteomic databases

MaxQBiP40422
PaxDbiP40422
PRIDEiP40422

PTM databases

iPTMnetiP40422

Interactioni

Subunit structurei

Component of the RNA polymerase I (Pol I), RNA polymerase II (Pol II) and RNA polymerase III (Pol III) complexes. Component of the RNA polymerase I (Pol I) complex consisting of 14 subunits: RPA135, RPA190, RPC40, RPA14, RPB5, RPO26, RPA43, RPB8, RPA12, RPB10, RPC19, RPC10, RPA49 and RPA34. The complex is composed of a horseshoe-shaped core containing ten subunits (RPA135, RPA190, RPB5, RPO26, RPB8, RPB10, RPC10, RPA12, RPC19 and RPC40) where RPA135 and RPA190 form the DNA-binding cleft. Outside of the core, RPA14 and RPA43 form the stalk that mediates interactions with transcription initiation factors and newly synthesized RNA. Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits: RPO21, RPB2, RPB3, RPB4, RPB5, RPO26, RPB7, RPB8, RPB9, RPB10 and RPC10. Component of the RNA polymerase III (Pol III) complex consisting of 17 subunits. Interacts, via its C-terminus, with TFIIIC subunit TFC4.7 Publications

Protein-protein interaction databases

BioGridi36577, 67 interactors
ComplexPortaliCPX-1664 DNA-directed RNA Polymerase I complex
CPX-2660 DNA-directed RNA polymerase III complex
CPX-2662 DNA-directed RNA polymerase II complex
DIPiDIP-936N
IntActiP40422, 14 interactors
MINTiP40422
STRINGi4932.YHR143W-A

Structurei

Secondary structure

170
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi28 – 31Combined sources4
Beta strandi32 – 34Combined sources3
Beta strandi36 – 38Combined sources3
Beta strandi41 – 44Combined sources4
Beta strandi46 – 48Combined sources3
Beta strandi49 – 51Combined sources3
Beta strandi56 – 58Combined sources3
Beta strandi65 – 67Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1I3QX-ray3.10L1-70[»]
1I50X-ray2.80L1-70[»]
1I6HX-ray3.30L1-70[»]
1K83X-ray2.80L1-70[»]
1NIKX-ray4.10L1-70[»]
1NT9X-ray4.20L1-70[»]
1PQVX-ray3.80L1-70[»]
1R5UX-ray4.50L1-70[»]
1R9SX-ray4.25L1-70[»]
1R9TX-ray3.50L1-70[»]
1SFOX-ray3.61L1-70[»]
1TWAX-ray3.20L1-70[»]
1TWCX-ray3.00L1-70[»]
1TWFX-ray2.30L1-70[»]
1TWGX-ray3.30L1-70[»]
1TWHX-ray3.40L1-70[»]
1WCMX-ray3.80L1-70[»]
1Y1VX-ray3.80L1-70[»]
1Y1WX-ray4.00L1-70[»]
1Y1YX-ray4.00L1-70[»]
1Y77X-ray4.50L1-70[»]
2B63X-ray3.80L1-70[»]
2B8KX-ray4.15L1-70[»]
2E2HX-ray3.95L1-70[»]
2E2IX-ray3.41L1-70[»]
2E2JX-ray3.50L1-70[»]
2JA5X-ray3.80L1-70[»]
2JA6X-ray4.00L1-70[»]
2JA7X-ray3.80L/X1-70[»]
2JA8X-ray3.80L1-70[»]
2NVQX-ray2.90L1-70[»]
2NVTX-ray3.36L1-70[»]
2NVXX-ray3.60L1-70[»]
2NVYX-ray3.40L1-70[»]
2NVZX-ray4.30L1-70[»]
2R7ZX-ray3.80L1-70[»]
2R92X-ray3.80L1-70[»]
2R93X-ray4.00L1-70[»]
2VUMX-ray3.40L1-70[»]
2YU9X-ray3.40L1-70[»]
3CQZX-ray2.80L1-70[»]
3FKIX-ray3.88L1-70[»]
3GTGX-ray3.78L1-70[»]
3GTJX-ray3.42L1-70[»]
3GTKX-ray3.80L1-70[»]
3GTLX-ray3.38L1-70[»]
3GTMX-ray3.80L1-70[»]
3GTOX-ray4.00L1-70[»]
3GTPX-ray3.90L1-70[»]
3GTQX-ray3.80L1-70[»]
3H3VX-ray4.00M1-70[»]
3HOUX-ray3.20L/X1-70[»]
3HOVX-ray3.50L1-70[»]
3HOWX-ray3.60L1-70[»]
3HOXX-ray3.65L1-70[»]
3HOYX-ray3.40L1-70[»]
3HOZX-ray3.65L1-70[»]
3I4MX-ray3.70L1-70[»]
3I4NX-ray3.90L1-70[»]
3J1Nelectron microscopy16.00L1-70[»]
3K1FX-ray4.30L1-70[»]
3K7AX-ray3.80L1-70[»]
3M3YX-ray3.18L1-70[»]
3M4OX-ray3.57L1-70[»]
3PO2X-ray3.30L1-70[»]
3PO3X-ray3.30L1-70[»]
3QT1X-ray4.30L1-70[»]
3RZDX-ray3.30L1-70[»]
3RZOX-ray3.00L1-70[»]
3S14X-ray2.85L1-70[»]
3S15X-ray3.30L1-70[»]
3S16X-ray3.24L1-70[»]
3S17X-ray3.20L1-70[»]
3S1MX-ray3.13L1-70[»]
3S1NX-ray3.10L1-70[»]
3S1QX-ray3.30L1-70[»]
3S1RX-ray3.20L1-70[»]
3S2DX-ray3.20L1-70[»]
3S2HX-ray3.30L1-70[»]
4A3BX-ray3.50L1-70[»]
4A3CX-ray3.50L1-70[»]
4A3DX-ray3.40L1-70[»]
4A3EX-ray3.40L1-70[»]
4A3FX-ray3.50L1-70[»]
4A3GX-ray3.50L1-70[»]
4A3IX-ray3.80L1-70[»]
4A3JX-ray3.70L1-70[»]
4A3KX-ray3.50L1-70[»]
4A3LX-ray3.50L1-70[»]
4A3MX-ray3.90L1-70[»]
4A93X-ray3.40L1-70[»]
4BBRX-ray3.40L1-70[»]
4BBSX-ray3.60L1-70[»]
4BXXX-ray3.28L1-70[»]
4BXZX-ray4.80L1-70[»]
4BY1X-ray3.60L1-70[»]
4BY7X-ray3.15L1-70[»]
4C2MX-ray2.801/L1-70[»]
4C3HX-ray3.27L1-70[»]
4C3IX-ray3.0L1-70[»]
4C3JX-ray3.35L1-70[»]
4V1Melectron microscopy6.60L1-70[»]
4V1Nelectron microscopy7.80L1-70[»]
4V1Oelectron microscopy9.70L1-70[»]
4X67X-ray4.10L1-70[»]
4X6AX-ray3.96L1-70[»]
4Y52X-ray3.50L1-70[»]
4Y7NX-ray3.30L1-70[»]
4YM7X-ray5.50AL/BL/CL/DL/EL/FL1-70[»]
5C3EX-ray3.70L1-70[»]
5C44X-ray3.95L1-70[»]
5C4AX-ray4.20L1-70[»]
5C4JX-ray4.00L1-70[»]
5C4XX-ray4.00L1-70[»]
5FJ8electron microscopy3.90L1-70[»]
5FJ9electron microscopy4.60L1-70[»]
5FJAelectron microscopy4.65L1-70[»]
5FMFelectron microscopy6.00L25-70[»]
5FYWelectron microscopy4.35L1-70[»]
5FZ5electron microscopy8.80L1-70[»]
5G5Lelectron microscopy4.80L1-70[»]
5IP7X-ray3.52L25-70[»]
5IP9X-ray3.90L25-70[»]
5LMXelectron microscopy4.90L1-70[»]
5M3Felectron microscopy3.80L1-70[»]
5M3Melectron microscopy4.00L1-70[»]
5M5Welectron microscopy3.80L1-70[»]
5M5Xelectron microscopy4.00L1-70[»]
5M5Yelectron microscopy4.00L1-70[»]
5M64electron microscopy4.60L1-70[»]
5N5Yelectron microscopy7.70L1-70[»]
5N5Zelectron microscopy7.70L1-70[»]
5N60electron microscopy7.70L1-70[»]
5N61electron microscopy3.40L1-70[»]
5OA1electron microscopy4.40L1-70[»]
5OQJelectron microscopy4.70L1-70[»]
5OQMelectron microscopy5.80L1-70[»]
5OT2X-ray3.20L1-70[»]
5SVAelectron microscopy15.30L1-70[»]
5U5QX-ray3.80L1-70[»]
5VVRelectron microscopy5.80L1-70[»]
5VVSelectron microscopy6.40L1-70[»]
5W5Yelectron microscopy3.80L1-70[»]
5W64electron microscopy4.20L1-70[»]
5W65electron microscopy4.30L1-70[»]
5W66electron microscopy3.90L1-70[»]
6BLOX-ray3.40L1-70[»]
6BLPX-ray3.20L1-70[»]
6BM2X-ray3.40L1-70[»]
6BM4X-ray2.95L1-70[»]
6BQFX-ray3.35L1-70[»]
6EU0electron microscopy4.00L1-70[»]
6EU1electron microscopy3.40L1-70[»]
6EU2electron microscopy3.40L1-70[»]
6EU3electron microscopy3.30L1-70[»]
6F40electron microscopy3.70L1-70[»]
6F41electron microscopy4.30L1-70[»]
6F42electron microscopy5.50L1-70[»]
6F44electron microscopy4.20L1-70[»]
DisProtiDP00818
ProteinModelPortaliP40422
SMRiP40422
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40422

Family & Domainsi

Sequence similaritiesi

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri31 – 51C4-typeAdd BLAST21

Keywords - Domaini

Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00390000008918
HOGENOMiHOG000191755
InParanoidiP40422
KOiK03009
OMAiKYICAEC
OrthoDBiEOG092C5YM4

Family and domain databases

InterProiView protein in InterPro
IPR006591 RNAP_P/RPABC4
IPR029040 RPABC4/Spt4
PfamiView protein in Pfam
PF03604 DNA_RNApol_7kD, 1 hit
SMARTiView protein in SMART
SM00659 RPOLCX, 1 hit
SUPFAMiSSF63393 SSF63393, 1 hit

Sequencei

Sequence statusi: Complete.

P40422-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSREGFQIPT NLDAAAAGTS QARTATLKYI CAECSSKLSL SRTDAVRCKD
60 70
CGHRILLKAR TKRLVQFEAR
Length:70
Mass (Da):7,716
Last modified:February 1, 1995 - v1
Checksum:i066A3D982EC7361E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U23378 Genomic DNA Translation: AAA64417.1
U10397 Genomic DNA Translation: AAB68994.1
AY558549 Genomic DNA Translation: AAS56875.1
BK006934 Genomic DNA Translation: DAA06837.1
PIRiS58932
RefSeqiNP_012013.1, NM_001179273.1

Genome annotation databases

EnsemblFungiiYHR143W-A; YHR143W-A; YHR143W-A
GeneIDi856547
KEGGisce:YHR143W-A

Similar proteinsi

Entry informationi

Entry nameiRPAB4_YEAST
AccessioniPrimary (citable) accession number: P40422
Secondary accession number(s): D3DL93
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 20, 2018
This is version 180 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health