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Protein

Formin-binding protein 1

Gene

FNBP1

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

May act as a link between RND2 signaling and regulation of the actin cytoskeleton (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during the late stage of clathrin-mediated endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization via the recruitment of WASL/N-WASP, which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. May be required for the lysosomal retention of FASLG/FASL.By similarity5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei166Mediates end-to-end attachment of dimers1

<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

  • identical protein binding Source: IntAct
  • lipid binding Source: UniProtKB-KW

GO - Biological processi

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

Biological processEndocytosis
LigandLipid-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-8856828 Clathrin-mediated endocytosis

<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:
Formin-binding protein 1
Alternative name(s):
Formin-binding protein 17
Short name:
hFBP17
<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:FNBP1
Synonyms:FBP17, KIAA0554
<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 9

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000187239.16

Human Gene Nomenclature Database

More...
HGNCi
HGNC:17069 FNBP1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
606191 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q96RU3

<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

Cell membrane, Coated pit, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Lysosome, Membrane

<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

A chromosomal aberration involving FNBP1 is found in acute leukemias. Translocation t(9;11)(q34;q23) with KMT2A/MLL1. The relatively low incidence of the KMT2A/MLL1-FNBP1 fusion protein in acute leukemia may reflect the marginal capacity of this fusion protein to induce cellular transformation.

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>Mutagenesisi7L → E: Impairs membrane tubulation but does not affect lipid-binding. 1 Publication1
Mutagenesisi33K → E: Abolishes membrane invagination. 2 Publications1
Mutagenesisi33K → Q: Impairs lipid-binding and induction of membrane tubulation; when associated with Q-35. 2 Publications1
Mutagenesisi35R → Q: Impairs lipid-binding and induction of membrane tubulation; when associated with Q-33. 1 Publication1
Mutagenesisi51 – 52KK → QQ: Impairs lipid-binding and induction of membrane tubulation. 1 Publication2
Mutagenesisi113 – 114RK → QQ: Impairs lipid-binding and induction of membrane tubulation. 1 Publication2
Mutagenesisi165T → A: Abolishes membrane invagination. 1 Publication1
Mutagenesisi166K → A: Abolishes membrane invagination. 1 Publication1
Mutagenesisi168D → A, N or R: No significant effect. 1 Publication1
Mutagenesisi210P → A: Disrupts helix kink and moderately increases diameter of the induced tubular membrane. 1 Publication1
Mutagenesisi515 – 520Missing : Abrogates interaction with TNKS. 1 Publication6
Mutagenesisi515R → A: Impairs interaction with TNKS. 1 Publication1
Mutagenesisi519D → A: Impairs interaction with TNKS; when associated with A-515. 1 Publication1
Mutagenesisi602P → L: Abrogates interaction with DNM1, DNM2 and DNM3. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
23048

Open Targets

More...
OpenTargetsi
ENSG00000187239

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA128394597

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
FNBP1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
118572321

<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_00002614301 – 617Formin-binding protein 1Add BLAST617

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 residuei66N6-acetyllysineCombined sources1
Modified residuei110N6-acetyllysineCombined sources1
Modified residuei296PhosphoserineCombined sources1
Modified residuei299PhosphoserineCombined sources1
Modified residuei349PhosphoserineCombined sources1
Modified residuei359PhosphoserineCombined sources1
Modified residuei497PhosphoserineBy similarity1
Modified residuei500PhosphotyrosineBy similarity1
Modified residuei521PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q96RU3

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q96RU3

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

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PaxDbi
Q96RU3

PeptideAtlas

More...
PeptideAtlasi
Q96RU3

PRoteomics IDEntifications database

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PRIDEi
Q96RU3

ProteomicsDB human proteome resource

More...
ProteomicsDBi
78035
78036 [Q96RU3-2]
78037 [Q96RU3-3]
78038 [Q96RU3-4]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q96RU3

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

More...
PhosphoSitePlusi
Q96RU3

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
Q96RU3

<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

Very highly expressed in the epithelial cells of the gastrointestinal tract, respiratory, reproductive and urinary systems. Also highly expressed in brown adipose tissue, cardiomyocytes, enteric ganglia and glucagon producing cells of the pancreas. Expressed in germ cells of the testis and all regions of the brain.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000187239 Expressed in 239 organ(s), highest expression level in corpus callosum

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q96RU3 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q96RU3 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA019691
HPA022119

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts specifically with GTP-bound RND2 and CDC42. Interacts with PDE6G and microtubules (By similarity). Homodimerizes, the dimers can polymerize end-to-end to form filamentous structures. Interacts with AKAP9, ARHGAP17, DAAM1, DIAPH1, DIAPH2, DNM1, DNM2, DNM3, FASLG/FASL, SNX2 and WASL/N-WASP. May interact with TNKS.By similarity11 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)

More...
BioGridi
116686, 28 interactors

Database of interacting proteins

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DIPi
DIP-35355N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
Q96RU3

Protein interaction database and analysis system

More...
IntActi
Q96RU3, 26 interactors

Molecular INTeraction database

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MINTi
Q96RU3

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000413625

<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

1617
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q96RU3

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

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SMRi
Q96RU3

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q96RU3

<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>Domaini1 – 264F-BARPROSITE-ProRule annotationAdd BLAST264
Domaini404 – 481REM-1PROSITE-ProRule annotationAdd BLAST78
Domaini550 – 611SH3PROSITE-ProRule annotationAdd BLAST62

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>Regioni1 – 335Interaction with microtubulesBy similarityAdd BLAST335
Regioni1 – 79Required for self-association and induction of membrane tubulationAdd BLAST79
Regioni251 – 617Required for self-association and induction of membrane tubulationAdd BLAST367
Regioni400 – 552Interaction with RND2By similarityAdd BLAST153
Regioni495 – 617Interaction with PDE6GBy similarityAdd BLAST123
Regioni514 – 617Required for interaction with TNKS1 PublicationAdd BLAST104
Regioni535 – 617Interaction with DNM1 and DNM31 PublicationAdd BLAST83
Regioni550 – 617Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH22 PublicationsAdd BLAST68
Regioni553 – 610Interaction with FASLGAdd BLAST58
Regioni553 – 609Interaction with DNM2 and WASLAdd BLAST57

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 coili67 – 2591 PublicationAdd BLAST193
Coiled coili398 – 490By similarityAdd BLAST93

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 biasi340 – 345Poly-Pro6

<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 F-BAR domain binds the phospholipid membrane with its concave surface. The end-to-end polymerization of dimers of these domains provides a curved surface that fits best membranes with around 600 A diameter, and may drive tubulation.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 FNBP1 family.Curated

Keywords - Domaini

Coiled coil, SH3 domain

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410INNY Eukaryota
ENOG410ZU0I LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00510000046403

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000231767

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG002489

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q96RU3

KEGG Orthology (KO)

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KOi
K20121

Identification of Orthologs from Complete Genome Data

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OMAi
SYIECTL

Database of Orthologous Groups

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OrthoDBi
EOG091G038P

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q96RU3

TreeFam database of animal gene trees

More...
TreeFami
TF351162

Family and domain databases

Conserved Domains Database

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CDDi
cd07676 F-BAR_FBP17, 1 hit
cd12071 SH3_FBP17, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.20.1270.60, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR027267 AH/BAR_dom_sf
IPR031160 F_BAR
IPR001060 FCH_dom
IPR028532 FNBP1/FBP17
IPR037449 FNBP1_F-BAR
IPR035492 FNBP1_SH3
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain

The PANTHER Classification System

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PANTHERi
PTHR43990:SF5 PTHR43990:SF5, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00611 FCH, 1 hit
PF14604 SH3_9, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00055 FCH, 1 hit
SM00326 SH3, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF103657 SSF103657, 1 hit
SSF50044 SSF50044, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51741 F_BAR, 1 hit
PS51860 REM_1, 1 hit
PS50002 SH3, 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 (5+)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 5 <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 5 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q96RU3-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MSWGTELWDQ FDNLEKHTQW GIDILEKYIK FVKERTEIEL SYAKQLRNLS
60 70 80 90 100
KKYQPKKNSK EEEEYKYTSC KAFISNLNEM NDYAGQHEVI SENMASQIIV
110 120 130 140 150
DLARYVQELK QERKSNFHDG RKAQQHIETC WKQLESSKRR FERDCKEADR
160 170 180 190 200
AQQYFEKMDA DINVTKADVE KARQQAQIRH QMAEDSKADY SSILQKFNHE
210 220 230 240 250
QHEYYHTHIP NIFQKIQEME ERRIVRMGES MKTYAEVDRQ VIPIIGKCLD
260 270 280 290 300
GIVKAAESID QKNDSQLVIE AYKSGFEPPG DIEFEDYTQP MKRTVSDNSL
310 320 330 340 350
SNSRGEGKPD LKFGGKSKGK LWPFIKKNKL MSLLTSPHQP PPPPPASASP
360 370 380 390 400
SAVPNGPQSP KQQKEPLSHR FNEFMTSKPK IHCFRSLKRG LSLKLGATPE
410 420 430 440 450
DFSNLPPEQR RKKLQQKVDE LNKEIQKEMD QRDAITKMKD VYLKNPQMGD
460 470 480 490 500
PASLDHKLAE VSQNIEKLRV ETQKFEAWLA EVEGRLPARS EQARRQSGLY
510 520 530 540 550
DSQNPPTVNN CAQDRESPDG SYTEEQSQES EMKVLATDFD DEFDDEEPLP
560 570 580 590 600
AIGTCKALYT FEGQNEGTIS VVEGETLYVI EEDKGDGWTR IRRNEDEEGY
610
VPTSYVEVCL DKNAKDS
Length:617
Mass (Da):71,307
Last modified:November 28, 2006 - v2
<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:iF06E847C6E631EC3
GO
Isoform 2 (identifier: Q96RU3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     391-395: Missing.
     616-617: DS → GAKTYI

Show »
Length:616
Mass (Da):71,184
Checksum:iE82282A5164793B3
GO
Isoform 3 (identifier: Q96RU3-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     330-358: Missing.
     616-617: DS → GAKTYI

Show »
Length:592
Mass (Da):68,883
Checksum:i0CB6B44D9E174667
GO
Isoform 4 (identifier: Q96RU3-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     329-394: Missing.

Show »
Length:551
Mass (Da):64,056
Checksum:iBA7F73CA1A28A467
GO
Isoform 5 (identifier: Q96RU3-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     391-395: Missing.

Note: No experimental confirmation available.
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Length:612
Mass (Da):70,752
Checksum:i9E2543B3EDF09004
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 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B7ZL14B7ZL14_HUMAN
FNBP1 protein
FNBP1
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>
H0Y7W6H0Y7W6_HUMAN
Formin-binding protein 1
FNBP1
568Annotation 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 AAH62463 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence AAK49824 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAA25480 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAA91451 differs from that shown. Reason: Erroneous initiation.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 conflicti388K → E in BAA91451 (PubMed:14702039).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_029388490S → N1 PublicationCorresponds to variant dbSNP:rs1023000Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_021693329 – 394Missing in isoform 4. 1 PublicationAdd BLAST66
Alternative sequenceiVSP_021694330 – 358Missing in isoform 3. 1 PublicationAdd BLAST29
Alternative sequenceiVSP_021695391 – 395Missing in isoform 2 and isoform 5. 2 Publications5
Alternative sequenceiVSP_021696616 – 617DS → GAKTYI in isoform 2 and isoform 3. 1 Publication2

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
AF265550 mRNA Translation: AAK49824.1 Different initiation.
AB011126 mRNA Translation: BAA25480.1 Different initiation.
AK000975 mRNA Translation: BAA91451.1 Different initiation.
AK023681 mRNA Translation: BAB14638.1
AL136141 Genomic DNA No translation available.
AL158207 Genomic DNA No translation available.
BC062463 mRNA Translation: AAH62463.1 Sequence problems.
BC101755 mRNA Translation: AAI01756.1
BC143513 mRNA Translation: AAI43514.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS48040.1 [Q96RU3-1]
CCDS87699.1 [Q96RU3-3]

NCBI Reference Sequences

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RefSeqi
NP_055848.1, NM_015033.2 [Q96RU3-1]
XP_005251880.1, XM_005251823.2 [Q96RU3-2]
XP_005251881.1, XM_005251824.2 [Q96RU3-5]
XP_005251886.1, XM_005251829.2

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.189409

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000355681; ENSP00000347907; ENSG00000187239 [Q96RU3-3]
ENST00000420781; ENSP00000407548; ENSG00000187239 [Q96RU3-5]
ENST00000446176; ENSP00000413625; ENSG00000187239 [Q96RU3-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
23048

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:23048

UCSC genome browser

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UCSCi
uc004byw.2 human [Q96RU3-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, 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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF265550 mRNA Translation: AAK49824.1 Different initiation.
AB011126 mRNA Translation: BAA25480.1 Different initiation.
AK000975 mRNA Translation: BAA91451.1 Different initiation.
AK023681 mRNA Translation: BAB14638.1
AL136141 Genomic DNA No translation available.
AL158207 Genomic DNA No translation available.
BC062463 mRNA Translation: AAH62463.1 Sequence problems.
BC101755 mRNA Translation: AAI01756.1
BC143513 mRNA Translation: AAI43514.1
CCDSiCCDS48040.1 [Q96RU3-1]
CCDS87699.1 [Q96RU3-3]
RefSeqiNP_055848.1, NM_015033.2 [Q96RU3-1]
XP_005251880.1, XM_005251823.2 [Q96RU3-2]
XP_005251881.1, XM_005251824.2 [Q96RU3-5]
XP_005251886.1, XM_005251829.2
UniGeneiHs.189409

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
2EFLX-ray2.61A1-300[»]
ProteinModelPortaliQ96RU3
SMRiQ96RU3
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116686, 28 interactors
DIPiDIP-35355N
ELMiQ96RU3
IntActiQ96RU3, 26 interactors
MINTiQ96RU3
STRINGi9606.ENSP00000413625

PTM databases

iPTMnetiQ96RU3
PhosphoSitePlusiQ96RU3

Polymorphism and mutation databases

BioMutaiFNBP1
DMDMi118572321

Proteomic databases

EPDiQ96RU3
MaxQBiQ96RU3
PaxDbiQ96RU3
PeptideAtlasiQ96RU3
PRIDEiQ96RU3
ProteomicsDBi78035
78036 [Q96RU3-2]
78037 [Q96RU3-3]
78038 [Q96RU3-4]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000355681; ENSP00000347907; ENSG00000187239 [Q96RU3-3]
ENST00000420781; ENSP00000407548; ENSG00000187239 [Q96RU3-5]
ENST00000446176; ENSP00000413625; ENSG00000187239 [Q96RU3-1]
GeneIDi23048
KEGGihsa:23048
UCSCiuc004byw.2 human [Q96RU3-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
23048
DisGeNETi23048
EuPathDBiHostDB:ENSG00000187239.16

GeneCards: human genes, protein and diseases

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GeneCardsi
FNBP1
HGNCiHGNC:17069 FNBP1
HPAiHPA019691
HPA022119
MIMi606191 gene
neXtProtiNX_Q96RU3
OpenTargetsiENSG00000187239
PharmGKBiPA128394597

Human Unidentified Gene-Encoded large proteins database

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HUGEi
Search...

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410INNY Eukaryota
ENOG410ZU0I LUCA
GeneTreeiENSGT00510000046403
HOGENOMiHOG000231767
HOVERGENiHBG002489
InParanoidiQ96RU3
KOiK20121
OMAiSYIECTL
OrthoDBiEOG091G038P
PhylomeDBiQ96RU3
TreeFamiTF351162

Enzyme and pathway databases

ReactomeiR-HSA-8856828 Clathrin-mediated endocytosis

Miscellaneous databases

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

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ChiTaRSi
FNBP1 human
EvolutionaryTraceiQ96RU3

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
FNBP1

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

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GenomeRNAii
23048
PMAP-CutDBiQ96RU3

Protein Ontology

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PROi
PR:Q96RU3

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000187239 Expressed in 239 organ(s), highest expression level in corpus callosum
ExpressionAtlasiQ96RU3 baseline and differential
GenevisibleiQ96RU3 HS

Family and domain databases

CDDicd07676 F-BAR_FBP17, 1 hit
cd12071 SH3_FBP17, 1 hit
Gene3Di1.20.1270.60, 1 hit
InterProiView protein in InterPro
IPR027267 AH/BAR_dom_sf
IPR031160 F_BAR
IPR001060 FCH_dom
IPR028532 FNBP1/FBP17
IPR037449 FNBP1_F-BAR
IPR035492 FNBP1_SH3
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
PANTHERiPTHR43990:SF5 PTHR43990:SF5, 1 hit
PfamiView protein in Pfam
PF00611 FCH, 1 hit
PF14604 SH3_9, 1 hit
SMARTiView protein in SMART
SM00055 FCH, 1 hit
SM00326 SH3, 1 hit
SUPFAMiSSF103657 SSF103657, 1 hit
SSF50044 SSF50044, 1 hit
PROSITEiView protein in PROSITE
PS51741 F_BAR, 1 hit
PS51860 REM_1, 1 hit
PS50002 SH3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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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 nameiFNBP1_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: Q96RU3
Secondary accession number(s): B7ZL12
, E9PGQ4, O60301, Q3MIN8, Q5TC87, Q5TC88, Q6P658, Q7LGG2, Q9H8H8, Q9NWD1
<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: November 28, 2006
Last sequence update: November 28, 2006
Last modified: November 7, 2018
This is version 148 of the entry and version 2 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. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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