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Entry version 201 (22 Apr 2020)
Sequence version 1 (01 Jan 1988)
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Protein

General transcription and DNA repair factor IIH helicase subunit XPD

Gene

RAD3

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

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

ATP-dependent 5'-3' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATP-dependent helicase activity of XPD/RAD3 is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription. XPD/RAD3 acts by forming a bridge between TFIIK and the core-TFIIH complex. Involved in the maintenance of the fidelity of DNA replication.4 Publications

Miscellaneous

Present with 14400 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

[4Fe-4S] cluster1 PublicationNote: Binds 1 [4Fe-4S] cluster.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi115Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi133Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi156Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi191Iron-sulfur (4Fe-4S)By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi42 – 49ATPPROSITE-ProRule annotation8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding, Helicase, Hydrolase
Biological processDNA damage, DNA repair, Transcription, Transcription regulation
Ligand4Fe-4S, ATP-binding, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-30331-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-113418 Formation of the Early Elongation Complex
R-SCE-2564818 Cytosolic iron-sulfur cluster assembly (yeast)
R-SCE-5696400 Dual Incision in GG-NER
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-72086 mRNA Capping
R-SCE-73772 RNA Polymerase I Promoter Escape
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-75955 RNA Polymerase II Transcription Elongation
R-SCE-76042 RNA Polymerase II Transcription Initiation And Promoter Clearance
R-SCE-77075 RNA Pol II CTD phosphorylation and interaction with CE

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
General transcription and DNA repair factor IIH helicase subunit XPD (EC:3.6.4.12)
Short name:
TFIIH subunit XPD
Alternative name(s):
DNA repair helicase RAD3
RNA polymerase II transcription factor B subunit RAD3
Short name:
TFB subunit RAD3
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:RAD3
Synonyms:REM1
Ordered Locus Names:YER171W
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome V

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YER171W

Saccharomyces Genome Database

More...
SGDi
S000000973 RAD3

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi48K → R or A: Abolishes ATPase and DNA helicase activities but not ATP-binding capacity. 3 Publications1
Mutagenesisi111R → H: Confers an UV-sensitive phenotype. 1 Publication1
Mutagenesisi115C → S: Confers an UV-sensitive phenotype. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001019831 – 778General transcription and DNA repair factor IIH helicase subunit XPDAdd BLAST778

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P06839

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P06839

PRoteomics IDEntifications database

More...
PRIDEi
P06839

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the 7-subunit TFIIH core complex composed of XPB/SSL2, XPD/RAD3, SSL1, TFB1, TFB2, TFB4 and TFB5, which is active in NER. The core complex associates with the 3-subunit CTD-kinase module TFIIK composed of CCL1, KIN28 and TFB3 to form the 10-subunit holoenzyme (holo-TFIIH) active in transcription.

3 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
36924, 191 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1659 General transcription factor complex TFIIH

Database of interacting proteins

More...
DIPi
DIP-2425N

Protein interaction database and analysis system

More...
IntActi
P06839, 71 interactors

Molecular INTeraction database

More...
MINTi
P06839

STRING: functional protein association networks

More...
STRINGi
4932.YER171W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P06839 protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P06839

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini7 – 285Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST279

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi235 – 238DEAH box4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi759 – 778Asp/Glu-rich (acidic)Add BLAST20

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the helicase family. RAD3/XPD subfamily.Curated

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_011312_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P06839

KEGG Orthology (KO)

More...
KOi
K10844

Identification of Orthologs from Complete Genome Data

More...
OMAi
PYFTARR

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006555 ATP-dep_Helicase_C
IPR010614 DEAD_2
IPR002464 DNA/RNA_helicase_DEAH_CS
IPR010643 HBB
IPR014013 Helic_SF1/SF2_ATP-bd_DinG/Rad3
IPR006554 Helicase-like_DEXD_c2
IPR027417 P-loop_NTPase
IPR013020 Rad3/Chl1-like
IPR001945 RAD3/XPD

The PANTHER Classification System

More...
PANTHERi
PTHR11472:SF1 PTHR11472:SF1, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF06733 DEAD_2, 1 hit
PF06777 HBB, 1 hit
PF13307 Helicase_C_2, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00852 XRODRMPGMNTD

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00488 DEXDc2, 1 hit
SM00491 HELICc2, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540 SSF52540, 2 hits

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00604 rad3, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00690 DEAH_ATP_HELICASE, 1 hit
PS51193 HELICASE_ATP_BIND_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P06839-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKFYIDDLPV LFPYPKIYPE QYNYMCDIKK TLDVGGNSIL EMPSGTGKTV
60 70 80 90 100
SLLSLTIAYQ MHYPEHRKII YCSRTMSEIE KALVELENLM DYRTKELGYQ
110 120 130 140 150
EDFRGLGLTS RKNLCLHPEV SKERKGTVVD EKCRRMTNGQ AKRKLEEDPE
160 170 180 190 200
ANVELCEYHE NLYNIEVEDY LPKGVFSFEK LLKYCEEKTL CPYFIVRRMI
210 220 230 240 250
SLCNIIIYSY HYLLDPKIAE RVSNEVSKDS IVIFDEAHNI DNVCIESLSL
260 270 280 290 300
DLTTDALRRA TRGANALDER ISEVRKVDSQ KLQDEYEKLV QGLHSADILT
310 320 330 340 350
DQEEPFVETP VLPQDLLTEA IPGNIRRAEH FVSFLKRLIE YLKTRMKVLH
360 370 380 390 400
VISETPKSFL QHLKQLTFIE RKPLRFCSER LSLLVRTLEV TEVEDFTALK
410 420 430 440 450
DIATFATLIS TYEEGFLLII EPYEIENAAV PNPIMRFTCL DASIAIKPVF
460 470 480 490 500
ERFSSVIITS GTISPLDMYP RMLNFKTVLQ KSYAMTLAKK SFLPMIITKG
510 520 530 540 550
SDQVAISSRF EIRNDPSIVR NYGSMLVEFA KITPDGMVVF FPSYLYMESI
560 570 580 590 600
VSMWQTMGIL DEVWKHKLIL VETPDAQETS LALETYRKAC SNGRGAILLS
610 620 630 640 650
VARGKVSEGI DFDHQYGRTV LMIGIPFQYT ESRILKARLE FMRENYRIRE
660 670 680 690 700
NDFLSFDAMR HAAQCLGRVL RGKDDYGVMV LADRRFSRKR SQLPKWIAQG
710 720 730 740 750
LSDADLNLST DMAISNTKQF LRTMAQPTDP KDQEGVSVWS YEDLIKHQNS
760 770
RKDQGGFIEN ENKEGEQDED EDEDIEMQ
Length:778
Mass (Da):89,786
Last modified:January 1, 1988 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i978BCA01751949B4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti2K → G AA sequence (PubMed:8269516).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X02368 Genomic DNA Translation: CAA26215.1
K03293 Genomic DNA Translation: AAA34943.1
U18922 Genomic DNA Translation: AAB64698.1
BK006939 Genomic DNA Translation: DAA07833.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A23308

NCBI Reference Sequences

More...
RefSeqi
NP_011098.3, NM_001179061.3

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YER171W_mRNA; YER171W; YER171W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
856918

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YER171W

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02368 Genomic DNA Translation: CAA26215.1
K03293 Genomic DNA Translation: AAA34943.1
U18922 Genomic DNA Translation: AAB64698.1
BK006939 Genomic DNA Translation: DAA07833.1
PIRiA23308
RefSeqiNP_011098.3, NM_001179061.3

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5FMFelectron microscopy6.00Y1-778[»]
5OQJelectron microscopy4.7001-778[»]
5OQMelectron microscopy5.8001-778[»]
5SVAelectron microscopy15.30Y1-778[»]
6GYMelectron microscopy6.7001-778[»]
SMRiP06839
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi36924, 191 interactors
ComplexPortaliCPX-1659 General transcription factor complex TFIIH
DIPiDIP-2425N
IntActiP06839, 71 interactors
MINTiP06839
STRINGi4932.YER171W

Proteomic databases

MaxQBiP06839
PaxDbiP06839
PRIDEiP06839

Genome annotation databases

EnsemblFungiiYER171W_mRNA; YER171W; YER171W
GeneIDi856918
KEGGisce:YER171W

Organism-specific databases

EuPathDBiFungiDB:YER171W
SGDiS000000973 RAD3

Phylogenomic databases

HOGENOMiCLU_011312_1_0_1
InParanoidiP06839
KOiK10844
OMAiPYFTARR

Enzyme and pathway databases

BioCyciYEAST:G3O-30331-MONOMER
ReactomeiR-SCE-113418 Formation of the Early Elongation Complex
R-SCE-2564818 Cytosolic iron-sulfur cluster assembly (yeast)
R-SCE-5696400 Dual Incision in GG-NER
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-72086 mRNA Capping
R-SCE-73772 RNA Polymerase I Promoter Escape
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-75955 RNA Polymerase II Transcription Elongation
R-SCE-76042 RNA Polymerase II Transcription Initiation And Promoter Clearance
R-SCE-77075 RNA Pol II CTD phosphorylation and interaction with CE

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P06839
RNActiP06839 protein

Family and domain databases

InterProiView protein in InterPro
IPR006555 ATP-dep_Helicase_C
IPR010614 DEAD_2
IPR002464 DNA/RNA_helicase_DEAH_CS
IPR010643 HBB
IPR014013 Helic_SF1/SF2_ATP-bd_DinG/Rad3
IPR006554 Helicase-like_DEXD_c2
IPR027417 P-loop_NTPase
IPR013020 Rad3/Chl1-like
IPR001945 RAD3/XPD
PANTHERiPTHR11472:SF1 PTHR11472:SF1, 1 hit
PfamiView protein in Pfam
PF06733 DEAD_2, 1 hit
PF06777 HBB, 1 hit
PF13307 Helicase_C_2, 1 hit
PRINTSiPR00852 XRODRMPGMNTD
SMARTiView protein in SMART
SM00488 DEXDc2, 1 hit
SM00491 HELICc2, 1 hit
SUPFAMiSSF52540 SSF52540, 2 hits
TIGRFAMsiTIGR00604 rad3, 1 hit
PROSITEiView protein in PROSITE
PS00690 DEAH_ATP_HELICASE, 1 hit
PS51193 HELICASE_ATP_BIND_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRAD3_YEAST
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P06839
Secondary accession number(s): D3DM79
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: April 22, 2020
This is version 201 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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