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Entry version 173 (13 Feb 2019)
Sequence version 1 (01 Aug 1998)
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Protein

Nibrin

Gene

NBN

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 MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. The complex is involved in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity, cell cycle checkpoint control 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. NBN modulate the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-PKcs to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. NBN also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. NBN is a major player in the control of intra-S-phase checkpoint and there is some evidence that NBN is involved in G1 and G2 checkpoints. The roles of NBS1/MRN encompass DNA damage sensor, signal transducer, and effector, which enable cells to maintain DNA integrity and genomic stability. Forms a complex with RBBP8 to link DNA double-strand break sensing to resection. Enhances AKT1 phosphorylation possibly by association with the mTORC2 complex.5 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>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

  • damaged DNA binding Source: GO_Central
  • protein N-terminus binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB

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

Biological processCell cycle, DNA damage, DNA repair, Meiosis

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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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
O60934

<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:
Nibrin
Alternative name(s):
Cell cycle regulatory protein p95
Nijmegen breakage syndrome protein 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:NBN
Synonyms:NBS, NBS1, P95
<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 8

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000104320.13

Human Gene Nomenclature Database

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HGNCi
HGNC:7652 NBN

Online Mendelian Inheritance in Man (OMIM)

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MIMi
602667 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_O60934

<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, 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 (NBS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder characterized by chromosomal instability, radiation sensitivity, microcephaly, growth retardation, immunodeficiency and predisposition to cancer, particularly to lymphoid malignancies.
See also OMIM:251260
Breast cancer (BC)1 Publication
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_025795150L → F in BC. 1 PublicationCorresponds to variant dbSNP:rs773119929Ensembl.1
Aplastic anemia (AA)1 Publication
Disease susceptibility may be associated with variations affecting the gene represented in this entry.
Disease descriptionA form of anemia in which the bone marrow fails to produce adequate numbers of peripheral blood elements. It is characterized by peripheral pancytopenia and marrow hypoplasia.
See also OMIM:609135
Defects in NBN might play a role in the pathogenesis of childhood acute lymphoblastic leukemia (ALL).1 Publication

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>Mutagenesisi28R → A: Disrupts nuclear foci formation and block phosphorylation in response to ionizing radiation. 1 Publication1
Mutagenesisi45H → A: Disrupts nuclear foci formation and block phosphorylation in response to ionizing radiation. 1 Publication1
Mutagenesisi136 – 137GG → EE: Disrupts nuclear foci formation and block phosphorylation in response to ionizing radiation. 1 Publication2
Mutagenesisi176Y → A: Disrupts nuclear foci formation and block phosphorylation in response to ionizing radiation. 1 Publication1
Mutagenesisi343S → A: Abrogates ATM-dependent phosphorylation. 1 Publication1
Mutagenesisi397S → A: Abrogates ATM-dependent phosphorylation. No loss of interaction with KPNA2. 2 Publications1
Mutagenesisi465 – 466KR → AA: Blocks the association with KPNA2, and reduces nuclear foci formation in response to ionizing radiation. 1 Publication2
Mutagenesisi583Q → K: No loss of interaction with KPNA2. 1 Publication1
Mutagenesisi615S → A: Abrogates ATM-dependent phosphorylation. 1 Publication1
Mutagenesisi736 – 737EE → AA: Decreases ATM binding. 1 Publication2
Mutagenesisi741 – 742DD → AA: Decreases ATM binding. 1 Publication2
Mutagenesisi745 – 746RY → AA: Decreases ATM binding. 1 Publication2

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

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DisGeNETi
4683

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

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GeneReviewsi
NBN

MalaCards human disease database

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MalaCardsi
NBN
MIMi114480 phenotype
251260 phenotype
609135 phenotype

Open Targets

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OpenTargetsi
ENSG00000104320

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

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Orphaneti
1331 Familial prostate cancer
145 Hereditary breast and ovarian cancer syndrome
647 Nijmegen breakage syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA31457

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
NBN

<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_00002310431 – 754NibrinAdd BLAST754

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 residuei278Phosphoserine; by ATM1 Publication1
Modified residuei337PhosphothreonineCombined sources1
Modified residuei343Phosphoserine; by ATMCombined sources2 Publications1
Modified residuei347PhosphoserineCombined sources1
Modified residuei397PhosphoserineCombined sources1 Publication1
Modified residuei402PhosphothreonineCombined sources1
Modified residuei432PhosphoserineCombined sources1
Modified residuei509PhosphoserineCombined sources1
Modified residuei518PhosphoserineCombined sources1
<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-linki529Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki571Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki582Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei615Phosphoserine1 Publication1
Modified residuei673PhosphoserineCombined sources1

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

Phosphorylated by ATM in response of ionizing radiation, and such phosphorylation is responsible intra-S phase checkpoint control and telomere maintenance.3 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O60934

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
O60934

MaxQB - The MaxQuant DataBase

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MaxQBi
O60934

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

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PaxDbi
O60934

PeptideAtlas

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PeptideAtlasi
O60934

PRoteomics IDEntifications database

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PRIDEi
O60934

ProteomicsDB human proteome resource

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ProteomicsDBi
49678

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O60934

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

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PhosphoSitePlusi
O60934

<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

Ubiquitous. Expressed at high levels in testis.

<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

Up-regulated by ionizing radiation (IR).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000104320 Expressed in 244 organ(s), highest expression level in endometrium epithelium

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O60934 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O60934 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB003836
HPA001429

<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:26215093, PubMed:9590181, PubMed:9705271, PubMed:11238951). As part of the MRN complex, interacts with 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). Interacts with histone H2AFX this requires phosphorylation of H2AFX on 'Ser-139' (PubMed:12419185). Interacts with HJURP (PubMed:17823411). Interacts with INTS3 (PubMed:19683501). Interacts with KPNA2 (PubMed:16188882). Interacts with TERF2 (PubMed:10888888). Interacts with RBBP8; the interaction links the role of the MRN complex in DNA double-strand break sensing to resection (PubMed:19759395). Interacts with SP100; recruits NBN to PML bodies (PubMed:12470659). Interacts with ATF2 (PubMed:15916964). Interacts with MTOR, MAPKAP1 isoform 2 and RICTOR; indicative for an association with the mTORC2 complex (PubMed:23762398). Interacts with MRNIP (PubMed:27568553).15 Publications
(Microbial infection) Interacts with herpes simplex virus 1 protein UL12.1 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
110763, 95 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
O60934

Database of interacting proteins

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DIPi
DIP-33605N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
O60934

Protein interaction database and analysis system

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IntActi
O60934, 39 interactors

Molecular INTeraction database

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MINTi
O60934

STRING: functional protein association networks

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STRINGi
9606.ENSP00000265433

<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

1754
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
5WQDX-ray3.00H/I/J/K/L/M/N423-438[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
O60934

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

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SMRi
O60934

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>Domaini24 – 83FHAPROSITE-ProRule annotationAdd BLAST60
Domaini105 – 181BRCTAdd BLAST77

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>Regioni111 – 328Mediates interaction with SP100By similarityAdd BLAST218
Regioni221 – 402Interaction with MTOR, MAPKAP1 and RICTOR1 PublicationAdd BLAST182

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>Motifi461 – 467Nuclear localization signal7
Motifi736 – 743EEXXXDDL motif8

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 biasi448 – 451Poly-Gln4

<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 FHA and BRCT domains are likely to have a crucial role for both binding to histone H2AFX and for relocalization of MRE11/RAD50 complex to the vicinity of DNA damage.1 Publication
The C-terminal domain contains a MRE11-binding site, and this interaction is required for the nuclear localization of the MRN complex.1 Publication
The EEXXXDDL motif at the C-terminus is required for the interaction with ATM and its recruitment to sites of DNA damage and promote the phosphorylation of ATM substrates, leading to the events of DNA damage response.1 Publication

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IK5M Eukaryota
ENOG410Y1R8 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000000521

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG053070

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O60934

KEGG Orthology (KO)

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KOi
K10867

Identification of Orthologs from Complete Genome Data

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OMAi
LWSTKEE

Database of Orthologous Groups

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OrthoDBi
831679at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O60934

TreeFam database of animal gene trees

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TreeFami
TF101103

Family and domain databases

Conserved Domains Database

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CDDi
cd00027 BRCT, 1 hit
cd00060 FHA, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.40.50.10190, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR001357 BRCT_dom
IPR036420 BRCT_dom_sf
IPR013908 DNA-repair_Nbs1_C
IPR000253 FHA_dom
IPR040227 Nibrin-rel
IPR032429 Nibrin_BRCT2
IPR016592 Nibrin_met
IPR008984 SMAD_FHA_dom_sf

The PANTHER Classification System

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PANTHERi
PTHR12162 PTHR12162, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00498 FHA, 1 hit
PF08599 Nbs1_C, 1 hit
PF16508 NIBRIN_BRCT_II, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF011869 Nibrin_animal, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00240 FHA, 1 hit
SM01348 Nbs1_C, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF49879 SSF49879, 1 hit
SSF52113 SSF52113, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50006 FHA_DOMAIN, 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>Sequence (1+)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 has 1 described isoform and 6 potential isoforms that are computationally mapped.Show allAlign All

O60934-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MWKLLPAAGP AGGEPYRLLT GVEYVVGRKN CAILIENDQS ISRNHAVLTA
60 70 80 90 100
NFSVTNLSQT DEIPVLTLKD NSKYGTFVNE EKMQNGFSRT LKSGDGITFG
110 120 130 140 150
VFGSKFRIEY EPLVACSSCL DVSGKTALNQ AILQLGGFTV NNWTEECTHL
160 170 180 190 200
VMVSVKVTIK TICALICGRP IVKPEYFTEF LKAVESKKQP PQIESFYPPL
210 220 230 240 250
DEPSIGSKNV DLSGRQERKQ IFKGKTFIFL NAKQHKKLSS AVVFGGGEAR
260 270 280 290 300
LITEENEEEH NFFLAPGTCV VDTGITNSQT LIPDCQKKWI QSIMDMLQRQ
310 320 330 340 350
GLRPIPEAEI GLAVIFMTTK NYCDPQGHPS TGLKTTTPGP SLSQGVSVDE
360 370 380 390 400
KLMPSAPVNT TTYVADTESE QADTWDLSER PKEIKVSKME QKFRMLSQDA
410 420 430 440 450
PTVKESCKTS SNNNSMVSNT LAKMRIPNYQ LSPTKLPSIN KSKDRASQQQ
460 470 480 490 500
QTNSIRNYFQ PSTKKRERDE ENQEMSSCKS ARIETSCSLL EQTQPATPSL
510 520 530 540 550
WKNKEQHLSE NEPVDTNSDN NLFTDTDLKS IVKNSASKSH AAEKLRSNKK
560 570 580 590 600
REMDDVAIED EVLEQLFKDT KPELEIDVKV QKQEEDVNVR KRPRMDIETN
610 620 630 640 650
DTFSDEAVPE SSKISQENEI GKKRELKEDS LWSAKEISNN DKLQDDSEML
660 670 680 690 700
PKKLLLTEFR SLVIKNSTSR NPSGINDDYG QLKNFKKFKK VTYPGAGKLP
710 720 730 740 750
HIIGGSDLIA HHARKNTELE EWLRQEMEVQ NQHAKEESLA DDLFRYNPYL

KRRR
Length:754
Mass (Da):84,959
Last modified:August 1, 1998 - 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:iCD602F09BA73DAB6
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
A0A0C4DG07A0A0C4DG07_HUMAN
Nibrin
NBN hCG_33061
672Annotation 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>
E5RGU1E5RGU1_HUMAN
Nibrin
NBN
159Annotation 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>
E5RGR7E5RGR7_HUMAN
Nibrin
NBN
164Annotation 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>
E5RGN7E5RGN7_HUMAN
Nibrin
NBN
92Annotation 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>
E2QRP0E2QRP0_HUMAN
Nibrin
NBN
58Annotation 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>
A0A087X1V5A0A087X1V5_HUMAN
Nibrin
NBN
124Annotation 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 AAI08651 differs from that shown. Contaminating sequence. Potential poly-A sequence starting in position 550.Curated
The sequence CAH56160 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.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 conflicti247G → R in BAD96976 (Ref. 6) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02579293S → L in some childhood acute lymphoblastic leukemia patients; uncertain pathological significance; rare variant. 1 PublicationCorresponds to variant dbSNP:rs12721593EnsemblClinVar.1
Natural variantiVAR_02579395D → N in some childhood acute lymphoblastic leukemia patients; uncertain pathological significance; rare variant. 1 PublicationCorresponds to variant dbSNP:rs61753720EnsemblClinVar.1
Natural variantiVAR_025794105K → N1 PublicationCorresponds to variant dbSNP:rs13312858Ensembl.1
Natural variantiVAR_051226142N → S. Corresponds to variant dbSNP:rs769414EnsemblClinVar.1
Natural variantiVAR_025795150L → F in BC. 1 PublicationCorresponds to variant dbSNP:rs773119929Ensembl.1
Natural variantiVAR_025796171I → V in some childhood acute lymphoblastic leukemia patients; uncertain pathological significance; rare variant; associated with aplastic anemia at homozygosity. 2 PublicationsCorresponds to variant dbSNP:rs61754966EnsemblClinVar.1
Natural variantiVAR_025797185E → Q6 PublicationsCorresponds to variant dbSNP:rs1805794EnsemblClinVar.1
Natural variantiVAR_025798210V → F1 PublicationCorresponds to variant dbSNP:rs61754796EnsemblClinVar.1
Natural variantiVAR_025799215R → W1 PublicationCorresponds to variant dbSNP:rs34767364EnsemblClinVar.1
Natural variantiVAR_025800216Q → K1 PublicationCorresponds to variant dbSNP:rs769416Ensembl.1
Natural variantiVAR_025801266P → L1 PublicationCorresponds to variant dbSNP:rs769420EnsemblClinVar.1
Natural variantiVAR_051227408K → E. Corresponds to variant dbSNP:rs34120922EnsemblClinVar.1
Natural variantiVAR_025802497T → A1 PublicationCorresponds to variant dbSNP:rs3026268EnsemblClinVar.1
Natural variantiVAR_025803574L → I1 PublicationCorresponds to variant dbSNP:rs142334798EnsemblClinVar.1
Natural variantiVAR_064738679Y → H Found in a renal cell carcinoma sample; somatic mutation. 1 Publication1

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
AF051334 mRNA Translation: AAC39732.1
AF058696 mRNA Translation: AAC39752.1
AB013139 Genomic DNA Translation: BAA28616.1
AF069291 Genomic DNA Translation: AAC62232.1
AK312410 mRNA Translation: BAG35323.1
AK223256 mRNA Translation: BAD96976.1
AY566246 Genomic DNA Translation: AAS59158.1
CH471060 Genomic DNA Translation: EAW91660.1
BC108650 mRNA Translation: AAI08651.1 Sequence problems.
BC136802 mRNA Translation: AAI36803.1
BC136803 mRNA Translation: AAI36804.1
BX640816 mRNA Translation: CAH56160.1 Different initiation.

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS6249.1

Protein sequence database of the Protein Information Resource

More...
PIRi
T00393

NCBI Reference Sequences

More...
RefSeqi
NP_001019859.1, NM_001024688.2
NP_002476.2, NM_002485.4
XP_011515347.1, XM_011517045.1

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.492208

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000265433; ENSP00000265433; ENSG00000104320

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
4683

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:4683

UCSC genome browser

More...
UCSCi
uc003yej.2 human

Keywords - Coding sequence diversityi

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

<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

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF051334 mRNA Translation: AAC39732.1
AF058696 mRNA Translation: AAC39752.1
AB013139 Genomic DNA Translation: BAA28616.1
AF069291 Genomic DNA Translation: AAC62232.1
AK312410 mRNA Translation: BAG35323.1
AK223256 mRNA Translation: BAD96976.1
AY566246 Genomic DNA Translation: AAS59158.1
CH471060 Genomic DNA Translation: EAW91660.1
BC108650 mRNA Translation: AAI08651.1 Sequence problems.
BC136802 mRNA Translation: AAI36803.1
BC136803 mRNA Translation: AAI36804.1
BX640816 mRNA Translation: CAH56160.1 Different initiation.
CCDSiCCDS6249.1
PIRiT00393
RefSeqiNP_001019859.1, NM_001024688.2
NP_002476.2, NM_002485.4
XP_011515347.1, XM_011517045.1
UniGeneiHs.492208

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5WQDX-ray3.00H/I/J/K/L/M/N423-438[»]
ProteinModelPortaliO60934
SMRiO60934
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110763, 95 interactors
CORUMiO60934
DIPiDIP-33605N
ELMiO60934
IntActiO60934, 39 interactors
MINTiO60934
STRINGi9606.ENSP00000265433

PTM databases

iPTMnetiO60934
PhosphoSitePlusiO60934

Polymorphism and mutation databases

BioMutaiNBN

Proteomic databases

EPDiO60934
jPOSTiO60934
MaxQBiO60934
PaxDbiO60934
PeptideAtlasiO60934
PRIDEiO60934
ProteomicsDBi49678

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265433; ENSP00000265433; ENSG00000104320
GeneIDi4683
KEGGihsa:4683
UCSCiuc003yej.2 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4683
DisGeNETi4683
EuPathDBiHostDB:ENSG00000104320.13

GeneCards: human genes, protein and diseases

More...
GeneCardsi
NBN
GeneReviewsiNBN
HGNCiHGNC:7652 NBN
HPAiCAB003836
HPA001429
MalaCardsiNBN
MIMi114480 phenotype
251260 phenotype
602667 gene
609135 phenotype
neXtProtiNX_O60934
OpenTargetsiENSG00000104320
Orphaneti1331 Familial prostate cancer
145 Hereditary breast and ovarian cancer syndrome
647 Nijmegen breakage syndrome
PharmGKBiPA31457

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IK5M Eukaryota
ENOG410Y1R8 LUCA
GeneTreeiENSGT00390000000521
HOVERGENiHBG053070
InParanoidiO60934
KOiK10867
OMAiLWSTKEE
OrthoDBi831679at2759
PhylomeDBiO60934
TreeFamiTF101103

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
SIGNORiO60934

Miscellaneous databases

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Nibrin

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

More...
GenomeRNAii
4683

Protein Ontology

More...
PROi
PR:O60934

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000104320 Expressed in 244 organ(s), highest expression level in endometrium epithelium
ExpressionAtlasiO60934 baseline and differential
GenevisibleiO60934 HS

Family and domain databases

CDDicd00027 BRCT, 1 hit
cd00060 FHA, 1 hit
Gene3Di3.40.50.10190, 1 hit
InterProiView protein in InterPro
IPR001357 BRCT_dom
IPR036420 BRCT_dom_sf
IPR013908 DNA-repair_Nbs1_C
IPR000253 FHA_dom
IPR040227 Nibrin-rel
IPR032429 Nibrin_BRCT2
IPR016592 Nibrin_met
IPR008984 SMAD_FHA_dom_sf
PANTHERiPTHR12162 PTHR12162, 1 hit
PfamiView protein in Pfam
PF00498 FHA, 1 hit
PF08599 Nbs1_C, 1 hit
PF16508 NIBRIN_BRCT_II, 1 hit
PIRSFiPIRSF011869 Nibrin_animal, 1 hit
SMARTiView protein in SMART
SM00240 FHA, 1 hit
SM01348 Nbs1_C, 1 hit
SUPFAMiSSF49879 SSF49879, 1 hit
SSF52113 SSF52113, 1 hit
PROSITEiView protein in PROSITE
PS50006 FHA_DOMAIN, 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 nameiNBN_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: O60934
Secondary accession number(s): B2R626
, B2RNC5, O60672, Q32NF7, Q53FM6, Q63HR6, Q7LDM2
<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: April 4, 2006
Last sequence update: August 1, 1998
Last modified: February 13, 2019
This is version 173 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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