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Entry version 185 (18 Sep 2019)
Sequence version 1 (01 Nov 1998)
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Protein

Barrier-to-autointegration factor

Gene

BANF1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

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

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

Plays fundamental roles in nuclear assembly, chromatin organization, gene expression and gonad development. May potently compress chromatin structure and be involved in membrane recruitment and chromatin decondensation during nuclear assembly. Contains 2 non-specific dsDNA-binding sites which may promote DNA cross-bridging.1 Publication
(Microbial infection) Exploited by retroviruses for inhibiting self-destructing autointegration of retroviral DNA, thereby promoting integration of viral DNA into the host chromosome. EMD and BAF are cooperative cofactors of HIV-1 infection. Association of EMD with the viral DNA requires the presence of BAF and viral integrase. The association of viral DNA with chromatin requires the presence of BAF and EMD.2 Publications
(Microbial infection) In case of poxvirus infection, has an antiviral activity by blocking viral DNA replication.1 Publication

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

GO - Biological processi

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

Molecular functionDNA-binding
Biological processHost-virus interaction

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-162592 Integration of provirus
R-HSA-164843 2-LTR circle formation
R-HSA-175567 Integration of viral DNA into host genomic DNA
R-HSA-177539 Autointegration results in viral DNA circles
R-HSA-180689 APOBEC3G mediated resistance to HIV-1 infection
R-HSA-180910 Vpr-mediated nuclear import of PICs
R-HSA-2980766 Nuclear Envelope Breakdown
R-HSA-2995383 Initiation of Nuclear Envelope Reformation

SIGNOR Signaling Network Open Resource

More...
SIGNORi
O75531

<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:
Barrier-to-autointegration factor
Alternative name(s):
Breakpoint cluster region protein 1
Cleaved into the following chain:
<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:BANF1
Synonyms:BAF, BCRG1
<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 11

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:17397 BANF1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
603811 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_O75531

<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, Cytoplasm, Nucleus

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

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

Nestor-Guillermo progeria syndrome (NGPS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn atypical progeroid syndrome characterized by normal development in the first years of life, later followed by the emergence of generalized lipoatrophy, severe osteoporosis, and marked osteolysis. The atrophic facial subcutaneous fat pad and the marked osteolysis of the maxilla and mandible result in a typical pseudosenile facial appearance with micrognathia, prominent subcutaneous venous patterning, a convex nasal ridge, and proptosis. Cognitive development is completely normal. Patients do not have cardiovascular dysfunction, atherosclerosis, or metabolic anomalies.
Related information in OMIM
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_06595412A → T in NGPS; shows a dramatic reduction in BANF1 protein levels indicating that the mutation impairs protein stability. 1 PublicationCorresponds to variant dbSNP:rs387906871EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi2 – 4TTS → AAA: 95% nuclear localization. Loss of BAF phosphorylation and ability to suppress vaccinia virus DNA replication. 2 Publications3
Mutagenesisi2 – 4TTS → DDD: 85% cytoplasmic localization. 1 Publication3
Mutagenesisi2 – 3TT → AA: No effect on the initial rate of phosphorylation but a second slow phase of phosphorylation is absent. 1 Publication2
Mutagenesisi4S → A: Delayed phosphorylation with a 10-fold decrease in the initial phosphorylation rate. 71% loss of binding to lamin A. 2 Publications1
Mutagenesisi4S → D: 75% cytoplasmic localization. 1 Publication1
Mutagenesisi4S → E: Complete loss of phosphorylation and mislocalization of EMD in nucleus. 1 Publication1
Mutagenesisi6K → A: Complete loss of LEMD3/MAN1 and histone H1/H3 binding. 4 Publications1
Mutagenesisi6K → E: Complete loss of dsDNA and LEMD3/MAN1 binding. 4 Publications1
Mutagenesisi8R → A: Enhances histone H1/H3 binding. 2 Publications1
Mutagenesisi8R → E: Complete loss of LEMD3/MAN1 binding. 2 Publications1
Mutagenesisi9D → A: Reduces binding to dsDNA, LEMD3/MAN1 and histone H1/H3. 3 Publications1
Mutagenesisi14P → A: No effect on LEMD3/MAN1 and enhances histone H1/H3 binding. 3 Publications1
Mutagenesisi18K → A: No effect on histone H1/H3 binding. 2 Publications1
Mutagenesisi25G → E: Complete loss of dsDNA, EMD, histone H1/H3 and LEMD3/MAN1 binding. 3 Publications1
Mutagenesisi25G → Q: Complete loss of EMD binding and reduces dsDNA binding. 3 Publications1
Mutagenesisi26I → A: Reduces histone H1/H3 and LEMD3/MAN1 binding. Fails to promote HIV-1 genome integration. 3 Publications1
Mutagenesisi26I → K: Fails to promote HIV-1 genome integration. 3 Publications1
Mutagenesisi27G → E: Fails to bind dsDNA. 1 Publication1
Mutagenesisi27G → Q: Reduces binding to dsDNA. 1 Publication1
Mutagenesisi29V → A: No effect on histone H1/H3 binding. 1 Publication1
Mutagenesisi32K → E: No effect on histone H1/H3 binding. 1 Publication1
Mutagenesisi33K → E: No effect on histone H1/H3 binding. 1 Publication1
Mutagenesisi37R → A: No effect on histone H1/H3 binding. 2 Publications1
Mutagenesisi37R → E: Reduces LEMD3/MAN1 binding. 2 Publications1
Mutagenesisi41K → A: No effect on histone H1/H3 and LEMD3/MAN1 binding. 3 Publications1
Mutagenesisi41K → E: Reduces histone H1/H3 binding. 3 Publications1
Mutagenesisi46L → E: Complete loss of dsDNA, histone H1/H3 and LEMD3/MAN1 binding. 3 Publications1
Mutagenesisi47G → E: Complete loss of EMD, histone H1/h3 and LEMD3/MAN1 binding. 3 Publications1
Mutagenesisi50L → A: Reduces LEMD3/MAN1 binding. No effect on Histone H1/H3 binding. 3 Publications1
Mutagenesisi50L → K: Fails to promote HIV-1 genome integration. 3 Publications1
Mutagenesisi51V → E: Complete loss of EMD, and histone H1/H3 binding. Reduces dsDNA and LEMD3/MAN1 binding. 3 Publications1
Mutagenesisi53K → A: No effect on LEMD3/MAN1 binding. Enhances histone H1/H3 binding. 4 Publications1
Mutagenesisi53K → E: Complete loss of EMD binding. Reduces LEMD3/MAN1 binding. Enhances histone H1/H3 binding. 4 Publications1
Mutagenesisi54K → A: Reduces LEMD3/MAN1 binding. No effect on histone H1/H3 binding. 4 Publications1
Mutagenesisi54K → E: Reduces binding to dsDNA. 4 Publications1
Mutagenesisi60R → E: No effect on histone H1/H3 binding. 1 Publication1
Mutagenesisi62W → A: Complete loss of LEMD3/MAN1 binding. Enhances histone H1/H3 binding. 3 Publications1
Mutagenesisi64K → E: Enhances histone H1/H3 binding. 1 Publication1
Mutagenesisi75R → E: Reduces binding to dsDNA. No effect on histone H1/H3 binding. 2 Publications1
Mutagenesisi80C → A: No effect on histone H1/H3 and LEMD3/MAN1 binding. 3 Publications1
Mutagenesisi82R → E: No effect on histone H1/H3 binding. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
8815

MalaCards human disease database

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MalaCardsi
BANF1
MIMi614008 phenotype

Open Targets

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OpenTargetsi
ENSG00000175334

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

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Orphaneti
280576 Nestor-Guillermo progeria syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA134903639

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
BANF1

<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_00004231901 – 89Barrier-to-autointegration factorAdd BLAST89
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved; alternateCombined sources
ChainiPRO_00002210262 – 89Barrier-to-autointegration factor, N-terminally processedAdd BLAST88

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 residuei1N-acetylmethionineCombined sources1
Modified residuei2N-acetylthreonine; in Barrier-to-autointegration factor, N-terminally processedCombined sources1
Modified residuei2Phosphothreonine; by viral VacV B1 kinase, VRK1 and VRK21 Publication1
Modified residuei3Phosphothreonine; by viral VacV B1 kinase, VRK1 and VRK21 Publication1
Modified residuei4Phosphoserine; by viral VacV B1 kinase, VRK1 and VRK22 Publications1

<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

Ser-4 is the major site of phosphorylation as compared to Thr-2 and Thr-3. Phosphorylation on Thr-2; Thr-3 and Ser-4 disrupts its ability to bind DNA and reduces its ability to bind LEM domain-containing proteins. Non phosphorylated BAF seems to enhance binding between EMD and LMNA. Dephosphorylated by protein phosphatase 2A (PP2A) following interaction with ANKLE2/LEM4 during mitotic exit, leading to mitotic nuclear envelope reassembly.3 Publications
(Microbial infection) Phosphorylated at the N-terminus by vaccinia virus (VacV) B1 kinase, leading to BANF1 relocalization to the cytoplasm, loss of dimerization and impaired DNA binding activity (PubMed:24600006, PubMed:16495336). Hyperphosphorylation is linked to the loss of ability to suppress vaccinia virus replication (PubMed:24600006).2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O75531

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
O75531

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
O75531

MaxQB - The MaxQuant DataBase

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MaxQBi
O75531

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

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PaxDbi
O75531

PeptideAtlas

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PeptideAtlasi
O75531

PRoteomics IDEntifications database

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PRIDEi
O75531

ProteomicsDB human proteome resource

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ProteomicsDBi
50071

Consortium for Top Down Proteomics

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TopDownProteomicsi
O75531

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O75531

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

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PhosphoSitePlusi
O75531

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
O75531

<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

Widely expressed. Expressed in colon, brain, heart, kidney, liver, lung, ovary, pancreas, placenta, prostate, skeletal muscle, small intestine, spleen and testis. Not detected in thymus and peripheral blood leukocytes.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000175334 Expressed in 92 organ(s), highest expression level in myometrium

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O75531 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O75531 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB032896
HPA039242

<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

Homodimer (PubMed:16337940, PubMed:22399800). Heterodimerizes with BAFL (PubMed:16337940).

Interacts with ANKLE2/LEM4, leading to decreased phosphorylation by VRK1 and promoting dephosphorylation by protein phosphatase 2A (PP2A) (PubMed:22770216). Binds non-specifically to double-stranded DNA, and is found as a hexamer or dodecamer upon DNA binding. Binds to LEM domain-containing nuclear proteins such as LEMD3/MAN1, TMPO/LAP2 and EMD (emerin) (PubMed:11792822, PubMed:15681850).

Interacts with ANKLE1 (via LEM domain); the interaction may favor BANF1 dimerization (PubMed:22399800).

Interacts with CRX and LMNA (lamin-A). Binds linker histone H1.1 and core histones H3 (PubMed:16203725).

6 Publications

(Microbial infection)

Interacts with HIV-1 pre-integration complex in cytoplasm by binding to viral matrix protein and Gag polyprotein.

2 Publications

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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
114342, 96 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
O75531

Database of interacting proteins

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DIPi
DIP-50395N

Protein interaction database and analysis system

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IntActi
O75531, 33 interactors

Molecular INTeraction database

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MINTi
O75531

STRING: functional protein association networks

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STRINGi
9606.ENSP00000310275

<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

189
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
O75531

Database of comparative protein structure models

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ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
O75531

<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>Domaini20 – 35HhH1 PublicationAdd BLAST16

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

Has a helix-hairpin-helix (HhH) structural motif conserved among proteins that bind non-specifically to DNA.1 Publication
LEM domain proteins bind centrally on the BAF dimer.1 Publication

<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 BAF family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG4233 Eukaryota
ENOG4111URU LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000018613

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O75531

KEGG Orthology (KO)

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KOi
K21870

Identification of Orthologs from Complete Genome Data

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OMAi
TDWCEEF

Database of Orthologous Groups

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OrthoDBi
1617480at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O75531

TreeFam database of animal gene trees

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TreeFami
TF315060

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.150.40, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR004122 BAF_prot
IPR036617 BAF_sf

The PANTHER Classification System

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PANTHERi
PTHR12912 PTHR12912, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF02961 BAF, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM01023 BAF, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF47798 SSF47798, 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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

O75531-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTTSQKHRDF VAEPMGEKPV GSLAGIGEVL GKKLEERGFD KAYVVLGQFL
60 70 80
VLKKDEDLFR EWLKDTCGAN AKQSRDCFGC LREWCDAFL
Length:89
Mass (Da):10,059
Last modified:November 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:i9A2180A2D284F5D0
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PJJ8E9PJJ8_HUMAN
Barrier-to-autointegration factor
BANF1
28Annotation 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 AAC08964 differs from that shown. Reason: Frameshift at position 87.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06595412A → T in NGPS; shows a dramatic reduction in BANF1 protein levels indicating that the mutation impairs protein stability. 1 PublicationCorresponds to variant dbSNP:rs387906871EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AF070447 mRNA Translation: AAC23575.1
AF044773 mRNA Translation: AAC08964.1 Frameshift.
AF068235 mRNA Translation: AAD15901.1
CR542140 mRNA Translation: CAG46937.1
BC005942 mRNA Translation: AAH05942.1
BC107702 mRNA Translation: AAI07703.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS8125.1

NCBI Reference Sequences

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RefSeqi
NP_001137457.1, NM_001143985.1
NP_003851.1, NM_003860.3
XP_016874003.1, XM_017018514.1
XP_016874004.1, XM_017018515.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000312175; ENSP00000310275; ENSG00000175334
ENST00000445560; ENSP00000416128; ENSG00000175334
ENST00000527348; ENSP00000432867; ENSG00000175334
ENST00000533166; ENSP00000433760; ENSG00000175334

Database of genes from NCBI RefSeq genomes

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GeneIDi
8815

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:8815

UCSC genome browser

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UCSCi
uc001ogo.4 human

<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
AF070447 mRNA Translation: AAC23575.1
AF044773 mRNA Translation: AAC08964.1 Frameshift.
AF068235 mRNA Translation: AAD15901.1
CR542140 mRNA Translation: CAG46937.1
BC005942 mRNA Translation: AAH05942.1
BC107702 mRNA Translation: AAI07703.1
CCDSiCCDS8125.1
RefSeqiNP_001137457.1, NM_001143985.1
NP_003851.1, NM_003860.3
XP_016874003.1, XM_017018514.1
XP_016874004.1, XM_017018515.1

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
1CI4X-ray1.90A/B1-89[»]
1QCKNMR-A/B1-89[»]
2BZFX-ray2.87A1-89[»]
2EZXNMR-A/B1-89[»]
2EZYNMR-A/B1-89[»]
2EZZNMR-A/B1-89[»]
2ODGNMR-A/B1-89[»]
6GHDX-ray2.10A/C/D/E2-89[»]
SMRiO75531
ModBaseiSearch...

Protein-protein interaction databases

BioGridi114342, 96 interactors
CORUMiO75531
DIPiDIP-50395N
IntActiO75531, 33 interactors
MINTiO75531
STRINGi9606.ENSP00000310275

PTM databases

iPTMnetiO75531
PhosphoSitePlusiO75531
SwissPalmiO75531

Polymorphism and mutation databases

BioMutaiBANF1

Proteomic databases

EPDiO75531
jPOSTiO75531
MassIVEiO75531
MaxQBiO75531
PaxDbiO75531
PeptideAtlasiO75531
PRIDEiO75531
ProteomicsDBi50071
TopDownProteomicsiO75531

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000312175; ENSP00000310275; ENSG00000175334
ENST00000445560; ENSP00000416128; ENSG00000175334
ENST00000527348; ENSP00000432867; ENSG00000175334
ENST00000533166; ENSP00000433760; ENSG00000175334
GeneIDi8815
KEGGihsa:8815
UCSCiuc001ogo.4 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
8815
DisGeNETi8815

GeneCards: human genes, protein and diseases

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GeneCardsi
BANF1
HGNCiHGNC:17397 BANF1
HPAiCAB032896
HPA039242
MalaCardsiBANF1
MIMi603811 gene
614008 phenotype
neXtProtiNX_O75531
OpenTargetsiENSG00000175334
Orphaneti280576 Nestor-Guillermo progeria syndrome
PharmGKBiPA134903639

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG4233 Eukaryota
ENOG4111URU LUCA
GeneTreeiENSGT00390000018613
InParanoidiO75531
KOiK21870
OMAiTDWCEEF
OrthoDBi1617480at2759
PhylomeDBiO75531
TreeFamiTF315060

Enzyme and pathway databases

ReactomeiR-HSA-162592 Integration of provirus
R-HSA-164843 2-LTR circle formation
R-HSA-175567 Integration of viral DNA into host genomic DNA
R-HSA-177539 Autointegration results in viral DNA circles
R-HSA-180689 APOBEC3G mediated resistance to HIV-1 infection
R-HSA-180910 Vpr-mediated nuclear import of PICs
R-HSA-2980766 Nuclear Envelope Breakdown
R-HSA-2995383 Initiation of Nuclear Envelope Reformation
SIGNORiO75531

Miscellaneous databases

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

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ChiTaRSi
BANF1 human
EvolutionaryTraceiO75531

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
Barrier_to_autointegration_factor_1

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

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GenomeRNAii
8815

Pharos

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Pharosi
O75531

Protein Ontology

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PROi
PR:O75531

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000175334 Expressed in 92 organ(s), highest expression level in myometrium
ExpressionAtlasiO75531 baseline and differential
GenevisibleiO75531 HS

Family and domain databases

Gene3Di1.10.150.40, 1 hit
InterProiView protein in InterPro
IPR004122 BAF_prot
IPR036617 BAF_sf
PANTHERiPTHR12912 PTHR12912, 1 hit
PfamiView protein in Pfam
PF02961 BAF, 1 hit
SMARTiView protein in SMART
SM01023 BAF, 1 hit
SUPFAMiSSF47798 SSF47798, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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 nameiBAF_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: O75531
Secondary accession number(s): O60558, Q6FGG7
<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: July 15, 1999
Last sequence update: November 1, 1998
Last modified: September 18, 2019
This is version 185 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  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
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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