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Protein

DNA repair protein RAD51 homolog 1

Gene

RAD51

Organism
Homo sapiens (Human)
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

Plays an important role in homologous strand exchange, a key step in DNA repair through homologous recombination (HR) (PubMed:28575658). Binds to single and double-stranded DNA and exhibits DNA-dependent ATPase activity. Catalyzes the recognition of homology and strand exchange between homologous DNA partners to form a joint molecule between a processed DNA break and the repair template. Binds to single-stranded DNA in an ATP-dependent manner to form nucleoprotein filaments which are essential for the homology search and strand exchange (PubMed:26681308). Part of a PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51C and XRCC3. Also involved in interstrand cross-link repair (PubMed:26253028).11 Publications

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 bindingi127 – 134ATPBy similarity8

<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
Biological processDNA damage, DNA recombination, DNA repair
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-5685938 HDR through Single Strand Annealing (SSA)
R-HSA-5685942 HDR through Homologous Recombination (HRR)
R-HSA-5693554 Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA)
R-HSA-5693568 Resolution of D-loop Structures through Holliday Junction Intermediates
R-HSA-5693579 Homologous DNA Pairing and Strand Exchange
R-HSA-5693616 Presynaptic phase of homologous DNA pairing and strand exchange
R-HSA-8953750 Transcriptional Regulation by E2F6
R-HSA-912446 Meiotic recombination

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
Q06609

SIGNOR Signaling Network Open Resource

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SIGNORi
Q06609

<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:
DNA repair protein RAD51 homolog 1
Short name:
HsRAD51
Short name:
hRAD51
Alternative name(s):
RAD51 homolog A
<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:RAD51
Synonyms:RAD51A, RECA
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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 15

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000051180.16

Human Gene Nomenclature Database

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HGNCi
HGNC:9817 RAD51

Online Mendelian Inheritance in Man (OMIM)

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MIMi
179617 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q06609

<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 Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Cytoplasm, Cytoskeleton, Mitochondrion, 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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Breast cancer (BC)2 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case.
See also OMIM:114480
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_010899150R → Q in BC; decreased ATPase activity in the presence of stoichiometric ss-DNA concentrations with respect to RAD51; 3 to 4-fold decrease of affinity for ATP. 2 PublicationsCorresponds to variant dbSNP:rs121917739EnsemblClinVar.1
Mirror movements 2 (MRMV2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by contralateral involuntary movements that mirror voluntary ones. While mirror movements are occasionally found in young children, persistence beyond the age of 10 is abnormal. Mirror movements occur more commonly in the upper extremities.
See also OMIM:614508
Fanconi anemia, complementation group R (FANCR)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair.
See also OMIM:617244
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_076870131T → P in FANCR; causes dominant negative loss of function in interstrand cross-link repair; shows high basal DNA-independent ATPase activity; results in decreased DNA binding. 1 Publication1
Natural variantiVAR_076593293A → T in FANCR; dominant negative; impaired function in DNA repair via homologous recombination; impaired DNA-binding and formation of nucleoprotein filaments; impaired DNA-dependent ATPase activity; no effect on subcellular location. 1 PublicationCorresponds to variant dbSNP:rs1057519413Ensembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi58K → R: Impaired ubiquitination; when associated with R-64. 1 Publication1
Mutagenesisi64K → R: Impaired ubiquitination; when associated with R-58. 1 Publication1
Mutagenesisi86F → A: Loss of homooligomerization. 1 Publication1
Mutagenesisi89A → E: Loss of homooligomerization. 1 Publication1
Mutagenesisi208 – 209SA → LE: Disrupts interaction with BRCA2, no effect on homooligomerization, promotes interaction with XPO1 and cytoplasmic localization. 2 Publications2
Mutagenesisi309T → A: Confers hypersensitivity to hydroxyurea. 1 Publication1

Keywords - Diseasei

Disease mutation, Fanconi anemia

Organism-specific databases

DisGeNET

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DisGeNETi
5888

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
RAD51

MalaCards human disease database

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MalaCardsi
RAD51
MIMi114480 phenotype
614508 phenotype
617244 phenotype

Open Targets

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OpenTargetsi
ENSG00000051180

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
238722 Familial congenital mirror movements
84 Fanconi anemia
145 Hereditary breast and ovarian cancer syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA34176

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2034807

Drug and drug target database

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DrugBanki
DB05216 MP470
DB04395 Phosphoaminophosphonic Acid-Adenylate Ester

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
RAD51

Domain mapping of disease mutations (DMDM)

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DMDMi
548663

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<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_00001229322 – 339DNA repair protein RAD51 homolog 1Add BLAST338

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 residuei2N-acetylalanineCombined sources1
Modified residuei54Phosphotyrosine; by ABL11 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki64Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei309Phosphothreonine; by CHEK11 Publication1

<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

Ubiquitinated by the SCF(FBH1) E3 ubiquitin ligase complex, regulating RAD51 subcellular location and preventing its association with DNA. Ubiquitinated by RFWD3 in response to DNA damage: ubiquitination leads to degradation by the proteasome, promoting homologous recombination (PubMed:28575658).2 Publications
Phosphorylated. Phosphorylation of Thr-309 by CHEK1 may enhance association with chromatin at sites of DNA damage and promote DNA repair by homologous recombination. Phosphorylation by ABL1 inhibits function.2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q06609

MaxQB - The MaxQuant DataBase

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MaxQBi
Q06609

PeptideAtlas

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PeptideAtlasi
Q06609

PRoteomics IDEntifications database

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PRIDEi
Q06609

ProteomicsDB human proteome resource

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ProteomicsDBi
58464
58465 [Q06609-2]
58466 [Q06609-3]
58467 [Q06609-4]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q06609

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q06609

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
Q06609

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Highly expressed in testis and thymus, followed by small intestine, placenta, colon, pancreas and ovary. Weakly expressed in breast.

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Stress-induced increase in the mitochondrial levels is seen.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000051180 Expressed in 133 organ(s), highest expression level in embryo

CleanEx database of gene expression profiles

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CleanExi
HS_RAD51

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q06609 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q06609 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB010381
HPA039310

<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

Forms linear homooligomers, giving rise to a RAD51 nucleoprotein filament, which is essential for strand-pairing reactions during DNA recombination. Interacts with BRCA1 and either directly or indirectly with p53. Interacts with XRCC3, RAD54L and RAD54B. Interacts with the BCDX2 subcomplex RAD51C:RAD51B. Interacts directly with PALB2 which may serve as a scaffold for a HR complex containing PALB2, BRCA2, RAD51C, RAD51 and XRCC3. Interacts with RAD51AP1 and RAD51AP2. Interacts with CHEK1, and this may require prior phosphorylation of CHEK1. Interacts with the MND1-PSMC3IP heterodimer. Found in a complex, at least composed of BLM, RAD51 and SPIDR; the complex formation is mediated by SPIDR. Interacts with SPIDR; the interaction is direct and recruits RAD51 to DNA damage sites. Interacts with FIGNL1 (via N-terminal one-half region); the interaction is direct. Interacts with RAD51AP1 (via C-terminal region); the interaction is direct. Interacts with NABP2, RPA1, PALB2 and RAD51. Interacts with SWI5/C9orf119, and at lower level with SFR1/MEIR5. Interacts with hyperphosphorylated RPA2; this interaction is necessary for efficient recruitment to chromatin in response to DNA damage. Interacts with SWSAP1; involved in homologous recombination repair. Interacts with PARPBP, BRCA2 and RECQL5; these interactions interfere with the formation of the RAD51-DNA homologous recombination structure. Interacts with POLQ; POLQ acts as an inhibitor of homology-recombination repair (HR) pathway by limiting RAD51 accumulation at resected ends (PubMed:25642963). Interacts with FBH1 (PubMed:23393192). Interacts with POLN (PubMed:19995904). Interacts with RFWD3 (PubMed:28575658). Interacts with the MCM8-MCM9 complex; the interaction recruits RAD51 to DNA damage sites (PubMed:23401855).28 Publications

<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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
111825, 165 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-955 BRCC ubiquitin ligase complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q06609

Database of interacting proteins

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DIPi
DIP-462N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
Q06609

Protein interaction database and analysis system

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IntActi
Q06609, 105 interactors

Molecular INTeraction database

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MINTi
Q06609

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q06609

<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

1339
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q06609

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

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SMRi
Q06609

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q06609

<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>Domaini48 – 77HhHAdd BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni184 – 257Interaction with PALB2Add BLAST74

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>Motifi245 – 260Nuclear export signal; masked by the interaction with BRCA21 PublicationAdd BLAST16

<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

The nuclear localization may reside in the C-terminus (between 259 and 339 AA).

<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 RecA family. RAD51 subfamily.Curated

Phylogenomic databases

Ensembl GeneTree

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GeneTreei
ENSGT00940000156157

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000227426

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG001504

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q06609

KEGG Orthology (KO)

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KOi
K04482

Identification of Orthologs from Complete Genome Data

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OMAi
YNTDHQT

Database of Orthologous Groups

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OrthoDBi
EOG091G09QY

Database for complete collections of gene phylogenies

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PhylomeDBi
Q06609

TreeFam database of animal gene trees

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TreeFami
TF101218

Family and domain databases

Conserved Domains Database

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CDDi
cd01123 Rad51_DMC1_radA, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR003593 AAA+_ATPase
IPR011941 DNA_recomb/repair_Rad51
IPR013632 DNA_recomb/repair_Rad51_C
IPR016467 DNA_recomb/repair_RecA-like
IPR010995 DNA_repair_Rad51/TF_NusA_a-hlx
IPR027417 P-loop_NTPase
IPR033925 Rad51_DMC1_RadA
IPR020588 RecA_ATP-bd
IPR020587 RecA_monomer-monomer_interface

Pfam protein domain database

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Pfami
View protein in Pfam
PF08423 Rad51, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF005856 Rad51, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00382 AAA, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47794 SSF47794, 1 hit
SSF52540 SSF52540, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR02239 recomb_RAD51, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50162 RECA_2, 1 hit
PS50163 RECA_3, 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>Sequences (4+)i

<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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 4 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q06609-1) [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
MAMQMQLEAN ADTSVEEESF GPQPISRLEQ CGINANDVKK LEEAGFHTVE
60 70 80 90 100
AVAYAPKKEL INIKGISEAK ADKILAEAAK LVPMGFTTAT EFHQRRSEII
110 120 130 140 150
QITTGSKELD KLLQGGIETG SITEMFGEFR TGKTQICHTL AVTCQLPIDR
160 170 180 190 200
GGGEGKAMYI DTEGTFRPER LLAVAERYGL SGSDVLDNVA YARAFNTDHQ
210 220 230 240 250
TQLLYQASAM MVESRYALLI VDSATALYRT DYSGRGELSA RQMHLARFLR
260 270 280 290 300
MLLRLADEFG VAVVITNQVV AQVDGAAMFA ADPKKPIGGN IIAHASTTRL
310 320 330
YLRKGRGETR ICKIYDSPCL PEAEAMFAIN ADGVGDAKD
Length:339
Mass (Da):36,966
Last modified:June 1, 1994 - 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:i26578E6206DEDEDA
GO
Isoform 2 (identifier: Q06609-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     77-173: Missing.

Note: No experimental confirmation available.
Show »
Length:242
Mass (Da):26,351
Checksum:iDFA9E12DC8429CA2
GO
Isoform 3 (identifier: Q06609-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     259-284: FGVAVVITNQVVAQVDGAAMFAADPK → IVSEERKRGNQNLQNLRLSLSS
     285-339: Missing.

Note: Mutagenesis of Arg-264 to Ala inhibits nuclear localization. Mutagenesis of Lys-264 to Gln inhibits nuclear localization. Deletion of 254-Arg-Lys-255 inhibits nuclear localization.1 Publication
Show »
Length:280
Mass (Da):31,001
Checksum:i1DFA22F6C0926FC2
GO
Isoform 4 (identifier: Q06609-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     76-114: AEAAKLVPMG...GSKELDKLLQ → TESRSVARLE...ASASRVVGTT

Note: No experimental confirmation available.
Show »
Length:340
Mass (Da):36,780
Checksum:iD8E2AAD35400FB04
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PNT5E9PNT5_HUMAN
DNA repair protein RAD51 homolog 1
RAD51
172Annotation score:

Annotation score:2 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>
Q9NZG9Q9NZG9_HUMAN
DNA repair protein RAD51 homolog 1
RAD51
75Annotation score:

Annotation score:1 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>
E9PJ30E9PJ30_HUMAN
DNA repair protein RAD51 homolog 1
RAD51
151Annotation score:

Annotation score:1 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>
E9PI54E9PI54_HUMAN
DNA repair protein RAD51 homolog 1
RAD51
100Annotation score:

Annotation score:1 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>
H0YD61H0YD61_HUMAN
DNA repair protein RAD51 homolog 1
RAD51
65Annotation score:

Annotation score:1 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 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 conflicti313K → Q in BAA02962 (PubMed:8358431).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_076870131T → P in FANCR; causes dominant negative loss of function in interstrand cross-link repair; shows high basal DNA-independent ATPase activity; results in decreased DNA binding. 1 Publication1
Natural variantiVAR_010899150R → Q in BC; decreased ATPase activity in the presence of stoichiometric ss-DNA concentrations with respect to RAD51; 3 to 4-fold decrease of affinity for ATP. 2 PublicationsCorresponds to variant dbSNP:rs121917739EnsemblClinVar.1
Natural variantiVAR_076593293A → T in FANCR; dominant negative; impaired function in DNA repair via homologous recombination; impaired DNA-binding and formation of nucleoprotein filaments; impaired DNA-dependent ATPase activity; no effect on subcellular location. 1 PublicationCorresponds to variant dbSNP:rs1057519413Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_04365576 – 114AEAAK…DKLLQ → TESRSVARLECNSVILVYCT LRLSGSSDSPASASRVVGTT in isoform 4. 1 PublicationAdd BLAST39
Alternative sequenceiVSP_00555677 – 173Missing in isoform 2. 1 PublicationAdd BLAST97
Alternative sequenceiVSP_041724259 – 284FGVAV…AADPK → IVSEERKRGNQNLQNLRLSL SS in isoform 3. 1 PublicationAdd BLAST26
Alternative sequenceiVSP_041725285 – 339Missing in isoform 3. 1 PublicationAdd BLAST55

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
D13804 mRNA Translation: BAA02962.1
D14134 mRNA Translation: BAA03189.1
AF165094
, AF165088, AF165089, AF165090, AF165091, AF165092, AF165093 Genomic DNA Translation: AAD49705.1
AF233744
, AF233740, AF233741, AF233742, AF236021, AF233743 Genomic DNA Translation: AAF69145.1
EU362635 mRNA Translation: ABY59731.1
AY196785 Genomic DNA Translation: AAN87149.1
AK131299 mRNA Translation: BAD18467.1
AK291969 mRNA Translation: BAF84658.1
AK313503 mRNA Translation: BAG36283.1
CR536559 mRNA Translation: CAG38796.1
AC012476 Genomic DNA No translation available.
AC022405 Genomic DNA No translation available.
CH471125 Genomic DNA Translation: EAW92434.1
CH471125 Genomic DNA Translation: EAW92432.1
CH471125 Genomic DNA Translation: EAW92435.1
BC001459 mRNA Translation: AAH01459.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS10062.1 [Q06609-1]
CCDS53931.1 [Q06609-4]
CCDS53932.1 [Q06609-3]

Protein sequence database of the Protein Information Resource

More...
PIRi
I58295

NCBI Reference Sequences

More...
RefSeqi
NP_001157741.1, NM_001164269.1 [Q06609-4]
NP_001157742.1, NM_001164270.1 [Q06609-3]
NP_002866.2, NM_002875.4 [Q06609-1]
NP_597994.3, NM_133487.3 [Q06609-4]
XP_006720689.1, XM_006720626.3 [Q06609-1]
XP_011520159.1, XM_011521857.2 [Q06609-1]
XP_011520160.1, XM_011521858.2 [Q06609-1]
XP_011520161.1, XM_011521859.2 [Q06609-1]
XP_011520162.1, XM_011521860.2 [Q06609-1]
XP_011520163.1, XM_011521861.2 [Q06609-3]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.631709

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000267868; ENSP00000267868; ENSG00000051180 [Q06609-1]
ENST00000382643; ENSP00000372088; ENSG00000051180 [Q06609-4]
ENST00000423169; ENSP00000406602; ENSG00000051180 [Q06609-3]
ENST00000532743; ENSP00000433924; ENSG00000051180 [Q06609-4]
ENST00000557850; ENSP00000454176; ENSG00000051180 [Q06609-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5888

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:5888

UCSC genome browser

More...
UCSCi
uc001zmi.5 human [Q06609-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13804 mRNA Translation: BAA02962.1
D14134 mRNA Translation: BAA03189.1
AF165094
, AF165088, AF165089, AF165090, AF165091, AF165092, AF165093 Genomic DNA Translation: AAD49705.1
AF233744
, AF233740, AF233741, AF233742, AF236021, AF233743 Genomic DNA Translation: AAF69145.1
EU362635 mRNA Translation: ABY59731.1
AY196785 Genomic DNA Translation: AAN87149.1
AK131299 mRNA Translation: BAD18467.1
AK291969 mRNA Translation: BAF84658.1
AK313503 mRNA Translation: BAG36283.1
CR536559 mRNA Translation: CAG38796.1
AC012476 Genomic DNA No translation available.
AC022405 Genomic DNA No translation available.
CH471125 Genomic DNA Translation: EAW92434.1
CH471125 Genomic DNA Translation: EAW92432.1
CH471125 Genomic DNA Translation: EAW92435.1
BC001459 mRNA Translation: AAH01459.1
CCDSiCCDS10062.1 [Q06609-1]
CCDS53931.1 [Q06609-4]
CCDS53932.1 [Q06609-3]
PIRiI58295
RefSeqiNP_001157741.1, NM_001164269.1 [Q06609-4]
NP_001157742.1, NM_001164270.1 [Q06609-3]
NP_002866.2, NM_002875.4 [Q06609-1]
NP_597994.3, NM_133487.3 [Q06609-4]
XP_006720689.1, XM_006720626.3 [Q06609-1]
XP_011520159.1, XM_011521857.2 [Q06609-1]
XP_011520160.1, XM_011521858.2 [Q06609-1]
XP_011520161.1, XM_011521859.2 [Q06609-1]
XP_011520162.1, XM_011521860.2 [Q06609-1]
XP_011520163.1, XM_011521861.2 [Q06609-3]
UniGeneiHs.631709

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
1B22NMR-A1-114[»]
1N0WX-ray1.70A97-339[»]
5H1Belectron microscopy4.40A/B/C1-339[»]
5H1Celectron microscopy4.50A/B/C1-339[»]
5JZCelectron microscopy4.20A/B/C/D/E/F/G1-339[»]
5NP7electron microscopy4.20A/B/C/D/E/F/G1-339[»]
5NWLX-ray3.93A/B/C/D/E/F/G/H/I/J/K/L/M/N1-339[»]
ProteinModelPortaliQ06609
SMRiQ06609
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111825, 165 interactors
ComplexPortaliCPX-955 BRCC ubiquitin ligase complex
CORUMiQ06609
DIPiDIP-462N
ELMiQ06609
IntActiQ06609, 105 interactors
MINTiQ06609

Chemistry databases

BindingDBiQ06609
ChEMBLiCHEMBL2034807
DrugBankiDB05216 MP470
DB04395 Phosphoaminophosphonic Acid-Adenylate Ester

PTM databases

iPTMnetiQ06609
PhosphoSitePlusiQ06609

Polymorphism and mutation databases

BioMutaiRAD51
DMDMi548663

Proteomic databases

EPDiQ06609
MaxQBiQ06609
PeptideAtlasiQ06609
PRIDEiQ06609
ProteomicsDBi58464
58465 [Q06609-2]
58466 [Q06609-3]
58467 [Q06609-4]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
5888
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000267868; ENSP00000267868; ENSG00000051180 [Q06609-1]
ENST00000382643; ENSP00000372088; ENSG00000051180 [Q06609-4]
ENST00000423169; ENSP00000406602; ENSG00000051180 [Q06609-3]
ENST00000532743; ENSP00000433924; ENSG00000051180 [Q06609-4]
ENST00000557850; ENSP00000454176; ENSG00000051180 [Q06609-2]
GeneIDi5888
KEGGihsa:5888
UCSCiuc001zmi.5 human [Q06609-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5888
DisGeNETi5888
EuPathDBiHostDB:ENSG00000051180.16

GeneCards: human genes, protein and diseases

More...
GeneCardsi
RAD51
GeneReviewsiRAD51
HGNCiHGNC:9817 RAD51
HPAiCAB010381
HPA039310
MalaCardsiRAD51
MIMi114480 phenotype
179617 gene
614508 phenotype
617244 phenotype
neXtProtiNX_Q06609
OpenTargetsiENSG00000051180
Orphaneti238722 Familial congenital mirror movements
84 Fanconi anemia
145 Hereditary breast and ovarian cancer syndrome
PharmGKBiPA34176

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

GeneTreeiENSGT00940000156157
HOGENOMiHOG000227426
HOVERGENiHBG001504
InParanoidiQ06609
KOiK04482
OMAiYNTDHQT
OrthoDBiEOG091G09QY
PhylomeDBiQ06609
TreeFamiTF101218

Enzyme and pathway databases

ReactomeiR-HSA-5685938 HDR through Single Strand Annealing (SSA)
R-HSA-5685942 HDR through Homologous Recombination (HRR)
R-HSA-5693554 Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA)
R-HSA-5693568 Resolution of D-loop Structures through Holliday Junction Intermediates
R-HSA-5693579 Homologous DNA Pairing and Strand Exchange
R-HSA-5693616 Presynaptic phase of homologous DNA pairing and strand exchange
R-HSA-8953750 Transcriptional Regulation by E2F6
R-HSA-912446 Meiotic recombination
SignaLinkiQ06609
SIGNORiQ06609

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
RAD51 human
EvolutionaryTraceiQ06609

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
RAD51

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
5888
PMAP-CutDBiQ06609

Protein Ontology

More...
PROi
PR:Q06609

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000051180 Expressed in 133 organ(s), highest expression level in embryo
CleanExiHS_RAD51
ExpressionAtlasiQ06609 baseline and differential
GenevisibleiQ06609 HS

Family and domain databases

CDDicd01123 Rad51_DMC1_radA, 1 hit
InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR011941 DNA_recomb/repair_Rad51
IPR013632 DNA_recomb/repair_Rad51_C
IPR016467 DNA_recomb/repair_RecA-like
IPR010995 DNA_repair_Rad51/TF_NusA_a-hlx
IPR027417 P-loop_NTPase
IPR033925 Rad51_DMC1_RadA
IPR020588 RecA_ATP-bd
IPR020587 RecA_monomer-monomer_interface
PfamiView protein in Pfam
PF08423 Rad51, 1 hit
PIRSFiPIRSF005856 Rad51, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 1 hit
SUPFAMiSSF47794 SSF47794, 1 hit
SSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR02239 recomb_RAD51, 1 hit
PROSITEiView protein in PROSITE
PS50162 RECA_2, 1 hit
PS50163 RECA_3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<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 nameiRAD51_HUMAN
<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: Q06609
Secondary accession number(s): B0FXP0
, B2R8T6, Q6FHX9, Q6ZNA8, Q9BV60
<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: June 1, 1994
Last sequence update: June 1, 1994
Last modified: December 5, 2018
This is version 211 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 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.

<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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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