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Entry version 178 (10 Apr 2019)
Sequence version 1 (01 Feb 1997)
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Protein

DNA repair protein RAD50

Gene

RAD50

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

Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis. The complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11. RAD50 may be required to bind DNA ends and hold them in close proximity. This could facilitate searches for short or long regions of sequence homology in the recombining DNA templates, and may also stimulate the activity of DNA ligases and/or restrict the nuclease activity of MRE11 to prevent nucleolytic degradation past a given point (PubMed:11741547, PubMed:9590181, PubMed:9705271, PubMed:9651580). The complex may also be required for DNA damage signaling via activation of the ATM kinase (PubMed:15064416). In telomeres the MRN complex may modulate t-loop formation (PubMed:10888888).6 Publications

Miscellaneous

In case of infection by adenovirus E4, the MRN complex is inactivated and degraded by viral oncoproteins, thereby preventing concatenation of viral genomes in infected cells.

<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

Zn2+By similarityNote: Binds 1 zinc ion per homodimer.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi681ZincPROSITE-ProRule annotation1
Metal bindingi684ZincPROSITE-ProRule annotation1

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 bindingi36 – 43ATPSequence analysis8

<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 functionHydrolase
Biological processCell cycle, DNA damage, DNA repair, Host-virus interaction, Meiosis
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-2559586 DNA Damage/Telomere Stress Induced Senescence
R-HSA-5685938 HDR through Single Strand Annealing (SSA)
R-HSA-5685939 HDR through MMEJ (alt-NHEJ)
R-HSA-5685942 HDR through Homologous Recombination (HRR)
R-HSA-5693548 Sensing of DNA Double Strand Breaks
R-HSA-5693554 Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA)
R-HSA-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-HSA-5693568 Resolution of D-loop Structures through Holliday Junction Intermediates
R-HSA-5693571 Nonhomologous End-Joining (NHEJ)
R-HSA-5693579 Homologous DNA Pairing and Strand Exchange
R-HSA-5693607 Processing of DNA double-strand break ends
R-HSA-5693616 Presynaptic phase of homologous DNA pairing and strand exchange
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
R-HSA-69473 G2/M DNA damage checkpoint
R-HSA-912446 Meiotic recombination

SIGNOR Signaling Network Open Resource

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SIGNORi
Q92878

<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 RAD50 (EC:3.6.-.-)
Short name:
hRAD50
<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:RAD50
<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 5

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000113522.13

Human Gene Nomenclature Database

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HGNCi
HGNC:9816 RAD50

Online Mendelian Inheritance in Man (OMIM)

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MIMi
604040 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q92878

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Nucleus, Telomere

<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

Nijmegen breakage syndrome-like disorder (NBSLD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder similar to Nijmegen breakage syndrome and characterized by chromosomal instability, radiation sensitivity, microcephaly, growth retardation, short stature and bird-like face. Immunodeficiency is absent.
See also OMIM:613078

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>Mutagenesisi42K → N: Abolishes ability to degrade ATP. 1 Publication1
Mutagenesisi1231D → A: Abolishes ability to degrade ATP. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
10111

MalaCards human disease database

More...
MalaCardsi
RAD50
MIMi613078 phenotype

Open Targets

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OpenTargetsi
ENSG00000113522

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

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Orphaneti
145 Hereditary breast and ovarian cancer syndrome
240760 Nijmegen breakage syndrome-like disorder

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA34175

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
RAD50

Domain mapping of disease mutations (DMDM)

More...
DMDMi
60392986

<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_00001386411 – 1312DNA repair protein RAD50Add BLAST1312

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 residuei635PhosphoserineCombined sources1
Modified residuei690PhosphothreonineCombined sources1
Modified residuei959N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q92878

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q92878

MaxQB - The MaxQuant DataBase

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MaxQBi
Q92878

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

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PaxDbi
Q92878

PeptideAtlas

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PeptideAtlasi
Q92878

PRoteomics IDEntifications database

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PRIDEi
Q92878

ProteomicsDB human proteome resource

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ProteomicsDBi
75562
75563 [Q92878-2]
75564 [Q92878-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q92878

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

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PhosphoSitePlusi
Q92878

<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

Expressed at very low level in most tissues, except in testis where it is expressed at higher level. Expressed in fibroblasts.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000113522 Expressed in 218 organ(s), highest expression level in corpus callosum

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q92878 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q92878 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB022103
CAB024979
HPA052291

<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

Component of the MRN complex composed of two heterodimers RAD50/MRE11 associated with a single NBN (PubMed:8756642, PubMed:9590181, PubMed:9705271, PubMed:10839544, PubMed:26215093). As part of the MRN complex, interacts with MCM8 and MCM9; the interaction recruits the complex to DNA repair sites (PubMed:26215093). Component of the BASC complex, at least composed of BRCA1, MSH2, MSH6, MLH1, ATM, BLM, RAD50, MRE11 and NBN (PubMed:10783165). Found in a complex with TERF2 (PubMed:10888888). Interacts with RINT1 (PubMed:11096100). Interacts with BRCA1 via its N-terminal domain (PubMed:10426999). Interacts with DCLRE1C/Artemis (PubMed:15456891, PubMed:15723659). Interacts with MRNIP (PubMed:27568553).12 Publications
(Microbial infection) Interacts with herpes simplex virus 1 protein UL12 (PubMed:20943970).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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
115417, 129 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q92878

Database of interacting proteins

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DIPi
DIP-33606N

Protein interaction database and analysis system

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IntActi
Q92878, 63 interactors

Molecular INTeraction database

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MINTi
Q92878

STRING: functional protein association networks

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STRINGi
9606.ENSP00000368100

<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

11312
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5GOXX-ray2.40A/B585-766[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q92878

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

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SMRi
Q92878

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...

<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>Domaini635 – 734Zinc-hookPROSITE-ProRule annotationAdd BLAST100

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili228 – 359Sequence analysisAdd BLAST132
Coiled coili401 – 598Sequence analysisAdd BLAST198
Coiled coili635 – 673Sequence analysisAdd BLAST39
Coiled coili706 – 734Sequence analysisAdd BLAST29
Coiled coili789 – 1079Sequence analysisAdd BLAST291

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 biasi1201 – 1238Ala/Asp-rich (DA-box)Add BLAST38

<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 zinc-hook, which separates the large intramolecular coiled coil regions, contains 2 Cys residues that coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another RAD50 molecule, thereby forming a V-shaped homodimer. The two heads of the homodimer, which constitute the ATP-binding domain, interact with the MRE11 homodimer (By similarity).By similarity

<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 SMC family. RAD50 subfamily.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0962 Eukaryota
COG0419 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000018781

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000090195

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG058033

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q92878

KEGG Orthology (KO)

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KOi
K10866

Identification of Orthologs from Complete Genome Data

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OMAi
GNRSYNY

Database of Orthologous Groups

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OrthoDBi
179362at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q92878

TreeFam database of animal gene trees

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TreeFami
TF101217

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR027417 P-loop_NTPase
IPR038729 Rad50/SbcC_AAA
IPR004584 Rad50_eukaryotes
IPR013134 Zn_hook_RAD50

Pfam protein domain database

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Pfami
View protein in Pfam
PF13476 AAA_23, 1 hit
PF04423 Rad50_zn_hook, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF52540 SSF52540, 2 hits

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR00606 rad50, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51131 ZN_HOOK, 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 (3+)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.

This entry describes 3 <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 3 described isoforms and 6 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q92878-1) [UniParc]FASTAAdd to basket
Also known as: RAD50-1, RAD50-2

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
MSRIEKMSIL GVRSFGIEDK DKQIITFFSP LTILVGPNGA GKTTIIECLK
60 70 80 90 100
YICTGDFPPG TKGNTFVHDP KVAQETDVRA QIRLQFRDVN GELIAVQRSM
110 120 130 140 150
VCTQKSKKTE FKTLEGVITR TKHGEKVSLS SKCAEIDREM ISSLGVSKAV
160 170 180 190 200
LNNVIFCHQE DSNWPLSEGK ALKQKFDEIF SATRYIKALE TLRQVRQTQG
210 220 230 240 250
QKVKEYQMEL KYLKQYKEKA CEIRDQITSK EAQLTSSKEI VKSYENELDP
260 270 280 290 300
LKNRLKEIEH NLSKIMKLDN EIKALDSRKK QMEKDNSELE EKMEKVFQGT
310 320 330 340 350
DEQLNDLYHN HQRTVREKER KLVDCHRELE KLNKESRLLN QEKSELLVEQ
360 370 380 390 400
GRLQLQADRH QEHIRARDSL IQSLATQLEL DGFERGPFSE RQIKNFHKLV
410 420 430 440 450
RERQEGEAKT ANQLMNDFAE KETLKQKQID EIRDKKTGLG RIIELKSEIL
460 470 480 490 500
SKKQNELKNV KYELQQLEGS SDRILELDQE LIKAERELSK AEKNSNVETL
510 520 530 540 550
KMEVISLQNE KADLDRTLRK LDQEMEQLNH HTTTRTQMEM LTKDKADKDE
560 570 580 590 600
QIRKIKSRHS DELTSLLGYF PNKKQLEDWL HSKSKEINQT RDRLAKLNKE
610 620 630 640 650
LASSEQNKNH INNELKRKEE QLSSYEDKLF DVCGSQDFES DLDRLKEEIE
660 670 680 690 700
KSSKQRAMLA GATAVYSQFI TQLTDENQSC CPVCQRVFQT EAELQEVISD
710 720 730 740 750
LQSKLRLAPD KLKSTESELK KKEKRRDEML GLVPMRQSII DLKEKEIPEL
760 770 780 790 800
RNKLQNVNRD IQRLKNDIEE QETLLGTIMP EEESAKVCLT DVTIMERFQM
810 820 830 840 850
ELKDVERKIA QQAAKLQGID LDRTVQQVNQ EKQEKQHKLD TVSSKIELNR
860 870 880 890 900
KLIQDQQEQI QHLKSTTNEL KSEKLQISTN LQRRQQLEEQ TVELSTEVQS
910 920 930 940 950
LYREIKDAKE QVSPLETTLE KFQQEKEELI NKKNTSNKIA QDKLNDIKEK
960 970 980 990 1000
VKNIHGYMKD IENYIQDGKD DYKKQKETEL NKVIAQLSEC EKHKEKINED
1010 1020 1030 1040 1050
MRLMRQDIDT QKIQERWLQD NLTLRKRNEE LKEVEEERKQ HLKEMGQMQV
1060 1070 1080 1090 1100
LQMKSEHQKL EENIDNIKRN HNLALGRQKG YEEEIIHFKK ELREPQFRDA
1110 1120 1130 1140 1150
EEKYREMMIV MRTTELVNKD LDIYYKTLDQ AIMKFHSMKM EEINKIIRDL
1160 1170 1180 1190 1200
WRSTYRGQDI EYIEIRSDAD ENVSASDKRR NYNYRVVMLK GDTALDMRGR
1210 1220 1230 1240 1250
CSAGQKVLAS LIIRLALAET FCLNCGIIAL DEPTTNLDRE NIESLAHALV
1260 1270 1280 1290 1300
EIIKSRSQQR NFQLLVITHD EDFVELLGRS EYVEKFYRIK KNIDQCSEIV
1310
KCSVSSLGFN VH
Length:1,312
Mass (Da):153,892
Last modified:February 1, 1997 - 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:i1F208C3817FC41FC
GO
Isoform 2 (identifier: Q92878-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-5: MSRIE → MLIFSVRDMFA

Show »
Length:1,318
Mass (Da):154,587
Checksum:i54B578956FC29852
GO
Isoform 3 (identifier: Q92878-3) [UniParc]FASTAAdd to basket
Also known as: RAD50-3

The sequence of this isoform differs from the canonical sequence as follows:
     1-139: Missing.

Show »
Length:1,173
Mass (Da):138,432
Checksum:iD6734A4E4D898AAE
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 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E7EN38E7EN38_HUMAN
DNA repair protein RAD50
RAD50
660Annotation 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>
E7ESD9E7ESD9_HUMAN
DNA repair protein RAD50
RAD50
551Annotation 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>
H7C0P8H7C0P8_HUMAN
DNA repair protein RAD50
RAD50
158Annotation 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>
E9PM98E9PM98_HUMAN
DNA repair protein RAD50
RAD50
102Annotation 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>
H7C0V2H7C0V2_HUMAN
DNA repair protein RAD50
RAD50
157Annotation 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>
C9JNH8C9JNH8_HUMAN
DNA repair protein RAD50
RAD50
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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAH62603 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated

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 conflicti204K → E in CAA99729 (Ref. 3) Curated1
Sequence conflicti723E → K in AAH62603 (PubMed:15489334).Curated1
Sequence conflicti723E → K in AAH73850 (PubMed:15489334).Curated1
Sequence conflicti733V → A in CAA99729 (Ref. 3) Curated1

Natural variant

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_02552694I → L1 PublicationCorresponds to variant dbSNP:rs28903085EnsemblClinVar.1
Natural variantiVAR_029168127V → I. Corresponds to variant dbSNP:rs28903086EnsemblClinVar.1
Natural variantiVAR_022085191T → I. Corresponds to variant dbSNP:rs2230017EnsemblClinVar.1
Natural variantiVAR_029169193R → W. Corresponds to variant dbSNP:rs28903087EnsemblClinVar.1
Natural variantiVAR_025527224R → H1 PublicationCorresponds to variant dbSNP:rs28903088EnsemblClinVar.1
Natural variantiVAR_034436315V → L. Corresponds to variant dbSNP:rs28903090EnsemblClinVar.1
Natural variantiVAR_061779469G → A. Corresponds to variant dbSNP:rs55653181EnsemblClinVar.1
Natural variantiVAR_020958616K → E1 PublicationCorresponds to variant dbSNP:rs1047380Ensembl.1
Natural variantiVAR_020959697V → A1 PublicationCorresponds to variant dbSNP:rs1047382Ensembl.1
Natural variantiVAR_029170842V → A. Corresponds to variant dbSNP:rs28903093EnsemblClinVar.1
Natural variantiVAR_020960964Y → H1 PublicationCorresponds to variant dbSNP:rs1047386Ensembl.1
Natural variantiVAR_020961973K → M1 PublicationCorresponds to variant dbSNP:rs1129482Ensembl.1
Natural variantiVAR_0209621038R → G. Corresponds to variant dbSNP:rs1047387Ensembl.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.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0125901 – 139Missing in isoform 3. 1 PublicationAdd BLAST139
Alternative sequenceiVSP_0125911 – 5MSRIE → MLIFSVRDMFA in isoform 2. 1 Publication5

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U63139 mRNA Translation: AAB07119.1
AF057299 mRNA Translation: AAD50325.1
AF057300 mRNA Translation: AAD50326.1
Z75311 mRNA Translation: CAA99729.1
AC116366 Genomic DNA No translation available.
AC004042 Genomic DNA No translation available.
CH471062 Genomic DNA Translation: EAW62329.1
BC062603 mRNA Translation: AAH62603.1 Sequence problems.
BC073850 mRNA Translation: AAH73850.1
BC136436 mRNA Translation: AAI36437.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS34233.1 [Q92878-1]

NCBI Reference Sequences

More...
RefSeqi
NP_005723.2, NM_005732.3 [Q92878-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.633509

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000378823; ENSP00000368100; ENSG00000113522 [Q92878-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
10111

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:10111

UCSC genome browser

More...
UCSCi
uc003kxi.4 human [Q92878-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<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
U63139 mRNA Translation: AAB07119.1
AF057299 mRNA Translation: AAD50325.1
AF057300 mRNA Translation: AAD50326.1
Z75311 mRNA Translation: CAA99729.1
AC116366 Genomic DNA No translation available.
AC004042 Genomic DNA No translation available.
CH471062 Genomic DNA Translation: EAW62329.1
BC062603 mRNA Translation: AAH62603.1 Sequence problems.
BC073850 mRNA Translation: AAH73850.1
BC136436 mRNA Translation: AAI36437.1
CCDSiCCDS34233.1 [Q92878-1]
RefSeqiNP_005723.2, NM_005732.3 [Q92878-1]
UniGeneiHs.633509

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5GOXX-ray2.40A/B585-766[»]
ProteinModelPortaliQ92878
SMRiQ92878
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115417, 129 interactors
CORUMiQ92878
DIPiDIP-33606N
IntActiQ92878, 63 interactors
MINTiQ92878
STRINGi9606.ENSP00000368100

PTM databases

iPTMnetiQ92878
PhosphoSitePlusiQ92878

Polymorphism and mutation databases

BioMutaiRAD50
DMDMi60392986

Proteomic databases

EPDiQ92878
jPOSTiQ92878
MaxQBiQ92878
PaxDbiQ92878
PeptideAtlasiQ92878
PRIDEiQ92878
ProteomicsDBi75562
75563 [Q92878-2]
75564 [Q92878-3]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000378823; ENSP00000368100; ENSG00000113522 [Q92878-1]
GeneIDi10111
KEGGihsa:10111
UCSCiuc003kxi.4 human [Q92878-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
10111
DisGeNETi10111
EuPathDBiHostDB:ENSG00000113522.13

GeneCards: human genes, protein and diseases

More...
GeneCardsi
RAD50
HGNCiHGNC:9816 RAD50
HPAiCAB022103
CAB024979
HPA052291
MalaCardsiRAD50
MIMi604040 gene
613078 phenotype
neXtProtiNX_Q92878
OpenTargetsiENSG00000113522
Orphaneti145 Hereditary breast and ovarian cancer syndrome
240760 Nijmegen breakage syndrome-like disorder
PharmGKBiPA34175

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0962 Eukaryota
COG0419 LUCA
GeneTreeiENSGT00390000018781
HOGENOMiHOG000090195
HOVERGENiHBG058033
InParanoidiQ92878
KOiK10866
OMAiGNRSYNY
OrthoDBi179362at2759
PhylomeDBiQ92878
TreeFamiTF101217

Enzyme and pathway databases

ReactomeiR-HSA-2559586 DNA Damage/Telomere Stress Induced Senescence
R-HSA-5685938 HDR through Single Strand Annealing (SSA)
R-HSA-5685939 HDR through MMEJ (alt-NHEJ)
R-HSA-5685942 HDR through Homologous Recombination (HRR)
R-HSA-5693548 Sensing of DNA Double Strand Breaks
R-HSA-5693554 Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA)
R-HSA-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-HSA-5693568 Resolution of D-loop Structures through Holliday Junction Intermediates
R-HSA-5693571 Nonhomologous End-Joining (NHEJ)
R-HSA-5693579 Homologous DNA Pairing and Strand Exchange
R-HSA-5693607 Processing of DNA double-strand break ends
R-HSA-5693616 Presynaptic phase of homologous DNA pairing and strand exchange
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
R-HSA-69473 G2/M DNA damage checkpoint
R-HSA-912446 Meiotic recombination
SIGNORiQ92878

Miscellaneous databases

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

More...
ChiTaRSi
RAD50 human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Rad50

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

More...
GenomeRNAii
10111

Protein Ontology

More...
PROi
PR:Q92878

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000113522 Expressed in 218 organ(s), highest expression level in corpus callosum
ExpressionAtlasiQ92878 baseline and differential
GenevisibleiQ92878 HS

Family and domain databases

InterProiView protein in InterPro
IPR027417 P-loop_NTPase
IPR038729 Rad50/SbcC_AAA
IPR004584 Rad50_eukaryotes
IPR013134 Zn_hook_RAD50
PfamiView protein in Pfam
PF13476 AAA_23, 1 hit
PF04423 Rad50_zn_hook, 1 hit
SUPFAMiSSF52540 SSF52540, 2 hits
TIGRFAMsiTIGR00606 rad50, 1 hit
PROSITEiView protein in PROSITE
PS51131 ZN_HOOK, 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 nameiRAD50_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: Q92878
Secondary accession number(s): B9EGF5
, O43254, Q6GMT7, Q6P5X3, Q9UP86
<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: February 1, 2005
Last sequence update: February 1, 1997
Last modified: April 10, 2019
This is version 178 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. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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