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Protein

Serine/threonine-protein kinase RAD53

Gene

RAD53

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

Controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints. Phosphorylates proteins on serine, threonine, and tyrosine. Prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. Seems to be involved in the phosphorylation of RPH1.5 Publications

Miscellaneous

Present with 6900 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei227ATPPROSITE-ProRule annotation1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei319Proton acceptor1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi204 – 212ATPPROSITE-ProRule annotation9

<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

  • ATP binding Source: UniProtKB-KW
  • DNA replication origin binding Source: SGD
  • protein serine/threonine/tyrosine kinase activity Source: SGD
  • protein serine/threonine kinase activity Source: GO_Central
  • protein tyrosine kinase activity Source: UniProtKB-KW

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 functionKinase, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase
Biological processCell cycle, DNA damage
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-34050-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.12.1 984

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-171007 p38MAPK events
R-SCE-2559580 Oxidative Stress Induced Senescence
R-SCE-3371453 Regulation of HSF1-mediated heat shock response
R-SCE-4420097 VEGFA-VEGFR2 Pathway
R-SCE-450302 activated TAK1 mediates p38 MAPK activation
R-SCE-450385 Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA
R-SCE-5687128 MAPK6/MAPK4 signaling

<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_and_taxonomy_section">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:
Serine/threonine-protein kinase RAD53 (EC:2.7.12.1)
Alternative name(s):
CHEK2 homolog
Serine-protein kinase 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:RAD53
Synonyms:MEC2, SAD1, SPK1
Ordered Locus Names:YPL153C
ORF Names:P2588
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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 XVI

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000006074 RAD53

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000865951 – 821Serine/threonine-protein kinase RAD53Add BLAST821

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei24PhosphoserineCombined sources1
Modified residuei175PhosphoserineCombined sources1
Modified residuei547PhosphoserineCombined sources1
Modified residuei560PhosphoserineCombined sources1
Modified residuei774PhosphoserineCombined sources1
Modified residuei793PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Autophosphorylated.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P22216

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

More...
PaxDbi
P22216

PRoteomics IDEntifications database

More...
PRIDEi
P22216

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P22216

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with PIN4.1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
36030, 586 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1322 RAD53-ASF1 complex

Database of interacting proteins

More...
DIPi
DIP-2322N

Protein interaction database and analysis system

More...
IntActi
P22216, 40 interactors

Molecular INTeraction database

More...
MINTi
P22216

STRING: functional protein association networks

More...
STRINGi
4932.YPL153C

<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

Secondary structure

1821
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P22216

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

More...
SMRi
P22216

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P22216

<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_and_domains_section">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>Domaini66 – 116FHA 1PROSITE-ProRule annotationAdd BLAST51
Domaini198 – 466Protein kinasePROSITE-ProRule annotationAdd BLAST269
Domaini601 – 664FHA 2PROSITE-ProRule annotationAdd BLAST64

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

FHA domains are phosphothreonine recognition modules, FHA 1 strongly selects for Asp at position +3 relative to phosphothreonine, whereas FHA 2 selects for Ile in this position.

<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

Keywords - Domaini

Repeat

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000074515

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P22216

KEGG Orthology (KO)

More...
KOi
K02831

Identification of Orthologs from Complete Genome Data

More...
OMAi
TQATQKY

Database of Orthologous Groups

More...
OrthoDBi
EOG092C2FDZ

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00060 FHA, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000253 FHA_dom
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
IPR016256 Ser/Thr_kinase_Rad53
IPR008984 SMAD_FHA_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00498 FHA, 2 hits
PF00069 Pkinase, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000661 Ser/Thr_PK_RAD53, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00240 FHA, 2 hits
SM00220 S_TKc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49879 SSF49879, 2 hits
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50006 FHA_DOMAIN, 2 hits
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

P22216-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MENITQPTQQ STQATQRFLI EKFSQEQIGE NIVCRVICTT GQIPIRDLSA
60 70 80 90 100
DISQVLKEKR SIKKVWTFGR NPACDYHLGN ISRLSNKHFQ ILLGEDGNLL
110 120 130 140 150
LNDISTNGTW LNGQKVEKNS NQLLSQGDEI TVGVGVESDI LSLVIFINDK
160 170 180 190 200
FKQCLEQNKV DRIRSNLKNT SKIASPGLTS STASSMVANK TGIFKDFSII
210 220 230 240 250
DEVVGQGAFA TVKKAIERTT GKTFAVKIIS KRKVIGNMDG VTRELEVLQK
260 270 280 290 300
LNHPRIVRLK GFYEDTESYY MVMEFVSGGD LMDFVAAHGA VGEDAGREIS
310 320 330 340 350
RQILTAIKYI HSMGISHRDL KPDNILIEQD DPVLVKITDF GLAKVQGNGS
360 370 380 390 400
FMKTFCGTLA YVAPEVIRGK DTSVSPDEYE ERNEYSSLVD MWSMGCLVYV
410 420 430 440 450
ILTGHLPFSG STQDQLYKQI GRGSYHEGPL KDFRISEEAR DFIDSLLQVD
460 470 480 490 500
PNNRSTAAKA LNHPWIKMSP LGSQSYGDFS QISLSQSLSQ QKLLENMDDA
510 520 530 540 550
QYEFVKAQRK LQMEQQLQEQ DQEDQDGKIQ GFKIPAHAPI RYTQPKSIEA
560 570 580 590 600
ETREQKLLHS NNTENVKSSK KKGNGRFLTL KPLPDSIIQE SLEIQQGVNP
610 620 630 640 650
FFIGRSEDCN CKIEDNRLSR VHCFIFKKRH AVGKSMYESP AQGLDDIWYC
660 670 680 690 700
HTGTNVSYLN NNRMIQGTKF LLQDGDEIKI IWDKNNKFVI GFKVEINDTT
710 720 730 740 750
GLFNEGLGML QEQRVVLKQT AEEKDLVKKL TQMMAAQRAN QPSASSSSMS
760 770 780 790 800
AKKPPVSDTN NNGNNSVLND LVESPINANT GNILKRIHSV SLSQSQIDPS
810 820
KKVKRAKLDQ TSKGPENLQF S
Length:821
Mass (Da):91,962
Last modified:August 1, 1991 - 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:i84A9612229CA72D1
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 conflicti204V → A in AAT93028 (PubMed:17322287).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
M55623 Genomic DNA Translation: AAA35070.1
X96770 Genomic DNA Translation: CAA65568.1
Z73509 Genomic DNA Translation: CAA97858.1
AY693009 Genomic DNA Translation: AAT93028.1
BK006949 Genomic DNA Translation: DAA11281.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A39616

NCBI Reference Sequences

More...
RefSeqi
NP_015172.1, NM_001183967.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YPL153C_mRNA; YPL153C_mRNA; YPL153C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
855950

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YPL153C

<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
M55623 Genomic DNA Translation: AAA35070.1
X96770 Genomic DNA Translation: CAA65568.1
Z73509 Genomic DNA Translation: CAA97858.1
AY693009 Genomic DNA Translation: AAT93028.1
BK006949 Genomic DNA Translation: DAA11281.1
PIRiA39616
RefSeqiNP_015172.1, NM_001183967.1

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
1DMZNMR-A573-730[»]
1FHQNMR-A573-730[»]
1FHRNMR-A573-730[»]
1G3GNMR-A1-164[»]
1G6GX-ray1.60A/B29-155[»]
1J4KNMR-A573-730[»]
1J4LNMR-A573-730[»]
1J4ONMR-A14-164[»]
1J4PNMR-A14-164[»]
1J4QNMR-A14-164[»]
1K2MNMR-A573-730[»]
1K2NNMR-A573-730[»]
1K3JNMR-A14-164[»]
1K3NNMR-A14-164[»]
1K3QNMR-A14-164[»]
1QU5NMR-A549-730[»]
2A0TNMR-A14-164[»]
2JQINMR-A14-164[»]
B3-12[»]
2JQLNMR-B3-12[»]
2YGVX-ray2.94E/F/G/H800-821[»]
4PDPX-ray2.59A/B170-512[»]
4PDSX-ray2.90A/B170-512[»]
5T2FX-ray2.66A/B/C/D22-162[»]
5T2SX-ray2.40A/C22-162[»]
5XZVX-ray3.10A/B1-466[»]
5XZWX-ray2.80A/B1-466[»]
6C4UX-ray2.60A/B/C/D/E/F29-162[»]
ProteinModelPortaliP22216
SMRiP22216
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36030, 586 interactors
ComplexPortaliCPX-1322 RAD53-ASF1 complex
DIPiDIP-2322N
IntActiP22216, 40 interactors
MINTiP22216
STRINGi4932.YPL153C

PTM databases

iPTMnetiP22216

Proteomic databases

MaxQBiP22216
PaxDbiP22216
PRIDEiP22216

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYPL153C_mRNA; YPL153C_mRNA; YPL153C
GeneIDi855950
KEGGisce:YPL153C

Organism-specific databases

SGDiS000006074 RAD53

Phylogenomic databases

HOGENOMiHOG000074515
InParanoidiP22216
KOiK02831
OMAiTQATQKY
OrthoDBiEOG092C2FDZ

Enzyme and pathway databases

BioCyciYEAST:G3O-34050-MONOMER
BRENDAi2.7.12.1 984
ReactomeiR-SCE-171007 p38MAPK events
R-SCE-2559580 Oxidative Stress Induced Senescence
R-SCE-3371453 Regulation of HSF1-mediated heat shock response
R-SCE-4420097 VEGFA-VEGFR2 Pathway
R-SCE-450302 activated TAK1 mediates p38 MAPK activation
R-SCE-450385 Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA
R-SCE-5687128 MAPK6/MAPK4 signaling

Miscellaneous databases

EvolutionaryTraceiP22216

Protein Ontology

More...
PROi
PR:P22216

Family and domain databases

CDDicd00060 FHA, 2 hits
InterProiView protein in InterPro
IPR000253 FHA_dom
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
IPR016256 Ser/Thr_kinase_Rad53
IPR008984 SMAD_FHA_dom_sf
PfamiView protein in Pfam
PF00498 FHA, 2 hits
PF00069 Pkinase, 1 hit
PIRSFiPIRSF000661 Ser/Thr_PK_RAD53, 1 hit
SMARTiView protein in SMART
SM00240 FHA, 2 hits
SM00220 S_TKc, 1 hit
SUPFAMiSSF49879 SSF49879, 2 hits
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS50006 FHA_DOMAIN, 2 hits
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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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 nameiRAD53_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: P22216
Secondary accession number(s): D6W3L5, Q6B1S1
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: December 5, 2018
This is version 209 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, Complete proteome, Reference proteome

Documents

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